|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-500 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 780.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAG 82
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSR 162
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 163 ILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMMVGRP 242
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 243 LSDLFNKeRDIPRGQPRLRVEDLTDGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIH 322
Cdd:COG1129 241 LEDLFPK-RAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 323 SPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDANWGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGN 402
Cdd:COG1129 320 SPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 403 QQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAG 482
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDRE 479
|
490
....*....|....*...
gi 496082746 483 DISQESIMTLATGVNDSH 500
Cdd:COG1129 480 EATEEAIMAAATGGAAAA 497
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-489 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 559.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAA 81
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 GITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQS 161
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMMVGR 241
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 242 PLSDLFNKErDIPRGQPRLRVEDLT---DGG--KVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDG 316
Cdd:COG3845 241 EVLLRVEKA-PAEPGEVVLEVENLSvrdDRGvpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 317 EPVVIHSPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERD--ANWGMLNRRKAQTISDDAIQLLNIRVPHAQVR 394
Cdd:COG3845 320 EDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPpfSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 395 AGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGA 474
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
490
....*....|....*
gi 496082746 475 IAGELQAGDISQESI 489
Cdd:COG3845 480 IVGEVPAAEATREEI 494
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-493 |
0e+00 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 550.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAG 82
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSR 162
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 163 ILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS------LVRDklnapELVR 236
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfddmaqVDRD-----QLVQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 237 MMVGRPLSDLFN-KERdiPRGQPRLRVEDLTDGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEID 315
Cdd:PRK11288 236 AMVGREIGDIYGyRPR--PLGEVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 316 GEPVVIHSPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDANWGM-LNRRKAQTISDDAIQLLNIRVPHAQVR 394
Cdd:PRK11288 314 GKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGClINNRWEAENADRFIRSLNIKTPSREQL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 395 AGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGA 474
Cdd:PRK11288 394 IMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
490
....*....|....*....
gi 496082746 475 IAGELQAGDISQESIMTLA 493
Cdd:PRK11288 474 IAGELAREQATERQALSLA 492
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-495 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 546.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYT--ATSGEILIDGKPQTIRGPKDALA 80
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 AGITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQ 160
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMMVG 240
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 241 RPLSDLFNKE-RDIprGQPRLRVEDLTDGGKVKPS-------SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRK-ATGGV 311
Cdd:PRK13549 242 RELTALYPREpHTI--GEVILEVRNLTAWDPVNPHikrvddvSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 312 IEIDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDANWGMLNRRKAQTISDDAIQLLNIRVPHA 391
Cdd:PRK13549 320 IFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 392 QVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMR 471
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMH 479
|
490 500
....*....|....*....|....
gi 496082746 472 EGAIAGELQAGDISQESIMTLATG 495
Cdd:PRK13549 480 EGKLKGDLINHNLTQEQVMEAALR 503
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-495 |
0e+00 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 516.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGI 83
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGSELA-RGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSR 162
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 163 ILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMMVGRP 242
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 243 LSDLFNKeRDIPRGQPRLRVEDLTdGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIH 322
Cdd:PRK10762 242 LEDQYPR-LDKAPGEVRLKVDNLS-GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 323 SPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDAN-WGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGG 401
Cdd:PRK10762 320 SPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRaGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 402 NQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQA 481
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTR 479
|
490
....*....|....
gi 496082746 482 GDISQESIMTLATG 495
Cdd:PRK10762 480 EQATQEKLMAAAVG 493
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-492 |
2.46e-176 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 505.09 E-value: 2.46e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATS--GEILIDGKPQTIRGPKDALAAGI 83
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSL--VRDKLNAPELVRMMVGR 241
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLdcRADEVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 242 PLSDLFnKERDIPRGQPRLRVEDLT-------DGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGV---RKATGGV 311
Cdd:NF040905 241 DLEDRY-PERTPKIGEVVFEVKNWTvyhplhpERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygRNISGTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 312 IeIDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDANWGMLNRRKAQTISDDAIQLLNIRVPHA 391
Cdd:NF040905 320 F-KDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 392 QVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMR 471
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
490 500
....*....|....*....|.
gi 496082746 472 EGAIAGELQAGDISQESIMTL 492
Cdd:NF040905 479 EGRITGELPREEASQERIMRL 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-494 |
2.92e-160 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 464.64 E-value: 2.92e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAG 82
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLGSELARG----GLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALH 158
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 159 RQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS-LVRDKLNApELVRM 237
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSgMVSDVSND-DIVRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 238 MVGRPLSDLFNKERDIPR---GQPRLRVEDLT--DGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVI 312
Cdd:PRK09700 241 MVGRELQNRFNAMKENVSnlaHETVFEVRNVTsrDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 313 EIDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDAN----WGMLNRRKAQTISDDAIQLLNIRV 388
Cdd:PRK09700 321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGykgaMGLFHEVDEQRTAENQRELLALKC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 389 PHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVY 468
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
|
490 500
....*....|....*....|....*..
gi 496082746 469 VMREGAIAGELQAGD-ISQESIMTLAT 494
Cdd:PRK09700 481 VFCEGRLTQILTNRDdMSEEEIMAWAL 507
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-495 |
2.89e-153 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 446.80 E-value: 2.89e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALA 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 AGITLIYQEMQLAPNLTVAENIFLGseLARGGLVQRKAmlsqaQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQ 160
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFG--LPKRQASMQKM-----KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMMV- 239
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 240 ---GRPLSD-------LFNKERDIPRGQPRLRVEDLTDGGkVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATG 309
Cdd:PRK15439 239 aarEKSLSAsqklwleLPGNRRQQAAGAPVLTVEDLTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 310 GVIEIDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDANWgmLNRRKAQTISDDAIQLLNIRVP 389
Cdd:PRK15439 318 GRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCALTHNRRGFW--IKPARENAVLERYRRALNIKFN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 390 HAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYV 469
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLV 475
|
490 500
....*....|....*....|....*.
gi 496082746 470 MREGAIAGELQAGDISQESIMTLATG 495
Cdd:PRK15439 476 MHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-493 |
2.27e-147 |
|
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: 431.56 E-value: 2.27e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYT--ATSGEILIDGKPQTIRGPKDALAAGI 83
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGSELA-RGGLVQRKAMLSQAQAVIDRLGAQFKASDR-VMTLTIAEQQQVEIARALHRQS 161
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITlPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMMVGR 241
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 242 PLSDLFNKE-RDIprGQPRLRVEDLTDGGKVKPS-------SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRK-ATGGVI 312
Cdd:TIGR02633 241 EITSLYPHEpHEI--GDVILEARNLTCWDVINPHrkrvddvSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 313 EIDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDANWGMLNRRKAQTISDDAIQLLNIRVPHAQ 392
Cdd:TIGR02633 319 FINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 393 VRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMRE 472
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
490 500
....*....|....*....|.
gi 496082746 473 GAIAGELQAGDISQESIMTLA 493
Cdd:TIGR02633 479 GKLKGDFVNHALTQEQVLAAA 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-494 |
4.59e-142 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 417.59 E-value: 4.59e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 9 MRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITLIYQ 88
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 89 EMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDE 168
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 169 PTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMMVGRPLSDLFN 248
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 249 KERDIPrGQPRLRVEDLTDggKVKPS----SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSP 324
Cdd:PRK10982 241 DKENKP-GEVILEVRNLTS--LRQPSirdvSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 325 REAIDLGIGFLTENRKEQGLFLELAAQENITMATLERDAN-WGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQ 403
Cdd:PRK10982 318 NEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNkVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 404 QKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGD 483
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKT 477
|
490
....*....|.
gi 496082746 484 ISQESIMTLAT 494
Cdd:PRK10982 478 TTQNEILRLAS 488
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
256-475 |
1.79e-86 |
|
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: 263.91 E-value: 1.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 256 GQPRLRVEDLTDGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFL 335
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 TENRKEQGLFLELAAQENITMATLerdanwgmlnrrkaqtisddaiqllnirvphaqvraggLSGGNQQKLLISRWVAIG 415
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 416 PRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-223 |
7.95e-83 |
|
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: 253.89 E-value: 7.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITLI 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQemqlapnltvaeniflgselargglvqrkamlsqaqavidrlgaqfkasdrvmtLTIAEQQQVEIARALHRQSRILVM 166
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 167 DEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-475 |
2.57e-65 |
|
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: 219.77 E-value: 2.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAF--GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTAT---SGEILIDGKPqTIRGPKDA 78
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD-LLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 79 LAAGITLIYQE--MQLAPnLTVAENIflgSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARA 156
Cdd:COG1123 81 RGRRIGMVFQDpmTQLNP-VTVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSL-VRDKLNAPEL 234
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGpPEEILAAPQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 235 VRmMVGRPLSDLFNKERDIPRGQPRLRVEDLT---DGGKVKPS------SLVVHAGEIVGLAGLVGAGRSELAQLIFGVR 305
Cdd:COG1123 237 LA-AVPRLGAARGRAAPAAAAAEPLLEVRNLSkryPVRGKGGVravddvSLTLRRGETLGLVGESGSGKSTLARLLLGLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 306 KATGGVIEIDGEPVVIHSPREAIDLGigfltenRKEQGLFLELAAQENITMaTLERD-----ANWGMLNRRKAQTISDDA 380
Cdd:COG1123 316 RPTSGSILFDGKDLTKLSRRSLRELR-------RRVQMVFQDPYSSLNPRM-TVGDIiaeplRLHGLLSRAERRERVAEL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 381 IQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPE 459
Cdd:COG1123 388 LERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAV 467
|
490
....*....|....*.
