|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-499 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 771.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAlEQLG 82
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA-QAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPQLDVTENIFMGREKSKNeilGWIDRERMEEETKKILSRLGQEsISPNDLIRDLGVGKQQMVEISKALS 162
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRG---GLIDWRAMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKMISYM 242
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 243 VGEDVDNKFPKMKVEPGKESLRVENLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV 322
Cdd:COG1129 237 VGRELEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 323 KIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSNLKKYRENGFLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLS 402
Cdd:COG1129 317 RIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 403 GGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRF 482
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
|
490
....*....|....*..
gi 433671570 483 NTDEASKEKIMSAATGG 499
Cdd:COG1129 477 DREEATEEAIMAAATGG 493
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-495 |
0e+00 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 573.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHtPT---EGEIYIEGKKLEDNDpQKALEQLG 82
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKD-IRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPQLDVTENIFMGREKSKNeilGWIDRERMEEETKKILSRLGQeSISPNDLIRDLGVGKQQMVEISKALS 162
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLGNERAKR---GVIDWNETNRRARELLAKVGL-DESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRV--DNLTEDKMIS 240
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCraDEVTEDRIIR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 241 YMVGEDVDNKFPKMKVEPGKESLRVENLN--------RKgVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGAD--SK 310
Cdd:NF040905 236 GMVGRDLEDRYPERTPKIGEVVFEVKNWTvyhplhpeRK-VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 311 DSGDIYVHGKKVKIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSNLKKYRENGFLNLQEQRKDAIRMVDNLNIK 390
Cdd:NF040905 315 ISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 391 TPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRI 470
Cdd:NF040905 395 TPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRI 474
|
490 500
....*....|....*....|....*
gi 433671570 471 LVVHEGKITGRFNTDEASKEKIMSA 495
Cdd:NF040905 475 YVMNEGRITGELPREEASQERIMRL 499
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-499 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 558.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGV--HTPTEGEIYIEGKKLEDNDpQKAL 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASN-IRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 79 EQLGITPIYQELNLIPQLDVTENIFMGREKSKNeilGWIDRERMEEETKKILSRLGQEsISPNDLIRDLGVGKQQMVEIS 158
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLGNEITPG---GIMDYDAMYLRAQKLLAQLKLD-INPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 159 KALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKM 238
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 239 ISYMVGEDVDNKFPKMKVEPGKESLRVENL--------NRKGVlNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGA-DS 309
Cdd:PRK13549 236 ITMMVGRELTALYPREPHTIGEVILEVRNLtawdpvnpHIKRV-DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 310 KDSGDIYVHGKKVKIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSNLKKYRENGFLNLQEQRKDAIRMVDNLNI 389
Cdd:PRK13549 315 RWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 390 KTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDR 469
Cdd:PRK13549 395 KTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDR 474
|
490 500 510
....*....|....*....|....*....|
gi 433671570 470 ILVVHEGKITGRFNTDEASKEKIMSAATGG 499
Cdd:PRK13549 475 VLVMHEGKLKGDLINHNLTQEQVMEAALRS 504
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-492 |
1.10e-178 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 511.11 E-value: 1.10e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEq 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPIYQELNLIPQLDVTENIFMGREKSKneiLGWIDRERMEEETKKILSRLGQEsISPNDLIRDLGVGKQQMVEISKA 160
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGLEPTK---GGRLDRKAARARIRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 161 LSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKMIS 240
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 241 YMVGEDVDNKFPKMKVEPGKESLRVENLNRKG-----VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDI 315
Cdd:COG3845 236 LMVGREVLLRVEKAPAEPGEVVLEVENLSVRDdrgvpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 316 YVHGKKVKIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIAssnLKKYRE-----NGFLNLQEQRKDAIRMVDNLNIK 390
Cdd:COG3845 316 RLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLI---LGRYRRppfsrGGFLDRKAIRAFAEELIEEFDVR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 391 TPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRI 470
Cdd:COG3845 393 TPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRI 472
|
490 500
....*....|....*....|..
gi 433671570 471 LVVHEGKITGRFNTDEASKEKI 492
Cdd:COG3845 473 AVMYEGRIVGEVPAAEATREEI 494
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-498 |
1.84e-178 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 510.70 E-value: 1.84e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPqKALEQLG 82
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP-KSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPQLDVTENIFMGREKSKneILGWIDRERMEEETKKILSRLGQeSISPNDLIRDLGVGKQQMVEISKALS 162
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVN--RFGRIDWKKMYAEADKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKMISYM 242
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 243 VGEDVDNKFPKMKVEPGKESLRVENLNRKGVlNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV 322
Cdd:PRK10762 238 VGRKLEDQYPRLDKAPGEVRLKVDNLSGPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 323 KIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSNLKKY-RENGFLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQL 401
Cdd:PRK10762 317 VTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFsRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 402 SGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGR 481
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
490
....*....|....*..
gi 433671570 482 FNTDEASKEKIMSAATG 498
Cdd:PRK10762 477 FTREQATQEKLMAAAVG 493
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-496 |
7.73e-177 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 506.37 E-value: 7.73e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQlG 82
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPQLDVTENIFMGREKSKneiLGWIDRERMEEETKKILSRLGqESISPNDLIRDLGVGKQQMVEISKALS 162
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHK---GGIVNRRLLNYEAREQLEHLG-VDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIIT-DRVDNLTEDKMISY 241
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 242 MVGEDVDNKFPKMKVEPGKESLRVENLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKK 321
Cdd:PRK11288 237 MVGREIGDIYGYRPRPLGEVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 322 VKIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSNLKKYRENG-FLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQ 400
Cdd:PRK11288 317 IDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGcLINNRWEAENADRFIRSLNIKTPSREQLIMN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITG 480
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476
|
490
....*....|....*.
gi 433671570 481 RFNTDEASKEKIMSAA 496
Cdd:PRK11288 477 ELAREQATERQALSLA 492
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-497 |
1.55e-155 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 452.70 E-value: 1.55e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAlEQ 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA-AQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPIYQELNLIPQLDVTENIFMGREKSKnEILG--WIDRERMEEETKKILSRLGQEsISPNDLIRDLGVGKQQMVEIS 158
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLYIGRHLTK-KVCGvnIIDWREMRVRAAMMLLRVGLK-VDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 159 KALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKM 238
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 239 ISYMVGEDVDNKFPKMKVE----PGKESLRVENLNRK--GVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDS 312
Cdd:PRK09700 238 VRLMVGRELQNRFNAMKENvsnlAHETVFEVRNVTSRdrKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 313 GDIYVHGKKVKIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSN-LKKYRENGFLNL---QEQRKDAIRMVDNLN 388
Cdd:PRK09700 318 GEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRsLKDGGYKGAMGLfheVDEQRTAENQRELLA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 389 IKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSD 468
Cdd:PRK09700 398 LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCD 477
|
490 500 510
....*....|....*....|....*....|
gi 433671570 469 RILVVHEGKITGRF-NTDEASKEKIMSAAT 497
Cdd:PRK09700 478 RIAVFCEGRLTQILtNRDDMSEEEIMAWAL 507
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-497 |
3.43e-153 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 445.71 E-value: 3.43e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQlGITPIY 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN-GISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 88 QELNLIPQLDVTENIFMGREKSKNeilGWIDRERMEEETKKILSRLGQEsISPNDLIRDLGVGKQQMVEISKALSVETKL 167
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKG---MFVDQDKMYRDTKAIFDELDID-IDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 168 LILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKMISYMVGEDV 247
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 248 DNKFPKMKVEPGKESLRVENLN--RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKID 325
Cdd:PRK10982 236 TQRFPDKENKPGEVILEVRNLTslRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 326 SPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSNLKKYREN-GFLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGG 404
Cdd:PRK10982 316 NANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKvGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 405 NQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNT 484
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDT 475
|
490
....*....|...
gi 433671570 485 DEASKEKIMSAAT 497
Cdd:PRK10982 476 KTTTQNEILRLAS 488
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-496 |
2.38e-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: 2.38e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGV--HTPTEGEIYIEGKKLEDNDPQKAlEQLGI 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDT-ERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLIPQLDVTENIFMGREKSKNEilGWIDRERMEEETKKILSRLgQESISPNDL-IRDLGVGKQQMVEISKALS 162
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPG--GRMAYNAMYLRAKNLLREL-QLDADNVTRpVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKMISYM 242
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 243 VGEDVDNKFPKMKVEPGKESLRVENL--------NRKGVlNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGA-DSKDSG 313
Cdd:TIGR02633 238 VGREITSLYPHEPHEIGDVILEARNLtcwdvinpHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 314 DIYVHGKKVKIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSNLKKYRENGFLNLQEQRKDAIRMVDNLNIKTPN 393
Cdd:TIGR02633 317 NVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTAS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 394 VQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVV 473
Cdd:TIGR02633 397 PFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
490 500
....*....|....*....|...
gi 433671570 474 HEGKITGRFNTDEASKEKIMSAA 496
Cdd:TIGR02633 477 GEGKLKGDFVNHALTQEQVLAAA 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-499 |
4.58e-127 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 379.78 E-value: 4.58e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAlEQLGI 83
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA-HQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLIPQLDVTENIFMGREKSKNeilgwiDRERMEEetkkILSRLGQeSISPNDLIRDLGVGKQQMVEISKALSV 163
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLPKRQA------SMQKMKQ----LLAALGC-QLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKMISYM- 242
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAIt 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 243 -VGEDVD-NKFPKMKVE---------PGKESLRVENLNRKGvLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKD 311
Cdd:PRK15439 238 pAAREKSlSASQKLWLElpgnrrqqaAGAPVLTVEDLTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 312 SGDIYVHGKKVKIDSPKVALENGIALLTEDRKEQGLFLKQSVKFNIASSNlkkYRENGFLnLQEQRKDAI--RMVDNLNI 389
Cdd:PRK15439 317 GGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCALT---HNRRGFW-IKPARENAVleRYRRALNI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 390 KTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDR 469
Cdd:PRK15439 393 KFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADR 472
|
490 500 510
....*....|....*....|....*....|
gi 433671570 470 ILVVHEGKITGRFNTDEASKEKIMSAATGG 499
Cdd:PRK15439 473 VLVMHQGEISGALTGAAINVDTIMRLAFGE 502
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
259-478 |
2.14e-83 |
|
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: 255.82 E-value: 2.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 259 GKESLRVENLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALL 338
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDRKEQGLFLKQSVKFNIASSNLkkyrengflnlqeqrkdairmvdnlniktpnvqtkclqLSGGNQQKVVIGKWLNTE 418
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-227 |
1.37e-76 |
|
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: 237.71 E-value: 1.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALeQLGITP 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR-RAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQelnlipqldvtenifmgrekskneilgwidrermeeetkkilsrlgqesispndlirdLGVGKQQMVEISKALSVET 165
Cdd:cd03216 80 VYQ----------------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIIT 227
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-486 |
3.02e-62 |
|
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: 211.69 E-value: 3.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPG--VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPT---EGEIYIEGKKLEDNDPQKA 77
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 78 LEQLGItpIYQE--LNLIPqLDVTENIFMGREkskneiLGWIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMV 155
Cdd:COG1123 82 GRRIGM--VFQDpmTQLNP-VTVGDQIAEALE------NLGLSRAEARARVLELLEAVGLERRL-DRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 156 EISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDN-L 233
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEiL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 234 TEDKMISYMVGEDVDNKFPKMKVEPGKESLRVENL------NRKG---VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAI 304
Cdd:COG1123 232 AAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLskrypvRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 305 VGADSKDSGDIYVHGKKVKidspkvalengiALLTEDRKEQG-------------LFLKQSVKFNIASSnlkkYRENGFL 371
Cdd:COG1123 312 LGLLRPTSGSILFDGKDLT------------KLSRRSLRELRrrvqmvfqdpyssLNPRMTVGDIIAEP----LRLHGLL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 372 NLQEQRKDAIRMVDNLNIKT------PNvqtkclQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIIND 445
Cdd:COG1123 376 SRAERRERVAELLERVGLPPdladryPH------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRD 449
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 433671570 446 LVKKGN-TVIMISSELPEILNMSDRILVVHEGKITGRFNTDE 486
Cdd:COG1123 450 LQRELGlTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-235 |
4.40e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 184.50 E-value: 4.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDnDPQKALEQLGITP 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iyQELNLIPQLDVTENI-FMGRekskneILGwIDRERMEEETKKILSRLGQESIsPNDLIRDLGVGKQQMVEISKALSVE 164
Cdd:COG1131 80 --QEPALYPDLTVRENLrFFAR------LYG-LPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 165 TKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTE 235
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-228 |
2.56e-52 |
|
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: 177.92 E-value: 2.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKaLEQLG 82
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPQLDVTENIFMG-----REKSKNEILGW----IDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQ 153
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAaharlGRGLLAALLRLprarREEREARERAEELLERVGLADRA-DEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 154 MVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKK-QGVTMIFISHKLDEVKKMADRVTVLRNGKyIITD 228
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGR-VIAE 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-225 |
4.57e-52 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 176.47 E-value: 4.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKaLEQLGITP 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMG-REKSKNEILGWIDRERMEEETKK---ILSRLGQESISpNDLIRDLGVGKQQMVEISKAL 161
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAaQARTGSGLLLARARREEREARERaeeLLERVGLADLA-DRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-223 |
5.72e-46 |
|
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: 158.33 E-value: 5.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdPQKALEQLGITP 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKE-PEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iyQELNLIPQLDVTENIfmgrekskneilgwidrermeeetkkILSRlgqesispndlirdlgvGKQQMVEISKALSVET 165
Cdd:cd03230 80 --EEPSLYENLTVRENL--------------------------KLSG-----------------GMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-223 |
4.62e-44 |
|
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: 154.57 E-value: 4.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLED-NDPQKAL-- 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 79 -EQLGItpIYQELNLIPQLDVTENIFMGREKSKneilgwIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEI 157
Cdd:cd03255 81 rRHIGF--VFQSFNLLPDLTALENVELPLLLAG------VPKKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 158 SKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKlDEVKKMADRVTVLRNGK 223
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-235 |
5.49e-44 |
|
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: 155.40 E-value: 5.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdNDPQKALEQLGITP 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iyQELNLIPQLDVTENIfmgreKSKNEILGwIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALSVET 165
Cdd:COG4555 81 --DERGLYDRLTVRENI-----RYFAELYG-LFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTE 235
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-236 |
4.93e-43 |
|
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: 152.20 E-value: 4.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALeQLGITP 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA-RAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMGREKSKNEILGWiDRERMEEETKKILSRLGQesispndLIRDLGVGKQQMVEISKALSVET 165
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKA-RLERVYELFPRLKERRKQ-------LAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTED 236
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-228 |
3.72e-42 |
|
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: 149.79 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGIt 84
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 pIYQElnliP--QL---DVTENIFMGrekSKNeiLGwIDRERMEEETKKILSRLGQESI---SPNDLIRdlgvGKQQMVE 156
Cdd:COG1122 80 -VFQN----PddQLfapTVEEDVAFG---PEN--LG-LPREEIRERVEEALELVGLEHLadrPPHELSG----GQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 157 ISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKyIITD 228
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR-IVAD 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-237 |
1.18e-41 |
|
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: 148.87 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdNDPQKALEQL--G 82
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDIN-KLKGKALRQLrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPQLDVTENIFMGREKSKN---EILGWIDrermEEETKKILSRLGQESISPNDLIR--DLGVGKQQMVEI 157
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRStwrSLFGLFP----KEEKQRALAALERVGLLDKAYQRadQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 158 SKALSVETKLLILDEPTSSLGKDETKELfdtMGTLKK----QGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQV---MDLLKRinreEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
....
gi 433671570 234 TEDK 237
Cdd:cd03256 233 TDEV 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-223 |
1.86e-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: 146.56 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITP 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMGrekskneilgwidrermeeetkkiLSrlGqesispndlirdlgvGKQQMVEISKALSVET 165
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------LS--G---------------GQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-223 |
3.38e-41 |
|
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: 146.91 E-value: 3.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITP 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMGREKSKNEilgwiDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALSVET 165
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGM-----SKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-223 |
4.00e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.11 E-value: 4.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFP----GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLED-NDPQKA 77
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 78 L---EQLGItpIYQELNLIPQLDVTENIFMGREKSKneilgwIDRERMEEETKKILSRLGqesISP--NDLIRDLGVGKQ 152
Cdd:COG1136 82 RlrrRHIGF--VFQFFNLLPELTALENVALPLLLAG------VSRKERRERARELLERVG---LGDrlDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 153 QMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHklD-EVKKMADRVTVLRNGK 223
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTH--DpELAARADRVIRLRDGR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-223 |
1.31e-40 |
|
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: 145.30 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 7 KIKNLTKEFPG--VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGIt 84
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 pIYQ--ELNLIpQLDVTENIFMGREKskneiLGwIDRERMEEETKKILSRLGQESIsPNDLIRDLGVGKQQMVEISKALS 162
Cdd:cd03225 80 -VFQnpDDQFF-GPTVEEEVAFGLEN-----LG-LPEEEIEERVEEALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
3.32e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.23 E-value: 3.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKklednDPQKALEQ 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGitpiYqelnlIPQ---------LDVTENIFMGREKSKNeILGWI---DRERMEEetkkILSRLGQESISpNDLIRDLG 148
Cdd:COG1121 77 IG----Y-----VPQraevdwdfpITVRDVVLMGRYGRRG-LFRRPsraDREAVDE----ALERVGLEDLA-DRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 149 VGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITD 228
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGP 221
|
....*...
gi 433671570 229 RVDNLTED 236
Cdd:COG1121 222 PEEVLTPE 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-223 |
7.94e-40 |
|
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: 143.80 E-value: 7.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDpQKALEQL 81
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 G--ITPIYQE----LNliPQLDVTENIfmgREKSKNEILGWiDRERMEEETKKILSRLGQESISPNDLIRDLGVGKQQMV 155
Cdd:cd03257 81 RkeIQMVFQDpmssLN--PRMTIGEQI---AEPLRIHGKLS-KKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 156 EISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-223 |
1.13e-39 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 142.66 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPqkalEQLGITP 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP----ERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMG---REKSKNEIlgwidRERMEEETKKI-LSRLGQESISpndlirDLGVGKQQMVEISKAL 161
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGlklRGVPKAEI-----RARVRELLELVgLEGLLNRYPH------ELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 162 SVETKLLILDEPTSSLG-------KDETKELFdtmgtlKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03259 146 AREPSLLLLDEPLSALDaklreelREELKELQ------RELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-231 |
3.00e-38 |
|
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: 139.14 E-value: 3.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALeql 81
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 gitpIYQELNLIPQLDVTENIFMGReksknEILGWIDRERmEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKAL 161
Cdd:cd03293 78 ----VFQQDALLPWLTVLDNVALGL-----ELQGVPKAEA-RERAEELLELVGLSGFE-NAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 162 SVETKLLILDEPTSSLgkDE-TKELF--DTMGTLKKQGVTMIFISHKLDEVKKMADRVTVL--RNGKYIITDRVD 231
Cdd:cd03293 147 AVDPDVLLLDEPFSAL--DAlTREQLqeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-223 |
1.94e-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: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 7 KIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGItpi 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 87 yqelnlIPQLdvtenifmgrekSKneilgwidrermeeetkkilsrlGQesispndlirdlgvgkQQMVEISKALSVETK 166
Cdd:cd00267 78 ------VPQL------------SG-----------------------GQ----------------RQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 167 LLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-236 |
2.12e-37 |
|
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: 137.42 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALeQLG 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA-RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPQLDVTENIFMG--REKSKNEIlgwidRERMEEetkkILS-------RLGQESispndliRDLGVGKQQ 153
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGayARRDRAEV-----RADLER----VYElfprlkeRRRQRA-------GTLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 154 MVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
...
gi 433671570 234 TED 236
Cdd:COG0410 224 LAD 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-223 |
2.45e-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: 136.98 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlGITP 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR----PVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMG---REKSKNEIlgwidRERMEEETKKI-LSRLGQESISpndlirDLGVGKQQMVEISKAL 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGlrlKKLPKAEI-----KERVAEALDLVqLEGYANRKPS------QLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-226 |
6.18e-37 |
|
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: 135.49 E-value: 6.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKaleqLGITP 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----IGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iyQELNLIPQLDVTEN-IFMGREK--SKNEILGWIDR--ERMEEETKKilsrlgqesispNDLIRDLGVGKQQMVEISKA 160
Cdd:cd03269 77 --EERGLYPKMKVIDQlVYLAQLKglKKEEARRRIDEwlERLELSEYA------------NKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 161 LSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYII 226
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-227 |
9.48e-37 |
|
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: 134.65 E-value: 9.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKklEDNDPQKALEQLGI-- 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGAli 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 -TPI-YQELNLIPQLDVTENIFMGREKSKNEILgwiDRERMEEETKKilsrlgqesispndLIRDLGVGKQQMVEISKAL 161
Cdd:cd03268 79 eAPGfYPNLTARENLRLLARLLGIRKKRIDEVL---DVVGLKDSAKK--------------KVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIIT 227
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-223 |
1.22e-36 |
|
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: 135.94 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITP 85
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iyQELNLIPQLDVTENIFMGREKSkneiLGWIDRERMEEETK--KILSRLGQESISpNDLIRDL-GvGKQQMVEISKALS 162
Cdd:COG1120 82 --QEPPAPFGLTVRELVALGRYPH----LGLFGRPSAEDREAveEALERTGLEHLA-DRPVDELsG-GERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 163 VETKLLILDEPTSSLgkDETK--ELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:COG1120 154 QEPPLLLLDEPTSHL--DLAHqlEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-175 |
1.28e-36 |
|
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: 132.39 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGItpIYQELNLIPQLDVTE 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGY--VFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 101 NIFMGReksknEILGWIDRErMEEETKKILSRLGQESIS---PNDLIRDLGVGKQQMVEISKALSVETKLLILDEPTS 175
Cdd:pfam00005 79 NLRLGL-----LLKGLSKRE-KDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
1.68e-36 |
|
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: 135.02 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEpflkIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDP-- 74
Cdd:cd03258 1 MIE----LKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 75 -QKALEQLGItpIYQELNLIPQLDVTENIFMGReksknEILGWIDRERmEEETKKILSRLGQESISpNDLIRDLGVGKQQ 153
Cdd:cd03258 77 lRKARRRIGM--IFQHFNLLSSRTVFENVALPL-----EIAGVPKAEI-EERVLELLELVGLEDKA-DAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 154 MVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDN 232
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
.
gi 433671570 233 L 233
Cdd:cd03258 228 V 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-223 |
3.83e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.97 E-value: 3.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDN--DPQKALEQLGI 83
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 tpIYQELNLIPQLDVTENIFMGREKSKNeilgwIDRERMEEETKKILSRLG---QESISPNDLirdLGvGKQQMVEISKA 160
Cdd:COG1126 82 --VFQQFNLFPHLTVLENVTLAPIKVKK-----MSKAEAEERAMELLERVGladKADAYPAQL---SG-GQQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 161 LSVETKLLILDEPTSSLgkD-E-TKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:COG1126 151 LAMEPKVMLFDEPTSAL--DpElVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-233 |
9.57e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.85 E-value: 9.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKaleqLGITP 85
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR----IGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 ----IYQELNLIPQLdvtenIFMGREK--SKNEIlgwidRERMEEetkkILSRLGQESiSPNDLIRDLGVGKQQMVEISK 159
Cdd:COG4152 78 eergLYPKMKVGEQL-----VYLARLKglSKAEA-----KRRADE----WLERLGLGD-RANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 160 ALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-219 |
8.78e-35 |
|
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: 129.58 E-value: 8.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 7 KIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdndpqKALEQLGITPI 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 87 YQELNLIPQLDVTENIFMGREKSKNeILGWI---DRERMEEetkkILSRLGQESISpNDLIRDLGVGKQQMVEISKALSV 163
Cdd:cd03235 76 RRSIDRDFPISVRDVVLMGLYGHKG-LFRRLskaDKAKVDE----ALERVGLSELA-DRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVL 219
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-478 |
2.85e-34 |
|
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: 135.32 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGV--HTPTEGEI-----------YIE------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 66 -----GKKLED--------NDPQKALEQLGITPIYQE-LNLIPQLDVTENIFmgreKSKNEIlGWIDRERMEEETKkiLS 131
Cdd:TIGR03269 81 pcpvcGGTLEPeevdfwnlSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVL----EALEEI-GYEGKEAVGRAVD--LI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 132 RLGQESISPNDLIRDLGVGKQQMVEISKALSVETKLLILDEPTSSLgKDETKELFDTM--GTLKKQGVTMIFISHKLDEV 209
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTL-DPQTAKLVHNAleEAVKASGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 210 KKMADRVTVLRNGKYIITDRVDNLTEDKMisymvgEDVDNKFPKMKVEPGKESLRVENLNR------KGVL---NNVSFK 280
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVAVFM------EGVSEVEKECEVEVGEPIIKVRNVSKryisvdRGVVkavDNVSLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 281 AYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENG------IALLtedRKEQGLFLKQSVK 354
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDGRgrakryIGIL---HQEYDLYPHRTVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 355 FNIASS-NLKKYRENGflnlqeQRKDAI--RMVDNLNIKTPNVQTKCL-QLSGGNQQKVVIGKWLNTEANIFIFDEPTRG 430
Cdd:TIGR03269 384 DNLTEAiGLELPDELA------RMKAVItlKMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 433671570 431 IDVGAKVEVFN-IINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:TIGR03269 458 MDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-223 |
1.43e-33 |
|
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: 127.07 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKalEQLGItp 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMG-------REKSKNEIlgwidRERMEEetkkiLSRLGQESISPNDLIRDLGVGKQQMVEIS 158
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlrvkprsERPPEAEI-----RAKVHE-----LLKLVQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 159 KALSVETKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-478 |
1.65e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 133.29 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEF--PGV--RALDGVDLEIKRGEVHAILGENGAGKS-TLIKVLTGVHTP----TEGEIYIEGKKLED 71
Cdd:PRK15134 1 MTQPLLAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 72 NDPQKaLEQL---GITPIYQE--LNLIPQLDVTENIF--------MGREKSKNEILGWIDRERMEEETKKIlsrlgqesi 138
Cdd:PRK15134 81 ASEQT-LRGVrgnKIAMIFQEpmVSLNPLHTLEKQLYevlslhrgMRREAARGEILNCLDRVGIRQAAKRL--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 139 spNDLIRDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVT 217
Cdd:PRK15134 151 --TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 218 VLRNGKYIITDRVDNLTEDKMISYMvgEDVDNKFPKMKVEPGKES----LRVENLN-----RKG----------VLNNVS 278
Cdd:PRK15134 229 VMQNGRCVEQNRAATLFSAPTHPYT--QKLLNSEPSGDPVPLPEPasplLDVEQLQvafpiRKGilkrtvdhnvVVKNIS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 279 FKAYEGEVLGIAGLVGAGRTEIARAIVGADSKdSGDIYVHGKKVKIDSPKvalengiALLTEDRKEQGLFLKQSVKFN-- 356
Cdd:PRK15134 307 FTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRR-------QLLPVRHRIQVVFQDPNSSLNpr 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 357 -----IASSNLKKYRENgfLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGI 431
Cdd:PRK15134 379 lnvlqIIEEGLRVHQPT--LSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 433671570 432 DVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-223 |
2.27e-33 |
|
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: 126.84 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP----GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQL 81
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GItpIYQE----LNliPQLDVTENIfmgREKSKneILGwidRERMEEETKKILSRLGqesISPNDLIR---DLGVGKQQM 154
Cdd:COG1124 82 QM--VFQDpyasLH--PRHTVDRIL---AEPLR--IHG---LPDREERIAELLEQVG---LPPSFLDRyphQLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 155 VEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-225 |
4.91e-33 |
|
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: 125.53 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFpGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlGITP 85
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR----DISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMGREKSKNeilgwiDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALSVET 165
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKV------DKKEIERKVLEIAEMLGIDHLL-NRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-223 |
5.13e-33 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 124.92 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVR--ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLeDNDPQKALEQLGI 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyQELNLIPQLDVTENI-FMGREKSKNeilgwidRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALS 162
Cdd:cd03263 80 CP--QFDALFDELTVREHLrFYARLKGLP-------KSEIKEEVELLLRVLGLTDKA-NKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-223 |
8.20e-33 |
|
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: 122.93 E-value: 8.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 7 KIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITPi 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 87 yQELNLIpqldvtenifmgreksknEILGWIDRErmeeetkkilsrlgqesispndlIRDLGVGKQQMVEISKALSVETK 166
Cdd:cd03214 80 -QALELL------------------GLAHLADRP-----------------------FNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 167 LLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-478 |
1.08e-32 |
|
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: 130.96 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKS----TLIKVLTGVHTPTEGEIYIEGKKLeDN 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-LG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 73 DPQKALEQL-G--ITPIYQE----LNliP------QldVTENIF----MGREKSKNEILGWIDRERMEEETKKI------ 129
Cdd:COG4172 81 LSERELRRIrGnrIAMIFQEpmtsLN--PlhtigkQ--IAEVLRlhrgLSGAAARARALELLERVGIPDPERRLdayphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 130 LSrlGqesispndlirdlgvGKQQMVEISKALSVETKLLILDEPTSSLgkDET--KELFDTMGTLKKQ-GVTMIFISHKL 206
Cdd:COG4172 157 LS--G---------------GQRQRVMIAMALANEPDLLIADEPTTAL--DVTvqAQILDLLKDLQRElGMALLLITHDL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 207 DEVKKMADRVTVLRNGKYIITDRVDNLTED-------KMISYMvgedvdnkfPKMKVEPGKES----LRVENLN-----R 270
Cdd:COG4172 218 GVVRRFADRVAVMRQGEIVEQGPTAELFAApqhpytrKLLAAE---------PRGDPRPVPPDapplLEARDLKvwfpiK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 271 KGVL----------NNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSkDSGDIYVHGKKVKIDSPKvalengiALLTE 340
Cdd:COG4172 289 RGLFrrtvghvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRR-------ALRPL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 341 DRKEQGLFlkQ------SVKFNIA---SSNLKKYRENgfLNLQEQRKDAIRMVD--NLNIKT----PNvqtkclQLSGGN 405
Cdd:COG4172 361 RRRMQVVF--QdpfgslSPRMTVGqiiAEGLRVHGPG--LSAAERRARVAEALEevGLDPAArhryPH------EFSGGQ 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 406 QQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
1.17e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 127.12 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEpflkIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGK---KLEDND 73
Cdd:COG1135 1 MIE----LENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 74 PQKALEQLGItpIYQELNLIPQLDVTENI-F-MgreksknEILGWiDRERMEEETKKILSRLGqesispndlIRD----- 146
Cdd:COG1135 77 LRAARRKIGM--IFQHFNLLSSRTVAENVaLpL-------EIAGV-PKAEIRKRVAELLELVG---------LSDkaday 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 147 ---LGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDtmgtL-----KKQGVTMIFISHKLDEVKKMADRVTV 218
Cdd:COG1135 138 psqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILD----LlkdinRELGLTIVLITHEMDVVRRICDRVAV 213
|
....*
gi 433671570 219 LRNGK 223
Cdd:COG1135 214 LENGR 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-225 |
1.57e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.03 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQkaleQ 80
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY----Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPIYQELNLIPQLDVTENIFMGREKSK----------NEILGWIdreRMEEETKKilsrlgqesiSPNdlirDLGVG 150
Cdd:PRK11607 91 RPINMMFQSYALFPHMTVEQNIAFGLKQDKlpkaeiasrvNEMLGLV---HMQEFAKR----------KPH----QLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 151 KQQMVEISKALSVETKLLILDEPTSSLgkdeTKELFDTM-----GTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGAL----DKKLRDRMqlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-219 |
1.72e-32 |
|
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: 126.32 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP---TEGEIYIEGKKLEDNDPqKAL 78
Cdd:COG0444 2 LEVRNLKVYFPTrrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSE-KEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 79 EQL---GITPIYQE----LNliPQLDV----TENIFMGREKSKNEIlgwidRERMEEetkkILSRLGqesIS-PNDLIRD 146
Cdd:COG0444 81 RKIrgrEIQMIFQDpmtsLN--PVMTVgdqiAEPLRIHGGLSKAEA-----RERAIE----LLERVG---LPdPERRLDR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 147 ----LGVGKQQMVEISKALSVETKLLILDEPTSSLgkDET--KELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVL 219
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTAL--DVTiqAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-223 |
2.04e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.05 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEpflkIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQ 80
Cdd:PRK09493 1 MIE----FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPIYQELNLIPQLDVTENIFMG----REKSKNEilgwidrerMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVE 156
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGplrvRGASKEE---------AEKQARELLAKVGLAERA-HHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 157 ISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-233 |
1.27e-31 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 121.32 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdNDPQKALEQLGITPiy 87
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREVRRRIGIVF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 88 QELNLIPQLDVTENIFM-GREKS-KNEILgwidRERMEEETKKIlsRLGQESispNDLIRDLGVGKQQMVEISKALSVET 165
Cdd:cd03265 80 QDLSVDDELTGWENLYIhARLYGvPGAER----RERIDELLDFV--GLLEAA---DRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKK-QGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-233 |
1.89e-31 |
|
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: 121.07 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDP---QKALEQLGIt 84
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRMGM- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 pIYQELNLIPQLDVTENI-FMGREKSKNeilgwiDRERMEEETKKILSRLG---QESISPndliRDLGVGKQQMVEISKA 160
Cdd:cd03261 82 -LFQSGALFDSLTVFENVaFPLREHTRL------SEEEIREIVLEKLEAVGlrgAEDLYP----AELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 161 LSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-223 |
2.10e-31 |
|
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: 120.75 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVH-----TPTEGEIYIEGKKLEDNDPQKALEQ 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPIYQELNLIPqLDVTENIFMGReksknEILGWIDRERMEEETKKILSRLG-QESISPNDLIRDLGVGKQQMVEISK 159
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-----RLHGIKLKEELDERVEEALRKAAlWDEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 160 ALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQgVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-223 |
2.21e-31 |
|
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: 120.44 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlGITP 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR----DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMG---REKSKNEIlgwidRERMeEETKKILsRLGQESispNDLIRDLGVGKQQMVEISKALS 162
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGlklRKVPKDEI-----DERV-REVAELL-QIEHLL---DRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 163 VETKLLILDEPTSSLG-------KDETKELfdtmgtLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03301 147 REPKVFLMDEPLSNLDaklrvqmRAELKRL------QQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-478 |
2.53e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 127.66 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEF----PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKL-----------E 70
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielsE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 71 DNDPQ-KALEQLGITPIYQE--LNLIPQLDVTENIF--------MGREKSKNEILGWIDRERMeEETKKILSRLGQEsis 139
Cdd:PRK10261 93 QSAAQmRHVRGADMAMIFQEpmTSLNPVFTVGEQIAesirlhqgASREEAMVEAKRMLDQVRI-PEAQTILSRYPHQ--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 140 pndlirdLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTV 218
Cdd:PRK10261 169 -------LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 219 LRNGKYIITDRVDNLTEDKMISY-------------MVGEDVDNKFP---------------KMKVEPGKESLRVENLN- 269
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHAPQHPYtrallaavpqlgaMKGLDYPRRFPlislehpakqeppieQDTVVDGEPILQVRNLVt 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 270 ----RKGVLN----------NVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKI--DSPKVALEN 333
Cdd:PRK10261 322 rfplRSGLLNrvtrevhaveKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlsPGKLQALRR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 334 GIALLTEDrKEQGLFLKQSVKFNIassnLKKYRENGFLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGK 413
Cdd:PRK10261 402 DIQFIFQD-PYASLDPRQTVGDSI----MEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIAR 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 414 WLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-223 |
3.59e-31 |
|
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: 119.82 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 9 KNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGK---KLEDNDPQKALEQLGIt 84
Cdd:cd03292 4 INVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYLRRKIGV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 pIYQELNLIPQLDVTENIFMGReksknEILGWIDRErMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALSVE 164
Cdd:cd03292 83 -VFQDFRLLPDRNVYENVAFAL-----EVTGVPPRE-IRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 165 TKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
7.97e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 119.85 E-value: 7.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEpflkIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDP---QKA 77
Cdd:PRK11264 3 AIE----VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 78 L-----EQLGItpIYQELNLIPQLDVTENIFMGREKSKNEilgwiDRERMEEETKKILSRL---GQESISPndliRDLGV 149
Cdd:PRK11264 79 LirqlrQHVGF--VFQNFNLFPHRTVLENIIEGPVIVKGE-----PKEEATARARELLAKVglaGKETSYP----RRLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 150 GKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-246 |
1.03e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 119.71 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdNDPQKALEQ 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPIYQELNLIPQLDVTENIFMGR-EKSKNEILGWI---------DRERMeEETKKILSRLGQESISpNDLIRDLGVG 150
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIENLLVAQhQQLKTGLFSGLlktpafrraESEAL-DRAATWLERVGLLEHA-NRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 151 KQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKYIITDR 229
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
250
....*....|....*...