gi 496082746 460 VVGMSDRVYVMREGAI 475
Cdd:COG1123 468 VRYIADRVAVMYDGRI 483
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-219 |
3.44e-58 |
|
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: 192.65 E-value: 3.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITLI 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGLV-------QRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHR 159
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 160 QSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-219 |
1.59e-56 |
|
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: 189.09 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAG 82
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLGSELARGGLV------------QRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQ 150
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 151 VEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-219 |
6.34e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.33 E-value: 6.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqTIRGPKDALAAgITLI 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED-VARDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGLVQRKAmlsQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVM 166
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARE---RIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 167 DEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-219 |
8.02e-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: 157.94 E-value: 8.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDALAAGITLI 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--IKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIflgsELARGglvqrkaMlsqaqavidrlgaqfkasdrvmtltiaeQQQVEIARALHRQSRILVM 166
Cdd:cd03230 79 PEEPSLYENLTVRENL----KLSGG-------M----------------------------KQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 167 DEPTAAL--SSRetQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03230 120 DEPTSGLdpESR--REFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-224 |
5.49e-45 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 158.10 E-value: 5.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRgPKDALAAgITL 85
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQ-IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILV 165
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 166 MDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ--YVGSL 224
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKvvAQGSL 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-219 |
8.53e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.13 E-value: 8.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAFG----KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDAL 79
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS-SLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 80 AA------GItlIYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEI 153
Cdd:COG1136 81 ARlrrrhiGF--VFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 154 ARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMaEVYELSDRVSVLRDGQ 219
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-221 |
8.58e-45 |
|
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: 156.83 E-value: 8.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITLI 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGlvQRKAMLSQAQAVIDRLGAqfKASDRVMTLTIAEQQQVEIARALHRQSRILVM 166
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRA--KRKARLERVYELFPRLKE--RRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 167 DEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-219 |
7.10e-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: 154.18 E-value: 7.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFG----KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqTIRGPKDALAA- 81
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTD-ISKLSEKELAAf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 ---GITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAmlsQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALH 158
Cdd:cd03255 80 rrrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRE---RAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 159 RQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMaEVYELSDRVSVLRDGQ 219
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-219 |
2.98e-43 |
|
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: 152.29 E-value: 2.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITLI 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGLVQRKAmlsQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVM 166
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRA---RVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 167 DEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
17-219 |
1.20e-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: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 17 GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQ--EMQLAp 94
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGLVFQnpDDQFF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 95 NLTVAENIFLGSELaRGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALS 174
Cdd:cd03225 90 GPTVEEEVAFGLEN-LG--LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 175 SRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-219 |
2.45e-40 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 145.17 E-value: 2.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 17 GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQ--EMQL-A 93
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE-LRRKVGLVFQnpDDQLfA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 94 PnlTVAENIFLGSElARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAAL 173
Cdd:COG1122 91 P--TVEEDVAFGPE-NLG--LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496082746 174 SSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-221 |
2.93e-40 |
|
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: 151.98 E-value: 2.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAF-----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPK 76
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 77 D--ALAAGITLIYQ--EMQLAPNLTVAEniflgsELARG----GLVQRKAMLSQAQAVIDR--LGAQFkASDRVMTLTIA 146
Cdd:COG1123 336 SlrELRRRVQMVFQdpYSSLNPRMTVGD------IIAEPlrlhGLLSRAERRERVAELLERvgLPPDL-ADRYPHELSGG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 147 EQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-219 |
3.85e-40 |
|
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: 144.74 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGI 83
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGSELARGGlvqrkamlSQAQAVIDRLGAQF-----KASDRVMTLTIAEQQQVEIARALH 158
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDR--------AEVRADLERVYELFprlkeRRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 159 RQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
7.27e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.46 E-value: 7.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKdala 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 agITLIYQEMQLAPN--LTVAENIFLGSeLARGGLVQR--KAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARA 156
Cdd:COG1121 77 --IGYVPQRAEVDWDfpITVRDVVLMGR-YGRRGLFRRpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQY 220
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
9.29e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.46 E-value: 9.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTAT-PVLEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGP 75
Cdd:COG1116 1 MSAAaPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 76 KdalaagITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAmlsQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIAR 155
Cdd:COG1116 81 D------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRE---RARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 156 ALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAE-VYeLSDRVSVLRDG 218
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEaVF-LADRVVVLSAR 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-171 |
2.30e-39 |
|
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: 139.71 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAAGITLIYQEMQLAPNLTVAEN 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 102 IFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVM----TLTIAEQQQVEIARALHRQSRILVMDEPTA 171
Cdd:pfam00005 80 LRLGLLLKG---LSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-219 |
5.21e-39 |
|
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: 140.01 E-value: 5.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP-QTIRGPKDALAAGITL 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLGselargglvqrkamLSQAQavidrlgaqfkasdrvmtltiaeQQQVEIARALHRQSRILV 165
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------LSGGQ-----------------------QQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 166 MDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-219 |
4.13e-38 |
|
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: 137.56 E-value: 4.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAfgkfYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGIT 84
Cdd:cd03215 3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LI---YQEMQLAPNLTVAENIFLGSELArGGlvqrkamlsqaqavidrlgaqfkasdrvmtltiaEQQQVEIARALHRQS 161
Cdd:cd03215 79 YVpedRKREGLVLDLSVAENIALSSLLS-GG----------------------------------NQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-219 |
7.06e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.16 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTirgpkdALAA- 81
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT------GLPPe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 --GITLIYQEMQLAPNLTVAENI-FlgselargGLVQRK----AMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIA 154
Cdd:COG3842 76 krNVGMVFQDYALFPHLTVAENVaF--------GLRMRGvpkaEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 155 RALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-221 |
8.56e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.04 E-value: 8.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKD--ALAA 81
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 GITLIYQEMQLAPNLTVAENIFLGSeLARGGLVQ------RKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIAR 155
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGR-LGRTSTWRsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 156 ALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-224 |
1.42e-37 |
|
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: 137.22 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFG----KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPkdalAAG 82
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP--VTGP----GPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGaqfkasdrvmtLTIAE-----------QQQV 151
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVG-----------LSGFEnayphqlsggmRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 152 EIARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVL--RDGQYVGSL 224
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-219 |
2.28e-37 |
|
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: 136.51 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPK-DALAAGITL 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLGSELARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILV 165
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 166 MDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-223 |
4.75e-37 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 136.21 E-value: 4.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTirgPKDALAAGITLI 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---NLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIdRLGAQfkASDRVMTLTIAEQQQVEIARALHRQSRILVM 166
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLV-QLEGY--ANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 167 DEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDG--QYVGS 223
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGkiQQIGT 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-221 |
1.63e-36 |
|
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: 134.33 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIrgpkdalAAGITLI 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-------AARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 Y--QEMQLAPNLTVAEN-IFLGSelARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:cd03269 74 YlpEERGLYPKMKVIDQlVYLAQ--LKG--LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-240 |
3.10e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 140.55 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHI-AKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGI 83
Cdd:COG3845 256 VVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQE---MQLAPNLTVAENIFLGS----ELARGGLVQRKAMLSQAQAVIDRlgaqFK-----ASDRVMTLTIAEQQQV 151
Cdd:COG3845 336 AYIPEDrlgRGLVPDMSVAENLILGRyrrpPFSRGGFLDRKAIRAFAEELIEE----FDvrtpgPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 152 EIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNA 231
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATR 491
|
....*....
gi 496082746 232 PELVRMMVG 240
Cdd:COG3845 492 EEIGLLMAG 500
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-219 |
3.76e-36 |
|
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: 131.60 E-value: 3.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 8 EMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKdALAAGITLIY 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 88 QemqlapnltvaeniflgselargglvqrkamLSQAQavidrlgaqfkasdrvmtltiaeQQQVEIARALHRQSRILVMD 167
Cdd:cd00267 80 Q-------------------------------LSGGQ-----------------------RQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496082746 168 EPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-219 |
6.02e-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: 134.02 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITL 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLGsELARGGLVQR--KAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALG-RYPHLGLFGRpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-233 |
6.19e-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: 133.48 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFG----KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKD--AL 79
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 80 AAGITLIYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHR 159
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAG---VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 160 QSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGS-LVRDKLNAPE 233
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEgTVEEVFANPQ 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-218 |
1.94e-35 |
|
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: 131.72 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGK----FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpQTIRGPKDALAaG 82
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF-DVVKEPAEARR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIflgseLARGGL--VQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQ 160
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENL-----EYFAGLygLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-475 |
3.93e-35 |
|
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: 137.89 E-value: 3.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGK----FYALKGVDLTVWPGEIHALMGENGAGKS----TLMKILAGAYTATSGEILIDGKP--- 69
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 70 ------QTIRGpkdalaAGITLIYQE-M-QLAPNLTVAENIFLGSELARGglVQRKAMLSQAQAVIDRLG---AQFKASD 138
Cdd:COG4172 81 lserelRRIRG------NRIAMIFQEpMtSLNPLHTIGKQIAEVLRLHRG--LSGAAARARALELLERVGipdPERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 139 RVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALS-SRETQRLfELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLR 216
Cdd:COG4172 153 YPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDvTVQAQIL-DLLKDLqRELGMALLLITHDLGVVRRFADRVAVMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 217 DGQYV--GSlVRDKLNAPE--LVRMmvgrplsdLFNKErdiPRGQPR---------LRVEDL-------------TDGGK 270
Cdd:COG4172 232 QGEIVeqGP-TAELFAAPQhpYTRK--------LLAAE---PRGDPRpvppdapplLEARDLkvwfpikrglfrrTVGHV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 --VKPSSLVVHAGEIVGLAGLVGAGRSELAQ----LIfgvrkATGGVIEIDGEPVVIHSPREAI----DLGIGF------ 334
Cdd:COG4172 300 kaVDGVSLTLRRGETLGLVGESGSGKSTLGLallrLI-----PSEGEIRFDGQDLDGLSRRALRplrrRMQVVFqdpfgs 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 335 ----------LTENRKEQGLFLELAAQENITMATLER---DANwgMLNrrkaqtisddaiqllniRVPHAqvraggLSGG 401
Cdd:COG4172 375 lsprmtvgqiIAEGLRVHGPGLSAAERRARVAEALEEvglDPA--ARH-----------------RYPHE------FSGG 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 402 NQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-219 |
3.93e-35 |
|
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: 130.45 E-value: 3.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITLI 86
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGL------VQRKAMLSQAQAVIDRLGAQfkasdrvmtLTIAEQQQVEIARALHRQ 160
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKdeiderVREVAELLQIEHLLDRKPKQ---------LSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 161 SRILVMDEPTAALSS--RETQRLfELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03301 149 PKVFLMDEPLSNLDAklRVQMRA-ELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-228 |
9.09e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 132.15 E-value: 9.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtiRGPKDALAAGitl 85
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 iY--QEMQLAPNLTVAENI-FLGsELaRGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSR 162
Cdd:COG4152 75 -YlpEERGLYPKMKVGEQLvYLA-RL-KG--LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 163 ILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV--GSL--VRDK 228
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsGSVdeIRRQ 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-223 |
9.56e-35 |
|
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: 129.26 E-value: 9.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpqTIRGPKDALA-AGITL 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRrIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEmqLAPNLTVAENIFLgseLARGGLVQRKAmlsqAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILV 165
Cdd:cd03268 79 EAPG--FYPNLTARENLRL---LARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 166 MDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-227 |
2.71e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqTIRGPKDALAA--- 81
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD-LSRLKRREIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 GITLIYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQS 161
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTG---KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQyvgsLVRD 227
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR----LVRD 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-236 |
3.06e-34 |
|
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: 128.84 E-value: 3.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFG-KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKD--ALAAGI 83
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGSeLARGGLVQ------RKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARAL 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGR-LGRRSTWRslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 158 HRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVR 236
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-221 |
3.32e-34 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 128.39 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAA 81
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 G--ITLIYQEMQLA--PNLTVAENIflgSELARGGLVQRKAmlSQAQAVIDRLGAQFKASDRVMTLTIAE-----QQQVE 152
Cdd:cd03257 81 RkeIQMVFQDPMSSlnPRMTIGEQI---AEPLRIHGKLSKK--EARKEAVLLLLVGVGLPEEVLNRYPHElsggqRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 153 IARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-219 |
4.89e-34 |
|
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: 127.62 E-value: 4.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGK--FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDALAAGIT 84
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS--IRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LIYQEMQLAPNLTVAENIFLGSELaRGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRIL 164
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARL-KG--LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 165 VMDEPTAALSSRETQRLFELILRLRdEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-219 |
6.62e-34 |
|
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: 125.96 E-value: 6.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFG--KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRG-PKDALAAGI 83
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD--LRDlDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLApNLTVAENIFlgSelarGGlvqrkamlsqaqavidrlgaqfkasdrvmtltiaEQQQVEIARALHRQSRI 163
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENIL--S----GG----------------------------------QRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRDeGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
260-487 |
1.66e-33 |
|
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: 126.90 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTD--GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAIDLgIGFL 335
Cdd:COG4555 2 IEVENLSKkyGKVpaLKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 TENRkeqGLFLELAAQENITM-ATLerdanWGMLNRRKAQTIsDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAI 414
Cdd:COG4555 80 PDER---GLYDRLTVRENIRYfAEL-----YGLFDEELKKRI-EELIELLGLE-EFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 415 GPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQE 487
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-218 |
4.50e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 126.26 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDALAA- 81
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH--IEGLPGHQIAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 -GITLIYQEMQLAPNLTVAENIF------LGSELARGGL-------VQRKAmLSQAQAVIDRLGAQFKASDRVMTLTIAE 147
Cdd:PRK11300 80 mGVVRTFQHVRLFREMTVIENLLvaqhqqLKTGLFSGLLktpafrrAESEA-LDRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 148 QQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-219 |
1.52e-32 |
|
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: 124.08 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKD 77
Cdd:COG4181 4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF-ALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 78 ALAA----GITLIYQEMQLAPNLTVAENIFLGSELARgglvQRKAMlSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEI 153
Cdd:COG4181 83 ARARlrarHVGFVFQSFQLLPTLTALENVMLPLELAG----RRDAR-ARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 154 ARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAeVYELSDRVSVLRDGQ 219
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPA-LAARCDRVLRLRAGR 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-219 |
1.92e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.80 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRgpKDALAAGITLI 86
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN--LPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENI-FlgselargGLVQRKAMLSQAQAVIDRLGAQFKASDrvmtltIAE---------QQQ-VEIAR 155
Cdd:COG1118 81 FQHYALFPHMTVAENIaF--------GLRVRPPSKAEIRARVEELLELVQLEG------LADrypsqlsggQRQrVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 156 ALHRQSRILVMDEPTAAL--SSRETQR--LFELilrLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALdaKVRKELRrwLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-219 |
2.00e-32 |
|
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: 123.94 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGK--PQTIRGPKDAL 79
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdiTGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 80 AAGITLIYQEMQLAPNLTVAENIFLGseLARGGLVQRKAMLSQAQAVIDRLGaqfkasdrvmtLTIAEQQ---------- 149
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFP--LREHTDLSEAEIRELVLEKLELVG-----------LPGAADKmpselsggmr 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 150 -QVEIARALHRQSRILVMDEPTAAL---SSREtqrLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1127 148 kRVALARALALDPEILLYDEPTAGLdpiTSAV---IDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-219 |
2.11e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 123.13 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqTIRGPKDALAA--- 81
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGED-VNRLRGRQLPLlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 GITLIYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQS 161
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENVALPLEVRG---KKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-229 |
2.49e-32 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 123.44 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAG-----AYTATSGEILIDGKPqtIRGPKD---A 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKD--IYDLDVdvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 79 LAAGITLIYQEmqlaPNL---TVAENIFLGSELArgGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIA--EQQQVEI 153
Cdd:cd03260 79 LRRRVGMVFQK----PNPfpgSIYDNVAYGLRLH--GIKLKEELDERVEEALRKAALWDEVKDRLHALGLSggQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 154 ARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKL 229
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-221 |
4.14e-32 |
|
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: 122.83 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYaLKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDAlaaGITLI 86
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAV--IDRLgaqfkaSDR-VMTLTIAEQQQVEIARALHRQSRI 163
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMlgIDHL------LNRkPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-223 |
5.55e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.57 E-value: 5.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITLI 86
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENI-FlgselargGLVQRKAmlsqAQAVIDRlgaqfkasdRVM----TLTIAE------------QQ 149
Cdd:COG3839 81 FQSYALYPHMTVYENIaF--------PLKLRKV----PKAEIDR---------RVReaaeLLGLEDlldrkpkqlsggQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 150 Q-VEIARALHRQSRILVMDEPTAAL--SSRETQRLfELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG--QYVGS 223
Cdd:COG3839 140 QrVALGRALVREPKVFLLDEPLSNLdaKLRVEMRA-EIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGriQQVGT 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-215 |
1.41e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 120.72 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 8 EMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITLIY 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 88 QEMqlapNLTVAENIFLGSELARGGLV-QRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVM 166
Cdd:cd03235 81 RDF----PISVRDVVLMGLYGHKGLFRrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 167 DEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVL 215
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-200 |
1.63e-31 |
|
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: 120.28 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDALAAGIT 84
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP--IRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LIYQEMQLAPNLTVAENI-FLGSelARGGLVQRkamlSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:COG4133 79 YLGHADGLKPELTVRENLrFWAA--LYGLRADR----EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISH 200
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
260-475 |
2.74e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.55 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTD--GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAIDLgIGFL 335
Cdd:COG1131 1 IEVRGLTKryGDKtaLDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 TEnrkEQGLFLELAAQENIT-MATLERdanwgmLNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAI 414
Cdd:COG1131 79 PQ---EPALYPDLTVRENLRfFARLYG------LPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 415 GPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-475 |
3.15e-31 |
|
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: 126.46 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAG--AYTATSGEILI----------------DGK 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 69 PQTIRG------------PKDALAAGIT-----LIYQEMQLAPNLTVAENIFlgSELARGGLVQRKAMlSQAQAVIDrlg 131
Cdd:TIGR03269 81 PCPVCGgtlepeevdfwnLSDKLRRRIRkriaiMLQRTFALYGDDTVLDNVL--EALEEIGYEGKEAV-GRAVDLIE--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 132 aQFKASDRVM----TLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVY 206
Cdd:TIGR03269 155 -MVQLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 207 ELSDRVSVLRDGQYVgslvrdKLNAPELV--RMMVGRPLsdlFNKERDIPRGQPRLRVEDLT------DGGKVKPS---S 275
Cdd:TIGR03269 234 DLSDKAIWLENGEIK------EEGTPDEVvaVFMEGVSE---VEKECEVEVGEPIIKVRNVSkryisvDRGVVKAVdnvS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 276 LVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEID-GEPVVIHSPREAIDLG-----IGFLtenRKEQGLFLELA 349
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRGrakryIGIL---HQEYDLYPHRT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENITMA-TLERDANwgmLNRRKAQTI-------SDDAIQLLNiRVPHAqvraggLSGGNQQKLLISRWVAIGPRILIL 421
Cdd:TIGR03269 382 VLDNLTEAiGLELPDE---LARMKAVITlkmvgfdEEKAEEILD-KYPDE------LSEGERHRVALAQVLIKEPRIVIL 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 422 DEPTRGVDVGAKSEIYR-IMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-219 |
4.06e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 120.48 E-value: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRGPKDALAA---G 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDG--EDLTDSKKDINKlrrK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLGSELARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSR 162
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPIKVKK--MSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 163 ILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-238 |
1.29e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 118.78 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITLI 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGLvqrkamlsqaQAVIDRLGAQFKASDRVMT-----LTIAEQQQVEIARALHRQS 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS----------RKIPDEIYELFPVLKEMLGrrggdLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMM 238
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYL 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-219 |
1.30e-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: 126.10 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 20 YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRG-PKDALAAGITLIYQEmqlaPNL-- 96