gi 433671570 230 VDNLTED-KMISYMVGED 246
Cdd:PRK11300 238 PEEIRNNpDVIKAYLGEA 255
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-223 |
1.45e-30 |
|
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: 117.98 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 25 DLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlGITPIYQELNLIPQLDVTENIFM 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR----PVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 105 GRekSKNEILGWIDRERMEeetkKILSRLGQESISPNdLIRDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKE 184
Cdd:cd03298 94 GL--SPGLKLTAEDRQAIE----VALARVGLAGLEKR-LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 433671570 185 LFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03298 167 MLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-223 |
1.58e-30 |
|
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: 118.94 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVR-ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGIt 84
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 pIYQELNLIPQLDVTENIFMgreksKNEILGWiDRERMEEETKKILSRLGQESISPNDLI-RDLGVGKQQMVEISKALSV 163
Cdd:cd03295 80 -VIQQIGLFPHMTVEENIAL-----VPKLLKW-PKEKIRERADELLALVGLDPAEFADRYpHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-225 |
2.40e-30 |
|
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: 118.90 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRAldgVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdNDPQKALEQL---GIT 84
Cdd:cd03294 30 ILKKTGQTVGVND---VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRELrrkKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 PIYQELNLIPQLDVTENIFMGREkskneiLGWIDRERMEEETKKILSRLGQESiSPNDLIRDLGVGKQQMVEISKALSVE 164
Cdd:cd03294 106 MVFQSFALLPHRTVLENVAFGLE------VQGVPRAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 165 TKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-223 |
3.54e-30 |
|
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: 124.56 E-value: 3.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG--VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyQELNLIPQlDVTENIFMGREKskneilgwIDRERMEEetkkILSRLG-QESIS--PNDL---IRDLGV----GKQQ 153
Cdd:COG2274 554 VL--QDVFLFSG-TIRENITLGDPD--------ATDEEIIE----AARLAGlHDFIEalPMGYdtvVGEGGSnlsgGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 154 MVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLkKQGVTMIFISHKLdEVKKMADRVTVLRNGK 223
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRL-STIRLADRIIVLDKGR 686
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-223 |
5.81e-30 |
|
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: 115.17 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG--VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyqelnlipqldvtenifmgrekskneilgwidrermeeetkkilsrlgQESISPNDLIRD--LGVGKQQMVEISKAL 161
Cdd:cd03228 81 VP-------------------------------------------------QDPFLFSGTIREniLSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-223 |
1.88e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.64 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlGITP 85
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR----NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMG---REKSKNEIlgwidRERMEEetkkILSRLGqesISP--NDLIRDLGVGKQQMVEISKA 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPlklRKVPKAEI-----DRRVRE----AAELLG---LEDllDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 161 LSVETKLLILDEPTSSLgkD---------ETKELFdtmgtlKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:COG3839 148 LVREPKVFLLDEPLSNL--DaklrvemraEIKRLH------RRLGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-223 |
1.89e-29 |
|
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: 115.08 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIK---RGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAL--EQLGITPIYQELNLIPQ 95
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 96 LDVTENIFMG-REKSKNEilgwiDRERMEEetkkILSRLGQESISpNDLIRDLGVGKQQMVEISKALSVETKLLILDEPT 174
Cdd:cd03297 90 LNVRENLAFGlKRKRNRE-----DRISVDE----LLDLLGLDHLL-NRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 433671570 175 SSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
263-480 |
2.02e-29 |
|
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: 113.29 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNRK--GV--LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIAll 338
Cdd:cd03216 1 LELRGITKRfgGVkaLDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 tedrkeqglflkqsvkfniassnlkkyrengflnlqeqrkdairMVdnlniktpnvqtkcLQLSGGNQQKVVIGKWLNTE 418
Cdd:cd03216 79 --------------------------------------------MV--------------YQLSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITG 480
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
2.85e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 114.76 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEpflkIKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdPQKALE 79
Cdd:COG2884 1 MIR----FENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRL-KRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 80 QL----GItpIYQELNLIPQLDVTENI-----FMGreKSKNEIlgwidRERMEEetkkILSRLGQESISpNDLIRDLGVG 150
Cdd:COG2884 76 YLrrriGV--VFQDFRLLPDRTVYENValplrVTG--KSRKEI-----RRRVRE----VLDLVGLSDKA-KALPHELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 151 KQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-479 |
2.92e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.55 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKkledndpqkalEQLGITPiy 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 88 QELNLIPQLDVTENIFMGR------EKSKNEILGWIDR------------ERMEE--------ETKKILSRLGqesISPN 141
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDaelralEAELEELEAKLAEpdedlerlaelqEEFEAlggweaeaRAEEILSGLG---FPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 142 DLIRDLGV--GKQQM-VEISKALSVETKLLILDEPTSSLgkDetkelFDTM----GTLKKQGVTMIFISHK---LDEVkk 211
Cdd:COG0488 145 DLDRPVSElsGGWRRrVALARALLSEPDLLLLDEPTNHL--D-----LESIewleEFLKNYPGTVLVVSHDryfLDRV-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 212 mADRVTVLRNGKYII--------------------------------------------------TDRVDNLteDKMISy 241
Cdd:COG0488 216 -ATRILELDRGKLTLypgnysayleqraerleqeaaayakqqkkiakeeefirrfrakarkakqaQSRIKAL--EKLER- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 242 mVGEDVDNKFPKMKVEPGKES----LRVENLNrKG-----VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDS 312
Cdd:COG0488 292 -EEPPRRDKTVEIRFPPPERLgkkvLELEGLS-KSygdktLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 313 GDIyVHGKKVKidspkvalengIALLTEDRKEqgLFLKQSVKfniasSNLKKYRENGflnlqeQRKDAIRMVDNLNIKTP 392
Cdd:COG0488 370 GTV-KLGETVK-----------IGYFDQHQEE--LDPDKTVL-----DELRDGAPGG------TEQEVRGYLGRFLFSGD 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 393 NVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKvevfNIINDLVK--KGnTVIMIS--SELpeILNMSD 468
Cdd:COG0488 425 DAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL----EALEEALDdfPG-TVLLVShdRYF--LDRVAT 497
|
570
....*....|.
gi 433671570 469 RILVVHEGKIT 479
Cdd:COG0488 498 RILEFEDGGVR 508
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-225 |
3.40e-29 |
|
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: 113.89 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALeqlgitpi 86
Cdd:cd03226 2 IENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 87 yqelNLIPQlDVTENIFMgrEKSKNEI-LGWIDRERMEEETKKILSRLGqesisPNDLI----RDLGVGKQQMVEISKAL 161
Cdd:cd03226 74 ----GYVMQ-DVDYQLFT--DSVREELlLGLKELDAGNEQAETVLKDLD-----LYALKerhpLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-222 |
4.54e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 118.41 E-value: 4.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyQELNLIPQLDVTENIFMGREKSKNEILGWIDRERMEEEtkKILSRLGQESISPNDlIRDLGVGKQQMVEISKALSV 163
Cdd:PRK09536 82 VP--QDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE--RAMERTGVAQFADRP-VTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNG 222
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-204 |
1.38e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.19 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAlEQLGI 83
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-RRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 tpIYQELNLIPQLDVTENI-----FMGREKSKNEILGWIdrERMEeetkkiLSRLGqesispNDLIRDLGVGKQQMVEIS 158
Cdd:COG4133 80 --LGHADGLKPELTVRENLrfwaaLYGLRADREAIDEAL--EAVG------LAGLA------DLPVRQLSAGQKRRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 433671570 159 KALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISH 204
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
2.66e-28 |
|
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: 112.38 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDpQKALEQ 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLS-EKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 L----GItpIYQELNLIPQLDVTENI-FMGREKSKneilgwIDRERMEEETKKILSRLGQESIspNDL-IRDLGVGKQQM 154
Cdd:COG1127 80 LrrriGM--LFQGGALFDSLTVFENVaFPLREHTD------LSEAEIRELVLEKLELVGLPGA--ADKmPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 155 VEISKALSVETKLLILDEPTSSL---GKDETKELfdtMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRV 230
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
250
....*....|.
gi 433671570 231 DNL--TEDKMI 239
Cdd:COG1127 227 EELlaSDDPWV 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
4.68e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 111.89 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAL-E 79
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 80 QLGITPiyQELNLIPQLDVTENIFMG-----REKSKNEIlgwidrERMEEETKKILSRLGQESISpndlirdLGVGKQQM 154
Cdd:PRK11614 81 AVAIVP--EGRRVFSRMTVEENLAMGgffaeRDQFQERI------KWVYELFPRLHERRIQRAGT-------MSGGEQQM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 155 VEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-230 |
4.86e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.51 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEpflkIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGK---KLEDND 73
Cdd:PRK11153 1 MIE----LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 74 PQKALEQLGItpIYQELNLIPQLDVTENIFMGRE---KSKNEIlgwidRERMEEetkkILSRLGQEsispnDLiRD---- 146
Cdd:PRK11153 77 LRKARRQIGM--IFQHFNLLSSRTVFDNVALPLElagTPKAEI-----KARVTE----LLELVGLS-----DK-ADrypa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 147 -LGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDtmgtLKKQ-----GVTMIFISHKLDEVKKMADRVTVLR 220
Cdd:PRK11153 140 qLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE----LLKDinrelGLTIVLITHEMDVVKRICDRVAVID 215
|
250
....*....|
gi 433671570 221 NGKYIITDRV 230
Cdd:PRK11153 216 AGRLVEQGTV 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-223 |
6.14e-28 |
|
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: 109.83 E-value: 6.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTkefpGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALeQLG 82
Cdd:cd03215 2 EPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI-RAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPI---YQELNLIPQLDVTENIFMGRekskneilgwidrermeeetkkILSrlGqesispndlirdlgvGKQQMVEISK 159
Cdd:cd03215 77 IAYVpedRKREGLVLDLSVAENIALSS----------------------LLS--G---------------GNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 160 ALSVETKLLILDEPTSslGKD-ETK-ELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03215 118 WLARDPRVLILDEPTR--GVDvGAKaEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-223 |
1.24e-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: 110.15 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEF----PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdPQKALEQL 81
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKE-PAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITPiyQELNLIPQLDVTENI-FMGRekskneiLGWIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKA 160
Cdd:cd03266 81 GFVS--DSTGLYDRLTARENLeYFAG-------LYGLKGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 161 LSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-223 |
2.98e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.73 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPqkalEQLGI 83
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA----ENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLIPQLDVTENIFMG---REKSKNEIlgwidRERMEEETKKI-LSRLGQESispndlIRDLGVGKQQMVEISK 159
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGlrmQKTPAAEI-----TPRVMEALRMVqLEEFAQRK------PHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 160 ALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-223 |
3.16e-27 |
|
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: 115.24 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGit 84
Cdd:COG4988 337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 piyqelnLIPQ------LDVTENIFMGREK-SKNEILGWIDRERMEEetkkILSRLgqesisPNDLIRDLG-------VG 150
Cdd:COG4988 415 -------WVPQnpylfaGTIRENLRLGRPDaSDEELEAALEAAGLDE----FVAAL------PDGLDTPLGeggrglsGG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 151 KQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGR 548
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-234 |
4.22e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.07 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG--VRAldgvDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPqkalEQLGI 83
Cdd:COG3840 2 LRLDDLTYRYGDfpLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLIPQLDVTENIFMGREKSKNeiLGWIDRERMEEetkkILSRLGQESISpNDLIRDLGVGKQQMVEISKALSV 163
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLGLRPGLK--LTAEQRAQVEQ----ALERVGLAGLL-DRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 164 ETKLLILDEPTSSLG---KDETKELFDTMGtlKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLT 234
Cdd:COG3840 147 KRPILLLDEPFSALDpalRQEMLDLVDELC--RERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-223 |
9.54e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.66 E-value: 9.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITP 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLipQLDVTENIFMGRekskneiLGWI-DRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKAL--- 161
Cdd:COG4559 82 QHSSLAF--PFTVEEVVALGR-------APHGsSAAQDRQIVREALALVGLAHLA-GRSYQTLSGGEQQRVQLARVLaql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 162 ----SVETKLLILDEPTSSLgkdetkelfD------TMGTLKK---QGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:COG4559 152 wepvDGGPRWLFLDEPTSAL---------DlahqhaVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-225 |
1.07e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKK--LEDNDPQKALEQL-- 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITPIYQELNLIPQLDVTENIFMGREKskneILGwIDRERMEEETKKILSRLGQESIS---PndliRDLGVGKQQMVEIS 158
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCR----VLG-LSKDQALARAEKLLERLRLKPYAdrfP----LHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 159 KALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-223 |
1.23e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 106.89 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGeVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdPQKALEQLGITP 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iyQELNLIPQLDVTENI-FMGRekskneiLGWIDRERMEEETKKILSRLGQESiSPNDLIRDLGVGKQQMVEISKALSVE 164
Cdd:cd03264 79 --QEFGVYPNFTVREFLdYIAW-------LKGIPSKEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 165 TKLLILDEPTSSLGKDEtKELFDTMgtLKKQGVTMIFI--SHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03264 149 PSILIVDEPTAGLDPEE-RIRFRNL--LSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGK 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-222 |
1.81e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 2 IEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHT---PTEGEIYIEGKKLE-----DND 73
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQregrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 74 PQKALEQLGItpIYQELNLIPQLDVTENIFMGREKSK---NEILGWIDRERmEEETKKILSRLGQESISpNDLIRDLGVG 150
Cdd:PRK09984 81 IRKSRANTGY--IFQQFNLVNRLSVLENVLIGALGSTpfwRTCFSWFTREQ-KQRALQALTRVGMVHFA-HQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 151 KQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNG 222
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
3.01e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.79 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGV--RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAL 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 79 EQLGItpIYQElnlipqldvTENIFMGREKSKNEILGW----IDRERMEEETKKILSRLGQESISPNDLIRdLGVGKQQM 154
Cdd:PRK13635 81 RQVGM--VFQN---------PDNQFVGATVQDDVAFGLenigVPREEMVERVDQALRQVGMEDFLNREPHR-LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 155 VEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-238 |
7.00e-26 |
|
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: 105.94 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRALDGVDLEIKRGEvH-AILGENGAGKSTLIKVLTGVHTPTEG-EIYIEGKKLEDNDPQKALEQ 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGE-HwAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGItpIYQELnlipQLDvteniFMGREKSKNEIL----GWIDR-----ERMEEETKKILSRLGQESISpNDLIRDLGVGK 151
Cdd:COG1119 80 IGL--VSPAL----QLR-----FPRDETVLDVVLsgffDSIGLyreptDEQRERARELLELLGLAHLA-DRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 152 QQMVEISKALSVETKLLILDEPTSSLgKDETKELF-DTMGTLKKQG-VTMIFISHKLDEVKKMADRVTVLRNGKyIITD- 228
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGL-DLGARELLlALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR-VVAAg 225
|
250
....*....|.
gi 433671570 229 -RVDNLTEDKM 238
Cdd:COG1119 226 pKEEVLTSENL 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
263-478 |
8.30e-26 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 105.28 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN-----RKG---VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENG 334
Cdd:cd03257 2 LEVKNLSvsfptGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 335 --IALLTEDR----------KEQglfLKQSVKFNIASSNLKKYRENGFLNLqEQRKDAIRMVDNLniktPNvqtkclQLS 402
Cdd:cd03257 82 keIQMVFQDPmsslnprmtiGEQ---IAEPLRIHGKLSKKEARKEAVLLLL-VGVGLPEEVLNRY----PH------ELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 403 GGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-223 |
8.46e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.21 E-value: 8.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLE---DNDPQ-- 75
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDGQlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 76 ----KALEQLG--ITPIYQELNLIPQLDVTENIFmgreKSKNEILGwIDRERMEEETKKILSRLGQESISPNDLIRDLGV 149
Cdd:PRK10619 81 vadkNQLRLLRtrLTMVFQHFNLWSHMTVLENVM----EAPIQVLG-LSKQEARERAVKYLAKVGIDERAQGKYPVHLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 150 GKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
263-478 |
9.41e-26 |
|
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: 103.25 E-value: 9.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALEngIALL 338
Cdd:cd03230 1 IEVRNLSkrygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR--IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDRkeqGLFLKQSVkfniassnlkkyRENgflnlqeqrkdairmvdnlniktpnvqtkcLQLSGGNQQKVVIGKWLNTE 418
Cdd:cd03230 79 PEEP---SLYENLTV------------REN------------------------------LKLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-223 |
2.11e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.11 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 5 FLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdpqkALEQLGIT 84
Cdd:PRK11432 6 FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR----SIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 PIYQELNLIPQLDVTENIFMGRE---KSKNEIlgwidRERMEEETkKILSRLGQEsispNDLIRDLGVGKQQMVEISKAL 161
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKmlgVPKEER-----KQRVKEAL-ELVDLAGFE----DRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-223 |
2.74e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.39 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP----------------------GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIY 63
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 64 IEGKkledndpqkaleqlgITPIYqELN--LIPQLDVTENIFM-GRekskneILGwIDRERMEEETKKIL---------- 130
Cdd:COG1134 85 VNGR---------------VSALL-ELGagFHPELTGRENIYLnGR------LLG-LSRKEIDEKFDEIVefaelgdfid 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 131 -----------SRLGqesispndlirdLGVgkqqmveiskALSVETKLLILDEPTsSLGkDET--KELFDTMGTLKKQGV 197
Cdd:COG1134 142 qpvktyssgmrARLA------------FAV----------ATAVDPDILLVDEVL-AVG-DAAfqKKCLARIRELRESGR 197
|
250 260
....*....|....*....|....*.
gi 433671570 198 TMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:COG1134 198 TVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
4.76e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 104.30 E-value: 4.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVR--ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQ 80
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGItpIYQEL-NLIPQLDVTENIFMGREKSKneilgwIDRERMeeetKKILSRLGQESISPNDLIRD---LGVGKQQMVE 156
Cdd:PRK13632 85 IGI--IFQNPdNQFIGATVEDDIAFGLENKK------VPPKKM----KDIIDDLAKKVGMEDYLDKEpqnLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 157 ISKALSVETKLLILDEPTSSL---GKDETKELfdtMGTLKKQGV-TMIFISHKLDEVKKmADRVTVLRNGKYIITDRVDN 232
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLdpkGKREIKKI---MVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKE 228
|
....*..
gi 433671570 233 LTEDKMI 239
Cdd:PRK13632 229 ILNNKEI 235
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-223 |
5.24e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 103.61 E-value: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTG--VHTPTEGEIYIEGKKLEDNDP-QKAleQLG 82
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPdERA--RAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 I-----TPIyqElnlIPQLDVTEniFMgREkSKNEILG-WIDRERMEEETKKILSRLGqesISPNDLIRDLGVG-----K 151
Cdd:COG0396 79 IflafqYPV--E---IPGVSVSN--FL-RT-ALNARRGeELSAREFLKLLKEKMKELG---LDEDFLDRYVNEGfsggeK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 152 QQMvEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHK---LDEVKkmADRVTVLRNGK 223
Cdd:COG0396 147 KRN-EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGR 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-227 |
5.37e-25 |
|
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: 102.22 E-value: 5.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVH--TPTEGEIYIEGKKLEDNDPQ-KAleQLG 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEeRA--RLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPQL-------DVTENiFMGREKSKNEILgwidrermeeetkkilsrlgqesispndlirdlgvgkqQMv 155
Cdd:cd03217 79 IFLAFQYPPEIPGVknadflrYVNEG-FSGGEKKRNEIL--------------------------------------QL- 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 156 eiskaLSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHK---LDEVKkmADRVTVLRNGKYIIT 227
Cdd:cd03217 119 -----LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKS 186
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-223 |
7.10e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.94 E-value: 7.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 16 PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITPiyQElnliPQ 95
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVP--QD----TF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 96 L---DVTENIFMGREKskneilgwIDRERMEEETKK-----ILSRLgqesisPNDL---IRDLGV----GKQQMVEISKA 160
Cdd:COG1132 425 LfsgTIRENIRYGRPD--------ATDEEVEEAAKAaqaheFIEAL------PDGYdtvVGERGVnlsgGQRQRIAIARA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 161 LSVETKLLILDEPTSSLgkD-ET-KELFDTMGTLKKqGVTMIFISHKLDEVkKMADRVTVLRNGK 223
Cdd:COG1132 491 LLKDPPILILDEATSAL--DtETeALIQEALERLMK-GRTTIVIAHRLSTI-RNADRILVLDDGR 551
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-225 |
1.57e-24 |
|
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: 101.53 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 5 FLKIKNLTKEF-PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyQELNLIPQlDVTENIFMGREKSKneilgwidrermEEETKKILSRLGQESI---SPNDLI-------RDLGVGKQQ 153
Cdd:cd03254 82 VL--QDTFLFSG-TIMENIRLGRPNAT------------DEEVIEAAKEAGAHDFimkLPNGYDtvlgengGNLSQGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 154 MVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKmADRVTVLRNGKYI 225
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
263-478 |
1.87e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 101.68 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNRK-G---VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVaLENgIALL 338
Cdd:COG1131 1 IEVRGLTKRyGdktALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEdrkEQGLFLKQSVKFNIAssNLKKYREngfLNLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVIGKWLNTE 418
Cdd:COG1131 79 PQ---EPALYPDLTVRENLR--FFARLYG---LPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
263-477 |
3.52e-24 |
|
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: 99.18 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKV-ALENGIAL 337
Cdd:cd03229 1 LELKNVskryGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDrkeQGLFLKQSVKFNIAssnlkkyrengflnlqeqrkdairmvdnlniktpnvqtkcLQLSGGNQQKVVIGKWLNT 417
Cdd:cd03229 81 VFQD---FALFPHLTVLENIA----------------------------------------LGLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 418 EANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGK 477
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
263-486 |
3.97e-24 |
|
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: 101.03 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN--------RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALeng 334
Cdd:COG1124 2 LEVRNLSvsygqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 335 ialltedRKEQGLFlkQ----SV--KFNIASSNLKKYRENGFLNLQEQRKDAIRMV---DNLNIKTPNvqtkclQLSGGN 405
Cdd:COG1124 79 -------RRVQMVF--QdpyaSLhpRHTVDRILAEPLRIHGLPDREERIAELLEQVglpPSFLDRYPH------QLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 406 QQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKITGRFNT 484
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
..
gi 433671570 485 DE 486
Cdd:COG1124 224 AD 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-223 |
5.11e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.00 E-value: 5.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyQELNLIPQLDVTENIFMGRekskneiLGW-IDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKAL- 161
Cdd:PRK13548 81 LP--QHSSLSFPFTVEEVVAMGR-------APHgLSRAEDDALVAAALAQVDLAHLA-GRDYPQLSGGEQQRVQLARVLa 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 162 -----SVETKLLILDEPTSSLgkdetkELF---DTMGTLK----KQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK13548 151 qlwepDGPPRWLLLDEPTSAL------DLAhqhHVLRLARqlahERGLAVIVVLHDLNLAARYADRIVLLHQGR 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-239 |
7.57e-24 |
|
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: 99.92 E-value: 7.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdNDPQKALEQLGITP 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIfmgreKSKNEILGwIDRERMEEETKKILSRLGQESISPNDLIRdLGVGKQQMVEISKALSVET 165
Cdd:cd03218 80 LPQEASIFRKLTVEENI-----LAVLEIRG-LSKKEREEKLEELLEEFHITHLRKSKASS-LSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKMI 239
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-216 |
8.67e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 99.43 E-value: 8.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP-----GVR--ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYI--EGKKLE--DNDP 74
Cdd:COG4778 5 LEVENLSKTFTlhlqgGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDlaQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 75 QKALE----QLGitpiY--QELNLIPQ---LDVTEN--IFMGrekskneilgwIDRERMEEETKKILSRLG-QE---SIS 139
Cdd:COG4778 85 REILAlrrrTIG----YvsQFLRVIPRvsaLDVVAEplLERG-----------VDREEARARARELLARLNlPErlwDLP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 140 PNDLIrdlGvGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRV 216
Cdd:COG4778 150 PATFS---G-GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRV 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
262-477 |
1.12e-23 |
|
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: 98.69 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLNRKgVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENgIALLTED 341
Cdd:cd03225 6 SFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 342 RKEQglFLKQSVKFNIASS--NLKKYRENgflnLQEQRKDAIRMVDNLNIKTPNVQTkclqLSGGNQQKVVIGKWLNTEA 419
Cdd:cd03225 84 PDDQ--FFGPTVEEEVAFGleNLGLPEEE----IEERVEEALELVGLEGLRDRSPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 420 NIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGK 477
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
264-477 |
1.22e-23 |
|
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: 96.93 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 264 RVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvALENGIALLt 339
Cdd:cd00267 1 EIENLSFryggRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 340 edrkeqglflkqsvkfniassnlkkyrengflnlqeqrkdairmvdnlniktpnvqtkcLQLSGGNQQKVVIGKWLNTEA 419
Cdd:cd00267 79 -----------------------------------------------------------PQLSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 420 NIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGK 477
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-223 |
1.86e-23 |
|
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: 96.90 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRA--LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyQELNLIPQlDVTENIFMGrekskneilgwidrermeeetkkilsrlgqesispndlirdlgvGKQQMVEISKALSV 163
Cdd:cd03246 81 LP--QDDELFSG-SIAENILSG--------------------------------------------GQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLdEVKKMADRVTVLRNGK 223
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-225 |
2.66e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.56 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLK--IKNLTK-EFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGkkledNDP----Q 75
Cdd:cd03267 16 EPGLIgsLKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPwkrrK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 76 KALEQLGITpIYQELNLIPQLDVTENIFMGREkskneILGwIDRERMEEETKKI--LSRLGQESISPndlIRDLGVGKQQ 153
Cdd:cd03267 91 KFLRRIGVV-FGQKTQLWWDLPVIDSFYLLAA-----IYD-LPPARFKKRLDELseLLDLEELLDTP---VRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 154 MVEISKALSVETKLLILDEPTSSL---GKDETKELFDTMGtlKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLdvvAQENIRNFLKEYN--RERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
273-478 |
2.82e-23 |
|
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: 98.34 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKValengialLTEDRKEQG------ 346
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAE--------LYRLRRRMGmlfqsg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 347 -LFLKQSVKFNIAsSNLkkyRENGFLNLQEQRK---DAIRMVdNLnikTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIF 422
Cdd:cd03261 87 aLFDSLTVFENVA-FPL---REHTRLSEEEIREivlEKLEAV-GL---RGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 423 IFDEPTRGIDVGAKVEVFNIINDLVK-KGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-269 |
7.47e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.01 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEpflkIKNLTKEF------PG---------------VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTE 59
Cdd:COG4586 1 IIE----VENLSKTYrvyekePGlkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 60 GEIYIEGKklednDPQKA----LEQLGIT-----------PIYQELNLIPQL-DVTENIFmgrekskneilgwidRERME 123
Cdd:COG4586 77 GEVRVLGY-----VPFKRrkefARRIGVVfgqrsqlwwdlPAIDSFRLLKAIyRIPDAEY---------------KKRLD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 124 EETKkilsRLGQESI--SPndlIRDLGVGkQQM-VEISKALSVETKLLILDEPTssLG-----KDETKELFDTMGtlKKQ 195
Cdd:COG4586 137 ELVE----LLDLGELldTP---VRQLSLG-QRMrCELAAALLHRPKILFLDEPT--IGldvvsKEAIREFLKEYN--RER 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 196 GVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTE----DKMISYmvgeDVDNKFPKMKVEPGKESLRVENLN 269
Cdd:COG4586 205 GTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKErfgpYKTIVL----ELAEPVPPLELPRGGEVIEREGNR 278
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
263-478 |
8.90e-23 |
|
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: 96.20 E-value: 8.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIdspkvALENGIALL 338
Cdd:cd03269 1 LEVENVTkrfgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDRkeqGLFLKQSVKfniasSNLKKYRENGFLNLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVIGKWLNTE 418
Cdd:cd03269 76 PEER---GLYPKMKVI-----DQLVYLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 419 ANIFIFDEPTRGIDVgAKVEVF-NIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03269 147 PELLILDEPFSGLDP-VNVELLkDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-219 |
9.66e-23 |
|
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: 101.21 E-value: 9.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVR-ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGIT 84
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 PiyqELNLIPQLDVTENIFMGRekskneilgwidRERMEEETKKILSRLG-QESIS--PNDLIRDLG-------VGKQQM 154
Cdd:TIGR02857 402 P---QHPFLFAGTIAENIRLAR------------PDASDAEIREALERAGlDEFVAalPQGLDTPIGeggaglsGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 155 VEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLkKQGVTMIFISHKLdEVKKMADRVTVL 219
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-223 |
2.19e-22 |
|
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: 101.63 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFP--GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdpQKALEQ- 80
Cdd:TIGR01257 927 PGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN--LDAVRQs 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPiyQELNLIPQLDVTENI-FMGREKSKNEILGWIDRERMEEETKKILSRlgqesispNDLIRDLGVGKQQMVEISK 159
Cdd:TIGR01257 1005 LGMCP--QHNILFHHLTVAEHIlFYAQLKGRSWEEAQLEMEAMLEDTGLHHKR--------NEEAQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 160 ALSVETKLLILDEPTSSLGKDETKELFDTMgtLK-KQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKyRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-226 |
2.69e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEF-PGV----RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEG-----KKLEDNDPQ 75
Cdd:PRK13637 3 IKIENLTHIYmEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 76 KaleQLGITPIYQELNLIPQlDVTENIFMGREK---SKNEIlgwidRERMEEETKKI-LSRLGQESISPndliRDLGVGK 151
Cdd:PRK13637 83 K---KVGLVFQYPEYQLFEE-TIEKDIAFGPINlglSEEEI-----ENRVKRAMNIVgLDYEDYKDKSP----FELSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 152 QQMVEISKALSVETKLLILDEPTSSL---GKDETKELFDTMGtlKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYII 226
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLdpkGRDEILNKIKELH--KEYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
2.88e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 96.30 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQ--KALEQLG 82
Cdd:PRK13639 2 LETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ItpIYQelNLIPQL---DVTENIFMGREKSKneilgwIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISK 159
Cdd:PRK13639 82 I--VFQ--NPDDQLfapTVEEDVAFGPLNLG------LSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 160 ALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-223 |
3.38e-22 |
|
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: 94.91 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKkledndpqkaleqlgITP 85
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------------VSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYqELN--LIPQLDVTENI-FMGRekskneILGwIDRERMEEETKKIL--SRLGQESISPndlIRDLGVGKQQMVEISKA 160
Cdd:cd03220 88 LL-GLGggFNPELTGRENIyLNGR------LLG-LSRKEIDEKIDEIIefSELGDFIDLP---VKTYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 161 LSVETKLLILDEPTsSLGKDETKE-LFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03220 157 TALEPDILLIDEVL-AVGDAAFQEkCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-225 |
3.88e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITP 85
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iyQELnLIPQ-LDVTENIFMGREKSKNEilgWidrERMEEETKKILSR-LGQESIS--PNDLIRDLGVGKQQMVEISKAL 161
Cdd:PRK11231 83 --QHH-LTPEgITVRELVAYGRSPWLSL---W---GRLSAEDNARVNQaMEQTRINhlADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-222 |
7.37e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFP----GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLED-NDPQKAL 78
Cdd:PRK11629 4 ILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 79 ---EQLGItpIYQELNLIPQLDVTENIFMGRekskneILGWIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMV 155
Cdd:PRK11629 84 lrnQKLGF--IYQFHHLLPDFTALENVAMPL------LIGKKKPAEINSRALEMLAAVGLEHRA-NHRPSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 156 EISKALSVETKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMaDRVTVLRNG 222
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-236 |
7.94e-22 |
|
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: 98.34 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGV-----RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIY-------IEGKKLE 70
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 71 DNDPQKALEQLGItpIYQELNLIPQLDVTENIfmgREKSKNEILGWIDRERM----------EEETKKILSRLGQEsisp 140
Cdd:TIGR03269 357 PDGRGRAKRYIGI--LHQEYDLYPHRTVLDNL---TEAIGLELPDELARMKAvitlkmvgfdEEKAEEILDKYPDE---- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 141 ndlirdLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDT-MGTLKKQGVTMIFISHKLDEVKKMADRVTVL 219
Cdd:TIGR03269 428 ------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSiLKAREEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
250
....*....|....*..
gi 433671570 220 RNGKYIITDRVDNLTED 236
Cdd:TIGR03269 502 RDGKIVKIGDPEEIVEE 518
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-228 |
8.42e-22 |
|
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: 93.81 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 14 EFPGVR---------ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGIT 84
Cdd:cd03245 4 EFRNVSfsypnqeipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 PiyQELNLIPQlDVTENIFMGR-EKSKNEILGWIDRERMEEETKKilsrlgqesiSPNDLIRDLG-------VGKQQMVE 156
Cdd:cd03245 84 P--QDVTLFYG-TLRDNITLGApLADDERILRAAELAGVTDFVNK----------HPNGLDLQIGergrglsGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 157 ISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLdEVKKMADRVTVLRNGKyIITD 228
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGR-IVAD 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
9.38e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 9.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdpQKALE 79
Cdd:PRK13636 1 MEDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYS--RKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 80 QL--GITPIYQEL-NLIPQLDVTENIFMGREKSKneilgwIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVE 156
Cdd:PRK13636 79 KLreSVGMVFQDPdNQLFSASVYQDVSFGAVNLK------LPEDEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 157 ISKALSVETKLLILDEPTSSLGKDETKELFDTM-GTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYII 226
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIL 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-233 |
1.06e-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: 93.70 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 20 ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGItpIYQElNLIPQLDVT 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV--VLQE-NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 100 ENIFMGREKskneilgwIDRERMEEETKK------ILS-RLGQESIspndlIRDLGV----GKQQMVEISKALSVETKLL 168
Cdd:cd03252 94 DNIALADPG--------MSMERVIEAAKLagahdfISElPEGYDTI-----VGEQGAglsgGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 169 ILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKmADRVTVLRNGKYIITDRVDNL 233
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-223 |
1.08e-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: 93.76 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 16 PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITPiyQElnliPQ 95
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVS--QE----PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 96 L---DVTENIFMGREKSKNEilgwidrerMEEETKKilsrlgQESISpnDLIRDL-----------GV----GKQQMVEI 157
Cdd:cd03249 88 LfdgTIAENIRYGKPDATDE---------EVEEAAK------KANIH--DFIMSLpdgydtlvgerGSqlsgGQKQRIAI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 158 SKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
254-499 |
1.23e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 94.00 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 254 MKVEPgkeSLRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKV 329
Cdd:COG1121 1 MMMMP---AIELENLtvsyGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 330 AlengialltedrkeqglFLKQSVKFN---------IASSNLkkYRENGFLNL--QEQRK---DAIRMVDNLNIKTPNVQ 395
Cdd:COG1121 78 G-----------------YVPQRAEVDwdfpitvrdVVLMGR--YGRRGLFRRpsRADREavdEALERVGLEDLADRPIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 396 tkclQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHE 475
Cdd:COG1121 139 ----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNR 214
|
250 260
....*....|....*....|....*
gi 433671570 476 GKIT-GrfNTDEASKEKIMSAATGG 499
Cdd:COG1121 215 GLVAhG--PPEEVLTPENLSRAYGG 237
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
264-473 |
1.46e-21 |
|
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: 92.98 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 264 RVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVAlengiallt 339
Cdd:cd03235 1 EVEDLtvsyGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 340 edrkeqglFLKQSVKFN----------IASSNLKKYRENGFLNlQEQRKD---AIRMVDNLNIKTPNVQtkclQLSGGNQ 406
Cdd:cd03235 72 --------YVPQRRSIDrdfpisvrdvVLMGLYGHKGLFRRLS-KADKAKvdeALERVGLSELADRQIG----ELSGGQQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 407 QKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVV 473
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-242 |
1.95e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.90 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGkkLEDNDPQKALE---QL 81
Cdd:PRK13644 2 IRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGirkLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITPIYQELNLIPQlDVTENIFMGREK---SKNEILGWIDRERMEEETKKILSRlgqesiSPndliRDLGVGKQQMVEIS 158
Cdd:PRK13644 80 GIVFQNPETQFVGR-TVEEDLAFGPENlclPPIEIRKRVDRALAEIGLEKYRHR------SP----KTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 159 KALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVkKMADRVTVLRNGKYIITDRVDNLTEDKM 238
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
....
gi 433671570 239 ISYM 242
Cdd:PRK13644 228 LQTL 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-228 |
2.23e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.49 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLE--DNDPQKA 77
Cdd:PRK10535 3 ALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtlDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 78 L--EQLGItpIYQELNLIPQLDVTEN-----IFMGREKSKNeilgwidRERMEEetkkILSRLGQE---SISPNdlirDL 147
Cdd:PRK10535 83 LrrEHFGF--IFQRYHLLSHLTAAQNvevpaVYAGLERKQR-------LLRAQE----LLQRLGLEdrvEYQPS----QL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 148 GVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKlDEVKKMADRVTVLRNGKyIIT 227
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGE-IVR 223
|
.
gi 433671570 228 D 228
Cdd:PRK10535 224 N 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-225 |
2.54e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGV-----HTPTEGEIYIEGKKLEDNDPQKALEQ 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGItpIYQELNLIPQLDVTENIFMGRE-----KSKNEI---LGW-IDRERMEEETKkilSRLGQESISpndlirdLGVGK 151
Cdd:PRK14247 84 VQM--VFQIPNPIPNLSIFENVALGLKlnrlvKSKKELqerVRWaLEKAQLWDEVK---DRLDAPAGK-------LSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 152 QQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQgVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-232 |
3.34e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.94 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 24 VDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAL--EQLGITPIYQELNLIPQLDVTEN 101
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppEKRRIGYVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 102 IFMGREKSkneilgwidrerMEEETKKILSRLGQESIspndLIR---DLGVGKQQMVEISKALSVETKLLILDEPTSSLG 178
Cdd:PRK11144 97 LRYGMAKS------------MVAQFDKIVALLGIEPL----LDRypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 179 KDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDN 232
Cdd:PRK11144 161 LPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
264-479 |
3.53e-21 |
|
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: 91.55 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 264 RVENLNRKG-----VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKidspkvalengiall 338
Cdd:cd03226 1 RIENISFSYkkgteILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDRKEQGLFLKQSVKFNIASSNLKK--YRENGFLNLQEQRKDAIrmVDNLNIKTPNVQTKcLQLSGGNQQKVVIGKWLN 416
Cdd:cd03226 66 AKERRKSIGYVMQDVDYQLFTDSVREelLLGLKELDAGNEQAETV--LKDLDLYALKERHP-LSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 417 TEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-227 |
5.96e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.89 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 19 RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlgITPIYQELNLIPQL-- 96
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKD-----IKQIRKKVGLVFQFpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 97 ------DVTENIFMGrekSKNEILGWIDRERMEEEtKKILSRLGQESISPNDLirDLGVGKQQMVEISKALSVETKLLIL 170
Cdd:PRK13649 96 sqlfeeTVLKDVAFG---PQNFGVSQEEAEALARE-KLALVGISESLFEKNPF--ELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 171 DEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIIT 227
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-229 |
6.30e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGV---------RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLE--DN 72
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 73 DPQKALeQLGITPIYQE----LNliPQLDVTENIfmgREKSKNeiLGWIDRERMEEETKKILSRLGqesISPNDLIR--- 145
Cdd:PRK10419 82 AQRKAF-RRDIQMVFQDsisaVN--PRKTVREII---REPLRH--LLSLDKAERLARASEMLRAVD---LDDSVLDKrpp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 146 DLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKy 224
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ- 229
|
....*
gi 433671570 225 IITDR 229
Cdd:PRK10419 230 IVETQ 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-227 |
7.94e-21 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 91.63 E-value: 7.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTG--VHTPTEGEIYIEGKKLEDNDPQKAlEQL 81
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEER-AHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITPIYQ---ELNLIPQLDVTENIFMGREKSKNeiLGWIDRERMEEETKKILSRLGqesISPNDLIRDLGV----GKQQM 154
Cdd:CHL00131 85 GIFLAFQypiEIPGVSNADFLRLAYNSKRKFQG--LPELDPLEFLEIINEKLKLVG---MDPSFLSRNVNEgfsgGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 155 VEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHK---LDEVKkmADRVTVLRNGKYIIT 227
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK--PDYVHVMQNGKIIKT 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-238 |
1.13e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 10 NLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLedndPQKA-LEQLGITPIYQ 88
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARArLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 89 ELNLIPQLDVTENIFM-GRekskneILGWIDRErMEEETKKIL--SRLGQESISPndlIRDLGVGKQQMVEISKALSVET 165
Cdd:PRK13536 122 FDNLDLEFTVRENLLVfGR------YFGMSTRE-IEAVIPSLLefARLESKADAR---VSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKM 238
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-240 |
1.57e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.34 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP-GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGIT 84
Cdd:PRK13647 5 IEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 ---PIYQELNLIPQLDVT---ENIFMGREKSKNEILGWIDRERMEEETKKilsrlgqesiSPNdlirDLGVGKQQMVEIS 158
Cdd:PRK13647 85 fqdPDDQVFSSTVWDDVAfgpVNMGLDKDEVERRVEEALKAVRMWDFRDK----------PPY----HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 159 KALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKM 238
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDI 230
|
..
gi 433671570 239 IS 240
Cdd:PRK13647 231 VE 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-225 |
1.81e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.79 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQkALEQ 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPiyQELNLIPQLDVTENIFM-GRE--KSKNEIlgwidRERMEEETKkiLSRLGQESISPndlIRDLGVGKQQMVEI 157
Cdd:PRK13537 82 VGVVP--QFDNLDPDFTVRENLLVfGRYfgLSAAAA-----RALVPPLLE--FAKLENKADAK---VGELSGGMKRRLTL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 158 SKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-223 |
2.80e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.95 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGItpIYQElnlipqldvTE 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGM--VFQN---------PD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 101 NIFMGREKSKNEILGW----IDRERMEEETKKILSRLGQESISPNDLIRdLGVGKQQMVEISKALSVETKLLILDEPTSS 176
Cdd:PRK13650 92 NQFVGATVEDDVAFGLenkgIPHEEMKERVNEALELVGMQDFKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 433671570 177 LGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVkKMADRVTVLRNGK 223
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
273-504 |
3.58e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALLTEdrkEQGLFLKQS 352
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQ---EPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIAssnlkkyrengfLNLQEQRKDAIRM---VDNLNIK-TPNVQTKCLQLSggNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:PRK15439 103 VKENIL------------FGLPKRQASMQKMkqlLAALGCQlDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 429 RGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDEASKEKIMSAATGGIKDVS 504
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAAREKS 244
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
264-479 |
4.23e-20 |
|
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: 87.49 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 264 RVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvALENGIALLt 339
Cdd:cd03214 1 EVENLsvgyGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK-ELARKIAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 340 edrkeqglflkqsvkfniassnlkkyrengflnLQeqrkdAIRMVDNLNIKTPNVQTkclqLSGGNQQKVVIGKWLNTEA 419
Cdd:cd03214 79 ---------------------------------PQ-----ALELLGLAHLADRPFNE----LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 420 NIFIFDEPTRGIDVGAKVEVFNIINDLVK-KGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-237 |
4.63e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 19 RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQL----GITPIYQELNLIP 94
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLrkkvSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 95 QlDVTENIFMGrekSKNeiLGWIDRErMEEETKKILSRLGQesisPNDLIR----DLGVGKQQMVEISKALSVETKLLIL 170
Cdd:PRK13641 101 N-TVLKDVEFG---PKN--FGFSEDE-AKEKALKWLKKVGL----SEDLISkspfELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 171 DEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDK 237
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-219 |
6.76e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.41 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFP---G-------VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLE 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrGlfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 71 DNDP--QKALEQlGITPIYQ----ELNliPQLDV----TENIFMGREKSKNEilgwiDRERMEEetkkILSRLGqesISP 140
Cdd:PRK11308 81 KADPeaQKLLRQ-KIQIVFQnpygSLN--PRKKVgqilEEPLLINTSLSAAE-----RREKALA----MMAKVG---LRP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 141 NDLIR---DLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRV 216
Cdd:PRK11308 146 EHYDRyphMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEV 225
|
...
gi 433671570 217 TVL 219
Cdd:PRK11308 226 MVM 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-225 |
8.23e-20 |
|
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: 86.98 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG--VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLedNDPQKALEQLgI 83
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSL-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLipqLDVTenifmgrekskneilgwidrermeeetkkILSRLGqesispndliRDLGVGKQQMVEISKALSV 163
Cdd:cd03247 78 SVLNQRPYL---FDTT-----------------------------LRNNLG----------RRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKMaDRVTVLRNGKYI 225
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-222 |
8.97e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 8.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALeqlgitp 85
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMGREkskneiLGWIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALSVET 165
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQ------LAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 166 KLLILDEPTSSLG---KDETKELFDTMgtLKKQGVTMIFISHKLDEVKKMADRVTVLRNG 222
Cdd:PRK11248 148 QLLLLDEPFGALDaftREQMQTLLLKL--WQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
9.33e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG-VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGIt 84
Cdd:PRK13652 4 IETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 pIYQEL-NLIPQLDVTENIFMGREKskneiLGwIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALSV 163
Cdd:PRK13652 83 -VFQNPdDQIFSPTVEQDIAFGPIN-----LG-LDEETVAHRVSSALHMLGLEELR-DRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-223 |
9.51e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 90.55 E-value: 9.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 10 NLTKEFPGvRALDgVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAL--EQLGITPIY 87
Cdd:COG4148 6 DFRLRRGG-FTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLppHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 88 QELNLIPQLDVTENIFMGREKSKNEIlgwiDRERMEEetkkILSRLGqesISP--NDLIRDLGVGKQQMVEISKALSVET 165
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRKRAPRAE----RRISFDE----VVELLG---IGHllDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 166 KLLILDEPTSSLGkDETK-ELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:COG4148 153 RLLLMDEPLAALD-LARKaEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGR 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
276-481 |
1.14e-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: 87.35 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 276 NVSFKAyEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKkVKIDSpkvalENGIALLTEDRK------EQGLFL 349
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDS-----RKKINLPPQQRKiglvfqQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 KQSVKFNIASSnLKKYRENgflnlqEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:cd03297 89 HLNVRENLAFG-LKRKRNR------EDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 433671570 430 GIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVHEGKITGR 481
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNiPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
263-478 |
1.43e-19 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 87.49 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALL 338
Cdd:cd03224 1 LEVENLNagygKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDRkeqGLFLKQSVkfniassnlkkyREN----GFLNLQEQRKDAIRMVDNLnikTPNVQTKCLQ----LSGGNQQKVV 410
Cdd:cd03224 81 PEGR---RIFPELTV------------EENlllgAYARRRAKRKARLERVYEL---FPRLKERRKQlagtLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 411 IGKWLNTEANIFIFDEPTRGIdvgAKV---EVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGL---APKiveEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-235 |
1.56e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.58 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP----TEGEIYIEGKKLEDNDPQ 75
Cdd:COG4170 2 PLLDIRNLTIEIDTpqgrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 76 KALEQLG--ITPIYQElnliPQ--LDVTENIFMGREKS--KNEILGWIDRERME--EETKKILSRLGqesispndlIRD- 146
Cdd:COG4170 82 ERRKIIGreIAMIFQE----PSscLDPSAKIGDQLIEAipSWTFKGKWWQRFKWrkKRAIELLHRVG---------IKDh 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 147 ----------LGVGKQQMVEISKALSVETKLLILDEPTSSLG---KDETKELFDTMGTLkkQGVTMIFISHKLDEVKKMA 213
Cdd:COG4170 149 kdimnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMEsttQAQIFRLLARLNQL--QGTSILLISHDLESISQWA 226
|
250 260
....*....|....*....|..
gi 433671570 214 DRVTVLRNGKYIITDRVDNLTE 235
Cdd:COG4170 227 DTITVLYCGQTVESGPTEQILK 248
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
263-478 |
1.64e-19 |
|
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: 86.80 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvalENGIALL 338
Cdd:cd03259 1 LELKGLSKtygsVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDRkeqGLFLKQSVKFNIASSnLKKyRENGFLNLQEQRKDAIRMVDNLNIktpnVQTKCLQLSGGNQQKVVIGKWLNTE 418
Cdd:cd03259 78 FQDY---ALFPHLTVAENIAFG-LKL-RGVPKAEIRARVRELLELVGLEGL----LNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-251 |
1.77e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.48 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 26 LEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEG---KKLEDNDpQKALEQLGITPIYQELNLIPQLDVTENI 102
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAE-LREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 103 FMGREkskneiLGWIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDET 182
Cdd:PRK10070 128 AFGME------LAGINAEERREKALDALRQVGLENYA-HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 183 KELFDTMGTLK-KQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVD----NLTEDKMISYMVGEDVDNKF 251
Cdd:PRK10070 201 TEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDeilnNPANDYVRTFFRGVDISQVF 274
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-223 |
1.99e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.70 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlGITPIY 87
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER----GVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 88 QELNLIPQLDVTENIFMGRE---KSKNEIlgwidRERMEE-----ETKKILSRlgqesiSPndliRDLGVGKQQMVEISK 159
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKlagAKKEEI-----NQRVNQvaevlQLAHLLDR------KP----KALSGGQRQRVAIGR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 160 ALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-233 |
2.35e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 89.09 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVhtpTEGEIYIEGKKLEDND------ 73
Cdd:PRK15093 2 PLLDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRFDDidllrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 74 -PQKALEQLG--ITPIYQElnliPQ--LDVTENIfmGREKSKNeILGWIDRERMEEETK-------KILSRLGQEsiSPN 141
Cdd:PRK15093 79 sPRERRKLVGhnVSMIFQE----PQscLDPSERV--GRQLMQN-IPGWTYKGRWWQRFGwrkrraiELLHRVGIK--DHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 142 DLIR----DLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRV 216
Cdd:PRK15093 150 DAMRsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKI 229
|
250
....*....|....*..
gi 433671570 217 TVLRNGKYIITDRVDNL 233
Cdd:PRK15093 230 NVLYCGQTVETAPSKEL 246
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-219 |
2.45e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 89.00 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLtkefpgvRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLED-NDPQKALEQLG 82
Cdd:PRK15079 27 FWQPPKTL-------KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQE----LNliPQLDVTENIFMGREKSKNEilgwIDRERMEEETKKILSRLGqesISPNDLIR---DLGVGKQQMV 155
Cdd:PRK15079 100 IQMIFQDplasLN--PRMTIGEIIAEPLRTYHPK----LSRQEVKDRVKAMMLKVG---LLPNLINRyphEFSGGQCQRI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 156 EISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVL 219
Cdd:PRK15079 171 GIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-226 |
2.62e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 20 ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLED-NDPQKALEQLGItpIYQEL-NLIPQLD 97
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeENLWDIRNKAGM--VFQNPdNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 98 VTENIFMGREK---SKNEIlgwidRERMEEETKKIlsRLGQESISPNDLirdLGVGKQQMVEISKALSVETKLLILDEPT 174
Cdd:PRK13633 103 VEEDVAFGPENlgiPPEEI-----RERVDESLKKV--GMYEYRRHAPHL---LSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 433671570 175 SSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKmADRVTVLRNGKYII 226
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVM 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-223 |
5.85e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.27 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIyiegkkLEDNDP-QKALEQlgIT 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPlAEARED--TR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 PIYQELNLIPQLDVTENIFMGREKSkneilgWIDRERMEEETKKILSRlgqesisPNDLIRDLGVGKQQMVEISKALSVE 164
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLKGQ------WRDAALQALAAVGLADR-------ANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 165 TKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-240 |
6.58e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG-----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALE- 79
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 80 -----------------------QLGITPIYQELNLIPQLDVTENIF----MGrekskneilgwIDRERMEEETKKILSR 132
Cdd:PRK13651 83 vleklviqktrfkkikkikeirrRVGVVFQFAEYQLFEQTIEKDIIFgpvsMG-----------VSKEEAKKRAAKYIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 133 LG-QESI---SPndliRDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDE 208
Cdd:PRK13651 152 VGlDESYlqrSP----FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDN 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 433671570 209 VKKMADRVTVLRNGK-------YIITDRVDNLTEDKMIS 240
Cdd:PRK13651 228 VLEWTKRTIFFKDGKiikdgdtYDILSDNKFLIENNMEP 266
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
263-478 |
7.03e-19 |
|
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: 85.00 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvalENGIALL 338
Cdd:cd03301 1 VELENVTKrfgnVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDrkeQGLFLKQSVKFNIASS-NLKKYRENgflNLQEQRKDAIRM--VDNLNIKTPNvqtkclQLSGGNQQKVVIGKWL 415
Cdd:cd03301 78 FQN---YALYPHMTVYDNIAFGlKLRKVPKD---EIDERVREVAELlqIEHLLDRKPK------QLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 416 NTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-223 |
1.19e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.02 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 25 DLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPqkalEQLGITPIYQELNLIPQLDVTENIFM 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP----SRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 105 GREKSKNeiLGWIDRERMEEetkkILSRLGQESISPNdLIRDLGVGKQQMVEISKALSVETKLLILDEPTSSLG---KDE 181
Cdd:PRK10771 95 GLNPGLK--LNAAQREKLHA----IARQMGIEDLLAR-LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 433671570 182 TKELFDTMGTlkKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK10771 168 MLTLVSQVCQ--ERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-224 |
1.32e-18 |
|
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: 89.69 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVR--ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdpqkaleqlgI 83
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN----------I 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLIPQLDVTENIFMGREK-SKNEILGWIDRERMEEETKKILSRLGQeSISPNDLIRDLGVGKQQMVEISKALS 162
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHlYLYARLRGVPAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKY 224
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
1.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.19 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRA--LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQ 80
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGI---TPIYQELNLIPQLDVTenifMGREKSKneilgwIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEI 157
Cdd:PRK13648 85 IGIvfqNPDNQFVGSIVKYDVA----FGLENHA------VPYDEMHRRVSEALKQVDMLERA-DYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 158 SKALSVETKLLILDEPTSSLGKDETKELFDTMGTLK-KQGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGT 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-225 |
2.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 19 RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlgITPIYQELNLI---PQ 95
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKE-----IKPVRKKVGVVfqfPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 96 LDVTENIFMGREKSKNEILGwIDRERMEEETKKILSRLGQESISPNDLIRDLGVGKQQMVEISKALSVETKLLILDEPTS 175
Cdd:PRK13643 95 SQLFEETVLKDVAFGPQNFG-IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 433671570 176 SLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-225 |
2.07e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.23 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 2 IEPFLKIKNLTKEF---------PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDN 72
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 73 DpqKALEQLGITPIYQE----LN---LIPQ-LDVTENIfmgrekskNEILGWIDRErmeeetKKILSRLGQESISPNDLI 144
Cdd:PRK15112 81 D--YSYRSQRIRMIFQDpstsLNprqRISQiLDFPLRL--------NTDLEPEQRE------KQIIETLRQVGLLPDHAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 145 ---RDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLK-KQGVTMIFISHKLDEVKKMADRVTVLR 220
Cdd:PRK15112 145 yypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMH 224
|
....*
gi 433671570 221 NGKYI 225
Cdd:PRK15112 225 QGEVV 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
263-478 |
2.18e-18 |
|
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: 83.71 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNRKG------VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGI- 335
Cdd:cd03263 1 LQIRNLTKTYkkgtkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 336 ----ALLTEdrkeqgLFLKQSVKFniaSSNLKkyrenGfLNLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVI 411
Cdd:cd03263 81 pqfdALFDE------LTVREHLRF---YARLK-----G-LPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 412 GKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDlVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-223 |
2.41e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.06 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLE--DNDPQKALEQLGITPIYQELNLIPQLDV 98
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARAKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 99 TENIFMG---REKSKNEilgwidrerMEEETKKILSRLGQESiSPNDLIRDLGVGKQQMVEISKALSVETKLLILDEPTS 175
Cdd:PRK10584 106 LENVELPallRGESSRQ---------SRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 433671570 176 SLGKDETKELFDTMGTL-KKQGVTMIFISHKlDEVKKMADRVTVLRNGK 223
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
274-498 |
3.19e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 87.09 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALLtedRKEQGLFLKQSV 353
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMV---HQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 354 KFNIAssnLKKYRENG-FLNLQEQRKDAIRMVDNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGID 432
Cdd:PRK10982 91 MDNMW---LGRYPTKGmFVDQDKMYRDTKAIFDELDIDI-DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 433 VGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDEASKEKIMSAATG 498
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
263-478 |
4.15e-18 |
|
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: 83.54 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNRKG---VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvalENGIALLT 339
Cdd:cd03299 1 LKVENLSKDWkefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 340 EDrkeQGLFLKQSVKFNIASSnLKKYRENGflnlQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVIGKWLNTEA 419
Cdd:cd03299 78 QN---YALFPHMTVYKNIAYG-LKKRKVDK----KEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 420 NIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-240 |
5.63e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.55 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVhTPTEGEIYIEGKKLEDN----DPQKALE 79
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVEFFNqniyERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 80 QL--GITPIYQELNLIPqLDVTENIFMGReksknEILGWidRERMEeetkkiLSRLGQESISPNDL-----------IRD 146
Cdd:PRK14258 85 RLrrQVSMVHPKPNLFP-MSVYDNVAYGV-----KIVGW--RPKLE------IDDIVESALKDADLwdeikhkihksALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 147 LGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLK-KQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
250
....*....|....*
gi 433671570 226 ITDRVDNLTEDKMIS 240
Cdd:PRK14258 231 IGQLVEFGLTKKIFN 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-225 |
7.90e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGItp 85
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDVTENIFMGREKSKNEILGWidRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKALSVET 165
Cdd:PRK10253 86 LAQNATTPGDITVQELVARGRYPHQPLFTRW--RKEDEEAVTKAMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-223 |
9.14e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.75 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGK---KLEDNDpqkalEQLG 82
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsRLHARD-----RKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ItpIYQELNLIPQLDVTENIFMG------REKSKNEIlgwIDRERMEEETKKILSRLGQESISpndlirDLGVGKQQMVE 156
Cdd:PRK10851 78 F--VFQHYALFRHMTVFDNIAFGltvlprRERPNAAA---IKAKVTQLLEMVQLAHLADRYPA------QLSGGQKQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 157 ISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGN 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
8-225 |
9.78e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 9.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITPiy 87
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 88 QELNLIPQLDVTENIFMGREKSKNEI--LGWIDRERMEEEtkkiLSRLGQESISpNDLIRDLGVGKQQMVEISKALSVET 165
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGRYPWHGALgrFGAADREKVEEA----ISLVGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-223 |
1.12e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 19 RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQL----GITPIYQELNLIP 94
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLrkkvGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 95 QlDVTENIFMG-------REKSKNEILGWIDRERMEEEtkkILSRlgqesiSPndliRDLGVGKQQMVEISKALSVETKL 167
Cdd:PRK13634 101 E-TVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEE---LLAR------SP----FELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 168 LILDEPTSSL---GKDETKELFDTMGtlKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK13634 167 LVLDEPTAGLdpkGRKEMMEMFYKLH--KEKGLTTVLVTHSMEDAARYADQIVVMHKGT 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
273-478 |
1.15e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.71 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKI--DSP---KVALENGIALLtedRKEQGL 347
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrDKDgqlKVADKNQLRLL---RTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 348 FLKQsvkFNIAS--SNLKKYRENGF----LNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANI 421
Cdd:PRK10619 97 VFQH---FNLWShmTVLENVMEAPIqvlgLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 422 FIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
263-478 |
1.16e-17 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 81.77 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL--------NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVhgkkvkidspkvaleNG 334
Cdd:cd03255 1 IELKNLsktyggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV---------------DG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 335 IALLTEDRKEQGLFLKQSVKFNIASSNLKKY---RENGFLNLQ-------EQRKDAIRMVDNLNIKTpNVQTKCLQLSGG 404
Cdd:cd03255 66 TDISKLSEKELAAFRRRHIGFVFQSFNLLPDltaLENVELPLLlagvpkkERRERAEELLERVGLGD-RLNHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 405 NQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSElPEILNMSDRILVVHEGKI 478
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-235 |
1.20e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIeGKKLedndpqkaleQLGitp 85
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG--- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iY--QELNlipQLDVTENifmgrekskneILGWIDRERMEEETKKILSRLGQESISPNDL---IRDLGVGKQQMVEISKA 160
Cdd:COG0488 382 -YfdQHQE---ELDPDKT-----------VLDELRDGAPGGTEQEVRGYLGRFLFSGDDAfkpVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 161 LSVETKLLILDEPTSSLgkD-ETKELFDTMgtLKK-QGvTMIFISHklDE--VKKMADRVTVLRNGKyiITDRVDNLTE 235
Cdd:COG0488 447 LLSPPNVLLLDEPTNHL--DiETLEALEEA--LDDfPG-TVLLVSH--DRyfLDRVATRILEFEDGG--VREYPGGYDD 516
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
263-478 |
2.02e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 81.44 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALL 338
Cdd:cd03218 1 LRAENLskryGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEdrkEQGLFLKQSVKFNIASSnlkkyRENGFLNLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVIGKWLNTE 418
Cdd:cd03218 81 PQ---EASIFRKLTVEENILAV-----LEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-230 |
2.50e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.51 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQ 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 ---------LGITPIYQELNLIPQLDVTENI---FMGrekskneiLGWIDRERMEEETKKILSRLgqeSISPN---DLIR 145
Cdd:PRK11701 82 errrllrteWGFVHQHPRDGLRMQVSAGGNIgerLMA--------VGARHYGDIRATAGDWLERV---EIDAAridDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 146 DLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGKY 224
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
....*....