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID--LRQiDPASLRRQIGVVLQD----VFLfs 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 97 -TVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKA--SDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAAL 173
Cdd:COG2274 563 gTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTvvGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496082746 174 SSRETQRLFELILRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:COG2274 643 DAETEAIILENLRRLL-KGRTVIIIAHRLSTI-RLADRIIVLDKGR 686
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-219 |
1.96e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 116.77 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 8 EMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKdalaagitliy 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 88 qemqlapnltvaeniflgsELARgglvqRKAMLSQAqavIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMD 167
Cdd:cd03214 70 -------------------ELAR-----KIAYVPQA---LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 168 EPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-219 |
3.01e-30 |
|
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: 117.83 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDAlaaGITLI 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGG------LVQRKAM----LSQAQAVIDRLGAQfkasdrvmtLTIAEQQQVEIARA 156
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSerppeaEIRAKVHellkLVQLDWLADRYPAQ---------LSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
275-487 |
4.18e-30 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 117.15 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTENRkeqGLFLELAAQENI 354
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPELTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMAtlerdanWGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:cd03224 97 LLG-------AYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 435 EIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQE 487
Cdd:cd03224 170 EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-236 |
5.96e-30 |
|
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: 116.87 E-value: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALA-AGITL 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKRArLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILV 165
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 166 MDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVR 236
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
275-478 |
6.39e-30 |
|
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: 114.83 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTEnrkeqglflelaaqeni 354
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 tmatlerdanwgmlnrrkaqtisddaiqllnirvphaqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496082746 435 EIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:cd03216 120 RLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-223 |
1.16e-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: 115.47 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 12 IAKAFGKFyALKgVDLTVwPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP------QTIRGPKDAlaaGITL 85
Cdd:cd03297 6 IEKRLPDF-TLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkKINLPPQQR---KIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLGSELARgglvqRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILV 165
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKRKR-----NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 166 MDEPTAAL-SSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:cd03297 155 LDEPFSALdRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-221 |
1.33e-29 |
|
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: 115.76 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQEMQLApNLTVAE 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRET 178
Cdd:cd03245 97 NITLGAPLADDERILRAAELAGVTDFVNKHpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 179 QRLFELILRLRdEGMAIIYISHRMAeVYELSDRVSVLRDGQYV 221
Cdd:cd03245 177 ERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-221 |
1.88e-29 |
|
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: 114.90 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 26 DLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITLIYQEMQLAPNLTVAENIFLG 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 106 -SELARGGLVQRKAMlsqaQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFEL 184
Cdd:cd03298 95 lSPGLKLTAEDRQAI----EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 496082746 185 ILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03298 171 VLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-218 |
2.91e-29 |
|
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: 114.43 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFY-ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqTIRGPKDALA---AG 82
Cdd:cd03292 1 IEFINVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-VSDLRGRAIPylrRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLGSEL--ARGGLVQRKAMlsqaqAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQ 160
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVtgVPPREIRKRVP-----AALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-221 |
3.10e-29 |
|
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: 116.20 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 12 IAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAA----GITLIY 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRElrrkKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 88 QEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMD 167
Cdd:cd03294 109 QSFALLPHRTVLENVAFGLEVQG---VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 168 EPTAALS---SRETQrlfELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03294 186 EAFSALDpliRREMQ---DELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-222 |
3.11e-29 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 114.91 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKD--ALAAGIT 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LIYQEMQLAPNLTVAENI-FLGSELARG--GLVQRKAMLsqaqaVIDRLGaqFKASDRVMTltiAE-----QQQVEIARA 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVaFPLREHTRLseEEIREIVLE-----KLEAVG--LRGAEDLYP---AElsggmKKRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVG 222
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-219 |
3.30e-29 |
|
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: 121.02 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAAGITLIYQEMQLaPNLTVAE 100
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRRQIAWVPQNPYL-FAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRET 178
Cdd:COG4988 430 NLRLGRPDASDEELEAALEAAGLDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 179 QRLFELILRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:COG4988 510 AEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGR 548
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-221 |
3.76e-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: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 11 HIAKAFGKFY-ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtiRGPKDALAAgITLIYQE 89
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKS-IGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 90 M--QLAPNlTVAENIFLGSELARGGlvqrkamLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMD 167
Cdd:cd03226 80 VdyQLFTD-SVREELLLGLKELDAG-------NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 168 EPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-221 |
3.86e-29 |
|
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: 114.63 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRG-PKDALAAGITLIYQEMQLAPNlTVA 99
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID--IRDiSRKSLRSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRE 177
Cdd:cd03254 95 ENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496082746 178 TQRLFELILRLRDEGMAIIyISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:cd03254 175 EKLIQEALEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDGKII 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-236 |
4.88e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 114.59 E-value: 4.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP----QTIRGPKDALA 80
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitdwQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 agitLIYQEMQLAPNLTVAENiflgseLARGGLVQRKamlSQAQAVIDRLGAQF-----KASDRVMTLTIAEQQQVEIAR 155
Cdd:PRK11614 84 ----IVPEGRRVFSRMTVEEN------LAMGGFFAER---DQFQERIKWVYELFprlheRRIQRAGTMSGGEQQMLAIGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 156 ALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELV 235
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
.
gi 496082746 236 R 236
Cdd:PRK11614 231 R 231
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-212 |
6.35e-29 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 113.48 E-value: 6.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 9 MRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRGPKDALAAG-----I 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNG--QETPPLNSKKASKfrrekL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAqavIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEA---LEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMaEVYELSDRV 212
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRV 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-219 |
7.61e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.44 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAAGITLI 86
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA-AWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGseLARGGLVQRKAmLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARAL-------HR 159
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALG--RAPHGSSAAQD-RQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 160 QSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISH--RMAEVYelSDRVSVLRDGQ 219
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlNLAAQY--ADRILLLHQGR 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-475 |
8.09e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 120.35 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKS----TLMKIL--AGAyTATSGEIL--------IDG 67
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGG-LVQCDKMLlrrrsrqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 68 KPQTIRGPKDALAAGITLIYQE--MQLAPNLTVAENIFLGSELARG-----GLVQRKAMLSQ-----AQAVIDRLGAQFK 135
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGasreeAMVEAKRMLDQvripeAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 136 ASDRvmtltiaeqQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSV 214
Cdd:PRK10261 171 GGMR---------QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 215 LRDGQYV--GSL-----------VRDKLNAPELVRMMVGR------PLSDLFNKERDIPR--------GQPRLRVEDLTD 267
Cdd:PRK10261 242 MYQGEAVetGSVeqifhapqhpyTRALLAAVPQLGAMKGLdyprrfPLISLEHPAKQEPPieqdtvvdGEPILQVRNLVT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 268 -----GGKVKPSSLVVHA----------GEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPR--EAIDL 330
Cdd:PRK10261 322 rfplrSGLLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 331 GIGFLTenrkeQGLFLELAAQENITMATLERDANWGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISR 410
Cdd:PRK10261 402 DIQFIF-----QDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIAR 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 411 WVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-473 |
1.06e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.04 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALK----GVDLTVWPGEIHALMGENGAGKS----TLMKIL-AGAYTATSGEILIDGKP---- 69
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTVRtvvnDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESllha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 70 --QTIRGPKdalAAGITLIYQE--MQLAPNLTVAENIFLGSELARGglVQRKAMLSQAQAVIDRLG---AQFKASDRVMT 142
Cdd:PRK15134 82 seQTLRGVR---GNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRG--MRREAARGEILNCLDRVGirqAAKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 143 LTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 222 GSLVRDKL-NAPE---LVRMMVGRPLSDLFNKERDIPrgqPRLRVEDL-------------TDGGK--VKPSSLVVHAGE 282
Cdd:PRK15134 237 EQNRAATLfSAPThpyTQKLLNSEPSGDPVPLPEPAS---PLLDVEQLqvafpirkgilkrTVDHNvvVKNISFTLRPGE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 283 IVGLAGLVGAGRS----ELAQLIfgvrkATGGVIEIDGEPVVIHSPREaidlgigFLTENRKEQGLFlelaaqenitmat 358
Cdd:PRK15134 314 TLGLVGESGSGKSttglALLRLI-----NSQGEIWFDGQPLHNLNRRQ-------LLPVRHRIQVVF------------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 359 leRDANWGMLNRRKAQTISDDAIQL----LNIRVPHAQVRAG----GL------------SGGNQQKLLISRWVAIGPRI 418
Cdd:PRK15134 369 --QDPNSSLNPRLNVLQIIEEGLRVhqptLSAAQREQQVIAVmeevGLdpetrhrypaefSGGQRQRIAIARALILKPSL 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 419 LILDEPTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-221 |
1.39e-28 |
|
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: 112.85 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG-----KPQTIRgpkdalaA 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvrEPREVR-------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 GITLIYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQS 161
Cdd:cd03265 74 RIGIVFQDLSVDDELTGWENLYIHARLYG---VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
7-223 |
1.51e-28 |
|
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: 116.35 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRhIAKAFGKFyALKgVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP-QtirgpkDAlAAGITL 85
Cdd:COG4148 3 LEVD-FRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQ------DS-ARGIFL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 ---------IYQEMQLAPNLTVAENIFLGseLARGGLVQRKAMLSQaqaVIDRLGAQFKASDRVMTLTIAEQQQVEIARA 156
Cdd:COG4148 73 pphrrrigyVFQEARLFPHLSVRGNLLYG--RKRAPRAERRISFDE---VVELLGIGHLLDRRPATLSGGERQRVAIGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-221 |
1.95e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.47 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKI---LAGAYTA--TSGEILIDGKpQTIRGPKDALA 80
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQ-DIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 AGITLIYQEMQLAPNLTVAENIFLGSELARggLVQRKAMLSQ--------AQ---AVIDRLGAQfkasdrVMTLTIAEQQ 149
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNR--LVKSKKELQErvrwalekAQlwdEVKDRLDAP------AGKLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 150 QVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-219 |
3.02e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 20 YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRG-PKDALAAGITLIYQEMQLApNLTV 98
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD--IRDlTLESLRRQIGVVPQDTFLF-SGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSR 176
Cdd:COG1132 431 RENIRYGRPDATDEEVEEAAKAAQAHEFIEALpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 177 ETQRLFELILRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:COG1132 511 TEALIQEALERLM-KGRTTIVIAHRLSTI-RNADRILVLDDGR 551
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
260-475 |
9.71e-28 |
|
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: 110.99 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTD--GG--KVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGfl 335
Cdd:cd03219 1 LEVRGLTKrfGGlvALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 tenRKEQ--GLFLELAAQENITMATLERDAN--WGMLNRRKAQTISDDAIQLLNiRV---PHAQVRAGGLSGGNQQKLLI 408
Cdd:cd03219 79 ---RTFQipRLFPELTVLENVMVAAQARTGSglLLARARREEREARERAEELLE-RVglaDLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 409 SRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-203 |
1.19e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRGPKDA-----LA 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDerlirQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 AGitLIYQEMQLAPNLTVAENIFLGSELARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQ 160
Cdd:PRK09493 79 AG--MVFQQFYLFPHLTALENVMFGPLRVRG--ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMA 203
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
260-473 |
2.11e-27 |
|
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: 107.87 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTD--GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvIHSPREAIDLGIGFL 335
Cdd:cd03230 1 IEVRNLSKryGKKtaLDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--IKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 TEnrkEQGLFLELAAQENITmatlerdanwgmlnrrkaqtisddaiqllnirvphaqvraggLSGGNQQKLLISRWVAIG 415
Cdd:cd03230 79 PE---EPSLYENLTVRENLK------------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 416 PRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-221 |
2.15e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPkdaLAAG 82
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLG---SELARGGLVQRKA-MLSQAQavidrlgAQFKASDRVMTLTIAEQQQVEIARALH 158
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGlkqDKLPKAEIASRVNeMLGLVH-------MQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 159 RQSRILVMDEPTAALSSRETQRL-FELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-242 |
5.48e-27 |
|
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: 108.93 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGK-FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqTIRGPKDALAAGITL 85
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED-IREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKasDRV-MTLTIAEQQQVEIARALHRQSRIL 164
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFA--DRYpHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 165 VMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKL---NAPELVRMMVG 240
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrsPANDFVAEFVG 237
|
..