gi 433671570 225 I---ITDRV 230
Cdd:PRK11701 231 VesgLTDQV 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-236 |
2.64e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.90 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 17 GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVhTPTEGEIYIEGKKLEDNDPQKALEQLGItpIYQElnliPQL 96
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSW--VGQN----PQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 97 ---DVTENIFMGREK-SKNEILGWIDRERMEEetkkILSRLgqesisPNDL---IRD----LGVGKQQMVEISKALSVET 165
Cdd:PRK11174 435 phgTLRDNVLLGNPDaSDEQLQQALENAWVSE----FLPLL------PQGLdtpIGDqaagLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 166 KLLILDEPTSSLGKDETKELfdtMGTLKK--QGVTMIFISHKLDEVKKMaDRVTVLRNGKYIITDRVDNLTED 236
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLV---MQALNAasRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQA 573
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
263-482 |
3.16e-17 |
|
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: 80.34 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKValeNGIALL 338
Cdd:cd03268 1 LKTNDLTKtygkKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL---RRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEdrkEQGLFLKQSvkfniASSNLKKYRengfLNLQEQRKDAIRMVDNLNIKTPNVQtKCLQLSGGNQQKVVIGKWLNTE 418
Cdd:cd03268 78 IE---APGFYPNLT-----ARENLRLLA----RLLGIRKKRIDEVLDVVGLKDSAKK-KVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRF 482
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-243 |
3.25e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.77 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 16 PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGItpIYQElnliPQ 95
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVAL--VGQE----PV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 96 L---DVTENIFMGrekskneilgwIDRERMEEETKKILSRLGQESIS--PNDLIRDLG-------VGKQQMVEISKALSV 163
Cdd:TIGR00958 566 LfsgSVRENIAYG-----------LTDTPDEEIMAAAKAANAHDFIMefPNGYDTEVGekgsqlsGGQKQRIAIARALVR 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMgtlKKQGVTMIFISHKLDEVKKmADRVTVLRNGKYIITDRVDNLTEDK-MISYM 242
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQgCYKHL 710
|
.
gi 433671570 243 V 243
Cdd:TIGR00958 711 V 711
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-225 |
3.65e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.11 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG--VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDpQKALEQlGI 83
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAALRQ-AI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLipqLDVT--ENIFMGREKSKNEILgwidrermeeetKKILSRLGQESISPND---------LIRDLGVGKQ 152
Cdd:PRK11160 417 SVVSQRVHL---FSATlrDNLLLAAPNASDEAL------------IEVLQQVGLEKLLEDDkglnawlgeGGRQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 153 QMVEISKALSVETKLLILDEPTSSLGKDETKE----LFDTMgtlkkQGVTMIFISHKLDEVKKMaDRVTVLRNGKYI 225
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQilelLAEHA-----QNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
262-478 |
4.06e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.63 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLN---------RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGkkVKIDSPKVALe 332
Cdd:PRK13637 2 SIKIENLThiymegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 333 ngiallTEDRKEQGLFLkQSVKFNIASSNLKKYRENGFLNL-------QEQRKDAIRMV----DNLNIKTPnvqtkcLQL 401
Cdd:PRK13637 79 ------SDIRKKVGLVF-QYPEYQLFEETIEKDIAFGPINLglseeeiENRVKRAMNIVgldyEDYKDKSP------FEL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 402 SGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-223 |
4.45e-17 |
|
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: 80.23 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 20 ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITPiyQElnliPQL--- 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIP--QD----PVLfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 97 DVTENIFMGREKSKNEILGWIDRERMEEETKKILSRLGQEsISPNDLirDLGVGKQQMVEISKALSVETKLLILDEPTSS 176
Cdd:cd03244 93 TIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTV-VEEGGE--NLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 433671570 177 LGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKMaDRVTVLRNGK 223
Cdd:cd03244 170 VDPETDALIQKTIREAFK-DCTVLTIAHRLDTIIDS-DRILVLDKGR 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-233 |
4.91e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 10 NLTKEFPGVR-ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGItpIYQ 88
Cdd:PRK13657 339 DVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV--VFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 89 ELNLIPQlDVTENIFMGREKSKN-EILGWIDR----ERMEEETKKILSRLGQESispndliRDLGVGKQQMVEISKALSV 163
Cdd:PRK13657 417 DAGLFNR-SIEDNIRVGRPDATDeEMRAAAERaqahDFIERKPDGYDTVVGERG-------RQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 164 ETKLLILDEPTSSLgkD-ET----KELFDTMgtlkKQGVTMIFISHKLDEVKKmADRVTVLRNGKYIITDRVDNL 233
Cdd:PRK13657 489 DPPILILDEATSAL--DvETeakvKAALDEL----MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-472 |
5.35e-17 |
|
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: 83.68 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 29 KRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEI-----------YIEGKKLedndpQKALEQL---GITPIY--QELNL 92
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTEL-----QDYFKKLangEIKVAHkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 93 IPQLdvteniFMGREKsknEILGWID-RERMEEetkkILSRLGQESISPNDlIRDLGVGKQQMVEISKALSVETKLLILD 171
Cdd:COG1245 172 IPKV------FKGTVR---ELLEKVDeRGKLDE----LAEKLGLENILDRD-ISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 172 EPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVL----------------RNG------------- 222
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILygepgvygvvskpksvRVGinqyldgylpeen 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 223 ----KYIITDRVDNLTEDKMISYMVgedvdnKFPKMKVEPGKESLRVEnlnrkgvlnnvSFKAYEGEVLGIAGLVGAGRT 298
Cdd:COG1245 318 vrirDEPIEFEVHAPRREKEEETLV------EYPDLTKSYGGFSLEVE-----------GGEIREGEVLGIVGPNGIGKT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 299 EIARAIVGADSKDSGDIYvhgKKVKIDSPKVALENGIALLTEDrkeqglFLKQSVKFNIASSnlkKYRENGF--LNLQeq 376
Cdd:COG1245 381 TFAKILAGVLKPDEGEVD---EDLKISYKPQYISPDYDGTVEE------FLRSANTDDFGSS---YYKTEIIkpLGLE-- 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 377 rkdaiRMVDNlNIKTpnvqtkclqLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLV-KKGNTVIM 455
Cdd:COG1245 447 -----KLLDK-NVKD---------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMV 511
|
490
....*....|....*..
gi 433671570 456 ISSELPEILNMSDRILV 472
Cdd:COG1245 512 VDHDIYLIDYISDRLMV 528
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-225 |
7.24e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.81 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG-VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQkaleQLGIT 84
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA----DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 PIYQELNLIPQLDVTENIFMG---REKSKNEIlgwidRERMeEETKKILSrLGQesispndLI----RDLGVGKQQMVEI 157
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGlkiRGMPKAEI-----EERV-AEAARILE-LEP-------LLdrkpRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 158 SKALSVETKLLILDEPTSSLgkD---------ETKELFDTMGTlkkqgvTMIFISHklDEVKKM--ADRVTVLrNGKYI 225
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNL--DaklrvqmrlEIQRLHRRLKT------TSLYVTH--DQVEAMtlADRVVVM-NGGVA 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-225 |
8.02e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.20 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGV-----HTPTEGEIYIEGKKL--EDND 73
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 74 PQKALEQLGItpIYQELNLIPqLDVTENIFMGReksknEILGWIDRERMEEETKKilsRLGQESI--SPNDLIRD----L 147
Cdd:PRK14239 81 TVDLRKEIGM--VFQQPNPFP-MSIYENVVYGL-----RLKGIKDKQVLDEAVEK---SLKGASIwdEVKDRLHDsalgL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 148 GVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQgVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-249 |
9.02e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.13 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEF-PG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKledndpqkaleq 80
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 lgIT--PIYQELNLI------------PQLDVTENIFMGREKSKNEILGW-IDRERMeEETKKILSRLGqesispNDLIR 145
Cdd:COG1101 70 --VTklPEYKRAKYIgrvfqdpmmgtaPSMTIEENLALAYRRGKRRGLRRgLTKKRR-ELFRELLATLG------LGLEN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 146 DLGV-------GKQQmveiskALS------VETKLLILDEPTSSLgkDE---------TKELfdtmgtLKKQGVTMIFIS 203
Cdd:COG1101 141 RLDTkvgllsgGQRQ------ALSllmatlTKPKLLLLDEHTAAL--DPktaalvlelTEKI------VEENNLTTLMVT 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 433671570 204 HKLDEVKKMADRVTVLRNGKyIITDRVD----NLTEDK---MISYMVGEDVDN 249
Cdd:COG1101 207 HNMEQALDYGNRLIMMHEGR-IILDVSGeekkKLTVEDlleLFEEIRGEELAD 258
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
274-428 |
1.00e-16 |
|
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: 77.30 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvALENGIALLTEDRkeqGLFLKQSV 353
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDP---QLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 354 KFNIASSNLKKYRENGflNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:pfam00005 77 RENLRLGLLLKGLSKR--EKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-173 |
1.40e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.92 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdNDP--QKAleQLGI 83
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPmhKRA--RLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TpiY--QELNLIPQLDVTENIFM---GREKSKNEIlgwidRERMEEetkkILSRLGqesISPndlIRD-LGV----GKQQ 153
Cdd:COG1137 81 G--YlpQEASIFRKLTVEDNILAvleLRKLSKKER-----EERLEE----LLEEFG---ITH---LRKsKAYslsgGERR 143
|
170 180
....*....|....*....|
gi 433671570 154 MVEISKALSVETKLLILDEP 173
Cdd:COG1137 144 RVEIARALATNPKFILLDEP 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-225 |
1.48e-16 |
|
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: 77.98 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 9 KNLTKEFPGVRA------LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP--TEGEIYIEGKKLEDNDPQKaleQ 80
Cdd:cd03213 7 RNLTVTVKSSPSksgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRK---I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPiyQELNLIPQLDVTENIFMGREkskneilgwidrermeeetkkilsrlgqesispndlIRDLGVGKQQMVEISKA 160
Cdd:cd03213 84 IGYVP--QDDILHPTLTVRETLMFAAK------------------------------------LRGLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 161 LSVETKLLILDEPTSSLgkDETKElFDTMGTLKK---QGVTMIFISHKL-DEVKKMADRVTVLRNGKYI 225
Cdd:cd03213 126 LVSNPSLLFLDEPTSGL--DSSSA-LQVMSLLRRladTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
263-478 |
1.53e-16 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 78.34 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVAlengiall 338
Cdd:cd03262 1 IEIKNLHKsfgdFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIN-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 tEDRKEQG-------LFLKQSVKFNI--ASSNLKKYRENGFLNLQEQRKDAIRMVDNLNiKTPNvqtkclQLSGGNQQKV 409
Cdd:cd03262 73 -ELRQKVGmvfqqfnLFPHLTVLENItlAPIKVKGMSKAEAEERALELLEKVGLADKAD-AYPA------QLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 410 VIGKWLNTEANIFIFDEPTRGID---VGakvEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
263-478 |
1.65e-16 |
|
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: 79.32 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDSPKVALEngIAL 337
Cdd:COG1120 2 LEAENLsvgyGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaSLSRRELARR--IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTedrkeqglflkQSvkfNIASSNLK--------KYRENGFLNlQEQRKD------AIRMVDNLNIKTPNVQTkclqLSG 403
Cdd:COG1120 80 VP-----------QE---PPAPFGLTvrelvalgRYPHLGLFG-RPSAEDreaveeALERTGLEHLADRPVDE----LSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 404 GNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVK-KGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-227 |
2.11e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.28 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLT-----KEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKledNDPQKALEQ 80
Cdd:PRK13631 22 LRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIY---IGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPIYQELNLIPQLDVTENI---FMGREKSKNEI----------LGwIDRERMEEETKKILSRLGQESISPNDLIRDL 147
Cdd:PRK13631 99 LITNPYSKKIKNFKELRRRVSMvfqFPEYQLFKDTIekdimfgpvaLG-VKKSEAKKLAKFYLNKMGLDDSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 148 GVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIIT 227
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-223 |
2.56e-16 |
|
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: 78.04 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG--VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyQELNLIPQlDVTENIFMGREKskneilgwIDRERMEEETKKILSrlgQESI--SPNDL---IRDLGV----GKQQM 154
Cdd:cd03251 81 VS--QDVFLFND-TVAENIAYGRPG--------ATREEVEEAARAANA---HEFImeLPEGYdtvIGERGVklsgGQRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 155 VEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-223 |
2.86e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.99 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVR-ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEG---KKLEDNDPQKALEQL 81
Cdd:PRK10908 2 IRFEHVSKAYLGGRqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GItpIYQELNLIPQLDVTENIFMGRekskneILGWIDRERMEEETKKILSRLGQESISPNDLIRdLGVGKQQMVEISKAL 161
Cdd:PRK10908 82 GM--IFQDHHLLMDRTVYDNVAIPL------IIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
273-478 |
3.25e-16 |
|
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: 77.41 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVkIDSPKVALENgIALLTEDRkeqGLFLKQS 352
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRR-LGFVSDST---GLYDRLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIAS----SNLKKYRENGFLnlqEQRKDAIRMVDNLNIKTPNvqtkclqLSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:cd03266 95 ARENLEYfaglYGLKGDELTARL---EELADRLGMEELLDRRVGG-------FSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 433671570 429 RGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03266 165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-225 |
3.47e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGV-----HTPTEGEIYIEGKKL--EDNDPQKALEQLGItpIYQELNLI 93
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIysPDVDPIEVRREVGM--VFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 94 PQLDVTENIFMGRE-----KSKNEIlgwidRERMEEETKK------ILSRLgqesispNDLIRDLGVGKQQMVEISKALS 162
Cdd:PRK14267 98 PHLTIYDNVAIGVKlnglvKSKKEL-----DERVEWALKKaalwdeVKDRL-------NDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQgVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-206 |
3.72e-16 |
|
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: 80.87 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPG-VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQL 81
Cdd:TIGR02868 332 KPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITPiyQELNLIPQlDVTENIFMGREkskneilgwidrERMEEETKKILSRLGQEsispnDLIRDL--GV---------- 149
Cdd:TIGR02868 412 SVCA--QDAHLFDT-TVRENLRLARP------------DATDEELWAALERVGLA-----DWLRALpdGLdtvlgeggar 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 150 ---GKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTM--GTlkkQGVTMIFISHKL 206
Cdd:TIGR02868 472 lsgGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLlaAL---SGRTVVLITHHL 530
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-223 |
3.74e-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: 77.66 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 16 PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITPiyQELNLIPQ 95
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP--QDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 96 lDVTENIFMGREKSKNE------ILGWIDR--ERMEEETKKILSRLGQEsispndlirdLGVGKQQMVEISKALSVETKL 167
Cdd:cd03253 90 -TIGYNIRYGRPDATDEevieaaKAAQIHDkiMRFPDGYDTIVGERGLK----------LSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 168 LILDEPTSSLGKDETKELFDTMGTLKKqGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-239 |
3.97e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.01 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIegkklEDND----PQKALEQL 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII-----DDEDisllPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITPIYQELNLIPQLDVTENIFMGREKSKNeilgwIDRERMEEETKKILSRLGQESISpNDLIRDLGVGKQQMVEISKAL 161
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRDD-----LSAEQREDRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNLTEDKMI 239
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-223 |
4.66e-16 |
|
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: 77.31 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 5 FLKIKNLTKEfpgVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTG---VHTPTEGEIYIEGKKLednDPQKALEQL 81
Cdd:cd03234 10 GLKAKNWNKY---ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR---KPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITPiyQELNLIPQLDVTE-----NIFMGREKSKNEIlgwidRERMEEETKkiLSRLGQESISpNDLIRDLGVGKQQMVE 156
Cdd:cd03234 84 AYVR--QDDILLPGLTVREtltytAILRLPRKSSDAI-----RKKRVEDVL--LRDLALTRIG-GNLVKGISGGERRRVS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 157 ISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHK-LDEVKKMADRVTVLRNGK 223
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGE 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-236 |
5.25e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.77 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVH--TP---TEGEIYIEGKKLedNDPQKA 77
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGEDI--YDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 78 LEQL----GItpIYQELNLIPqLDVTENIFMG----REKSKNEIlgwidRERME---------EETKKILSRLGQeSISP 140
Cdd:COG1117 87 VVELrrrvGM--VFQKPNPFP-KSIYDNVAYGlrlhGIKSKSEL-----DEIVEeslrkaalwDEVKDRLKKSAL-GLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 141 ndlirdlgvGKQQMVEISKALSVETKLLILDEPTSSLgkD--ETKELFDTMGTLKKQgVTMIFISHKLDEVKKMADRVTV 218
Cdd:COG1117 158 ---------GQQQRLCIARALAVEPEVLLMDEPTSAL--DpiSTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAF 225
|
250 260
....*....|....*....|....*..
gi 433671570 219 LRNGKyII----TDRV-----DNLTED 236
Cdd:COG1117 226 FYLGE-LVefgpTEQIftnpkDKRTED 251
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
273-486 |
7.40e-16 |
|
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: 76.85 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKValengialLTEDRKEQGLFLKQs 352
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKE--------LRKARRRIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 vkFNIASSnlKKYRENGFLNLQ---EQRKDAIRMVDNLnIKTPNVQTKC----LQLSGGNQQKVVIGKWLNTEANIFIFD 425
Cdd:cd03258 91 --FNLLSS--RTVFENVALPLEiagVPKAEIEERVLEL-LELVGLEDKAdaypAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 426 EPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDE 486
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-236 |
7.98e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.05 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEpflkIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQ 80
Cdd:COG4604 1 MIE----IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPiyQELNLIPQLDVTENIFMGR---EKSKneiLGWIDRERMEEEtkkiLSRLGQESISpNDLIRDLGVGKQQMVEI 157
Cdd:COG4604 77 LAILR--QENHINSRLTVRELVAFGRfpySKGR---LTAEDREIIDEA----IAYLDLEDLA-DRYLDELSGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 158 SKALSVETKLLILDEPTSSLgkdETKELFDTMGTLKK----QGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDN- 232
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNL---DMKHSVQMMKLLRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEi 223
|
....
gi 433671570 233 LTED 236
Cdd:COG4604 224 ITPE 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
273-478 |
8.80e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 76.51 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVkIDSPkvALENGIALLTEDrkeQGLFLKQS 352
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLP--PHKRPVNTVFQN---YALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIASS-NLKKYRENgflNLQEQRKDAIRMV--DNLNIKTPNvqtkclQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:cd03300 89 VFENIAFGlRLKKLPKA---EIKERVAEALDLVqlEGYANRKPS------QLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 433671570 430 GIDV----GAKVEVFNIINDLvkkGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03300 160 ALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
263-478 |
1.00e-15 |
|
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: 76.32 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNRK--GV--LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIAll 338
Cdd:cd03219 1 LEVRGLTKRfgGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 tedRKEQ--GLFLKQSVKFNIASSNLKKYRENGFL-----NLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVI 411
Cdd:cd03219 79 ---RTFQipRLFPELTVLENVMVAAQARTGSGLLLararrEEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 412 GKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
260-497 |
1.04e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.36 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 260 KESLRVENLN------RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSpkvalen 333
Cdd:PRK13635 3 EEIIRVEHISfrypdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 334 gialLTEDRKEQGL--------FLKQSVKFNIASsnlkkyrenGFLNLQEQRKDAIRMVDNLnIKTPNVQTKCLQ----L 401
Cdd:PRK13635 76 ----VWDVRRQVGMvfqnpdnqFVGATVQDDVAF---------GLENIGVPREEMVERVDQA-LRQVGMEDFLNRephrL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 402 SGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNmSDRILVVHEGKItg 480
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEI-- 218
|
250
....*....|....*..
gi 433671570 481 rfnTDEASKEKIMSAAT 497
Cdd:PRK13635 219 ---LEEGTPEEIFKSGH 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
274-498 |
1.76e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALLTEdrkEQGLFLKQSV 353
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQ---ELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 354 KFNIASSNL--KKYRENGFLNLQEQRKDAIRMVDNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGI 431
Cdd:PRK09700 98 LENLYIGRHltKKVCGVNIIDWREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 432 DVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDEASKEKIMSAATG 498
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
273-478 |
1.76e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.57 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALEN-GIALLTEDRKeqglFLKQ 351
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKiGIIFQNPDNQ----FIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIASsnlkkyrenGFLNLQEQRKDAIRMVDNLNIKT---PNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:PRK13632 100 TVEDDIAF---------GLENKKVPPKKMKDIIDDLAKKVgmeDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 433671570 429 RGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKL 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
273-477 |
1.77e-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: 74.34 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENgIALLTedrkeQGLFL-KQ 351
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVP-----QDPFLfSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIassnlkkyrengflnlqeqrkdairmvdnlniktpnvqtkclqLSGGNQQKVVIGKWLNTEANIFIFDEPTRGI 431
Cdd:cd03228 91 TIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 433671570 432 DVGAKVEVFNIINDLvKKGNTVIMISSELPEILNMsDRILVVHEGK 477
Cdd:cd03228 128 DPETEALILEALRAL-AKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
263-479 |
2.08e-15 |
|
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: 75.40 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDSPKVAlENGIAL 337
Cdd:COG0410 4 LEVENLHagygGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHRIA-RLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDRkeqGLFLKQSVKFN--IASSNLKKYRENG---------FLNLQEQRKdairmvdnlniktpnvqTKCLQLSGGNQ 406
Cdd:COG0410 83 VPEGR---RIFPSLTVEENllLGAYARRDRAEVRadlervyelFPRLKERRR-----------------QRAGTLSGGEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 407 QKVVIGKWLNTEANIFIFDEPTRGIdvgAKV---EVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGL---APLiveEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-472 |
2.40e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 28 IKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEI-----------YIEGKKLedndpQKALEQL---GITPIY--QELN 91
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTEL-----QNYFKKLyngEIKVVHkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 92 LIPQLdvteniFMGREKsknEILGWID-RERMEEetkkILSRLGQESISPNDlIRDLGVGKQQMVEISKALSVETKLLIL 170
Cdd:PRK13409 171 LIPKV------FKGKVR---ELLKKVDeRGKLDE----VVERLGLENILDRD-ISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 171 DEPTSSLgkdETKELFDTMGTLKK--QGVTMIFISHKLDEVKKMADRVTVL--RNGKY-IITD----RVD-N------LT 234
Cdd:PRK13409 237 DEPTSYL---DIRQRLNVARLIRElaEGKYVLVVEHDLAVLDYLADNVHIAygEPGAYgVVSKpkgvRVGiNeylkgyLP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 235 EDKM------ISYMV-------GEDVDNKFPKMKVEPGKESLRVEnlnrkgvlnnvSFKAYEGEVLGIAGLVGAGRTEIA 301
Cdd:PRK13409 314 EENMrirpepIEFEErpprdesERETLVEYPDLTKKLGDFSLEVE-----------GGEIYEGEVIGIVGPNGIGKTTFA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 302 RAIVGADSKDSGDIYvhgKKVKIDSpkvalengialltedrKEQGLFLKQ--SVKFNIASSNlKKYRENGFLNLQEQRKD 379
Cdd:PRK13409 383 KLLAGVLKPDEGEVD---PELKISY----------------KPQYIKPDYdgTVEDLLRSIT-DDLGSSYYKSEIIKPLQ 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 380 AIRMVDNlNIKTpnvqtkclqLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLV-KKGNTVIMISS 458
Cdd:PRK13409 443 LERLLDK-NVKD---------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDH 512
|
490
....*....|....
gi 433671570 459 ELPEILNMSDRILV 472
Cdd:PRK13409 513 DIYMIDYISDRLMV 526
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-225 |
2.50e-15 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 75.60 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGV--HTPTEGEIYIEGKKLEDNDPQ-KALEqlG 82
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEdRAGE--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITPIYQELNLIPqlDVTENIFMG------REKSKNEILGWIDRERMEEETKKILSRlgqesisPNDLI-RDLGV----GK 151
Cdd:PRK09580 80 IFMAFQYPVEIP--GVSNQFFLQtalnavRSYRGQEPLDRFDFQDLMEEKIALLKM-------PEDLLtRSVNVgfsgGE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 152 QQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHK---LDEVKkmADRVTVLRNGKYI 225
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK--PDYVHVLYQGRIV 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
273-499 |
2.84e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALLTEDRKeqgLFLKQS 352
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIASSnlkkyrenGFLNLQEQRKDAIRMVDNLnikTPNVQTKCLQ----LSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:PRK11614 97 VEENLAMG--------GFFAERDQFQERIKWVYEL---FPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 429 RGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRfNTDEA--SKEKIMSAATGG 499
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE-DTGDAllANEAVRSAYLGG 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
274-498 |
3.09e-15 |
|
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: 77.94 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDS--GDIYVHGKKVKIDSPKVALENGIALLtedRKEQGLFLKQ 351
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIVII---HQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIASSNlKKYRENGFLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGI 431
Cdd:TIGR02633 94 SVAENIFLGN-EITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 432 DVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDEASKEKIMSAATG 498
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-228 |
3.30e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.99 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 20 ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP---TEGEIYIEGKKLEDNDPQKALEQLGItpIYQElnlipql 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGI--VFQN------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 97 dvTENIFMGREKSKNEILGWIDRERMEEETKKILSRLgQESISPNDLIR----DLGVGKQQMVEISKALSVETKLLILDE 172
Cdd:PRK13640 93 --PDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDV-LADVGMLDYIDsepaNLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 173 PTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVkKMADRVTVLRNGKYIITD 228
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
273-478 |
3.57e-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: 74.83 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVK-IDSPKVALENGIALltedrkEQGLFLKQ 351
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlADPAWLRRQVGVVL------QENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIASSNLKKYREngflnlqeQRKDAIRMVD--NLNIKTPN-----VQTKCLQLSGGNQQKVVIGKWLNTEANIFIF 424
Cdd:cd03252 91 SIRDNIALADPGMSME--------RVIEAAKLAGahDFISELPEgydtiVGEQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 433671570 425 DEPTRGIDVGAKVEVFNIINDLVkKGNTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-223 |
3.61e-15 |
|
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: 74.81 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 16 PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQlgITPIYQElnliPQ 95
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK--VSLVGQE----PV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 96 L---DVTENIFMGrekskneiLGWIDRERMEEETKK-----ILSRLGQE-SISPNDLIRDLGVGKQQMVEISKALSVETK 166
Cdd:cd03248 99 LfarSLQDNIAYG--------LQSCSFECVKEAAQKahahsFISELASGyDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 167 LLILDEPTSSLgkdetkelfDTMGTLKKQGV--------TMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:cd03248 171 VLILDEATSAL---------DAESEQQVQQAlydwperrTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
262-478 |
3.94e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVkidSPKVAleNGIAL 337
Cdd:COG4152 1 MLELKGLTKrfgdKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDR--RRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDRkeqGLFLKQSVKFNIAssnlkkY--RENGfLNLQEQRKDAIRMVDNLNI---KTPNVQTkclqLSGGNQQKV--- 409
Cdd:COG4152 76 LPEER---GLYPKMKVGEQLV------YlaRLKG-LSKAEAKRRADEWLERLGLgdrANKKVEE----LSKGNQQKVqli 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 410 --VIGkwlntEANIFIFDEPTRGID-VGakVEVF-NIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:COG4152 142 aaLLH-----DPELLILDEPFSGLDpVN--VELLkDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
262-478 |
5.13e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 74.68 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLNRK----GVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVkidSPKVALENGIAL 337
Cdd:cd03296 2 SIEVRNVSKRfgdfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEdrkEQGLFLKQSVKFNIA------------SSNLKKYRENGFLNLQEqrkdairmVDNLNIKTPNvqtkclQLSGGN 405
Cdd:cd03296 79 VFQ---HYALFRHMTVFDNVAfglrvkprserpPEAEIRAKVHELLKLVQ--------LDWLADRYPA------QLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 406 QQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-223 |
1.05e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.84 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 7 KIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTG-VHTPT-EGEIYIEGKKLEdndpQKALEQLGIt 84
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPT----KQILKRTGF- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 pIYQELNLIPQLDVTENIFMGREKSKNEILGWIDRERMEEEtkkILSRLG----QESISPNDLIRDLGVGKQQMVEISKA 160
Cdd:PLN03211 145 -VTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAES---VISELGltkcENTIIGNSFIRGISGGERKRVSIAHE 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 161 LSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHK-LDEVKKMADRVTVLRNGK 223
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-225 |
1.37e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.05 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 20 ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKAleqlgITPIYQELNLIPQL--- 96
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKY-----IRPVRKRIGMVFQFpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 97 -----DVTENIFMGREKSKneilgwIDRERMEEETKKILSRLGQE----SISPndliRDLGVGKQQMVEISKALSVETKL 167
Cdd:PRK13646 97 qlfedTVEREIIFGPKNFK------MNLDEVKNYAHRLLMDLGFSrdvmSQSP----FQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 168 LILDEPTSSLgkdETKELFDTMGTLKK----QGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK13646 167 IVLDEPTAGL---DPQSKRQVMRLLKSlqtdENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
264-478 |
1.38e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 73.07 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 264 RVENLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKD---SGDIYVHGKKVKidsPKVALENGIALLTE 340
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK---PDQFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 341 DRKEQGLFLKQSVKF--NIASSNLKKYRENGFLNLQEQRKD-AIRMVDNLNIKtpnvqtkclQLSGGNQQKVVIGKWLNT 417
Cdd:cd03234 90 DILLPGLTVRETLTYtaILRLPRKSSDAIRKKRVEDVLLRDlALTRIGGNLVK---------GISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 418 EANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIM-ISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-236 |
1.41e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVhTPTEGEIYIEGKKLEDNDPQKA------LEQ----LGITPIYQEL 90
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELarhrayLSQqqspPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 91 NL-IPQLDVTENIfmgrEKSKNEILgwidrERMEEETKkiLSR-LGQESispndlirdlGvGKQQMVEISKA-LSV---- 163
Cdd:COG4138 91 ALhQPAGASSEAV----EQLLAQLA-----EALGLEDK--LSRpLTQLS----------G-GEWQRVRLAAVlLQVwpti 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 164 --ETKLLILDEPTSSLgkDETKEL-FDTM-GTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDN-LTED 236
Cdd:COG4138 149 npEGQLLLLDEPMNSL--DVAQQAaLDRLlRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEvMTPE 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-225 |
1.60e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGV------HTPTEGEIYIEGKKLEDNDPQKALEQLGItpIYQELNLIP 94
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRKEVGM--VFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 95 QLDVTENIFMGRE----KSKNEIlgwidRERMEEETKKI-LSRLGQESIspNDLIRDLGVGKQQMVEISKALSVETKLLI 169
Cdd:PRK14246 104 HLSIYDNIAYPLKshgiKEKREI-----KKIVEECLRKVgLWKEVYDRL--NSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 170 LDEPTSSLGKDETKELFDTMGTLKKQgVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-225 |
1.64e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.89 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 19 RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDN-----DPQKALEQLGITPIYQELNLI 93
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 94 pQLDVTENIFMGREKskneiLGwidrERMEEETKKILSRLGQESIsPNDLIR----DLGVGKQQMVEISKALSVETKLLI 169
Cdd:PRK13645 105 -QETIEKDIAFGPVN-----LG----ENKQEAYKKVPELLKLVQL-PEDYVKrspfELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 170 LDEPTSSL---GKDETKELFDTMGtlKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK13645 174 LDEPTGGLdpkGEEDFINLFERLN--KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-223 |
1.91e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.76 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEG----KKLEdNDPQKAL-------------EQLGI 83
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivARLQ-QDPPRNVegtvydfvaegieEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLIPQLDVTENIF--MGREKSKNEIL-GWidreRMEEETKKILSRLGqesISPNDLIRDLGVGKQQMVEISKA 160
Cdd:PRK11147 98 LKRYHDISHLVETDPSEKNLneLAKLQEQLDHHnLW----QLENRINEVLAQLG---LDPDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 161 LSVETKLLILDEPTSSLGKD--ETKELFdtmgtLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIEtiEWLEGF-----LKTFQGSIIFISHDRSFIRNMATRIVDLDRGK 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
263-478 |
2.08e-14 |
|
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: 72.60 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL-----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKValengial 337
Cdd:cd03256 1 IEVENLsktypNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDRKEQG-------LFLKQSVKFNIASSNL---KKYRenGFLNL--QEQRKDAIRMVDNLNIKTpNVQTKCLQLSGGN 405
Cdd:cd03256 73 LRQLRRQIGmifqqfnLIERLSVLENVLSGRLgrrSTWR--SLFGLfpKEEKQRALAALERVGLLD-KAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 406 QQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDL-VKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
274-478 |
2.95e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.23 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSP-KVALENGIALLTEDRKEQGLFLKQS 352
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIassnlkkyrENGFLNLQEQRK---DAIRMVDNLNIKTpnvqTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:PRK13650 103 VAFGL---------ENKGIPHEEMKErvnEALELVGMQDFKE----REPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 433671570 430 GIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEIlNMSDRILVVHEGKI 478
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQmTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-223 |
3.40e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdndpqkaLEQLGITPIYQELNLIPQlDVTE 100
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-------YSKRGLLALRQQVATVFQ-DPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 101 NIF--------------MGREKSK-----NEILGWIDRERMEEETKKILSRlgqesispndlirdlgvGKQQMVEISKAL 161
Cdd:PRK13638 89 QIFytdidsdiafslrnLGVPEAEitrrvDEALTLVDAQHFRHQPIQCLSH-----------------GQKKRVAIAGAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
262-478 |
3.96e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKvkIDSPKVALENGIAL 337
Cdd:COG4161 2 SIQLKNINCfygsHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQ--FDFSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LtedRKEQGLFLKQ-------SVKFNIASSNLKKYRengfLNLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVV 410
Cdd:COG4161 80 L---RQKVGMVFQQynlwphlTVMENLIEAPCKVLG----LSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 411 IGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-223 |
4.13e-14 |
|
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: 69.40 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIyiegkkledndpqkaleqlgITP 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------TWG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQLDvtenifmGREKSKneilgwidrermeeetkkilsrlgqesispndlirdlgvgkqqmVEISKALSVET 165
Cdd:cd03221 61 STVKIGYFEQLS-------GGEKMR--------------------------------------------LALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 166 KLLILDEPTSSLgkD-ETKELFDTMgtLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:cd03221 90 NLLLLDEPTNHL--DlESIEALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
259-478 |
5.89e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.58 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 259 GKESLRVENL---------NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSG-----DIYVHGKKVKI 324
Cdd:PRK13631 18 DDIILRVKNLycvfdekqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 325 DSPKVALENGIALLTEDRKEQGlFLKQSVKFNIASSNLKKYRENGFLNL----QEQRKDAIRMVDNLNIKTPNVQTKCLQ 400
Cdd:PRK13631 98 ELITNPYSKKIKNFKELRRRVS-MVFQFPEYQLFKDTIEKDIMFGPVALgvkkSEAKKLAKFYLNKMGLDDSYLERSPFG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
263-478 |
6.09e-14 |
|
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: 69.94 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL------NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGdiyvhgkKVKIDspkvalenGIA 336
Cdd:cd03246 1 LEVENVsfrypgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSG-------RVRLD--------GAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 337 LLTEDRKEQGLFLkqsvkfniassnlkkyrenGFLnLQEqrkdairmvDNL-------NIktpnvqtkclqLSGGNQQKV 409
Cdd:cd03246 66 ISQWDPNELGDHV-------------------GYL-PQD---------DELfsgsiaeNI-----------LSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 410 VIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSElPEILNMSDRILVVHEGKI 478
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-219 |
6.18e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIyiegkkledndpqKALEQLGI 83
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELNLIPQLDVTENIFMgrekskneilgwidreRMEEETKK--ILSRLgqESISPNDLI----RDLGVGKQQMVEI 157
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFL----------------RLRPGTKKedILPAL--KRVQAGHLIdapmQKLSGGETQRVLL 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 158 SKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVL 219
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
265-478 |
7.03e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 265 VENLNRK----GVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVhgKKVKIDSPKVAlengiallte 340
Cdd:PRK11264 6 VKNLVKKfhgqTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--GDITIDTARSL---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 341 dRKEQGLF--LKQSVKFNIASSNLKKYR-------ENGFLNLQEQRKDAIRMVDNLNIK---TPNVQTKCLQLSGGNQQK 408
Cdd:PRK11264 74 -SQQKGLIrqLRQHVGFVFQNFNLFPHRtvleniiEGPVIVKGEPKEEATARARELLAKvglAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 409 VVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
268-478 |
7.57e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 268 LNRKGvLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVkidspkvALENGIALLTEDRKEQGL 347
Cdd:PRK13641 18 MEKKG-LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-------TPETGNKNLKKLRKKVSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 348 FLkQSVKFNIASSNLKKYRENGFLNL----QEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFI 423
Cdd:PRK13641 90 VF-QFPEAQLFENTVLKDVEFGPKNFgfseDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 424 FDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
270-478 |
7.86e-14 |
|
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: 69.89 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 270 RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVG--ADSKDSGDIYVHGKKVKIDSPKVAlengIALLTEDrkeqgl 347
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI----IGYVPQD------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 348 flkqsvkfNIASSNLKkYRENgflnLQeqrkdairmvdnlniktpnVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEP 427
Cdd:cd03213 91 --------DILHPTLT-VRET----LM-------------------FAAKLRGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 428 TRGIDVGAKVEVFNIINDLVKKGNTVIMI----SSelpEILNMSDRILVVHEGKI 478
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGRV 190
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-223 |
8.03e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 24 VDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQkALEQLgITPIYQELNLIPQLDVTEnif 103
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-DYRKL-FSAVFTDFHLFDQLLGPE--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 104 mGREKSKNEILGWIDRERMEEETkkilsRLGQESISpnDLirDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETK 183
Cdd:PRK10522 417 -GKPANPALVEKWLERLKMAHKL-----ELEDGRIS--NL--KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 433671570 184 ELF-DTMGTLKKQGVTMIFISHKlDEVKKMADRVTVLRNGK 223
Cdd:PRK10522 487 EFYqVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
284-478 |
8.62e-14 |
|
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: 70.21 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 284 GEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvalENGIALLTEdrkEQGLFLKQSVKFNIA---SS 360
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSMLFQ---ENNLFAHLTVEQNVGlglSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 361 NLKkyrengfLNLQEQRK-DAI--RM-VDNLNIKTPNvqtkclQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAK 436
Cdd:cd03298 98 GLK-------LTAEDRQAiEVAlaRVgLAGLEKRLPG------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 433671570 437 VEVFNIINDL-VKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03298 165 AEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-242 |
9.63e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 9 KNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDpqkaLE---QLGitp 85
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD----IAtrrRVG--- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iY--QELNLIPQLDVTEN------IF-MGREKSkneilgwidRERMEEetkkILSRLGQESIS---PNDLirDLGVgKQQ 153
Cdd:NF033858 343 -YmsQAFSLYGELTVRQNlelharLFhLPAAEI---------AARVAE----MLERFDLADVAdalPDSL--PLGI-RQR 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 154 MveiSKALSV--ETKLLILDEPTSslGKD-ETKELF-DTMGTL-KKQGVTmIFIS-HKLDEvkkmA---DRVTVLRNGKY 224
Cdd:NF033858 406 L---SLAVAVihKPELLILDEPTS--GVDpVARDMFwRLLIELsREDGVT-IFIStHFMNE----AercDRISLMHAGRV 475
|
250 260
....*....|....*....|....*.
gi 433671570 225 IITDRVDNLT--------EDKMISYM 242
Cdd:NF033858 476 LASDTPAALVaargaatlEEAFIAYL 501
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
263-478 |
1.02e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.55 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN-RKGVLN-NVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPkvalengialltE 340
Cdd:COG3840 2 LRLDDLTyRYGDFPlRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP------------A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 341 DRK------EQGLFLKQSVKFNIA---SSNLKkyrengfLNlQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVI 411
Cdd:COG3840 70 ERPvsmlfqENNLFPHLTVAQNIGlglRPGLK-------LT-AEQRAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 412 GKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
263-479 |
1.27e-13 |
|
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: 69.91 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN----RKGVLNNVSFKAYEGeVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKValengiall 338
Cdd:cd03264 1 LQLENLTkrygKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 tedRKEQGlFLKQSVKFniaSSNLKKYRengFLNLQ---------EQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKV 409
Cdd:cd03264 71 ---RRRIG-YLPQEFGV---YPNFTVRE---FLDYIawlkgipskEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 410 VIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKkgNTVIMISSELPE-ILNMSDRILVVHEGKIT 479
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-225 |
1.34e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFP-----------GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLeD 71
Cdd:PRK10261 311 EPILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI-D 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 72 NDPQKALEQL--GITPIYQE--LNLIPQLDVTENIFmgrekSKNEILGWIDRERMEEETKKILSRLGqesISPNDLIR-- 145
Cdd:PRK10261 390 TLSPGKLQALrrDIQFIFQDpyASLDPRQTVGDSIM-----EPLRVHGLLPGKAAAARVAWLLERVG---LLPEHAWRyp 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 146 -DLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK10261 462 hEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
..
gi 433671570 224 YI 225
Cdd:PRK10261 542 IV 543
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
273-478 |
1.45e-13 |
|
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: 70.34 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHG---KKVKIDSpkvaLENGIALLTEDRKeqgLFl 349
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDS----LRRAIGVVPQDTV---LF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 KQSVKFNIASSNLKKYREngflnlqEQRKDAIR-MVDNLNIKTPN-----VQTKCLQLSGGNQQKVVIGKWLNTEANIFI 423
Cdd:cd03253 88 NDTIGYNIRYGRPDATDE-------EVIEAAKAaQIHDKIMRFPDgydtiVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 424 FDEPTRGIDVGAKVEVFNIINDlVKKGNTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRD-VSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-225 |
1.98e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.51 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEF---PGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLG 82
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ItpIYQEL-NLIPQLDVTENIFMGREKSKneilgwIDRERMEEETKKILSRLGQESISPNDLIRdLGVGKQQMVEISKAL 161
Cdd:PRK13642 85 M--VFQNPdNQFVGATVEDDVAFGMENQG------IPREEMIKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLK-KQGVTMIFISHKLDEVKKmADRVTVLRNGKYI 225
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
285-494 |
2.89e-13 |
|
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: 70.91 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 285 EVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKkVKIDSPKvalenGIALLTEDRK------EQGLFLKQSVKfnia 358
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-TLFDSRK-----GIFLPPEKRRigyvfqEARLFPHLSVR---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 359 sSNLKKYRENGFLNLQEQRKDAIrmVDNLNIKtPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVE 438
Cdd:TIGR02142 94 -GNLRYGMKRARPSERRISFERV--IELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 439 VFNIINDLVKKGNT-VIMISSELPEILNMSDRILVVHEGKITGRFNTDEASKEKIMS 494
Cdd:TIGR02142 170 ILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLP 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
273-479 |
3.72e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKidSPKVAlENGIalltedRKEQGLFLKQs 352
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVD-ERLI------RQEAGMVFQQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 vkFNI-----ASSNLkkyrenGFLNLQ---EQRKDAIRMVDNLNIKT---------PNvqtkclQLSGGNQQKVVIGKWL 415
Cdd:PRK09493 86 --FYLfphltALENV------MFGPLRvrgASKEEAEKQARELLAKVglaerahhyPS------ELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 416 NTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-229 |
4.11e-13 |
|
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: 68.21 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEF-PGV-RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:cd03369 7 IEVENLSVRYaPDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 tpiyqelnlIPQlDVTenIFMGREKSKneilgwIDRERMEEEtKKILSRLgqeSISPNDLirDLGVGKQQMVEISKALSV 163
Cdd:cd03369 87 ---------IPQ-DPT--LFSGTIRSN------LDPFDEYSD-EEIYGAL---RVSEGGL--NLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 164 ETKLLILDEPTSSLGKDETKELFDTMGTLkKQGVTMIFISHKLDEVKKMaDRVTVLRNGKYIITDR 229
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
274-478 |
4.17e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvalengIALLTEDRKEQGLFLkQSV 353
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKK------IKEVKRLRKEIGLVF-QFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 354 KFNIASSNLKKYRENGFLNLQEQRKDAIRMVDNL----NIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:PRK13645 100 EYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELlklvQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 433671570 430 GIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-219 |
5.50e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 ---TPiyqelnlipqldvtenIFMGREKSKNEILGWIDRERMEEEtKKILSRLGQESISPNDL---IRDLGVGKQQMVEI 157
Cdd:PRK10247 86 caqTP----------------TLFGDTVYDNLIFPWQIRNQQPDP-AIFLDDLERFALPDTILtknIAELSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 158 SKALSVETKLLILDEPTSSLGKDETKELFDTM-GTLKKQGVTMIFISHKLDEVKKmADRVTVL 219
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-225 |
5.83e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEG-----EIYIEGKKLED-NDPQKA 77
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNyRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 78 LEQLGItpIYQELNLIPqLDVTENIFMGREKSKneilgWIDRERMEEETKKILSRLGQESiSPNDLIRD----LGVGKQQ 153
Cdd:PRK14271 100 RRRVGM--LFQRPNPFP-MSIMDNVLAGVRAHK-----LVPRKEFRGVAQARLTEVGLWD-AVKDRLSDspfrLSGGQQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 154 MVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQgVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
271-476 |
6.63e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.74 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 271 KGVlNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKValengialLTEDRKE-QGLFL 349
Cdd:PRK15079 35 KAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDE--------WRAVRSDiQMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 KQSVKFN-------IASSNLKKYRENgfLNLQEQRKDAIRMVDNLNIkTPNVQTKC-LQLSGGNQQKVVIGKWLNTEANI 421
Cdd:PRK15079 106 DPLASLNprmtigeIIAEPLRTYHPK--LSRQEVKDRVKAMMLKVGL-LPNLINRYpHEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 422 FIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEG 476
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-223 |
6.92e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.75 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPG----VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP---TEGEIYIEGKKLEdNDPQ 75
Cdd:PRK09473 10 DALLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIL-NLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 76 KALEQL---GITPIYQE----LNliPQLDVTENIF--------MGREKSKNEILGWIDRERMEEETKKIlsrlgqeSISP 140
Cdd:PRK09473 89 KELNKLraeQISMIFQDpmtsLN--PYMRVGEQLMevlmlhkgMSKAEAFEESVRMLDAVKMPEARKRM-------KMYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 141 NDLirdlGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQ-GVTMIFISHKLDEVKKMADRVTVL 219
Cdd:PRK09473 160 HEF----SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 235
|
....
gi 433671570 220 RNGK 223
Cdd:PRK09473 236 YAGR 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-73 |
8.71e-13 |
|
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: 70.60 E-value: 8.71e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 433671570 24 VDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDND 73
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN 400
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
269-489 |
9.04e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.46 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 269 NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKD---SGDIYVHGKKvkIDSPKVALENG--------IAL 337
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMP--IDAKEMRAISAyvqqddlfIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDrkEQGLFlkqSVKFNIASSNLKKYRengflnlQEQRKDAIRMVD-----NLNIKTPNvQTKclQLSGGNQQKVVIG 412
Cdd:TIGR00955 114 LTVR--EHLMF---QAHLRMPRRVTKKEK-------RERVDEVLQALGlrkcaNTRIGVPG-RVK--GLSGGERKRLAFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 413 KWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMI----SSELPEILnmsDRILVVHEGKITGRFNTDEAS 488
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGRVAYLGSPDQAV 255
|
.
gi 433671570 489 K 489
Cdd:TIGR00955 256 P 256
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
273-478 |
1.01e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.52 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVkidspkVALEN-GIALLtedRKEQGLFLKQ 351
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV------ATLDAdALAQL---RREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 svKFNI-----ASSNLKKYRENGFLNLQEQRKDAIRMVDNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDE 426
Cdd:PRK10535 94 --RYHLlshltAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED-RVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 433671570 427 PTRGIDVGAKVEVFNIINDLVKKGNTVIMISSElPEILNMSDRILVVHEGKI 478
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-233 |
1.10e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 17 GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLedndpQKALEQ--LGITPIYQELNLIP 94
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-----RQALQKnlVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 95 QLDVTENIFMGREKSkneiLGWIDR--ERMEEETKKILSRLGQESISPNDlIRDLGVGKQQMVEISKALSVETKLLILDE 172
Cdd:PRK15056 94 PVLVEDVVMMGRYGH----MGWLRRakKRDRQIVTAALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 173 PTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMAD-----RVTVLRNGKYIITDRVDNL 233
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDytvmvKGTVLASGPTETTFTAENL 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
263-486 |
1.25e-12 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 67.21 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAI-----VGADSKDSGDIYVHGKKVKIDSPKValen 333
Cdd:cd03260 1 IELRDLNVyygdKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 334 giallTEDRKEQGLFLKQ------SVKFNIASSnLKKYRENGFLNLQEQRKDAIRMV---DNLNIKTpnvqtKCLQLSGG 404
Cdd:cd03260 77 -----LELRRRVGMVFQKpnpfpgSIYDNVAYG-LRLHGIKLKEELDERVEEALRKAalwDEVKDRL-----HALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 405 NQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNT 484
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
..
gi 433671570 485 DE 486
Cdd:cd03260 225 EQ 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
273-478 |
1.31e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.18 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSP---KVALENGIALLTEDRKEQGLFL 349
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTVGIVFQNPDDQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 KQSVKFniASSNLKKYRENgflnLQEQRKDAIRMVDNLNI--KTPNvqtkclQLSGGNQQKVVIGKWLNTEANIFIFDEP 427
Cdd:PRK13639 97 EEDVAF--GPLNLGLSKEE----VEKRVKEALKAVGMEGFenKPPH------HLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 433671570 428 TRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-236 |
1.77e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 27 EIKRGEVHAILGENGAGKSTLIKVLTGVhTPTEGEIYIEGKKLEDNDP-----QKA-LEQ----LGITPIYQELNL-IPQ 95
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelarHRAyLSQqqtpPFAMPVFQYLTLhQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 96 LDVTENIfmgrEKSKNEIlgwIDRERMeeeTKKILSRLGQesispndlirdLGVGKQQMV-------EISKALSVETKLL 168
Cdd:PRK03695 97 KTRTEAV----ASALNEV---AEALGL---DDKLGRSVNQ-----------LSGGEWQRVrlaavvlQVWPDINPAGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 169 ILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDN-LTED 236
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvLTPE 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
262-486 |
1.78e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLNR--KG--VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIAL 337
Cdd:PRK10895 3 TLTAKNLAKayKGrrVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEdrkEQGLFLKQSVKFNIASsnLKKYRENgfLNlQEQRKD-AIRMVDNLNIKtpNVQTKCLQ-LSGGNQQKVVIGKWL 415
Cdd:PRK10895 83 LPQ---EASIFRRLSVYDNLMA--VLQIRDD--LS-AEQREDrANELMEEFHIE--HLRDSMGQsLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 416 NTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDE 486
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
273-478 |
2.85e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDI---YVHGK-KVKIDSPKVALENGIALLTEDRK----- 343
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKnKKKTKEKEKVLEKLVIQKTRFKKikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 344 -------------EQGLFlKQSVKFNIA----SSNLKKyrengflnlQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQ 406
Cdd:PRK13651 102 eirrrvgvvfqfaEYQLF-EQTIEKDIIfgpvSMGVSK---------EEAKKRAAKYIELVGLDESYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 407 QKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
269-479 |
3.34e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 65.03 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 269 NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKidSPKVALENGIALLTedrkeQGLF 348
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLISVLN-----QRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 349 LkqsvkFNiassnlkkyrengflnlqeqrkDAIRmvDNLNIktpnvqtkclQLSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:cd03247 86 L-----FD----------------------TTLR--NNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 433671570 429 RGIDVGAKVEVFNIINDlVKKGNTVIMISSELPEILNMsDRILVVHEGKIT 479
Cdd:cd03247 127 VGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
273-479 |
3.63e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.94 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvALENGIALLTEDrkeqglflkQS 352
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVASVPQD---------TS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIassNLKKYRENG-------FLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFD 425
Cdd:PRK09536 88 LSFEF---DVRQVVEMGrtphrsrFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 433671570 426 EPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-433 |
3.75e-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: 68.42 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRA-LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEiyiegkkledndpqkALEQLGITPI 86
Cdd:TIGR03719 7 MNRVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE---------------ARPQPGIKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 87 Y--QELNLIPQLDVTENIFMGREksknEILGWIDR-----ERMEEET---KKILSRLG--QESISPNDL----------- 143
Cdd:TIGR03719 72 YlpQEPQLDPTKTVRENVEEGVA----EIKDALDRfneisAKYAEPDadfDKLAAEQAelQEIIDAADAwdldsqleiam 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 144 -----------IRDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETK--ELFdtmgtLKKQGVTMIFISHK---LD 207
Cdd:TIGR03719 148 dalrcppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlERH-----LQEYPGTVVAVTHDryfLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 208 EVkkmADRVTVLRNGKYI------------ITDRVDNltEDK------------------------------MISY--MV 243
Cdd:TIGR03719 223 NV---AGWILELDRGRGIpwegnysswleqKQKRLEQ--EEKeesarqktlkrelewvrqspkgrqakskarLARYeeLL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 244 GEDVD--NKFPKMKVEP----GKESLRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSG 313
Cdd:TIGR03719 298 SQEFQkrNETAEIYIPPgprlGDKVIEAENLTKafgdKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 314 DIYVhGKKVKI---DSPKVALENGIALLTEdrKEQGLFLKQSVKFNIASsnlKKYrengflnlqeqrkdairmVDNLNIK 390
Cdd:TIGR03719 378 TIEI-GETVKLayvDQSRDALDPNKTVWEE--ISGGLDIIKLGKREIPS---RAY------------------VGRFNFK 433
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 433671570 391 TPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDV 433
Cdd:TIGR03719 434 GSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
274-478 |
3.79e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 66.70 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSpkvalengialLTEDRKEQGL------ 347
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN-----------FEKLRKHIGIvfqnpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 348 --FLKQSVKFNIA---SSNLKKYREngflnLQEQRKDAIRMVDNLNIKTPNVQTkclqLSGGNQQKVVIGKWLNTEANIF 422
Cdd:PRK13648 94 nqFVGSIVKYDVAfglENHAVPYDE-----MHRRVSEALKQVDMLERADYEPNA----LSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 423 IFDEPTRGIDVGAKVEVFNIINDL-VKKGNTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
286-479 |
3.88e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.59 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 286 VLGIAGLVGAGRTEIARAIVGADSKDSGDIyVHGKKVKIDSpkvalENGIALLTEDRK------EQGLFLKQSVKFNIas 359
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRVLFDA-----EKGICLPPEKRRigyvfqDARLFPHYKVRGNL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 360 snlkKYrenGFLNLQEQRKDAIrmVDNLNIKT-----PnvqtkcLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVG 434
Cdd:PRK11144 98 ----RY---GMAKSMVAQFDKI--VALLGIEPlldryP------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 433671570 435 AKVEVFNIINDLVKKGNTVIM-ISSELPEILNMSDRILVVHEGKIT 479
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILyVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
262-478 |
4.19e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKvkIDSPKVALENGIAL 337
Cdd:PRK11124 2 SIQLNGINCfygaHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH--FDFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LtedRKEQGLFLKQ-------SVKFNIASSNLKKYRengfLNLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVV 410
Cdd:PRK11124 80 L---RRNVGMVFQQynlwphlTVQQNLIEAPCRVLG----LSKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 411 IGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-180 |
4.77e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.07 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLED--NDPQKALEQLGI 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyqelNLIPQLDVTENI-FMgrekskNEILGwiDRERMEEETkkiLSRLGQESISpNDLIRDLGVGKQQMVEISKALS 162
Cdd:TIGR01189 81 LP-----GLKPELSALENLhFW------AAIHG--GAQRTIEDA---LAAVGLTGFE-DLPAAQLSAGQQRRLALARLWL 143
|
170
....*....|....*...
gi 433671570 163 VETKLLILDEPTSSLGKD 180
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKA 161
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-223 |
5.35e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEF-PGVRALDGVDLEI-KRGEVhAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQkALEQlGITP 85
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVpSRGFV-ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQ-GVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNLIPQlDVTENIFMGREKSKNEILGWIDRERMEEETKK----ILSRLGQESispndliRDLGVGKQQMVEISKAL 161
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGRDISEEQVWQALETVQLAELARSlpdgLYTPLGEQG-------NNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQgVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQ 551
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
271-478 |
5.59e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.28 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 271 KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPkvalengialltEDR------KE 344
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA------------ENRhvntvfQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 345 QGLFLKQSVKFNIASS-NLKKYrenGFLNLQEQRKDAIRMV--DNLniktpnVQTKCLQLSGGNQQKVVIGKWLNTEANI 421
Cdd:PRK09452 95 YALFPHMTVFENVAFGlRMQKT---PAAEITPRVMEALRMVqlEEF------AQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 422 FIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
273-485 |
6.78e-12 |
|
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: 64.80 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALengiaLLTEDRkeqgLFLKQS 352
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGY-----VFQQDA----LLPWLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIA---SSNLKKYREngflnLQEQRKDAIRMV---DNLNiKTPNvqtkclQLSGGNQQKVVIGKWLNTEANIFIFDE 426
Cdd:cd03293 90 VLDNVAlglELQGVPKAE-----ARERAEELLELVglsGFEN-AYPH------QLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 427 PTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVV--HEGKITGRFNTD 485
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-214 |
6.96e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.57 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVH--TPT---EGEIYIEGKKLEDN--DPQKAL 78
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGfrvEGKVTFHGKNLYAPdvDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 79 EQLGItpIYQELNLIPQlDVTENIFMGREkskneILGWidRERMEEETKKILSR--LGQESispNDLIRDLGV----GKQ 152
Cdd:PRK14243 91 RRIGM--VFQKPNPFPK-SIYDNIAYGAR-----INGY--KGDMDELVERSLRQaaLWDEV---KDKLKQSGLslsgGQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 153 QMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQgVTMIFISHKLDEVKKMAD 214
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
252-477 |
9.73e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 252 PKMKVEPGKESLRVENLN--------RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVK 323
Cdd:PRK10261 2 PHSDELDARDVLAVENLNiafmqeqqKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 324 IDSPKValengIALLTEDRKEQglflkQSVK------------------FNIASSNLKKYRENGFLNLQEQRKDAIRMVD 385
Cdd:PRK10261 82 RRSRQV-----IELSEQSAAQM-----RHVRgadmamifqepmtslnpvFTVGEQIAESIRLHQGASREEAMVEAKRMLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 386 NLNIktPNVQTKCL----QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNT-VIMISSEL 460
Cdd:PRK10261 152 QVRI--PEAQTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDM 229
|
250
....*....|....*..