gi 496082746 241 RP 242
Cdd:cd03295 238 AD 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-215 |
8.09e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.18 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFY----ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPkdalA 80
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP--VTGP----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 AGITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAmlsQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQ 160
Cdd:COG4525 76 ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRA---RAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVL 215
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-241 |
8.11e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 113.17 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITLIYQEMQ---LAPNLTV 98
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGS--ELAR-GGLVQRKAmlsQAQAVIDRLGAqFKASDRVMTLTIAE-----QQQVEIARALHRQSRILVMDEPT 170
Cdd:PRK10762 348 KENMSLTAlrYFSRaGGSLKHAD---EQQAVSDFIRL-FNIKTPSMEQAIGLlsggnQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 171 AALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMMVGR 241
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLMAAAVGK 494
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
260-475 |
8.94e-27 |
|
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: 108.01 E-value: 8.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTD--GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFL 335
Cdd:cd03218 1 LRAENLSKryGKRkvVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 TEnrkEQGLFLELAAQENItMATLERDAnwgmLNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIG 415
Cdd:cd03218 81 PQ---EASIFRKLTVEENI-LAVLEIRG----LSKKEREEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 416 PRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-350 |
9.99e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.55 E-value: 9.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAA- 81
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 -GITLIYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQ 160
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENVALPLEIAG---VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV--GSlVRDKLNAP--ELV 235
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVeqGP-VLDVFANPqsELT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 236 RMMVGRPLSDlfnkerDIPRGQPRLRVEDLTDGGKVKpsslVVHAGEIVGLAGLvgagrSELAQlIFGVRKAT--GGVIE 313
Cdd:COG1135 238 RRFLPTVLND------ELPEELLARLREAAGGGRLVR----LTFVGESADEPLL-----SELAR-RFGVDVNIlsGGIEE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 496082746 314 IDGEP-----VVIHSPREAIDLGIGFLtenrKEQGLFLELAA 350
Cdd:COG1135 302 IQGTPvgrliVELEGDDAAIDAALAYL----REQGVVVEVLG 339
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
260-476 |
1.03e-26 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 107.80 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLT----DGGKV-KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLgIGF 334
Cdd:COG1122 1 IELENLSfsypGGTPAlDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 335 LTENRKEQgLFlelaaqenitMATLERD-----ANWGmLNRRKAQTISDDAIQLLNI-----RVPHAqvraggLSGGNQQ 404
Cdd:COG1122 80 VFQNPDDQ-LF----------APTVEEDvafgpENLG-LPREEIRERVEEALELVGLehladRPPHE------LSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 405 KLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
275-473 |
1.03e-26 |
|
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: 107.17 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDLGIGFLTENRKEQglflelaaqenI 354
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGLVFQNPDDQ-----------F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMLN----RRKAQTISDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:cd03225 89 FGPTVEEEVAFGLENlglpEEEIEERVEEALELVGLeglrdRSPFT------LSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 426 RGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
275-478 |
1.77e-26 |
|
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: 107.38 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTENRkeqGLFLELAAQENI 354
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGR---RIFPSLTVEENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDAnwgmlnRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRG-----VD 429
Cdd:COG0410 100 LLGAYARRD------RAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGlapliVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 430 vgaksEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:COG0410 174 -----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-221 |
1.21e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 104.20 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGeIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRGPKDALAAGITLI 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAEniFLGSELARGGLVQRKAMlSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVM 166
Cdd:cd03264 78 PQEFGVYPNFTVRE--FLDYIAWLKGIPSKEVK-ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 167 DEPTAALSSRETQRLFELILRLrDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-219 |
1.49e-25 |
|
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: 103.06 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPkDALAAGITLIYQEMQLAPNlTVAEN 101
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFlgselaRGGLVQRkamlsqaqavidrlgaqfkasdrvmtltiaeqqqVEIARALHRQSRILVMDEPTAALSSRETQRL 181
Cdd:cd03246 96 IL------SGGQRQR----------------------------------LGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 496082746 182 FELILRLRDEGMAIIYISHRMaEVYELSDRVSVLRDGQ 219
Cdd:cd03246 136 NQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-225 |
2.36e-25 |
|
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: 106.29 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAY---TATSGEILIDGKP--------- 69
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDllklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 70 QTIRGPKdalaagITLIYQE-MQ-LAPNLTVAENIflgSE-LARGGLVQRKAMLSQAQAVIDRLGaqfkasdrvmtLTIA 146
Cdd:COG0444 81 RKIRGRE------IQMIFQDpMTsLNPVMTVGDQI---AEpLRIHGGLSKAEARERAIELLERVG-----------LPDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 147 EQ--------------QQVEIARALHRQSRILVMDEPTAAL-SSRETQRLfELILRLRDE-GMAIIYISHRMAEVYELSD 210
Cdd:COG0444 141 ERrldryphelsggmrQRVMIARALALEPKLLIADEPTTALdVTIQAQIL-NLLKDLQRElGLAILFITHDLGVVAEIAD 219
|
250
....*....|....*
gi 496082746 211 RVSVLrdgqYVGSLV 225
Cdd:COG0444 220 RVAVM----YAGRIV 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-221 |
2.61e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAAGIT 84
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LIYQEMQLAPNLTVAENIFLGselaRGGLVQRKAMLSQA-QAVIDRLGAQFKASDRVMTLTIAEQQQVEIARAL---HRQ 160
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAMG----RAPHGLSRAEDDALvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlWEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 161 S---RILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISH--RMAEVYelSDRVSVLRDGQYV 221
Cdd:PRK13548 156 DgppRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHdlNLAARY--ADRIVLLHQGRLV 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
271-478 |
3.71e-25 |
|
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: 103.22 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAiDLGIGFLTENRkeqGLFLELAA 350
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEA-RRRLGFVSDST---GLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENitmatLERDANWGMLNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDV 430
Cdd:cd03266 96 REN-----LEYFAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 431 GAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-221 |
6.02e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG---------KPQTIRgpkd 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpSEKAIR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 78 ALAAGITLIYQEMQLAPNLTVAENIfLGSELARGGLVQRKAMlSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARAL 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENL-IEAPCKVLGLSKEQAR-EKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 158 HRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
257-476 |
9.51e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.86 E-value: 9.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDLT---DGGKV-KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPReaidlgI 332
Cdd:COG1121 4 MPAIELENLTvsyGGRPVlEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 333 GFLtenrkEQglFLELAAQENIT---MATLERDANWGMLNR--RKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLL 407
Cdd:COG1121 78 GYV-----PQ--RAEVDWDFPITvrdVVLMGRYGRRGLFRRpsRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 408 ISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-219 |
1.40e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.78 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFG----KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTI---R 73
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 74 GPKDALAAGITLIYQEMQLAPNLTVAENIFLGSeLARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEI 153
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPA-LLRG--ESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 154 ARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRmAEVYELSDRVSVLRDGQ 219
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-221 |
2.09e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.12 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPkDAL 79
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA-DAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 80 AA----GITLIYQEMQLAPNLTVAEN-----IFLGSElargglvqRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQ 150
Cdd:PRK10535 81 AQlrreHFGFIFQRYHLLSHLTAAQNvevpaVYAGLE--------RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 151 VEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRmAEVYELSDRVSVLRDGQYV 221
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-215 |
4.15e-24 |
|
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: 105.45 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqTIRGPKDALAAGI 83
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNlTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQS 161
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRdEGMAIIYISHRMAeVYELSDRVSVL 215
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-221 |
4.30e-24 |
|
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: 100.77 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFG-KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRGPK-DALAAGIT 84
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG--QDIREVTlDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LIYQEMQLApNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSR 162
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 163 ILVMDEPTAALSSRETQRLFELILRLRdEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
4.41e-24 |
|
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: 100.62 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaagiTLIYQEMQLAPNLTVAEN 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR------MVVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLGSELARGGL--VQRKAMLSQAqavIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQ 179
Cdd:TIGR01184 75 IALAVDRVLPDLskSERRAIVEEH---IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496082746 180 RLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:TIGR01184 152 NLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-221 |
5.30e-24 |
|
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: 100.38 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRGPK-DALAAGITLIYQEMQLApNLTVA 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDVRDYTlASLRRQIGLVSQDVFLF-NDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSrE 177
Cdd:cd03251 94 ENIAYGRPGATREEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-E 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496082746 178 TQRLFELILRLRDEGMAIIYISHRMAEVyELSDRVSVLRDGQYV 221
Cdd:cd03251 173 SERLVQAALERLMKNRTTFVIAHRLSTI-ENADRIVVLEDGKIV 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-219 |
5.31e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRG-PkdAL 79
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG--QDITHvP--AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 80 AAGITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIdRLgAQFkASDRVMTLTIAEQQQVEIARALHR 159