gi 433671570 461 PEILNMSDRILVVHEGK 477
Cdd:PRK10261 230 GVVAEIADRVLVMYQGE 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
275-477 |
1.24e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 275 NNVSFKAYEGEVLGIAGLVGAGRTEIARAIVG---ADSKDSGDIYVHGKKVkIDSPKVALeNGIalltedRKEQglflkQ 351
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREI-LNLPEKEL-NKL------RAEQ-----I 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIASSNLKKYRENG-----------FLNLQEQRKDAIRMVDNlnIKTPNVQTKCL----QLSGGNQQKVVIGKWLN 416
Cdd:PRK09473 100 SMIFQDPMTSLNPYMRVGeqlmevlmlhkGMSKAEAFEESVRMLDA--VKMPEARKRMKmyphEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 417 TEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNT-VIMISSELPEILNMSDRILVVHEGK 477
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
246-478 |
1.38e-11 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 66.78 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 246 DVDNKFPKMKVEPGKESLRVENL------NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHG 319
Cdd:COG2274 457 EREEGRSKLSLPRLKGDIELENVsfrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 320 KKVKIDSPKvALENGIALLTEDrkeqGLFLKQSVKFNIASSNLKkyrengfLNLQEQRKdAIRM------VDNLniktPN 393
Cdd:COG2274 537 IDLRQIDPA-SLRRQIGVVLQD----VFLFSGTIRENITLGDPD-------ATDEEIIE-AARLaglhdfIEAL----PM 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 394 -----VQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELpEILNMSD 468
Cdd:COG2274 600 gydtvVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRL-STIRLAD 677
|
250
....*....|
gi 433671570 469 RILVVHEGKI 478
Cdd:COG2274 678 RIIVLDKGRI 687
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
274-478 |
1.45e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 63.97 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDSPKVA-LENGIALLTEDRKeqgLFLKQ 351
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIPyLRRKIGVVFQDFR---LLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIASS---NLKKYREngflnLQEQRKDAIRMVDnLNIKTpnvQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:cd03292 94 NVYENVAFAlevTGVPPRE-----IRKRVPAALELVG-LSHKH---RALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 433671570 429 RGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
273-478 |
1.46e-11 |
|
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: 64.15 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVaLENGIALLTEDrkeQGLFlKQS 352
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQD---VTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIASSNLkkyrengflNLQEQR-KDAIRM--VDNLNIKTPN-----VQTKCLQLSGGNQQKVVIGKWLNTEANIFIF 424
Cdd:cd03245 94 LRDNITLGAP---------LADDERiLRAAELagVTDFVNKHPNgldlqIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 433671570 425 DEPTRGIDVGAKVEVFNIINDLVkKGNTVIMISSELPeILNMSDRILVVHEGKI 478
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-204 |
1.47e-11 |
|
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: 63.67 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDP--QKALEQLGI 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsiARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPIYQELnlipqLDVTENI-FMGREKSKNEILGWIDRERMEeetkkilsrlGQESISPNdlirDLGVGKQQMVEISKALS 162
Cdd:cd03231 81 APGIKTT-----LSVLENLrFWHADHSDEQVEEALARVGLN----------GFEDRPVA----QLSAGQQRRVALARLLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 433671570 163 VETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISH 204
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
266-478 |
1.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 266 ENLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALEN--GIALLTEDRK 343
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNkaGMVFQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 344 EQGLFLKQSVKFN-----IASSNLKKYRENGF--LNLQEQRKDAIRMvdnlniktpnvqtkclqLSGGNQQKVVIGKWLN 416
Cdd:PRK13633 98 IVATIVEEDVAFGpenlgIPPEEIRERVDESLkkVGMYEYRRHAPHL-----------------LSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 417 TEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
271-477 |
2.09e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.24 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 271 KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGkkVKIDSPKVALENGIALLTE-DRKEQGLFL 349
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARARIGVVPQfDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 KQsvkfniassNLKKYRENGFLNLQEQRKDAIRMVDNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:PRK13536 132 RE---------NLLVFGRYFGMSTREIEAVIPSLLEFARLES-KADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 433671570 430 GIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGK 477
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
269-486 |
2.17e-11 |
|
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: 63.78 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 269 NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKiDSPKVALENGIALLTEDrkeQGLF 348
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQD---TFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 349 lKQSVKFNIASSNLKKYREngflnlQEQRKDAIRMVDNLNIKTPN-----VQTKCLQLSGGNQQKVVIGKWLNTEANIFI 423
Cdd:cd03254 90 -SGTIMENIRLGRPNATDE------EVIEAAKEAGAHDFIMKLPNgydtvLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 424 FDEPTRGIDVGAKVEVFNIInDLVKKGNTVIMISSELPEILNmSDRILVVHEGKITGRFNTDE 486
Cdd:cd03254 163 LDEATSNIDTETEKLIQEAL-EKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
274-478 |
2.33e-11 |
|
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: 64.20 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvalengiALLTEDRKE-----Q--G 346
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRK-------ELRELRRKKismvfQsfA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 347 LFLKQSVKFNIASSnlkkyRENGFLNLQEQRKDAIRMVDNLNIKtPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDE 426
Cdd:cd03294 113 LLPHRTVLENVAFG-----LEVQGVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 433671570 427 PTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-186 |
2.40e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGitp 85
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 iyqELN-LIPQLDVTENIFMGReksknEILGwiDRERMEEETkkiLSRLGQESISpnDL-IRDLGVGKQQMVEISKALSV 163
Cdd:PRK13539 80 ---HRNaMKPALTVAENLEFWA-----AFLG--GEELDIAAA---LEAVGLAPLA--HLpFGYLSAGQKRRVALARLLVS 144
|
170 180
....*....|....*....|...
gi 433671570 164 ETKLLILDEPTSSLGKDeTKELF 186
Cdd:PRK13539 145 NRPIWILDEPTAALDAA-AVALF 166
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-211 |
2.49e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 2 IEPFLKIKNLTKEFPGV-----------------------RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVH--T 56
Cdd:COG2401 4 YNPFFVLMRVTKVYSSVldlservaivleafgvelrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 57 PTEGEIyiegkKLEDNdpqkaleqlgitPIYQELNLIPQLdvtenifmGREKSKNeilgwidrermeeETKKILSRLGqe 136
Cdd:COG2401 84 PVAGCV-----DVPDN------------QFGREASLIDAI--------GRKGDFK-------------DAVELLNAVG-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 137 sISPNDLIR----DLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKlDEVKK 211
Cdd:COG2401 124 -LSDAVLWLrrfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHH-YDVID 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-229 |
3.26e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.63 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 22 DGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGkkleDNDPQKALEQL-----GITPIYQELNLIPQL 96
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG----ENIPAMSRSRLytvrkRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 97 DVTENI-FMGREKSK--NEILGWIDRERMEEetkkiLSRLGQESISPNdlirDLGVGKQQMVEISKALSVETKLLILDEP 173
Cdd:PRK11831 100 NVFDNVaYPLREHTQlpAPLLHSTVMMKLEA-----VGLRGAAKLMPS----ELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 174 TssLGKDETkelfdTMGTLKK--------QGVTMIFISHKLDEVKKMADRVtvlrngkYIITDR 229
Cdd:PRK11831 171 F--VGQDPI-----TMGVLVKliselnsaLGVTCVVVSHDVPEVLSIADHA-------YIVADK 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-225 |
3.67e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.43 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPG--VRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 tpIYQELNLIPQlDVTENIFMGREK--SKNEI---------LGWIdrERMEEETKKIlsrLGQESISpndlirdLGVGKQ 152
Cdd:PRK11176 422 --VSQNVHLFND-TIANNIAYARTEqySREQIeeaarmayaMDFI--NKMDNGLDTV---IGENGVL-------LSGGQR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 153 QMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGvTMIFISHKLDEVKKmADRVTVLRNGKYI 225
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
273-478 |
3.68e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.87 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKvkIDSPK---VALENGIALLTEDRKEQGLFl 349
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP--LDYSKrglLALRQQVATVFQDPEQQIFY- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 kQSVKFNIASSnlkkYRENGFLNLQEQRK--DAIRMVDNLNIKTPNVQtkCLqlSGGNQQKVVIGKWLNTEANIFIFDEP 427
Cdd:PRK13638 93 -TDIDSDIAFS----LRNLGVPEAEITRRvdEALTLVDAQHFRHQPIQ--CL--SHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 433671570 428 TRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
271-486 |
4.04e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 271 KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVkidspkvALENgialLTEDRKEQGLFLk 350
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-------TKEN----IREVRKFVGLVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 351 QSVKFNIASSNLKKYRENGFLNL-------QEQRKDAIRMV--DNLNIKTPNvqtkclQLSGGNQQKVVIGKWLNTEANI 421
Cdd:PRK13652 85 QNPDDQIFSPTVEQDIAFGPINLgldeetvAHRVSSALHMLglEELRDRVPH------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 422 FIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDE 486
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
273-479 |
4.41e-11 |
|
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: 62.74 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALlteDRKEQ---GLFL 349
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF---GQKTQlwwDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 KQSVKFNIASSNLKKYRengflnlqeQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:cd03267 113 IDSFYLLAAIYDLPPAR---------FKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 433671570 430 GIDVGAKVEVFNIINDLVK-KGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
263-477 |
4.60e-11 |
|
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: 62.11 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALEngIALL 338
Cdd:COG4133 3 LEAENLscrrGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDrkeQGLFLKQSVkfniassnlkkyREN-----GFLNLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVIGK 413
Cdd:COG4133 81 GHA---DGLKPELTV------------RENlrfwaALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 414 -WLnTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNmsDRILVVHEGK 477
Cdd:COG4133 145 lLL-SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDLGDFK 206
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-246 |
5.53e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.35 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDndpqkaleqLGITPIYQELNLIPQLDVte 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK---------IGLHDLRFKITIIPQDPV-- 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 101 nIFMGR---------EKSKNEILGWIDRERMEEETKKILSRLGQESISPNDlirDLGVGKQQMVEISKALSVETKLLILD 171
Cdd:TIGR00957 1371 -LFSGSlrmnldpfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE---NLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 172 EPTSSLGKdETKELFDTMGTLKKQGVTMIFISHKLDEVKKMAdRVTVLRNGKYIITDRVDNLTEDKMISYMVGED 246
Cdd:TIGR00957 1447 EATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKD 1519
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
265-478 |
6.28e-11 |
|
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: 62.00 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 265 VENLNRK----GVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKValENGIALLTE 340
Cdd:cd03265 3 VENLVKKygdfEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV--RRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 341 DRK-EQGLFLKQSVKFNIASSNLKKYRengflnLQEQRKDAIRMVDNLNIKTPNVQTkclqLSGGNQQKVVIGKWLNTEA 419
Cdd:cd03265 81 DLSvDDELTGWENLYIHARLYGVPGAE------RRERIDELLDFVGLLEAADRLVKT----YSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 420 NIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSE-LPEILNMSDRILVVHEGKI 478
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHyMEEAEQLCDRVAIIDHGRI 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
263-496 |
6.38e-11 |
|
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: 64.44 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNRK----GVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADS--KDSGDIYVH----------------GK 320
Cdd:TIGR03269 1 IEVKNLTKKfdgkEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 321 KVKIDSPKVALENgIALLTEDRKEQGLFLKQS---VKFNIASSNLKKYRENGFLNLQE---QRKDAIRMVDNLnIKTPNV 394
Cdd:TIGR03269 81 PCPVCGGTLEPEE-VDFWNLSDKLRRRIRKRIaimLQRTFALYGDDTVLDNVLEALEEigyEGKEAVGRAVDL-IEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 395 QTKCLQ----LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEIL-NMSDR 469
Cdd:TIGR03269 159 SHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIeDLSDK 238
|
250 260
....*....|....*....|....*..
gi 433671570 470 ILVVHEGKITGRFNTDEASkEKIMSAA 496
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVV-AVFMEGV 264
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-223 |
6.48e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 61.72 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLT-----KEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKkledndpqkaleq 80
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGITPiyQElNLIPQLDVTENIFMGREkskneilgwIDRERMEEETK--------KILS-----RLGQESISpndlirdL 147
Cdd:cd03250 68 IAYVS--QE-PWIQNGTIRENILFGKP---------FDEERYEKVIKacalepdlEILPdgdltEIGEKGIN-------L 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 148 GVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDT--MGTLKKqGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
269-478 |
7.16e-11 |
|
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: 62.32 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 269 NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPkVALENGIALLTEdrkEQGLF 348
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGYVIQ---QIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 349 LKQSVKFNIAS-SNLKKYRENgflNLQEQRKDAIRMVD----NLNIKTPNvqtkclQLSGGNQQKVVIGKWLNTEANIFI 423
Cdd:cd03295 88 PHMTVEENIALvPKLLKWPKE---KIRERADELLALVGldpaEFADRYPH------ELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 424 FDEPTRGIDV---GAKVEVFNIINDLVKKgnTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:cd03295 159 MDEPFGALDPitrDQLQEEFKRLQQELGK--TIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
258-478 |
9.03e-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: 61.27 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 258 PGKESLRVENL------NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKiDSPKVAL 331
Cdd:cd03369 2 PEHGEIEVENLsvryapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 332 ENGIALLTEDrkeqGLFLKQSVKfniasSNLKKYRENGflnlQEQRKDAIRmvdnlniktpnVQTKCLQLSGGNQQKVVI 411
Cdd:cd03369 81 RSSLTIIPQD----PTLFSGTIR-----SNLDPFDEYS----DEEIYGALR-----------VSEGGLNLSQGQRQLLCL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 412 GKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVkKGNTVIMISSELPEILNMsDRILVVHEGKI 478
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-222 |
1.06e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 19 RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPT--------EGEIYIEGKKLEDNDPQKALEQLGITPiyQEL 90
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLP--QAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 91 NLIPQLDVTENIFMGREKSKNEILGWIDRERmeEETKKILSRLGQESISPNDlIRDLGVGKQQMVEISKALS-------- 162
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARRAGALTHRDG--EIAWQALALAGATALVGRD-VTTLSGGELARVQFARVLAqlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 163 -VETKLLILDEPTSSLGKDETKELFDTMGTLKKQ---GVtmIFISHKLDEVKKMADRVTVLRNG 222
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlGV--LAIVHDPNLAARHADRIAMLADG 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
273-478 |
1.08e-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: 61.86 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHG---KKVKIDSpkvaLENGIALLTEDrkeqgLFL 349
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLAS----LRRQIGLVSQD-----VFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 -KQSVKFNIASSNLKKYREngflnlqeQRKDAIRMV--DNLNIKTPN-VQTKC----LQLSGGNQQKVVIGKWLNTEANI 421
Cdd:cd03251 88 fNDTVAENIAYGRPGATRE--------EVEEAARAAnaHEFIMELPEgYDTVIgergVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 422 FIFDEPTRGIDVGAKVEVFNIINDLVkKGNTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
274-476 |
1.83e-10 |
|
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: 60.94 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPK--VALENgialltedrkeQGLFLKQ 351
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmVVFQN-----------YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIAssnLKKYRENGFLNLQEQRK---DAIRMVdNLnikTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:TIGR01184 70 TVRENIA---LAVDRVLPDLSKSERRAiveEHIALV-GL---TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 433671570 429 RGIDVGAK----VEVFNIINDlvkKGNTVIMISSELPEILNMSDRILVVHEG 476
Cdd:TIGR01184 143 GALDALTRgnlqEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
263-478 |
1.84e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.20 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDSPKVALEnGIAL 337
Cdd:COG1137 4 LEAENLvksyGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDItHLPMHKRARL-GIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEdrkEQGLFLKQSVKFNIASsnlkkYRENGFLNLQEQRKDAIRMVDNLNIkTPNVQTKCLQLSGGNQQKVVIGKWLNT 417
Cdd:COG1137 83 LPQ---EASIFRKLTVEDNILA-----VLELRKLSKKEREERLEELLEEFGI-THLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 418 EANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
263-478 |
2.18e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.65 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNRK-------GVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGdiyvhgkKVKIDSPKVALEN-- 333
Cdd:PRK13642 5 LEVENLVFKyekesdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-------KVKIDGELLTAENvw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 334 ------GIALLTEDRKEQGLFLKQSVKFNIASSNLKKYRengflnLQEQRKDAIRMVDNLNIKTpnvqTKCLQLSGGNQQ 407
Cdd:PRK13642 78 nlrrkiGMVFQNPDNQFVGATVEDDVAFGMENQGIPREE------MIKRVDEALLAVNMLDFKT----REPARLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 408 KVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-210 |
2.50e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 20 ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKledndpqkaleqlGITPIYQELNliPQLDVT 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------------ALIAISSGLN--GQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 100 ENIFMgreksKNEILGwIDRERMEEETKKIL--SRLGQESISPndlIRDLGVGKQQMVEISKALSVETKLLILDEPTSSL 177
Cdd:PRK13545 104 ENIEL-----KGLMMG-LTKEKIKEIIPEIIefADIGKFIYQP---VKTYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190
....*....|....*....|....*....|...
gi 433671570 178 GKDETKELFDTMGTLKKQGVTMIFISHKLDEVK 210
Cdd:PRK13545 175 DQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVK 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-223 |
2.86e-10 |
|
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: 62.53 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNdPQKAL-EQLGITP---------IYqel 90
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV-TQASLrAAIGIVPqdtvlfndtIA--- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 91 nlipqldvtENIFMGREKSkneilgwiDRERMEEETKkiLSRLGqesispnDLIRDL-----------GV----GKQQMV 155
Cdd:COG5265 450 ---------YNIAYGRPDA--------SEEEVEAAAR--AAQIH-------DFIESLpdgydtrvgerGLklsgGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 156 EISKALSVETKLLILDEPTSSLgkdetkelfDT------MGTLKK--QGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSAL---------DSrteraiQAALREvaRGRTTLVIAHRLSTIVD-ADEILVLEAGR 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
273-478 |
2.89e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 62.83 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKiDSPKVALENGIALLTEDRkeqgLFLKQS 352
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK-DIDRHTLRQFINYLPQEP----YIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNI---ASSNLKKYRENGFLNLQEQRKDAIRMvdNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:TIGR01193 564 ILENLllgAKENVSQDEIWAACEIAEIKDDIENM--PLGYQT-ELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 433671570 430 GIDVgakVEVFNIINDLVK-KGNTVIMISSELpEILNMSDRILVVHEGKI 478
Cdd:TIGR01193 641 NLDT---ITEKKIVNNLLNlQDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-177 |
3.07e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.50 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 27 EIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdNDPQKaleqlgitpiyqelnLIPQLDVTENIFMgr 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQY---------------IKADYEGTVRDLL-- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 107 eKSKNEILGWIDRERMEeetkkILSRLGQESISPNDLiRDLGVGKQQMVEISKALSVETKLLILDEPTSSL 177
Cdd:cd03237 83 -SSITKDFYTHPYFKTE-----IAKPLQIEQILDREV-PELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
256-478 |
3.10e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.83 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 256 VEPGKESLRVENLNR-------KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARA------IVGADSKDSGDIYVHGKKV 322
Cdd:PRK14246 1 MEAGKSAEDVFNISRlylyindKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 323 -KIDSPKVALENGIaLLTEDRKEQGLFLKQSVKFNIASSNLKKYREngflnLQEQRKDAIRMVDNLNIKTPNVQTKCLQL 401
Cdd:PRK14246 81 fQIDAIKLRKEVGM-VFQQPNPFPHLSIYDNIAYPLKSHGIKEKRE-----IKKIVEECLRKVGLWKEVYDRLNSPASQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 402 SGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-204 |
3.39e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 5 FLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQ--KALEQLG 82
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 ITP-IYQELNlipqldVTENI-FMGRekskneILGWIDRERMEEetkkILSR---LGQESIspndLIRDLGVGKQQMVEI 157
Cdd:PRK13538 81 HQPgIKTELT------ALENLrFYQR------LHGPGDDEALWE----ALAQvglAGFEDV----PVRQLSAGQQRRVAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 433671570 158 SKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISH 204
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-243 |
3.45e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 14 EFPGVraLDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdndpqkaleQLGITPIYQELNLI 93
Cdd:PLN03130 1250 ELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS---------KFGLMDLRKVLGII 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 94 PQLDVtenIFMG---------REKSKNEILGWIDRERMEEETKKILSRLGQESISPNDlirDLGVGKQQMVEISKALSVE 164
Cdd:PLN03130 1319 PQAPV---LFSGtvrfnldpfNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGE---NFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 165 TKLLILDEPTSS-------LGKDETKELFDTmgtlkkqgVTMIFISHKLDEVKKmADRVTVLRNGKYIITDRVDNL--TE 235
Cdd:PLN03130 1393 SKILVLDEATAAvdvrtdaLIQKTIREEFKS--------CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLlsNE 1463
|
....*...
gi 433671570 236 DKMISYMV 243
Cdd:PLN03130 1464 GSAFSKMV 1471
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
267-471 |
3.45e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 267 NLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIyVHGKKVKID--SPKVALENGIALLTEdrke 344
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKLRIGyvPQKLYLDTTLPLTVN---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 345 QGLFLKQSVKFNIASSNLKKYRENGFLNLQEQRkdairmvdnlniktpnvqtkclqLSGGNQQKVVIGKWLNTEANIFIF 424
Cdd:PRK09544 88 RFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------------------LSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 433671570 425 DEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRIL 471
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVL 192
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
274-478 |
3.45e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.77 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIALLTEDRKEQglFLKQSV 353
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQ--FVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 354 KFNIASSNlkkyrENGFLNLQEQRKDAIRMVDNLNIKTPNVQTKcLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDV 433
Cdd:PRK13644 96 EEDLAFGP-----ENLCLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 433671570 434 GAKVEVFNIINDLVKKGNTVIMISSELPEiLNMSDRILVVHEGKI 478
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
270-478 |
3.66e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.97 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 270 RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVG---ADSKDSGDIYVHGKKVKIDSP-KVALENGIALLTEDRKEQ 345
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTAKTVwDIREKVGIVFQNPDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 346 GLFLKQSVKFNIassnlkkyrENGFLNLQEQRK---DAIRMVDNLNIKTPNVQtkclQLSGGNQQKVVIGKWLNTEANIF 422
Cdd:PRK13640 99 GATVGDDVAFGL---------ENRAVPRPEMIKivrDVLADVGMLDYIDSEPA----NLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 423 IFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEIlNMSDRILVVHEGKI 478
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-177 |
5.22e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRaLDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGK---KledndPQKale 79
Cdd:PRK13409 338 ETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisyK-----PQY--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 80 qlgITPIYqelnlipqlDVTENIFMgreKSKNEILG--WIDRErmeeetkkILSRLGQESISPNDLiRDLGVGKQQMVEI 157
Cdd:PRK13409 409 ---IKPDY---------DGTVEDLL---RSITDDLGssYYKSE--------IIKPLQLERLLDKNV-KDLSGGELQRVAI 464
|
170 180
....*....|....*....|
gi 433671570 158 SKALSVETKLLILDEPTSSL 177
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHL 484
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-306 |
6.21e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYiegkkledNDPQK----ALEQL 81
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ--------SQFSHitrlSFEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 G--ITPIYQELN---LIPQLDVTenifmGREKSKNEILGWIDRERMEEETKKilsrLGQESIspndLIRD---LGVGKQQ 153
Cdd:PRK10938 76 QklVSDEWQRNNtdmLSPGEDDT-----GRTTAEIIQDEVKDPARCEQLAQQ----FGITAL----LDRRfkyLSTGETR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 154 MVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 234 TEDKMISYMV-GEDVDN-KFPKMKVEPGKESL-----RVE------NLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEI 300
Cdd:PRK10938 223 LQQALVAQLAhSEQLEGvQLPEPDEPSARHALpanepRIVlnngvvSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTL 302
|
....*.
gi 433671570 301 ARAIVG 306
Cdd:PRK10938 303 LSLITG 308
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
262-479 |
7.84e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.67 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIvGADSKDSGDIYVHGKkVKIDSPKVaLENGIAL 337
Cdd:PRK14258 7 AIKVNNLsfyyDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGR-VEFFNQNI-YERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDRKEQGLFLK-----QSVKFNIA-SSNLKKYRENgfLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVI 411
Cdd:PRK14258 84 NRLRRQVSMVHPKpnlfpMSVYDNVAyGVKIVGWRPK--LEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 412 GKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVH--EGKIT 479
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKgnENRIG 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-177 |
8.51e-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: 60.95 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 1 MIEPFLKIKNLTKEFPGVRaLDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGK---KledndPQKa 77
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisyK-----PQY- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 78 leqlgITPIYQElnlipqlDVTENIfmgREKSKNEILG-WIdrermEEEtkkILSRLGQESISPNDLiRDLGVGKQQMVE 156
Cdd:COG1245 410 -----ISPDYDG-------TVEEFL---RSANTDDFGSsYY-----KTE---IIKPLGLEKLLDKNV-KDLSGGELQRVA 465
|
170 180
....*....|....*....|.
gi 433671570 157 ISKALSVETKLLILDEPTSSL 177
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHL 486
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-233 |
9.72e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.33 E-value: 9.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVrALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP----TEGEIYIEGKKLEDNDpqkaLEQL 81
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCA----LRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITPIYQE-------LNLIPQLDVTENIFMGREKSKNEILgwidrERME----EETKKILSRLGQEsispndlirdLGVG 150
Cdd:PRK10418 80 KIATIMQNprsafnpLHTMHTHARETCLALGKPADDATLT-----AALEavglENAARVLKLYPFE----------MSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 151 KQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDR 229
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
....
gi 433671570 230 VDNL 233
Cdd:PRK10418 225 VETL 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
274-479 |
1.36e-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: 61.11 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGdiyvhgkkvkidspKVALENGIALLTEDRKEQGLFLKQSV 353
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 354 KFNIASsNLKKYRengflnlqeQRKDAIRMVDNLNIKTPNVQT----KCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:TIGR00957 720 LFGKAL-NEKYYQ---------QVLEACALLPDLEILPSGDRTeigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 430 GIDVGAKVEVF-NIINDL-VKKGNTVIMIS---SELPEIlnmsDRILVVHEGKIT 479
Cdd:TIGR00957 790 AVDAHVGKHIFeHVIGPEgVLKNKTRILVThgiSYLPQV----DVIIVMSGGKIS 840
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
245-481 |
1.46e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 60.18 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 245 EDVDNKFPKMKVEPGKESLRVENL-----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHG 319
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVsfsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 320 KKVKiDSPKVALENGIALLTEDrkeQGLFlKQSVKFNI------ASsnlkkyrengflnlQEQRKDAIRM------VDNL 387
Cdd:COG1132 402 VDIR-DLTLESLRRQIGVVPQD---TFLF-SGTIRENIrygrpdAT--------------DEEVEEAAKAaqahefIEAL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 388 niktPN-----VQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKkGNTVIMISSELPE 462
Cdd:COG1132 463 ----PDgydtvVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLST 537
|
250
....*....|....*....
gi 433671570 463 ILNMsDRILVVHEGKITGR 481
Cdd:COG1132 538 IRNA-DRILVLDDGRIVEQ 555
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
401-471 |
2.92e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.18 E-value: 2.92e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 401 LSGGNQQKVVIGKWL--NTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSElPEILNMSDRIL 471
Cdd:cd03238 88 LSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWII 159
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
262-478 |
3.02e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.56 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKidspkvalengiAL 337
Cdd:PRK10851 2 SIEIANIKksfgRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS------------RL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDRK------EQGLFLKQSVKFNIAS--SNLKKyRENgfLNLQEQRKDAIRMVDnlniktpNVQTKCL------QLSG 403
Cdd:PRK10851 70 HARDRKvgfvfqHYALFRHMTVFDNIAFglTVLPR-RER--PNAAAIKAKVTQLLE-------MVQLAHLadrypaQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 404 GNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
247-477 |
3.20e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 247 VDNKFPKMKVEPGKES---LRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHG 319
Cdd:PRK11607 1 MNDAIPRPQAKTRKALtplLEIRNLTKsfdgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 320 KKVKIDSPkvaLENGIALLTEdrkEQGLFLKQSVKFNIA--------SSNLKKYRENGFLNLQEQRKDAIRmvdnlnikt 391
Cdd:PRK11607 81 VDLSHVPP---YQRPINMMFQ---SYALFPHMTVEQNIAfglkqdklPKAEIASRVNEMLGLVHMQEFAKR--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 392 pnvqtKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAK----VEVFNIindLVKKGNTVIMISSELPEILNMS 467
Cdd:PRK11607 146 -----KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdrmqLEVVDI---LERVGVTCVMVTHDQEEAMTMA 217
|
250
....*....|
gi 433671570 468 DRILVVHEGK 477
Cdd:PRK11607 218 GRIAIMNRGK 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-233 |
3.65e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.29 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 11 LTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP---TEGEIYIEGKKLeDNDPQKALEQLgitpIY 87
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI-DAKEMRAISAY----VQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 88 QELNLIPQLDVTEN-IFMGREKSKNEILGWIDRERMEEetkkILSRLGQES-----ISPNDLIRDLGVGKQQMVEISKAL 161
Cdd:TIGR00955 106 QDDLFIPTLTVREHlMFQAHLRMPRRVTKKEKRERVDE----VLQALGLRKcantrIGVPGRVKGLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 162 SVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHK-LDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
274-478 |
4.69e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGAdskdsgdiyvhgkkvkIDSP-KVALE----NGIALLTEDRKEQGLF 348
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL----------------IDYPgRVMAEklefNGQDLQRISEKERRNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 349 LKQSVK--FNIASSNLKKYRENGFL-----------NLQEQRKDAIRMVDNLNIKTPNVQTKCL--QLSGGNQQKVVIGK 413
Cdd:PRK11022 87 VGAEVAmiFQDPMTSLNPCYTVGFQimeaikvhqggNKKTRRQRAIDLLNQVGIPDPASRLDVYphQLSGGMSQRVMIAM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 414 WLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-233 |
5.31e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAG--KSTLIKVLTGvhtPTEGEIYIEGKKLEDNdpQKALEQ-LG 82
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCAN--RRALRRtIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 83 I-TPIyqELNLIPQLDVTENIFM-GREKSkneilgwIDRERMEEETKKILSRLGQESISPNDLIRDLGvGKQQMVEISKA 160
Cdd:NF000106 89 *hRPV--R*GRRESFSGRENLYMiGR*LD-------LSRKDARARADELLERFSLTEAAGRAAAKYSG-GMRRRLDLAAS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 161 LSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGKYIITDRVDNL 233
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
266-479 |
5.47e-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: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 266 ENLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGAdskdsgdiyvHGKKVKIdspkvalENGIALLTEDRKEQ 345
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR----------TEGNVSV-------EGDIHYNGIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 346 GLFLKQSVKFNIASSNLKKYrengfLNLQEQRKDAIRMVDNLNIKTpnvqtkclqLSGGNQQKVVIGKWLNTEANIFIFD 425
Cdd:cd03233 78 AEKYPGEIIYVSEEDVHFPT-----LTVRETLDFALRCKGNEFVRG---------ISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 426 EPTRGIDVGAKVEVFNIINDLVKKGNTVIMIS----SelPEILNMSDRILVVHEGKIT 479
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaS--DEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
268-480 |
5.69e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.42 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 268 LNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDSPKVA-LENGIALLTEDRKeq 345
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNREVPfLRRQIGMIFQDHH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 346 gLFLKQSVKFNI--------ASSNLKKYRENGFLnlqeqrkDAIRMVDnlniKTPNVQtkcLQLSGGNQQKVVIGKWLNT 417
Cdd:PRK10908 90 -LLMDRTVYDNVaipliiagASGDDIRRRVSAAL-------DKVGLLD----KAKNFP---IQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 418 EANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITG 480
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
271-477 |
6.52e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.12 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 271 KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVALENGIAL----LTEDRKEQG 346
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPqfdnLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 347 LFLKQSVKFNIASSNLKKyRENGFLNLQ--EQRKDAirmvdnlniktpnvqtKCLQLSGGNQQKVVIGKWLNTEANIFIF 424
Cdd:PRK13537 100 NLLVFGRYFGLSAAAARA-LVPPLLEFAklENKADA----------------KVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 433671570 425 DEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGK 477
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
371-478 |
7.03e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 371 LNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDL-VKK 449
Cdd:PRK13646 116 MNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDE 195
|
90 100
....*....|....*....|....*....
gi 433671570 450 GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13646 196 NKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
253-486 |
7.08e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 253 KMKVEPGKESLRVENLN------RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKiDS 326
Cdd:PRK11176 332 KRVIERAKGDIEFRNVTftypgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR-DY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 327 PKVALENGIALLTEDRKeqgLFlKQSVKFNIASSNLKKYRengflnlQEQRKDAIRMVDNLN--IKTPN-----VQTKCL 399
Cdd:PRK11176 411 TLASLRNQVALVSQNVH---LF-NDTIANNIAYARTEQYS-------REQIEEAARMAYAMDfiNKMDNgldtvIGENGV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 400 QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELPEILNmSDRILVVHEGKIT 479
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
....*..
gi 433671570 480 GRFNTDE 486
Cdd:PRK11176 558 ERGTHAE 564
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
270-478 |
7.46e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 270 RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKidspkvalengiALLTEDRKE----- 344
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA------------KLNRAQRKAfrrdi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 345 QGLFLKQSVKFNIASSNLKKYRE--NGFLNLQEQRKDA-----IRMVDnlniKTPNVQTKC-LQLSGGNQQKVVIGKWLN 416
Cdd:PRK10419 92 QMVFQDSISAVNPRKTVREIIREplRHLLSLDKAERLArasemLRAVD----LDDSVLDKRpPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 417 TEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTV-IMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
262-496 |
9.12e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.18 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvALENGIAL 337
Cdd:PRK11231 2 TLRTENLTvgygTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR-QLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTedrkeQGLFLKQsvkfNIASSNLKKYRENGFLNL-----QEQRKDAIRMVDNLNIKTpnVQTKCL-QLSGGNQQKVVI 411
Cdd:PRK11231 81 LP-----QHHLTPE----GITVRELVAYGRSPWLSLwgrlsAEDNARVNQAMEQTRINH--LADRRLtDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 412 GKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGrfntdEASKEK 491
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA-----QGTPEE 224
|
....*
gi 433671570 492 IMSAA 496
Cdd:PRK11231 225 VMTPG 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-205 |
9.17e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLeDNDPQKALEQLGITP 85
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 86 IYQELNliPQLDVTENIFMGREKSKNEilgwidrerMEEETKKILSRLGQESISPNDLirdLGVGKQQMVEISKALSVET 165
Cdd:PRK13540 81 HRSGIN--PYLTLRENCLYDIHFSPGA---------VGITELCRLFSLEHLIDYPCGL---LSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 433671570 166 KLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHK 205
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
226-476 |
1.05e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 226 ITDRVDNLTEDK--MISYMVGEDVDNKFPKMKVEPGKESLRVENLnrkgvlnnvSFKAYEGEVLGIAGLVGAGRTEIARA 303
Cdd:TIGR01257 1914 IFDEDDDVAEERqrIISGGNKTDILRLNELTKVYSGTSSPAVDRL---------CVGVRPGECFGLLGVNGAGKTTTFKM 1984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 304 IVGADSKDSGDIYVHGKKVKIDSPKVALENGIAlltedrkeqglflkqsVKFNiASSNLKKYRENGFL--NLQEQRKDAI 381
Cdd:TIGR01257 1985 LTGDTTVTSGDATVAGKSILTNISDVHQNMGYC----------------PQFD-AIDDLLTGREHLYLyaRLRGVPAEEI 2047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 382 RMVDNLNIKTP--NVQTKCL--QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMIS 457
Cdd:TIGR01257 2048 EKVANWSIQSLglSLYADRLagTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTS 2127
|
250
....*....|....*....
gi 433671570 458 SELPEILNMSDRILVVHEG 476
Cdd:TIGR01257 2128 HSMEECEALCTRLAIMVKG 2146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-222 |
1.12e-08 |
|
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: 58.00 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKkledndpqkaleqLGITPiyqELNLIPQLDVTE 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSP---QTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 101 NIFMGREKSKNEILGWIDRERMEEETKKILSR----LGQESISpndlirdLGVGKQQMVEISKALSVETKLLILDEPTSS 176
Cdd:TIGR01271 506 NIIFGLSYDEYRYTSVIKACQLEEDIALFPEKdktvLGEGGIT-------LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 433671570 177 LGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKmADRVTVLRNG 222
Cdd:TIGR01271 579 LDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
245-476 |
1.14e-08 |
|
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: 58.00 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 245 EDVDNKFPKmkvepGKESLRVENLNRKG--VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYvHGKKV 322
Cdd:TIGR01271 416 NNKARKQPN-----GDDGLFFSNFSLYVtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRI 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 323 KIdSPKVALengialltedrkeqglFLKQSVKFNIA-SSNLKKYRENGFLNLQEQRKDaIRMVDNLNiKTPnVQTKCLQL 401
Cdd:TIGR01271 490 SF-SPQTSW----------------IMPGTIKDNIIfGLSYDEYRYTSVIKACQLEED-IALFPEKD-KTV-LGEGGITL 549
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 402 SGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFN--IINDLVKKgnTVIMISSELpEILNMSDRILVVHEG 476
Cdd:TIGR01271 550 SGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
263-478 |
1.19e-08 |
|
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: 54.84 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVG-ADSK-DSGDIYVHGkkvkidspkvalENGIA 336
Cdd:cd03217 1 LEIKDLhvsvGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhPKYEvTEGEILFKG------------EDITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 337 LLTEDRKEQGLFLkqsvkfniassnlkkyrenGFlnlqeQRKDAIRMVDNLN-IKTPNVQtkclqLSGGNQQKVVIGKWL 415
Cdd:cd03217 69 LPPEERARLGIFL-------------------AF-----QYPPEIPGVKNADfLRYVNEG-----FSGGEKKRNEILQLL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 416 NTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMIsSELPEILNM--SDRILVVHEGKI 478
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDYikPDRVHVLYDGRI 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-223 |
1.64e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 14 EFPGVraLDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdndpqkaleQLGITPIYQELNLI 93
Cdd:PLN03232 1247 GLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA---------KFGLTDLRRVLSII 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 94 PQLDVtenIFMGREK-------SKNEILGWIDRERmeEETKKILSR----------LGQESISpndlirdlgVGKQQMVE 156
Cdd:PLN03232 1316 PQSPV---LFSGTVRfnidpfsEHNDADLWEALER--AHIKDVIDRnpfgldaevsEGGENFS---------VGQRQLLS 1381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 157 ISKALSVETKLLILDEPTSSLGKdETKELFDTMGTLKKQGVTMIFISHKLDEVKKmADRVTVLRNGK 223
Cdd:PLN03232 1382 LARALLRRSKILVLDEATASVDV-RTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
6-223 |
1.75e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVR--------------------ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIE 65
Cdd:PRK13546 5 VNIKNVTKEYRIYRtnkermkdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 66 GkkledndpqkaleQLGITPIYQELNliPQLDVTENIfmgreKSKNEILGWiDRERMEEETKKIL--SRLGQESISPndl 143
Cdd:PRK13546 85 G-------------EVSVIAISAGLS--GQLTGIENI-----EFKMLCMGF-KRKEIKAMTPKIIefSELGEFIYQP--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 144 IRDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK13546 141 VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-216 |
1.87e-08 |
|
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: 53.87 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 18 VRALDGVDLEIKRGEVHAILGENGAGKSTLIKvltgvhtptEGeIYIEGKKLEDNDPQKALEQLGItpiyqelnLIPQLd 97
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EG-LYASGKARLISFLPKFSRNKLI--------FIDQL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 98 vtenifmgrekskneilgwidrermeeetkKILSRLGQESISPNDLIRDLGVGKQQMVEISKALSVETK--LLILDEPTS 175
Cdd:cd03238 69 ------------------------------QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 433671570 176 SLGKDETKELFDTMGTLKKQGVTMIFISHKLDeVKKMADRV 216
Cdd:cd03238 119 GLHQQDINQLLEVIKGLIDLGNTVILIEHNLD-VLSSADWI 158
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
367-478 |
2.01e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 367 ENGFLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDL 446
Cdd:PRK13643 111 QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI 190
|
90 100 110
....*....|....*....|....*....|..
gi 433671570 447 VKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13643 191 HQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-62 |
2.11e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 2.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEI 62
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
273-479 |
2.16e-08 |
|
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: 54.85 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKkvkiDSPKVALENGI--------------ALL 338
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----VSSLLGLGGGFnpeltgreniylngRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 TEDRKEqglfLKQSVKFNIASSNLKKYRengflnlqeqrkdairmvdNLNIKTpnvqtkclqLSGGNQQKVVIGKWLNTE 418
Cdd:cd03220 113 GLSRKE----IDEKIDEIIEFSELGDFI-------------------DLPVKT---------YSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
278-474 |
2.62e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.07 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 278 SFKAY------EGEVLGIAGLVGAGRTEIARAIVGADSKDSGDiyvHGKKVKIDS-----PKVALENGIALLTED----- 341
Cdd:cd03236 14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEildefRGSELQNYFTKLLEGdvkvi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 342 RKEQGL-FLKQSVKFNIaSSNLKKYRENGFLNLqeqrkdairMVDNLNIKtPNVQTKCLQLSGGNQQKVVIGKWLNTEAN 420
Cdd:cd03236 91 VKPQYVdLIPKAVKGKV-GELLKKKDERGKLDE---------LVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 421 IFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELpEILNM-SDRILVVH 474
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL-AVLDYlSDYIHCLY 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-178 |
3.15e-08 |
|
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: 53.79 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 9 KNLTKEFPGV----RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP--TEGEIYIEGKKLEDNDPQKA--LEQ 80
Cdd:cd03232 7 KNLNYTVPVKggkrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQRSTgyVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 81 LGItpiyqelnLIPQLDVtenifmgrekskneilgwidRERMEeetkkilsrlgqesISPNdlIRDLGVGKQQMVEISKA 160
Cdd:cd03232 87 QDV--------HSPNLTV--------------------REALR--------------FSAL--LRGLSVEQRKRLTIGVE 122
|
170
....*....|....*...
gi 433671570 161 LSVETKLLILDEPTSSLG 178
Cdd:cd03232 123 LAAKPSILFLDEPTSGLD 140
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
401-478 |
3.42e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.42 E-value: 3.42e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
273-478 |
3.99e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 53.65 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGkkvkIDSPKVALE---NGIALLTEDRkeqglFL 349
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG----VDISKIGLHdlrSRISIIPQDP-----VL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 350 KQ-SVKFNIASsnLKKYREngflnlqEQRKDAIRMV------DNLNIKTPNVQTKC-LQLSGGNQQKVVIGKWLNTEANI 421
Cdd:cd03244 90 FSgTIRSNLDP--FGEYSD-------EELWQALERVglkefvESLPGGLDTVVEEGgENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 422 FIFDEPTRGIDvgakVEVFNIINDLVK---KGNTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:cd03244 161 LVLDEATASVD----PETDALIQKTIReafKDCTVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
273-478 |
4.88e-08 |
|
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: 53.70 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvALENGIALLTEdrkEQGLFLKqS 352
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR-WLRSQIGLVSQ---EPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIASSnlKKYREngflnlQEQRKDAIRMV--DNLNIKTPN-----VQTKCLQLSGGNQQKVVIGKWLNTEANIFIFD 425
Cdd:cd03249 93 IAENIRYG--KPDAT------DEEVEEAAKKAniHDFIMSLPDgydtlVGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 433671570 426 EPTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:cd03249 165 EATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
263-478 |
5.42e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.78 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL-----NRKGvLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDI-YVHGKKVKIDspkvalengIA 336
Cdd:PRK11701 7 LSVRGLtklygPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRD---------LY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 337 LLTEDRK---------------EQGLFLKQSVKFNIA-------SSNLKKYRENGFLNLQEQRKDAIRMVDnlnikTPNv 394
Cdd:PRK11701 77 ALSEAERrrllrtewgfvhqhpRDGLRMQVSAGGNIGerlmavgARHYGDIRATAGDWLERVEIDAARIDD-----LPT- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 395 qtkclQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVV 473
Cdd:PRK11701 151 -----TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVM 225
|
....*
gi 433671570 474 HEGKI 478
Cdd:PRK11701 226 KQGRV 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
255-476 |
6.06e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.09 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 255 KVEPGKESLRVENLNRKG--VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYvHGKKVKIDS------ 326
Cdd:cd03291 32 KHSSDDNNLFFSNLCLVGapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGRISFSSqfswim 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 327 PKVALENGIALLTEDRKEqglfLKQSVKFNIASSNLKKYREngflnlqeqrKDAIRMVDNlniktpnvqtkCLQLSGGNQ 406
Cdd:cd03291 111 PGTIKENIIFGVSYDEYR----YKSVVKACQLEEDITKFPE----------KDNTVLGEG-----------GITLSGGQR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 407 QKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELpEILNMSDRILVVHEG 476
Cdd:cd03291 166 ARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKM-EHLKKADKILILHEG 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
262-473 |
6.71e-08 |
|
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: 54.99 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 262 SLRVENLN-----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvALENGIA 336
Cdd:TIGR02857 321 SLEFSGVSvaypgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 337 LLTEdrkeQGLFLKQSVKFNIASSNlkkyRENGFLNLQE--QRKDAIRMVDNL--NIKTPnVQTKCLQLSGGNQQKVVIG 412
Cdd:TIGR02857 400 WVPQ----HPFLFAGTIAENIRLAR----PDASDAEIREalERAGLDEFVAALpqGLDTP-IGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 413 KWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVkKGNTVIMISSELPEILNMsDRILVV 473
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
273-495 |
8.32e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.04 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGAdSKDSgdIYVHGKKVKID-------SP----KVALENGIALLTE- 340
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDN--WRVTADRMRFDdidllrlSPrerrKLVGHNVSMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 341 ----DRKEQ-GLFLKQSVKFniassnlKKYRENGFLNLQEQRKDAIRMVDNLNIKTPNVQTKCL--QLSGGNQQKVVIGK 413
Cdd:PRK15093 99 qsclDPSERvGRQLMQNIPG-------WTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFpyELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 414 WLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVI-MISSELPEILNMSDRILVVHEGKitgrfNTDEASKEKI 492
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDLQMLSQWADKINVLYCGQ-----TVETAPSKEL 246
|
...
gi 433671570 493 MSA 495
Cdd:PRK15093 247 VTT 249
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
273-479 |
8.53e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 52.75 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDspkvalENGIALLtedRKEQG----- 346
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsRLK------RREIPYL---RRRIGvvfqd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 347 --LFLKQSVKFNIAssnL------KKYREngflnLQEQRKDAIRMVDNLNIKtpnvQTKCLQLSGGNQQKVVIGKWLNTE 418
Cdd:COG2884 88 frLLPDRTVYENVA---LplrvtgKSRKE-----IRRRVREVLDLVGLSDKA----KALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
263-498 |
8.77e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKdSGDIYVHGKKVKiDSPKVALENGIALLTEDR 342
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLE-AWSAAELARHRAYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 343 KE-------QGLFLKQSVKFNIASSNLKKYRENGFLNLQeqrkdairmvDNLNiktPNVQtkclQLSGGNQQKV-----V 410
Cdd:PRK03695 79 TPpfampvfQYLTLHQPDKTRTEAVASALNEVAEALGLD----------DKLG---RSVN----QLSGGEWQRVrlaavV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 411 IGKW--LNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDEAS 488
Cdd:PRK03695 142 LQVWpdINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
250
....*....|
gi 433671570 489 KEKIMSAATG 498
Cdd:PRK03695 222 TPENLAQVFG 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-236 |
8.79e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 7 KIKNLTK-EFPGVR----------ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYI-EGKKLEDNDP 74
Cdd:PTZ00265 376 KLKDIKKiQFKNVRfhydtrkdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 75 QKALEQLGITP-------------IYQELNLIPQLDV-----TENIFMGREKSK-------------NEILGWIDRERME 123
Cdd:PTZ00265 456 KWWRSKIGVVSqdpllfsnsiknnIKYSLYSLKDLEAlsnyyNEDGNDSQENKNkrnscrakcagdlNDMSNTTDSNELI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 124 EETKKILSRLGQE--SISPNDLIRD-------------------LGVGKQQMVEISKALSVETKLLILDEPTSSLGKDET 182
Cdd:PTZ00265 536 EMRKNYQTIKDSEvvDVSKKVLIHDfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 183 KELFDTMGTLK-KQGVTMIFISHKLDEVkKMADRVTVLRNGKYIITDRVDNLTED 236
Cdd:PTZ00265 616 YLVQKTINNLKgNENRITIIIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIGED 669
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
273-478 |
1.09e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.96 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKidspKVALEN-GIALLTEdrkEQGLFLKQ 351
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSIQQrDICMVFQ---SYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIASS--NLKKYRENgflnLQEQRKDAIRMVDNLNIKTPNVQtkclQLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:PRK11432 94 SLGENVGYGlkMLGVPKEE----RKQRVKEALELVDLAGFEDRYVD----QISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 433671570 430 GIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNiTSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
278-501 |
1.25e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 52.66 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 278 SFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvalENGIALLTEdrkEQGLFLKQSVKFNI 357
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVSMLFQ---ENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 358 A---SSNLKkyrengfLNlQEQRKDAIRMVDNLNIktpnvqTKCL-----QLSGGNQQKVVIGKWLNTEANIFIFDEPTR 429
Cdd:PRK10771 93 GlglNPGLK-------LN-AAQREKLHAIARQMGI------EDLLarlpgQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 430 GIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVHEGKITGRFNTDEASKEKIMSAATGGIK 501
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIK 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-222 |
1.33e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.94 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKkledndpqkaleqlgITPIYQELNLIPQlDVTE 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---------------ISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 101 NIFMGREKSKNEILGWIDRERMEEETKKILSR----LGQESISpndlirdLGVGKQQMVEISKALSVETKLLILDEPTSS 176
Cdd:cd03291 117 NIIFGVSYDEYRYKSVVKACQLEEDITKFPEKdntvLGEGGIT-------LSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 433671570 177 LGKDETKELFDTMGTLKKQGVTMIFISHKLDEVKKmADRVTVLRNG 222
Cdd:cd03291 190 LDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-225 |
1.56e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVdleIKRGEVHAILGENGAGKSTLIKVLT----GVHTPTEGEIYIEGKKLEDNDPQKALEQL 81
Cdd:TIGR00956 65 LKKFRDTKTFDILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 82 GITpiyQELNLIPQLDVTENI-FMGREKS-KNEILGWIDRERMEEETKKILSRLG----QESISPNDLIRDLGVGKQQMV 155
Cdd:TIGR00956 142 YNA---ETDVHFPHLTVGETLdFAARCKTpQNRPDGVSREEYAKHIADVYMATYGlshtRNTKVGNDFVRGVSGGERKRV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 156 EISKALSVETKLLILDEPTSSLGKDETKEL---FDTMGTLKKQGVTMIfISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSATALEFiraLKTSANILDTTPLVA-IYQCSQDAYELFDKVIVLYEGYQI 290
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
276-478 |
1.82e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.25 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 276 NVSFkaYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKValengialltedRKEQGLFLKQSVKF 355
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV------------RQSLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 356 N--IASSNLKKYRENGFLNLQEQRKDAIRMVDNLNIKTPNvQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDV 433
Cdd:TIGR01257 1016 HhlTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 433671570 434 GAKVEVFNIINDLvKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:TIGR01257 1095 YSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
263-496 |
2.05e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDSPKVALEngIAL 337
Cdd:PRK10253 8 LRGEQLTlgygKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARR--IGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDRKEQGLFLKQSVkfnIASSnlkKY-RENGFLNLQEQRKDAI----RMVDNLNIKTPNVQTkclqLSGGNQQKVVIG 412
Cdd:PRK10253 86 LAQNATTPGDITVQEL---VARG---RYpHQPLFTRWRKEDEEAVtkamQATGITHLADQSVDT----LSGGQRQRAWIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 413 KWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVK-KGNTVIMISSELPEILNMSDRILVVHEGKITGrfntdEASKEK 491
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVA-----QGAPKE 230
|
....*
gi 433671570 492 IMSAA 496
Cdd:PRK10253 231 IVTAE 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
274-496 |
2.39e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.05 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvALENGIALLTEDRKEQgLF---LK 350
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK-WVRSKVGLVFQDPDDQ-VFsstVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 351 QSVKFNIASSNLKKYRengflnLQEQRKDAIRMVD--NLNIKTPNvqtkclQLSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:PRK13647 99 DDVAFGPVNMGLDKDE------VERRVEEALKAVRmwDFRDKPPY------HLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 429 RGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDEASKEKIMSAA 496
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQA 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
260-487 |
2.43e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.01 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 260 KESLRVENLNRKG---VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGkkvKIDSPkvaLENGIA 336
Cdd:COG1134 25 KELLLRRRRTRREefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSAL---LELGAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 337 L---LTedrkeqGlflkqsvkfniassnlkkyRENGFLN---LQEQRKDAIRMVDnlniktpnvqtKCLQLSGgnqqkvv 410
Cdd:COG1134 99 FhpeLT------G-------------------RENIYLNgrlLGLSRKEIDEKFD-----------EIVEFAE------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 411 IGKWLNT---------------------EANIFIFDEptrGIDVG-----AKveVFNIINDLVKKGNTVIMISSELPEIL 464
Cdd:COG1134 136 LGDFIDQpvktyssgmrarlafavatavDPDILLVDE---VLAVGdaafqKK--CLARIRELRESGRTVIFVSHSMGAVR 210
|
250 260
....*....|....*....|...
gi 433671570 465 NMSDRILVVHEGKITGRFNTDEA 487
Cdd:COG1134 211 RLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-267 |
2.63e-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: 53.41 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEdnDPQKAleqlgitpiyqelnLIPQLDVTE 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAY--VPQQA--------------WIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 101 NIFMGREKSKN---------------EILGWIDRermeeetkkilSRLGQESIspndlirDLGVGKQQMVEISKALSVET 165
Cdd:TIGR00957 718 NILFGKALNEKyyqqvleacallpdlEILPSGDR-----------TEIGEKGV-------NLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 166 KLLILDEPTSSLGKDETKELFDT----MGTLKkqGVTMIFISHKLDEVKKMaDRVTVLRNGKY-------IITDRvDNLT 234
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHvigpEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKIsemgsyqELLQR-DGAF 855
|
250 260 270
....*....|....*....|....*....|....*.
gi 433671570 235 EDKMISYMVGED---VDNKFPKMKVEPGKESLRVEN 267
Cdd:TIGR00957 856 AEFLRTYAPDEQqghLEDSWTALVSGEGKEAKLIEN 891
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-204 |
2.74e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYI-EGKKL-------EDNDPQKA 77
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLayvdqsrDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 78 leqlgitpIYQELNlipqlDVTENIFMGrekskneilgwidrermeeeTKKILSR--LGQESISPND---LIRDLGVGKQ 152
Cdd:TIGR03719 403 --------VWEEIS-----GGLDIIKLG--------------------KREIPSRayVGRFNFKGSDqqkKVGQLSGGER 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 433671570 153 QMVEISKALSVETKLLILDEPTSSLGKDETKELFDtmGTLKKQGVTMIfISH 204
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEE--ALLNFAGCAVV-ISH 498
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-180 |
2.87e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 24 VDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDNDPQKALEQLGITPiyqelNLIPQLDVTENI- 102
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP-----GLKADLSTLENLh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 103 ----FMGREKskneilgwidrERMEEETKKILSRLGQEsispNDLIRDLGVGKQQMVEISKALSVETKLLILDEPTSSLG 178
Cdd:PRK13543 105 flcgLHGRRA-----------KQMPGSALAIVGLAGYE----DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
..
gi 433671570 179 KD 180
Cdd:PRK13543 170 LE 171
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
274-493 |
2.97e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.16 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKvalengialLTEDRKEQGLFLkQSV 353
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG---------LMKLRESVGMVF-QDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 354 KFNIASSNLKKYRENGFLNLQEQRKDAIRMVDNLNIKT-----PNVQTKCLqlSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:PRK13636 92 DNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTgiehlKDKPTHCL--SFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 429 RGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDEASKEKIM 493
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
263-477 |
2.99e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.53 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN-RKGVL---NNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVK-IDSPKVA------- 330
Cdd:PRK11300 6 LSVSGLMmRFGGLlavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGHQIArmgvvrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 331 LENgIALLTEDRKEQGLFLKQ--SVKFNIASSNLK--KYR--ENGFLNLQEQRKDAIRMVDNLNIKTPNvqtkclqLSGG 404
Cdd:PRK11300 86 FQH-VRLFREMTVIENLLVAQhqQLKTGLFSGLLKtpAFRraESEALDRAATWLERVGLLEHANRQAGN-------LAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 405 NQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGK 477
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-204 |
3.17e-07 |
|
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: 50.23 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 25 DLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYiegkKLEDND----PQKALEQLGitpiyqelNLIPQLdvte 100
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG----MPEGEDllflPQRPYLPLG--------TLREQL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 101 nifmgrekskneILGWidrermeeetKKILSrlgqesispndlirdlgVGKQQMVEISKALSVETKLLILDEPTSSLGKD 180
Cdd:cd03223 85 ------------IYPW----------DDVLS-----------------GGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....
gi 433671570 181 ETKELFDtmgTLKKQGVTMIFISH 204
Cdd:cd03223 126 SEDRLYQ---LLKELGITVISVGH 146
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-204 |
3.19e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.89 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFPGVRAL-DGVDLEIKRGEVHAILGENGAGKSTLIKVLTG--------VHTPTEGEI-------YI----- 64
Cdd:COG4178 363 LALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgrIARPAGARVlflpqrpYLplgtl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 65 --------EGKKLEDNDPQKALEQLGITpiyqelNLIPQLDVTENifmgrekskneilgWIdrermeeetkKILSrlgqe 136
Cdd:COG4178 443 reallypaTAEAFSDAELREALEAVGLG------HLAERLDEEAD--------------WD----------QVLS----- 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 137 sispndlirdlgVGKQQMVEISKALSVETKLLILDEPTSSLgkDETKElFDTMGTLKKQ--GVTMIFISH 204
Cdd:COG4178 488 ------------LGEQQRLAFARLLLHKPDWLFLDEATSAL--DEENE-AALYQLLREElpGTTVISVGH 542
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
263-478 |
3.53e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSgdiyVHGKKVKIDSPKVALENGIAL- 337
Cdd:PRK09984 5 IRVEKLaktfNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK----SAGSHIELLGRTVQREGRLARd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 338 LTEDRKEQGLFLKQ-------SVKFNI-----ASSNLKKYRENGFLNLQEQRK-DAIRMVDNLNIKTPNVQTkclqLSGG 404
Cdd:PRK09984 81 IRKSRANTGYIFQQfnlvnrlSVLENVligalGSTPFWRTCFSWFTREQKQRAlQALTRVGMVHFAHQRVST----LSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 405 NQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-225 |
4.08e-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: 50.72 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 13 KEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVhtpTEGEIYIEGK-KLEDNDPQKALEQLGITPIY--QE 89
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDiHYNGIPYKEFAEKYPGEIIYvsEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 90 LNLIPQLDVTENI-FMGREKSkneilgwidrermeeetkkilsrlgqesispNDLIRDLGVGKQQMVEISKALSVETKLL 168
Cdd:cd03233 92 DVHFPTLTVRETLdFALRCKG-------------------------------NEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 169 ILDEPTSSLGKDETKELFDTMGTLKKQ--GVTMIFISHKLDEVKKMADRVTVLRNGKYI 225
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
273-478 |
4.40e-07 |
|
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: 50.93 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVaLENGIALLTEdrkEQGLFlKQS 352
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY-LHSKVSLVGQ---EPVLF-ARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIA-----------SSNLKKYRENGFLNLQEQRKDAirmvdnlniktpNVQTKCLQLSGGNQQKVVIGKWLNTEANI 421
Cdd:cd03248 104 LQDNIAyglqscsfecvKEAAQKAHAHSFISELASGYDT------------EVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 422 FIFDEPTRGIDVGAKVEVFNIINDLVKKgNTVIMISSELPEIlNMSDRILVVHEGKI 478
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
273-460 |
4.73e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDS-PKVALENgialltedrKEQGlFLK 350
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSaAKAELRN---------QKLG-FIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 351 QS----VKFNiASSNLKKYRENGFLNLQEQRKDAIRMVDNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDE 426
Cdd:PRK11629 94 QFhhllPDFT-ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*
gi 433671570 427 PTRGIDVGAKVEVFNIINDL-VKKGNTVIMISSEL 460
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
273-478 |
4.89e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.42 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKiDSPKVALENGIALLTEdrkEQGLFlKQS 352
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHHYLHRQVALVGQ---EPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIASSnLKKYRENGFLNL-QEQRKDAIRMVDNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGI 431
Cdd:TIGR00958 571 VRENIAYG-LTDTPDEEIMAAaKAANAHDFIMEFPNGYDT-EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 433671570 432 DVGAKVEVFniiNDLVKKGNTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:TIGR00958 649 DAECEQLLQ---ESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-225 |
5.34e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 60 GEIYIEGKKLEDNDpQKALEQLgITPIYQELNLIpQLDVTENIFMGREKSKNEILGWIDRERMEEETKKILSRLGQESIS 139
Cdd:PTZ00265 1277 GKILLDGVDICDYN-LKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVG 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 140 PNDliRDLGVGKQQMVEISKALSVETKLLILDEPTSSLGKDETKELFDTMGTLK-KQGVTMIFISHKLDEVKKmADRVTV 218
Cdd:PTZ00265 1354 PYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKR-SDKIVV 1430
|
170
....*....|.
gi 433671570 219 L----RNGKYI 225
Cdd:PTZ00265 1431 FnnpdRTGSFV 1441
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
400-474 |
5.70e-07 |
|
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: 52.09 E-value: 5.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 400 QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELpEILNM-SDRILVVH 474
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL-AILDYlADYVHILY 286
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
399-493 |
5.75e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 399 LQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELpEILNMSDRILVVHEGKI 478
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
90
....*....|....*
gi 433671570 479 TGRFNTDEASKEKIM 493
Cdd:PLN03232 818 KEEGTFAELSKSGSL 832
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-204 |
5.83e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIeGKKLE----DNdpqkaleqlgi 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfDQ----------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 tpiYQElNLIPQLDVTENIFMGreKSKNEILGwidRERmeeetkKILSRLGQESISPndlirdlgvgKQQMVEIsKALSV 163
Cdd:PRK11147 390 ---HRA-ELDPEKTVMDNLAEG--KQEVMVNG---RPR------HVLGYLQDFLFHP----------KRAMTPV-KALSG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 164 ETK--------------LLILDEPTSSLgkD-ETKELFDTMGTlKKQGvTMIFISH 204
Cdd:PRK11147 444 GERnrlllarlflkpsnLLILDEPTNDL--DvETLELLEELLD-SYQG-TVLLVSH 495
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
401-471 |
7.07e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 49.54 E-value: 7.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRIL 471
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
258-477 |
7.34e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.80 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 258 PGKESLRVENLNRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVG--ADSKDSGDIYVHGKKvkidsPKVALENGI 335
Cdd:PLN03211 68 KPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRK-----PTKQILKRT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 336 ALLTEDrkeQGLFLKQSVKFNIASSNLKKYRENgfLNLQEQRKDAIRMVDNLNIktpnvqTKCLQ----------LSGGN 405
Cdd:PLN03211 143 GFVTQD---DILYPHLTVRETLVFCSLLRLPKS--LTKQEKILVAESVISELGL------TKCENtiignsfirgISGGE 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 406 QQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIM-ISSELPEILNMSDRILVVHEGK 477
Cdd:PLN03211 212 RKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
263-469 |
7.76e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.54 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENL----NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAI-----VGADSKDSGDIYVHGKKvkIDSPKVALen 333
Cdd:PRK14239 6 LQVSDLsvyyNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHN--IYSPRTDT-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 334 giallTEDRKEQGLFLKQSVKF--NIASSNLKKYRENGFLN---LQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQK 408
Cdd:PRK14239 82 -----VDLRKEIGMVFQQPNPFpmSIYENVVYGLRLKGIKDkqvLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 409 VVIGKWLNTEANIFIFDEPTRGID--VGAKVE--VFNIindlvKKGNTVIMISSELPEILNMSDR 469
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDpiSAGKIEetLLGL-----KDDYTMLLVTRSMQQASRISDR 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
229-478 |
7.85e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.75 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 229 RVDNLTEDKmisymvgedVDNKFPKM-KVEPGKESLRVENL------NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIA 301
Cdd:PRK11160 313 RINEITEQK---------PEVTFPTTsTAAADQVSLTLNNVsftypdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 302 RAIVGADSKDSGDIYVHGKKVKiDSPKVALENGIALLTedrkeqglflkQSVkfNIASSNLkkyRENgfLNLQEQRKDAI 381
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIA-DYSEAALRQAISVVS-----------QRV--HLFSATL---RDN--LLLAAPNASDE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 382 RMVDNLNiktpNVQTKCL----------------QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIIND 445
Cdd:PRK11160 445 ALIEVLQ----QVGLEKLleddkglnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
250 260 270
....*....|....*....|....*....|...