Cdd:PRK09452 85 NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMV-QL-EEF-AQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 160 QSRILVMDEPTAALSSR-ETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK09452 162 KPKVLLLDESLSALDYKlRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-219 |
5.34e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.54 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 9 MRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpqtIRGPKDaLAAGitliyq 88
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---VSALLE-LGAG------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 89 emqLAPNLTVAENIFLGSELArgGLvQRKAMLSQAQAVID---------------------RLGaqFkasdrvmtltiae 147
Cdd:COG1134 99 ---FHPELTGRENIYLNGRLL--GL-SRKEIDEKFDEIVEfaelgdfidqpvktyssgmraRLA--F------------- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 148 qqqveiARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1134 158 ------AVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-219 |
5.38e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.54 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSG-EILIDGKPqtiRGPKD--ALA 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGER---RGGEDvwELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 AGITLIYQEMQLA--PNLTVAENI---FLGSElargGLVQR--KAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEI 153
Cdd:COG1119 78 KRIGLVSPALQLRfpRDETVLDVVlsgFFDSI----GLYREptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 154 ARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEG-MAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-225 |
5.97e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.50 E-value: 5.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAF-----------GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP 69
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 70 QTIRGPKD--ALAAGITLIYQEMQ--LAPNLTVAENIflGSELARGGLVQRKAMLSQAQAVIDRLG----------AQFK 135
Cdd:COG4608 82 ITGLSGRElrPLRRRMQMVFQDPYasLNPRMTVGDII--AEPLRIHGLASKAERRERVAELLELVGlrpehadrypHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 136 ASDRvmtltiaeqQQVEIARALHRQSRILVMDEPTAALS-SRETQRLfELILRLRDE-GMAIIYISHRMAEVYELSDRVS 213
Cdd:COG4608 160 GGQR---------QRIGIARALALNPKLIVCDEPVSALDvSIQAQVL-NLLEDLQDElGLTYLFISHDLSVVRHISDRVA 229
|
250
....*....|..
gi 496082746 214 VLrdgqYVGSLV 225
Cdd:COG4608 230 VM----YLGKIV 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-218 |
7.19e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRgpkDALAAG-- 82
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL---SARAASrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLG-----SELARGGLVQRKAMlsqaQAVIDRLG-AQFKASDrVMTLTIAEQQQVEIARA 156
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGrtphrSRFDTWTETDRAAV----ERAMERTGvAQFADRP-VTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
275-473 |
9.12e-24 |
|
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: 98.89 E-value: 9.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIhSPREAIdlgiGFLTEnrkEQGLFLELAAQEN- 353
Cdd:cd03269 20 SFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-AARNRI----GYLPE---ERGLYPKMKVIDQl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 354 ITMATLErdanwGMlNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAK 433
Cdd:cd03269 92 VYLAQLK-----GL-KKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496082746 434 SEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:cd03269 165 ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-219 |
1.21e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.11 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRG--PKDa 78
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqQRD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 79 laagITLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQfkasDR-VMTLTIAEQQQVEIARAL 157
Cdd:PRK11432 80 ----ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFE----DRyVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 158 HRQSRILVMDEPTAAL------SSRETQRlfELILRLrdeGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLdanlrrSMREKIR--ELQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-221 |
1.32e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAG--AYTATSGEILIDGKPQTIRGPKDALAAGITLIYQ---EMqlaPNL 96
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDERARAGIFLAFQypvEI---PGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 97 TVAEniFLGSELA--RGGLVQRKAMLSQAQAVIDRLGaqfkasdrvMTLTIA-----------EQQQVEIARALHRQSRI 163
Cdd:COG0396 93 SVSN--FLRTALNarRGEELSAREFLKLLKEKMKELG---------LDEDFLdryvnegfsggEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISH--RMAEvYELSDRVSVLRDGQYV 221
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqRILD-YIKPDFVHVLVDGRIV 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-221 |
1.42e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.42 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 8 EMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAA-- 81
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 GITLIYQEMQLAPNLTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQS 161
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAG---TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-219 |
1.82e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.67 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 26 DLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITLIYQEMQLAPNLTVAENIFLG 105
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 106 selARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELI 185
Cdd:COG3840 96 ---LRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190
....*....|....*....|....*....|....*
gi 496082746 186 LRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG3840 173 DELCRErGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-219 |
3.34e-23 |
|
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: 97.89 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAF------GK-FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIrgpk 76
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 77 D-ALAAGITLIY----------QEMQLAPNLT----VAENIflgseLARGglVQRKAMLSQAQAVIDRLGAQfkasDRVM 141
Cdd:COG4778 78 DlAQASPREILAlrrrtigyvsQFLRVIPRVSaldvVAEPL-----LERG--VDREEARARARELLARLNLP----ERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 142 TLTIA-----EQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLR 216
Cdd:COG4778 147 DLPPAtfsggEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 496082746 217 DGQ 219
Cdd:COG4778 227 PFS 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-219 |
3.92e-23 |
|
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: 97.54 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKdALAAGITLIYQEMQLAPNlTVAEN 101
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK-YLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSrETQ 179
Cdd:cd03248 108 IAYGLQSCSFECVKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA-ESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496082746 180 RLFELILRLRDEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:cd03248 187 QQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-221 |
4.49e-23 |
|
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: 102.19 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAF-----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILI----DGKPQTIRGP 75
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 76 KDALAAG--ITLIYQEMQLAPNLTVAEN------IFLGSELARgglvqRKAMLS---------QAQAVIDRLGAQfkasd 138
Cdd:TIGR03269 358 DGRGRAKryIGILHQEYDLYPHRTVLDNlteaigLELPDELAR-----MKAVITlkmvgfdeeKAEEILDKYPDE----- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 139 rvmtLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRD 217
Cdd:TIGR03269 428 ----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
....
gi 496082746 218 GQYV 221
Cdd:TIGR03269 504 GKIV 507
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
260-475 |
5.17e-23 |
|
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: 97.19 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDL-----TDGGK---VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLG 331
Cdd:cd03257 2 LEVKNLsvsfpTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 332 --IGFLtenrkEQGLFLELAAQENITMATLERDANWGMLNRRKAQTIsddAIQLLNIRVPHAQVRAG----GLSGGNQQK 405
Cdd:cd03257 82 keIQMV-----FQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKE---AVLLLLVGVGLPEEVLNryphELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 406 LLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
261-475 |
6.63e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 96.56 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 261 RVEDLTDGGKVKPS-----SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIdlgiGFL 335
Cdd:cd03226 1 RIENISFSYKKGTEilddlSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI----GYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 TENRKEQgLFlelaaqenitMATLERDANWGMLNRRKAQTISDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISR 410
Cdd:cd03226 77 MQDVDYQ-LF----------TDSVREELLLGLKELDAGNEQAETVLKDLDLyalkeRHPLS------LSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 411 WVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-219 |
1.29e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 101.00 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAF--GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRG-PKDAL 79
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD--LRDlDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 80 AAGITLIYQEMQLApNLTVAENIFLGSELArgGLVQRKAMLSQAQ--AVIDRL-----------GAQFKAsdrvmtltiA 146
Cdd:COG4987 408 RRRIAVVPQRPHLF-DTTLRENLRLARPDA--TDEELWAALERVGlgDWLAALpdgldtwlgegGRRLSG---------G 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 147 EQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLrDEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGL-ERMDRILVLEDGR 546
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-219 |
1.45e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 100.98 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRG-PKDALAAGITLIYQEMQLAPNlTVAE 100
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG--ADLSQwDREELGRHIGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NIflgselARGG-----LVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAAL 173
Cdd:COG4618 425 NI------ARFGdadpeKVVAAAKLAGVHEMILRLpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496082746 174 SSRETQRLFELILRLRDEGMAIIYISHRMAeVYELSDRVSVLRDGQ 219
Cdd:COG4618 499 DDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGR 543
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
275-470 |
1.93e-22 |
|
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: 95.29 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPReaidlgIGFLTENRkeqglflELAAQENI 354
Cdd:cd03235 19 SFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVPQRR-------SIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 T-----MATLERDANWGMLNRRKAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:cd03235 86 SvrdvvLMGLYGHKGLFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 430 VGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVM 470
Cdd:cd03235 165 PKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-223 |
2.10e-22 |
|
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: 94.90 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAG--AYTATSGEILIDGKPQTIRGPKDALAAGITLIYQEMQLAPNLTVA 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 EniFLGS--ELARGGlvqrkamlsqaqavidrlgaqfkasdrvmtltiaEQQQVEIARALHRQSRILVMDEPTAALSSRE 177
Cdd:cd03217 96 D--FLRYvnEGFSGG----------------------------------EKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 178 TQRLFELILRLRDEGMAIIYISH--RMAEvYELSDRVSVLRDGQYVGS 223
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHyqRLLD-YIKPDRVHVLYDGRIVKS 186
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-225 |
2.78e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.87 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKIL-------AGAytATSGEILIDGKPqtIRG 74
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGA--RVEGEILLDGED--IYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 75 PK---DALAAGITLIYQEmqlaPN---LTVAENIFLGSELArgGLVQRKAM-------LSQA---QAVIDRLgaqfkaSD 138
Cdd:COG1117 83 PDvdvVELRRRVGMVFQK----PNpfpKSIYDNVAYGLRLH--GIKSKSELdeiveesLRKAalwDEVKDRL------KK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 139 RVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEgMAIIYISHRMAEVYELSDRVSVLrdg 218
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFF--- 226
|
....*..