gi 433671570 446 LVkKGNTVIMISSELPEILNMsDRILVVHEGKI 478
Cdd:PRK11160 521 HA-QNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
271-502 |
9.91e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.48 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 271 KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSK-----DSGDIYVHGKKVKIDSPKVALENGIALLTEDRKEQ 345
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 346 GLFLKQSVKFNIASSNLKKYREngFLNLQEQRKDAIRMVDNLNIKtpnVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFD 425
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKE--FRGVAQARLTEVGLWDAVKDR---LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 426 EPTRGIDVGAKVEVFNIINDLVKKgNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDE-------ASKEKIMSAATG 498
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQlfsspkhAETARYVAGLSG 267
|
....
gi 433671570 499 GIKD 502
Cdd:PRK14271 268 DVKD 271
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-214 |
1.21e-06 |
|
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: 51.17 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 132 RLGQESISpndlirdLGVGKQQMVEISKALSVETK---LLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDe 208
Cdd:TIGR00630 822 RLGQPATT-------LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD- 893
|
....*.
gi 433671570 209 VKKMAD 214
Cdd:TIGR00630 894 VIKTAD 899
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
250-477 |
1.22e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.71 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 250 KFPKMKVEPGKESLRVEnlnrKGVLNnvsfkayEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIyvhgkkvkidspkv 329
Cdd:cd03237 2 TYPTMKKTLGEFTLEVE----GGSIS-------ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 330 alenGIALLTEDRKEQGLflkqSVKFNIASSNLKKYRENGFLNLQEQRKDAIR--MVDNLniktpnVQTKCLQLSGGNQQ 407
Cdd:cd03237 57 ----EIELDTVSYKPQYI----KADYEGTVRDLLSSITKDFYTHPYFKTEIAKplQIEQI------LDREVPELSGGELQ 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 433671570 408 KVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRiLVVHEGK 477
Cdd:cd03237 123 RVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEkTAFVVEHDIIMIDYLADR-LIVFEGE 192
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
400-479 |
1.69e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 400 QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:PRK13649 145 ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-177 |
1.93e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 9 KNLTKEFP----GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP---TEGEIYIEGKKLEDNDPQKA--LE 79
Cdd:TIGR00956 763 RNLTYEVKikkeKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRSIgyVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 80 QlgitpiyQELNLiPQLDVTEN-IFMGREKSKNEIlgwIDRERMeEETKKILSRLGQESISpnDLIrdLGV-GKQQMVEI 157
Cdd:TIGR00956 843 Q-------QDLHL-PTSTVRESlRFSAYLRQPKSV---SKSEKM-EYVEEVIKLLEMESYA--DAV--VGVpGEGLNVEQ 906
|
170 180
....*....|....*....|....*..
gi 433671570 158 SKALS--VE----TKLLI-LDEPTSSL 177
Cdd:TIGR00956 907 RKRLTigVElvakPKLLLfLDEPTSGL 933
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
385-492 |
2.13e-06 |
|
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: 47.95 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 385 DNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEI 463
Cdd:cd03222 56 DEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL 135
|
90 100 110
....*....|....*....|....*....|
gi 433671570 464 LNMSDRILVVH-EGKITGRFNTDEASKEKI 492
Cdd:cd03222 136 DYLSDRIHVFEgEPGVYGIASQPKGTREGI 165
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
401-496 |
2.47e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFN--IINDLvkKGNTVIMISSELpEILNMSDRILVVHEGKI 478
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDEL--RGKTRVLVTNQL-HFLSQVDRIILVHEGMI 817
|
90 100
....*....|....*....|...
gi 433671570 479 TGRFNTDEASK-----EKIMSAA 496
Cdd:PLN03130 818 KEEGTYEELSNngplfQKLMENA 840
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
401-498 |
2.82e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEIlNMSDRILVVHEGKIT 479
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIITIAHRIASI-KRSDKIVVFNNPDRT 1437
|
90
....*....|....*....
gi 433671570 480 GRFNTDEASKEKIMSAATG 498
Cdd:PTZ00265 1438 GSFVQAHGTHEELLSVQDG 1456
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
256-460 |
2.94e-06 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 49.67 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 256 VEPGKESLRVENLN-----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKiDSPKVA 330
Cdd:TIGR02868 328 VGLGKPTLELRDLSagypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 331 LENGIALLTEDRKeqgLFlkqsvkfniASS---NLKKYRENGflnLQEQRKDAIRMV----------DNLNIKtpnVQTK 397
Cdd:TIGR02868 407 VRRRVSVCAQDAH---LF---------DTTvreNLRLARPDA---TDEELWAALERVgladwlralpDGLDTV---LGEG 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 398 CLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDlVKKGNTVIMISSEL 460
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-106 |
3.09e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 8 IKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKLEDndpQKALEQLG--ITP 85
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVCprIAY 80
|
90 100
....*....|....*....|....
gi 433671570 86 IYQEL--NLIPQLDVTENI-FMGR 106
Cdd:NF033858 81 MPQGLgkNLYPTLSVFENLdFFGR 104
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-64 |
3.54e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 3.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 9 KNLTKEFpGVRAL-DGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYI 64
Cdd:PRK11819 328 ENLSKSF-GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
401-478 |
3.55e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 3.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
269-478 |
3.63e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 269 NRKgVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVkidsPKVALENgialLTEDRKEQ--- 345
Cdd:PRK11831 19 NRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI----PAMSRSR----LYTVRKRMsml 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 346 ----GLFLKQSVKFNIASSnlkkYRENGFLNLQEQRKDAIRMVDNLNIKTPnVQTKCLQLSGGNQQKVVIGKWLNTEANI 421
Cdd:PRK11831 90 fqsgALFTDMNVFDNVAYP----LREHTQLPAPLLHSTVMMKLEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 422 FIFDEPTRG---IDVGAKVEVFNIINDLVkkGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK11831 165 IMFDEPFVGqdpITMGVLVKLISELNSAL--GVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
401-484 |
4.33e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.46 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELPEILNMsDRILVVHEGKI-- 478
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIvq 563
|
....*.
gi 433671570 479 TGRFNT 484
Cdd:PRK11174 564 QGDYAE 569
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
273-455 |
5.90e-06 |
|
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: 46.97 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKvkidspkvalengIALLTEDRKEQGLFLKQS 352
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-------------LAEQRDEPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 --VKFNI-ASSNLKKYREngfLNLQEQRK--DAIRMVDNLNIKtpnvQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEP 427
Cdd:TIGR01189 82 pgLKPELsALENLHFWAA---IHGGAQRTieDALAAVGLTGFE----DLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180
....*....|....*....|....*....
gi 433671570 428 TRGIDVgAKVEVFN-IINDLVKKGNTVIM 455
Cdd:TIGR01189 155 TTALDK-AGVALLAgLLRAHLARGGIVLL 182
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-213 |
6.29e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 36 ILGENGAGKSTLIKVLTGVHTPTEGEIYIegKKLEDNDPQKALeqlgITPIYQELNLIPQLDVTENIFMGRE--KSKNEI 113
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAKPY----CTYIGHNLGLKLEMTVFENLKFWSEiyNSAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 114 LGWIDRERMEE-ETKKILSrlgqesispndlirdLGVGKQQMVEISKALSVETKLLILDEPTSSLGKdETKELFDTMGTL 192
Cdd:PRK13541 105 YAAIHYFKLHDlLDEKCYS---------------LSSGMQKIVAIARLIACQSDLWLLDEVETNLSK-ENRDLLNNLIVM 168
|
170 180
....*....|....*....|.
gi 433671570 193 KKQGVTMIFISHKLDEVKKMA 213
Cdd:PRK13541 169 KANSGGIVLLSSHLESSIKSA 189
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
269-473 |
6.71e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.57 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 269 NRKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKidspKVALENGIALLTEDRKEQGLF 348
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 349 --LKQSVKFniassnLKKYRENGFLNLQEQR-----KDAIRMVDNLNIKTPNVQtkclQLSGGNQQKVVIGKWLNTEANI 421
Cdd:PRK15056 94 pvLVEDVVM------MGRYGHMGWLRRAKKRdrqivTAALARVDMVEFRHRQIG----ELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 433671570 422 FIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVV 473
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
273-468 |
7.55e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.87 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPK-------VALENGIalltedrkEQ 345
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyqkqlcfVGHRSGI--------NP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 346 GLFLKQSVKFNIASSnlkkyreNGFLNLQEQRKdaIRMVDNLnIKTPnvqtkCLQLSGGNQQKVVIGKWLNTEANIFIFD 425
Cdd:PRK13540 88 YLTLRENCLYDIHFS-------PGAVGITELCR--LFSLEHL-IDYP-----CGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 433671570 426 EPTRGIDVGAKVEVFNIINDLVKKGNTVIMIS-SELPeiLNMSD 468
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTShQDLP--LNKAD 194
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
274-477 |
7.76e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVhgkkvkidspkvaleNGIALLTEDRKEQGLfLKQSV 353
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY---------------QGQDLLKADPEAQKL-LRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 354 K--FN--IASSNLKKYRE---------NGFLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEAN 420
Cdd:PRK11308 95 QivFQnpYGSLNPRKKVGqileeplliNTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 421 IFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGK 477
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
276-486 |
9.11e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.48 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 276 NVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKvkidspkvaLENG--------IALLTED------ 341
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP---------LHFGdysyrsqrIRMIFQDpstsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 342 -RKEQGLFLKQSVKFNIAssnlkkyrengfLNLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEAN 420
Cdd:PRK15112 102 pRQRISQILDFPLRLNTD------------LEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 421 IFIFDEPTRGIDVGAKVEVFNIINDLV-KKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDE 486
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
400-473 |
1.04e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 1.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 400 QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVkKGNTVIMISSELPeILNM-SDRILVV 473
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLA-VLDYlADNVHIA 284
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
401-478 |
1.34e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 46.59 E-value: 1.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKK-GNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
398-476 |
1.34e-05 |
|
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: 45.43 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 398 CLQLSGGNQQKV----VIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMIsSELPEILNMSD---RI 470
Cdd:cd03227 75 RLQLSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVI-THLPELAELADkliHI 153
|
....*.
gi 433671570 471 LVVHEG 476
Cdd:cd03227 154 KKVITG 159
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-223 |
1.37e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 19 RALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTG-VHTPteGEIYIEGKKLEDND----PQKALEQL---GITPIYQE- 89
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYP--GRVMAEKLEFNGQDlqriSEKERRNLvgaEVAMIFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 90 -LNLIPQLDVTENIFmgrEKSKNEILGwiDRERMEEETKKILSRLG-QESISPNDLI-RDLGVGKQQMVEISKALSVETK 166
Cdd:PRK11022 99 mTSLNPCYTVGFQIM---EAIKVHQGG--NKKTRRQRAIDLLNQVGiPDPASRLDVYpHQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 167 LLILDEPTSSLGKDETKELFDTMGTL-KKQGVTMIFISHKLDEVKKMADRVTVLRNGK 223
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-173 |
1.48e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 3 EPFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHtptegeiyiegkkledndPQ---KALE 79
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH------------------PQgysNDLT 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 80 QLG--------ITPIYQELNLIP---QLD--VTENIfmgreksKNEIL-GWIDR--------ERMEEETKKILSRLGQES 137
Cdd:PRK10938 320 LFGrrrgsgetIWDIKKHIGYVSsslHLDyrVSTSV-------RNVILsGFFDSigiyqavsDRQQKLAQQWLDILGIDK 392
|
170 180 190
....*....|....*....|....*....|....*.
gi 433671570 138 ISPNDLIRDLGVGKQQMVEISKALSVETKLLILDEP 173
Cdd:PRK10938 393 RTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEP 428
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-66 |
1.74e-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: 45.26 E-value: 1.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 433671570 27 EIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEG 66
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG 60
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
366-486 |
2.50e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 366 RENGFL---NLQEQRKDAIRMVDNLNIK---TPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEV 439
Cdd:NF000106 104 RENLYMigr*LDLSRKDARARADELLERfslTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 433671570 440 FNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDE 486
Cdd:NF000106 184 WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDE 230
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-216 |
2.86e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 129 ILSRLGQESISPNDLIRDLGVGKQQMVEISKALSVETK--LLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKl 206
Cdd:PRK00635 459 ILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD- 537
|
90
....*....|
gi 433671570 207 DEVKKMADRV 216
Cdd:PRK00635 538 EQMISLADRI 547
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
274-486 |
3.55e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.18 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGkkvkIDSPKVAlengIALLTEDRKEQGLFLKQSV 353
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG----VDIAKIS----DAELREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 354 KFNIASSNLKKYRENGFL------NLQEQRKDAIRMV--DNLNIKTPNvqtkclQLSGGNQQKVVIGKWLNTEANIFIFD 425
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELaginaeERREKALDALRQVglENYAHSYPD------ELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 426 EPTRGIDVGAKVEVFNIINDL-VKKGNTVIMISSELPEILNMSDRILVVHEGKITGRFNTDE 486
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-62 |
4.21e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 4.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 4 PFLKIKNLTKEFPGVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEI 62
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-177 |
4.27e-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: 46.44 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP--GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTpTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:TIGR01271 1218 MDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 TPiyQELNlipqldvtenIFMGR-EKSKNEILGWIDrermeEETKKILSRLGQESIS---PNDL---IRD----LGVGKQ 152
Cdd:TIGR01271 1297 IP--QKVF----------IFSGTfRKNLDPYEQWSD-----EEIWKVAEEVGLKSVIeqfPDKLdfvLVDggyvLSNGHK 1359
|
170 180
....*....|....*....|....*
gi 433671570 153 QMVEISKALSVETKLLILDEPTSSL 177
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHL 1384
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
261-478 |
4.31e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 45.15 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 261 ESLRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPK-------- 328
Cdd:PRK13548 1 AMLEARNLSvrlgGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 329 ----------------VALenGIALLTEDRKEqglfLKQSVKFNIASSNLKKYRENGFlnlqeqrkdairmvdnlniktp 392
Cdd:PRK13548 81 lpqhsslsfpftveevVAM--GRAPHGLSRAE----DDALVAAALAQVDLAHLAGRDY---------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 393 nvqtkcLQLSGGNQQKV----V---------IGKWLnteanifIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISS 458
Cdd:PRK13548 133 ------PQLSGGEQQRVqlarVlaqlwepdgPPRWL-------LLDEPTSALDLAHQHHVLRLARQLAHERGlAVIVVLH 199
|
250 260
....*....|....*....|....
gi 433671570 459 ElpeiLNM----SDRILVVHEGKI 478
Cdd:PRK13548 200 D----LNLaaryADRIVLLHQGRL 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-105 |
5.98e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 9 KNLTKEFPGVRA-LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEiyiegkkledndpqkALEQLGITPIY 87
Cdd:PRK11819 10 NRVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE---------------ARPAPGIKVGY 74
|
90 100
....*....|....*....|
gi 433671570 88 --QELNLIPQLDVTENIFMG 105
Cdd:PRK11819 75 lpQEPQLDPEKTVRENVEEG 94
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-57 |
6.45e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 40.66 E-value: 6.45e-05
10 20 30
....*....|....*....|....*....|....*.
gi 433671570 22 DGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP 57
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
263-477 |
6.59e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 42.82 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLNR----KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGdIYVHGKKVKIdspkvalengiall 338
Cdd:cd03221 1 IELENLSKtyggKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVKI-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 339 tedrkeqglflkqsvkfniassnlkkyrenGFLNlqeqrkdairmvdnlniktpnvqtkclQLSGGNQQKVVIGKWLNTE 418
Cdd:cd03221 66 ------------------------------GYFE---------------------------QLSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 419 ANIFIFDEPTRGIDVGAKVEvfnIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGK 477
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEA---LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
401-471 |
7.55e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 7.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 433671570 401 LSGGNQQKVVIGKWLNTEAN---IFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELpEILNMSDRIL 471
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTADYII 902
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
274-476 |
8.09e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 43.86 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDiyVHGKKVKIDSPKVALENGIALLTEDRKEQG-LFLKQS 352
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK--VHWSNKNESEPSFEATRSRNRYSVAYAAQKpWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIA-SSNLKKYRENGFLnlqeqrkDAIRMVDNLNIKTPNVQTKC----LQLSGGNQQKVVIGKWLNTEANIFIFDEP 427
Cdd:cd03290 95 VEENITfGSPFNKQRYKAVT-------DACSLQPDIDLLPFGDQTEIgergINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 433671570 428 TRGIDVGAKVEVFN--IINDLVKKGNTVIMISSELpEILNMSDRILVVHEG 476
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
263-478 |
8.97e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 263 LRVENLN----RKGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSK--DSGDIYVHGKKVkidspkvalengIA 336
Cdd:PRK09580 2 LSIKDLHvsveDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDL------------LE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 337 LLTEDRKEQGLFLK---------QSVKF--NIASSNLKKYREN------GFLNLQEQRKDAIRMVDNLNIKTPNVQtkcl 399
Cdd:PRK09580 70 LSPEDRAGEGIFMAfqypveipgVSNQFflQTALNAVRSYRGQepldrfDFQDLMEEKIALLKMPEDLLTRSVNVG---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 400 qLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELPEILNM--SDRILVVHEGK 477
Cdd:PRK09580 146 -FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYikPDYVHVLYQGR 223
|
.
gi 433671570 478 I 478
Cdd:PRK09580 224 I 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
421-478 |
1.21e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.31 E-value: 1.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 421 IFIFDEPTRGIDVGAKVEVFNIINDLVKKGN-TVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGtTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
273-477 |
1.34e-04 |
|
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: 43.23 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGkkvkidspKVA-------LENGialltedrkeq 345
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAyvsqepwIQNG----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 346 glflkqSVKFNIAssnlkkyrenGFLNLQEQR-KDAIR---MVDNLNIKTPNVQT----KCLQLSGGNQQKVVIGKWLNT 417
Cdd:cd03250 81 ------TIRENIL----------FGKPFDEERyEKVIKacaLEPDLEILPDGDLTeigeKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 418 EANIFIFDEPTRGID--VGAKveVF-NIINDLVKKGNTVIMISSELpEILNMSDRILVVHEGK 477
Cdd:cd03250 145 DADIYLLDDPLSAVDahVGRH--IFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
132-214 |
1.40e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.76 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 132 RLGQESISpndlirdLGVGKQQMVEISKALSVETK---LLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDe 208
Cdd:cd03271 162 KLGQPATT-------LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD- 233
|
....*.
gi 433671570 209 VKKMAD 214
Cdd:cd03271 234 VIKCAD 239
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
274-319 |
1.92e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 1.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHG 319
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
271-481 |
2.09e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.94 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 271 KGVLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKVKIDSPKVaLENGIALLTEDRkeqgLFLK 350
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV-LRQGVAMVQQDP----VVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 351 QSVKFNIASSnlKKYRENGFLNLQE--QRKDAIR-MVDNLNIKtpnVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEP 427
Cdd:PRK10790 429 DTFLANVTLG--RDISEEQVWQALEtvQLAELARsLPDGLYTP---LGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 433671570 428 TRGIDVGAKVEVFNIINdLVKKGNTVIMISSELPEILNmSDRILVVHEGKITGR 481
Cdd:PRK10790 504 TANIDSGTEQAIQQALA-AVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
150-215 |
3.37e-04 |
|
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: 41.19 E-value: 3.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 150 GKQQMVEISKALSVETK----LLILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLdEVKKMADR 215
Cdd:cd03227 81 GEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP-ELAELADK 149
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
374-497 |
3.56e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 42.47 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 374 QEQRKDAIRMVDnlniKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVK-KGNT 452
Cdd:PRK10575 125 REKVEEAISLVG----LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQeRGLT 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 433671570 453 VIMIsseLPEIlNMS----DRILVVHEGKITGrfntdEASKEKIMSAAT 497
Cdd:PRK10575 201 VIAV---LHDI-NMAarycDYLVALRGGEMIA-----QGTPAELMRGET 240
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
259-433 |
3.88e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 259 GKESLRVENLnRKG----VL-NNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVhGKKVKI---DSPKVA 330
Cdd:PRK11819 321 GDKVIEAENL-SKSfgdrLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLayvDQSRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 331 LENgialltedrkeqglflKQSVKFNIASSNlkkyrengflnlqeqrkDAIRM----------VDNLNIKTPNVQTKCLQ 400
Cdd:PRK11819 399 LDP----------------NKTVWEEISGGL-----------------DIIKVgnreipsrayVGRFNFKGGDQQKKVGV 445
|
170 180 190
....*....|....*....|....*....|...
gi 433671570 401 LSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDV 433
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
401-456 |
3.95e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 3.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 401 LSGGNQQKVVIGKWL---NTEANIFIFDEPTRGI---DVGAKVEVFNiinDLVKKGNTVIMI 456
Cdd:COG0178 827 LSGGEAQRVKLASELskrSTGKTLYILDEPTTGLhfhDIRKLLEVLH---RLVDKGNTVVVI 885
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
400-479 |
5.05e-04 |
|
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: 41.65 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 400 QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGID--VGAKVEvfniinDLV-----KKGNTVIMISSElPEILNMSDRILV 472
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQII------DLLfelnrERGTTLVLVTHD-PALAARCDRVLR 218
|
....*..
gi 433671570 473 VHEGKIT 479
Cdd:COG4181 219 LRAGRLV 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
273-478 |
5.61e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGkkvkIDSPKVALENGIALLTEDRKEQGLFlKQS 352
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD----CDVAKFGLTDLRRVLSIIPQSPVLF-SGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFNIasSNLKKYRENGFLNLQEQR--KDAIRmvDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPTRG 430
Cdd:PLN03232 1326 VRFNI--DPFSEHNDADLWEALERAhiKDVID--RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 433671570 431 IDVGAKVEVFNIINDLVKKGnTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSC-TMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
401-471 |
6.63e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.45 E-value: 6.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 433671570 401 LSGGNQQKVVIGKWLNTEAN---IFIFDEPTRGI---DVGAKVEVFNiinDLVKKGNTVIMISSELpEILNMSDRIL 471
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEVLQ---RLVDKGNTVVVIEHNL-DVIKCADWII 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
273-478 |
7.17e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.44 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAI-----VGADSKDSGDIYVHGKKVkIDSPKVALENGIALLTE-DRKEQG 346
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDI-FKMDVIELRRRVQMVFQiPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 347 LFLKQSVKFNIASSNLKKYRENgflnLQEQRKDAIRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDE 426
Cdd:PRK14247 97 LSIFENVALGLKLNRLVKSKKE----LQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 433671570 427 PTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK14247 173 PTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
273-478 |
7.66e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGkkvkIDSPKVAlengialLTEDRKEQGLFLKQS 352
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG----CDISKFG-------LMDLRKVLGIIPQAP 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 353 VKFN-IASSNLKKYRENGFLNLQE--QR---KDAIRMvDNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDE 426
Cdd:PLN03130 1323 VLFSgTVRFNLDPFNEHNDADLWEslERahlKDVIRR-NSLGLDA-EVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 433671570 427 PTRGIDVGAKVEVFNIINDLVKKGnTVIMISSELPEILNmSDRILVVHEGKI 478
Cdd:PLN03130 1401 ATAAVDVRTDALIQKTIREEFKSC-TMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-222 |
8.29e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 14 EFPGVR---------ALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEIYIEGKKledndpqkaLEQLGIT 84
Cdd:PTZ00243 1310 VFEGVQmryreglplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE---------IGAYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 85 PIYQELNLIPQ----LD--VTENIFMGREKSKNEILGWID----RERMEEETKKILSRLgQESISpndlirDLGVGKQQM 154
Cdd:PTZ00243 1381 ELRRQFSMIPQdpvlFDgtVRQNVDPFLEASSAEVWAALElvglRERVASESEGIDSRV-LEGGS------NYSVGQRQL 1453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 155 VEISKALSVETKLLIL-DEPTSSLGKDETKELFDTMGTlKKQGVTMIFISHKLDEVKKMaDRVTVLRNG 222
Cdd:PTZ00243 1454 MCMARALLKKGSGFILmDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQY-DKIIVMDHG 1520
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
401-471 |
1.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433671570 401 LSGGNQQKVVIGKWLNTEAN--IFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSElPEILNMSDRIL 471
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRII 548
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1-51 |
1.04e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 433671570 1 MIEpFLKIKNLtkefpgvRALDGVDLEIkrGEVHAILGENGAGKSTLIKVL 51
Cdd:COG4637 1 MIT-RIRIKNF-------KSLRDLELPL--GPLTVLIGANGSGKSNLLDAL 41
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-177 |
1.08e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 21 LDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVHTP--TEGEIYIEGKkledndPQKAlEQLGITPIYQELNLI--PQL 96
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGF------PKKQ-ETFARISGYCEQNDIhsPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 97 DVTENIF------MGREKSKNEILGWIDR--ERMEEETKKilsrlgqESISPNDLIRDLGVGKQQMVEISKALSVETKLL 168
Cdd:PLN03140 969 TVRESLIysaflrLPKEVSKEEKMMFVDEvmELVELDNLK-------DAIVGLPGVTGLSTEQRKRLTIAVELVANPSII 1041
|
....*....
gi 433671570 169 ILDEPTSSL 177
Cdd:PLN03140 1042 FMDEPTSGL 1050
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
38-214 |
1.12e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 38 GENGAGKSTLIKVLTGVHTPTEGEIYIE-----GKKLEDndpQKALEQLGItpiyqelnlipqLDVtenIFMGRE---KS 109
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKLRQD---QFAFEEFTV------------LDT---VIMGHTelwEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 110 KNEilgwidRERM-------EEETKKIL---------------SRLGqesispnDLIRDLGVGKQQ----MVEIS----- 158
Cdd:PRK15064 96 KQE------RDRIyalpemsEEDGMKVAdlevkfaemdgytaeARAG-------ELLLGVGIPEEQhyglMSEVApgwkl 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 433671570 159 -----KALSVETKLLILDEPTSSLGKDETKELFDtmgTLKKQGVTMIFISHK---LDEV-KKMAD 214
Cdd:PRK15064 163 rvllaQALFSNPDILLLDEPTNNLDINTIRWLED---VLNERNSTMIIISHDrhfLNSVcTHMAD 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-177 |
1.37e-03 |
|
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: 40.61 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 6 LKIKNLTKEFP--GVRALDGVDLEIKRGEVHAILGENGAGKSTLIKVLTGVhTPTEGEIYIEGKKLEDNDPQKALEQLGI 83
Cdd:cd03289 3 MTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 84 tpiyqelnlIPQldvTENIFMGREKSKNEILG-WIDRE--RMEEET--KKILSRL-GQESISPNDLIRDLGVGKQQMVEI 157
Cdd:cd03289 82 ---------IPQ---KVFIFSGTFRKNLDPYGkWSDEEiwKVAEEVglKSVIEQFpGQLDFVLVDGGCVLSHGHKQLMCL 149
|
170 180
....*....|....*....|
gi 433671570 158 SKALSVETKLLILDEPTSSL 177
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHL 169
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-177 |
1.57e-03 |
|
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: 40.43 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 29 KRGEVHAILGENGAGKSTLIKVLTGVHTPTEGEI-----------YIEGKKLedndpQKALEQL---GITPIY--QELNL 92
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSEL-----QNYFTKLlegDVKVIVkpQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 93 IPqldvteNIFMGrekSKNEILGWIDRERMEEEtkkILSRLGQESISPNDlIRDLGVGKQQMVEISKALSVETKLLILDE 172
Cdd:cd03236 99 IP------KAVKG---KVGELLKKKDERGKLDE---LVDQLELRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFFDE 165
|
....*
gi 433671570 173 PTSSL 177
Cdd:cd03236 166 PSSYL 170
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
400-478 |
1.70e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.21 E-value: 1.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 400 QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLvKKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
401-456 |
1.84e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 1.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 433671570 401 LSGGNQQKVVIGKWLNTEAN---IFIFDEPTRGI---DVGAKVEVfniINDLVKKGNTVIMI 456
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIRKLLEV---LHRLVDKGNTVVVI 889
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
400-478 |
2.26e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.68 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 400 QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLV-KKGNTVIMISSELPEILNMSDRILVVHEGKI 478
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVqKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
400-496 |
2.30e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 400 QLSGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMISSELPEILNMSDRILVVHEGKIt 479
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTL- 213
|
90
....*....|....*..
gi 433671570 480 grfnTDEASKEKIMSAA 496
Cdd:PRK10938 214 ----AETGEREEILQQA 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
274-479 |
3.45e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIyVHGKKVKI-----DSPKVALENGIALLTEDRKEQGLF 348
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLIVarlqqDPPRNVEGTVYDFVAEGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 349 LKQ------SVKFNIASSNLKKYREngflnLQEQ-------RKDAiRMVDNLNIKTPNVQTKCLQLSGGNQQKVVIGKWL 415
Cdd:PRK11147 98 LKRyhdishLVETDPSEKNLNELAK-----LQEQldhhnlwQLEN-RINEVLAQLGLDPDAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 433671570 416 NTEANIFIFDEPTRGIDVGAK--VEVFniindLVKKGNTVIMISSELPEILNMSDRILVVHEGKIT 479
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIewLEGF-----LKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
273-478 |
7.02e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 38.22 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 273 VLNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHGKKV-KIDspkvalENGIALLtedRKEQGLFLKQ 351
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhQMD------EEARAKL---RAKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 352 SVKFNIASSNLKKYRENGFL---NLQEQRKDAIRMVDNLNIKTpNVQTKCLQLSGGNQQKVVIGKWLNTEANIFIFDEPT 428
Cdd:PRK10584 96 SFMLIPTLNALENVELPALLrgeSSRQSRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 433671570 429 RGID--VGAKVE--VFNIINDLvkkGNTVIMISSElPEILNMSDRILVVHEGKI 478
Cdd:PRK10584 175 GNLDrqTGDKIAdlLFSLNREH---GTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
274-319 |
7.16e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 7.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 433671570 274 LNNVSFKAYEGEVLGIAGLVGAGRTEIARAIVGADSKDSGDIYVHG 319
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
402-478 |
7.73e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.94 E-value: 7.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 433671570 402 SGGNQQKVVIGKWLNTEANIFIFDEPTRGIDVGAKVEVFNIINDLVKKGNTVIMIS--SELPEILNMSDRILVVHEGKI 478
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQ 289
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-216 |
8.73e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.01 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 18 VRALDGVDLEIKRGEVHAILGENGAGKSTLikvltgvhtpTEGEIYIEGKK--LEDNDP--QKALEQLGiTPIYQEL-NL 92
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQRryVESLSAyaRQFLGQMD-KPDVDSIeGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433671570 93 IPQLDVTENIFMGREKS----KNEILGWID--------RERMeeetkKILSRLGQESISPNDLIRDLGVGKQQMVEISKA 160
Cdd:cd03270 77 SPAIAIDQKTTSRNPRStvgtVTEIYDYLRllfarvgiRERL-----GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 433671570 161 LSVE-TKLL-ILDEPTSSLGKDETKELFDTMGTLKKQGVTMIFISHKLDEVkKMADRV 216
Cdd:cd03270 152 IGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTI-RAADHV 208
|
|
| |