gi 496082746 219 qYVGSLV 225
Cdd:COG1117 227 -YLGELV 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-222 |
5.84e-22 |
|
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: 93.38 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAG--AYTATSGEILIDGKPQTIRGPKDALAagitLIYQEMQLAPNLTVA 99
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKIIG----YVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELA--RGGlvQRKamlsqaqavidrlgaqfkasdrvmtltiaeqqQVEIARALHRQSRILVMDEPTAALSSRE 177
Cdd:cd03213 101 ETLMFAAKLRglSGG--ERK--------------------------------RVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 178 TQRLFELILRLRDEGMAIIYISHRM-AEVYELSDRVSVLRDGQ--YVG 222
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRviYFG 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-221 |
6.32e-22 |
|
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: 94.53 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG---KPQTIRgpkdALAAGITLIYQEMQLAPNlTV 98
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLR----WLRSQIGLVSQEPVLFDG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSR 176
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 177 ETQRLFELILRLRdEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:cd03249 174 SEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-219 |
7.49e-22 |
|
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: 92.76 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDALAAGITLIYQEMQLApNLTVAE 100
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP--VSDLEKALSSLISVLNQRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NiflgselargglvqrkamlsqaqavidrLGAQFKAsdrvmtltiAEQQQVEIARALHRQSRILVMDEPTAALSSRETQR 180
Cdd:cd03247 94 N----------------------------LGRRFSG---------GERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 496082746 181 LFELILRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:cd03247 137 LLSLIFEVL-KDKTLIWITHHLTGI-EHMDKILFLENGK 173
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-219 |
8.52e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 8.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAF--GKFYA--LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP--QTIRGPKD 77
Cdd:PRK11629 3 KILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 78 ALA-AGITLIYQEMQLAPNLTVAENIFLgsELARGGlVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARA 156
Cdd:PRK11629 83 ELRnQKLGFIYQFHHLLPDFTALENVAM--PLLIGK-KKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSvLRDGQ 219
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGR 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
8.80e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.74 E-value: 8.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLeMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILidgkpqTIRGPKDALAAGI 83
Cdd:PRK11247 11 TPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGselARGGLvqRKAMLSQAQAVidrlGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLG---LKGQW--RDAALQALAAV----GLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
275-473 |
9.10e-22 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 93.72 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvIHSPREAIDLGIGFLTENRkeqGLFLELAAQENI 354
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS--IRTDRKAARQSLGYCPQFD---ALFDELTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 T-MATLerdanWGmLNRRKAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQQKLLisrwVAI----GPRILILDEPTRGVD 429
Cdd:cd03263 97 RfYARL-----KG-LPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLS----LAIaligGPSVLLLDEPTSGLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496082746 430 VGAKSEIYRIMNDMaRQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:cd03263 166 PASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-219 |
1.11e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.94 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALA-AGI 83
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPMHKRArLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLsqaQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERL---EELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 164 LVMDEPTAA---LSSRETQRlfeLILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1137 158 ILLDEPFAGvdpIAVADIQK---IIRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
257-484 |
1.52e-21 |
|
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: 97.67 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDLT----DGGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATG---GVIEIDGEPVVIHSPREa 327
Cdd:COG1123 2 TPLLEVRDLSvrypGGDVpaVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 328 IDLGIGFLtenrkeqglFLELAAQENitMATLERDANWGMLN----RRKAQTISDDAIQLLNI-----RVPHAqvraggL 398
Cdd:COG1123 81 RGRRIGMV---------FQDPMTQLN--PVTVGDQIAEALENlglsRAEARARVLELLEAVGLerrldRYPHQ------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 399 SGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIAG 477
Cdd:COG1123 144 SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
....*..
gi 496082746 478 ELQAGDI 484
Cdd:COG1123 224 DGPPEEI 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-219 |
2.17e-21 |
|
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: 98.55 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpqTIRGPKDALAAGITLIYQEMQLAPNLTVAE 100
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NIFLGSELArgGLVQRKAMLsQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQR 180
Cdd:TIGR01257 1023 HILFYAQLK--GRSWEEAQL-EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190
....*....|....*....|....*....|....*....
gi 496082746 181 LFELILRLRdEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:TIGR01257 1100 IWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-221 |
2.17e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.34 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 8 EMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRG-PKDALAAGITL 85
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTvTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLApNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDR--LGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRdEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-219 |
2.87e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.15 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSG-----EILIDGKPQTIRGPKDALA 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 --AGITLIYQEMQLAPNLTVAENIFLGselARGGLVQRKAMLS--------QAQAVIDRLGAQFKASDRVMTLTIAEQQQ 150
Cdd:PRK09984 84 srANTGYIFQQFNLVNRLSVLENVLIG---ALGSTPFWRTCFSwftreqkqRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 151 VEIARALHRQSRILVMDEPTAALSSrETQRLFELILR--LRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDP-ESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-204 |
3.27e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.84 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPkdalAAGITLI 86
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGP----GAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKasdRVMTLTIAEQQQVEIARALHRQSRILVM 166
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 496082746 167 DEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAE 204
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEE 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
271-473 |
6.35e-21 |
|
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: 89.94 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSP-REAIDLGIGFLTEnrkEQGLFLELA 349
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDeLPPLRRRIGMVFQ---DFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENITMatlerdanwgmlnrrkaqtisddaiqllnirvphaqvragGLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:cd03229 93 VLENIAL----------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 430 VGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:cd03229 133 PITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-200 |
6.45e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 91.61 E-value: 6.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG---------KPQTIRgpkd 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpSDKAIR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 78 ALAAGITLIYQEMQLAPNLTVAENIfLGSELARGGLVQRKAMlSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARAL 157
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNL-IEAPCRVLGLSKDQAL-ARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 158 HRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISH 200
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH 199
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-221 |
7.30e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKIL-----AGAYTATSGEILIDGKpqTIRGPKD-- 77
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGH--NIYSPRTdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 78 -ALAAGITLIYQEmqlaPN---LTVAENIFLGSELARgglVQRKAMLSQA------QAVI-----DRLgaqfkaSDRVMT 142
Cdd:PRK14239 82 vDLRKEIGMVFQQ----PNpfpMSIYENVVYGLRLKG---IKDKQVLDEAvekslkGASIwdevkDRL------HDSALG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 143 LTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-218 |
7.43e-21 |
|
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: 91.24 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRgpKDALAAGITLIY-QEMQLAPNLTVA 99
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKR--RKKFLRRIGVVFgQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELARGGLVQRKAMLSQAQAVIDrLGAQFKASDRvmTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQ 179
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDELSELLD-LEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496082746 180 RLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:cd03267 191 NIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-219 |
8.23e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.18 E-value: 8.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 26 DLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITLIYQEMQLAPNLTVAENIFLG 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR---RPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 106 seLARG---GLVQRKAMLSQAQAV-----IDRLGAQFKASDRvmtltiaeqQQVEIARALHRQSRILVMDEPTAALSSRE 177
Cdd:PRK10771 96 --LNPGlklNAAQREKLHAIARQMgiedlLARLPGQLSGGQR---------QRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 178 TQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK10771 165 RQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-219 |
8.79e-21 |
|
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: 91.05 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 17 GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGpkdaLAAGitliyqemqLAPNL 96
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG----LGGG---------FNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 97 TVAENIFLgselaRGGL--VQRKAMLSQAQAVID--RLGAQFkaSDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAA 172
Cdd:cd03220 100 TGRENIYL-----NGRLlgLSRKEIDEKIDEIIEfsELGDFI--DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 173 LSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
275-475 |
9.84e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 90.63 E-value: 9.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidlgigfLTENRKEQ--------GLFL 346
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE--------LAAFRRRHigfvfqsfNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 347 ELAAQENITMAtlerdanwGMLNRRKAQTISDDAIQLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDE 423
Cdd:cd03255 96 DLTALENVELP--------LLLAGVPKKERRERAEELLE-RVglgDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 424 PTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSElPEVVGMSDRVYVMREGAI 475
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
271-473 |
1.13e-20 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 88.46 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDlGIGFLTEnrkeqglflelaa 350
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 qenitmatlerdanwgmlnrrkaqtisddaiqllnirvphaqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDV 430
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 431 GAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-232 |
1.52e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 92.66 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRH----IAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGA----YTATSGEILIDGK---PQTIR 73
Cdd:COG4170 2 PLLDIRNltieIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnWHVTADRFRWNGIdllKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 74 GPKDALAAGITLIYQEMQ--LAPNLTV----AENIFlgSELARGGLVQR-KAMLSQAQAVIDRLGaqFKASDRVMT---- 142
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSscLDPSAKIgdqlIEAIP--SWTFKGKWWQRfKWRKKRAIELLHRVG--IKDHKDIMNsyph 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 143 -LTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQY 220
Cdd:COG4170 158 eLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQT 237
|
250
....*....|...
gi 496082746 221 VGSLVRDK-LNAP 232
Cdd:COG4170 238 VESGPTEQiLKSP 250
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-221 |
1.53e-20 |
|
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: 90.62 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 20 YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPkDALAAGITLIYQEMQLApNLTVA 99
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAAL---S 174
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALdyeS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 175 SRETQRLFELILrlrdEGMAIIYISHRMAEVyELSDRVSVLRDGQYV 221
Cdd:cd03252 174 EHAIMRNMHDIC----AGRTVIIIAHRLSTV-KNADRIIVMEKGRIV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
275-479 |
1.59e-20 |
|
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: 89.84 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPreaiDLGIGFltenrKEQGLFLELAAQENI 354
Cdd:cd03293 24 SLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRGYVF-----QQDALLPWLTVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMAtLERDAnwgmLNRRKAQTISDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:cd03293 95 ALG-LELQG----VPKAEARERAEELLELVGLsgfenAYPHQ------LSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 430 VGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVM--REGAIAGEL 479
Cdd:cd03293 164 ALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEV 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-221 |
1.85e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.79 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKdALAAGITLIYQEMQLApNLTVAEN 101
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH-YLHRQVALVGQEPVLF-SGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQ 179
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496082746 180 RLFELILRlrdEGMAIIYISHRMAEVyELSDRVSVLRDGQYV 221
Cdd:TIGR00958 655 LLQESRSR---ASRTVLLIAHRLSTV-ERADQILVLKKGSVV 692
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-221 |
2.10e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 94.37 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAF-----------GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAyTATSGEILIDGKPQ 70
Cdd:COG4172 271 DAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 71 TIRGPKDALAagitlIYQEMQ---------LAPNLTVAENIFLGSELARGGL--VQRKAMLSQA-------QAVIDRLGA 132
Cdd:COG4172 350 DGLSRRALRP-----LRRRMQvvfqdpfgsLSPRMTVGQIIAEGLRVHGPGLsaAERRARVAEAleevgldPAARHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 133 QFKASDRvmtltiaeqQQVEIARALHRQSRILVMDEPTAALsSRETQ-RLFELILRLRDE-GMAIIYISHRMAEVYELSD 210
Cdd:COG4172 425 EFSGGQR---------QRIAIARALILEPKLLVLDEPTSAL-DVSVQaQILDLLRDLQREhGLAYLFISHDLAVVRALAH 494
|
250
....*....|.
gi 496082746 211 RVSVLRDGQYV 221
Cdd:COG4172 495 RVMVMKDGKVV 505
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-425 |
2.21e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 9 MRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpqtirgpkdalaaGITLIY- 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLRIGYl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 88 -QEMQLAPNLTVAENIFLG--------SELARggLVQRKAMLSQAQAVIDRLGAQFKASD---------RVMT---LTIA 146
Cdd:COG0488 67 pQEPPLDDDLTVLDTVLDGdaelraleAELEE--LEAKLAEPDEDLERLAELQEEFEALGgweaearaeEILSglgFPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 147 EQQQ------------VEIARALHRQSRILVMDEPTAALSsretqrlFELILRLRD-----EGmAIIYISH------RMA 203
Cdd:COG0488 145 DLDRpvselsggwrrrVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEEflknyPG-TVLVVSHdryfldRVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 204 -EVYELSDRVSVLRDGQYVGSLV---------------RDKLNAPEL--VRMMVGRP------------LSDLFNKERDI 253
Cdd:COG0488 217 tRILELDRGKLTLYPGNYSAYLEqraerleqeaaayakQQKKIAKEEefIRRFRAKArkakqaqsrikaLEKLEREEPPR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 254 PRGQPRLR-------------VEDLT--DGGKV--KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIdG 316
Cdd:COG0488 297 RDKTVEIRfppperlgkkvleLEGLSksYGDKTllDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 317 EPVVihspreaidlgIGFLTENRKEqgLFLELAAQENItmatleRDAnwgmlnRRKAQTISddAIQLL---NIRVPHAQV 393
Cdd:COG0488 376 ETVK-----------IGYFDQHQEE--LDPDKTVLDEL------RDG------APGGTEQE--VRGYLgrfLFSGDDAFK 428
|
490 500 510
....*....|....*....|....*....|..
gi 496082746 394 RAGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:COG0488 429 PVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
260-478 |
2.38e-20 |
|
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: 89.20 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTD--GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVihspREAIDLG-IGF 334
Cdd:cd03268 1 LKTNDLTKtyGKKrvLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEALRrIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 335 LTEnrkEQGLFLELAAQENitmatLERDANWGMLNRRKAqtisDDAIQLLNIRVpHAQVRAGGLSGGNQQKLLISRWVAI 414
Cdd:cd03268 77 LIE---APGFYPNLTAREN-----LRLLARLLGIRKKRI----DEVLDVVGLKD-SAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 415 GPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-219 |
2.60e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGI 83
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 tlIYQEMQLAPNLTVAENIFLGSelargglvqRKAMLSQAQA------VIDRLGAQFKASDRVMTLTIAEQQQVEIARAL 157
Cdd:PRK13537 85 --VPQFDNLDPDFTVRENLLVFG---------RYFGLSAAAAralvppLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 158 HRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-219 |
2.68e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.53 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGK-----FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAA 81
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-KLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 GITLIYQEMQL--APNLTVAENIFLGSE------LARGGLVQRKAMLSQAQAVIDrLGAQFKASDRVMTLTIAEQQQVEI 153
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEENLALAYRrgkrrgLRRGLTKKRRELFRELLATLG-LGLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 154 ARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
281-477 |
2.83e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 89.28 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 281 GEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGepVVIHSPREAIDL-----GIGFLTENrkeQGLFLELAAQENIT 355
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKINLppqqrKIGLVFQQ---YALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 356 MATLERdanwgmlnRRKAQTISDDAI-QLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:cd03297 98 FGLKRK--------RNREDRISVDELlDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496082746 435 EIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIAG 477
Cdd:cd03297 169 QLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
258-454 |
4.06e-20 |
|
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: 88.30 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 258 PRLRVEDLT---DGGKV-KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvIHSPREAIDLGIG 333
Cdd:COG4133 1 MMLEAENLScrrGERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP--IRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 334 FLTEnrkEQGLFLELAAQENITMATlerdanwGMLNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVA 413
Cdd:COG4133 79 YLGH---ADGLKPELTVRENLRFWA-------ALYGLRADREAIDEALEAVGLA-GLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 414 IGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMIS 454
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTT 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-258 |
4.29e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 90.14 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDALAA-----GITLIYQEMQL-AP 94
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP--IKYDKKSLLEvrktvGIVFQNPDDQLfAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 95 nlTVAENIFLGSelARGGL----VQRKAMlsQAQAVIDRLGAQFKASDRvmtLTIAEQQQVEIARALHRQSRILVMDEPT 170
Cdd:PRK13639 95 --TVEEDVAFGP--LNLGLskeeVEKRVK--EALKAVGMEGFENKPPHH---LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 171 AALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS-LVRDKLNAPELVRMMVGR-----PLS 244
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEgTPKEVFSDIETIRKANLRlprvaHLI 245
|
250
....*....|....
gi 496082746 245 DLFNKERDIPRGQP 258
Cdd:PRK13639 246 EILNKEDNLPIKMG 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-221 |
6.43e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.21 E-value: 6.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRgpkdALA 80
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR----DLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 A--------------GITLIYQEMQLAPNLTVAENIflGSEL-ARG----GLVQRKAM--LSQAQAVIDRLgaqfkaSDR 139
Cdd:PRK11701 77 AlseaerrrllrtewGFVHQHPRDGLRMQVSAGGNI--GERLmAVGarhyGDIRATAGdwLERVEIDAARI------DDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 140 VMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
...
gi 496082746 219 QYV 221
Cdd:PRK11701 229 RVV 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-218 |
6.48e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQtirgPKDALAA--GIT 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLAraRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LIYQEMQLAPNLTVAENIFLGSELARGGLVQRKAMLSqaqAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRIL 164
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIP---SLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 165 VMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-221 |
7.03e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.04 E-value: 7.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSG-----EILIDGKpQTIRGPKD---A 78
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTA-RSLSQQKGlirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 79 LAAGITLIYQEMQLAPNLTVAENIFLGSELARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALH 158
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 159 RQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-225 |
7.10e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 7.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDA--LAAG 82
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQEMQLAPNLTVAENIFLGSEL--ARGGLVQRKAmlsqaQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQ 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIagASGDDIRRRV-----SAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 161 SRILVMDEPTAALSsretQRLFELILRLRDE----GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLV 225
Cdd:PRK10908 156 PAVLLADEPTGNLD----DALSEGILRLFEEfnrvGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
257-473 |
8.29e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.89 E-value: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDLTD--GG--KVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGI 332
Cdd:PRK11300 3 QPLLSVSGLMMrfGGllAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 333 GFLTENRKeqgLFLELAAQENITMATlERDANWGMLN--------RRKAQTISDDAIQLLNiRV---PHAQVRAGGLSGG 401
Cdd:PRK11300 83 VRTFQHVR---LFREMTVIENLLVAQ-HQQLKTGLFSgllktpafRRAESEALDRAATWLE-RVgllEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 402 NQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
258-475 |
8.30e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.55 E-value: 8.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 258 PRLRVEDLTD--GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVV---IHspREAIdL 330
Cdd:COG1137 2 MTLEAENLVKsyGKRtvVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpMH--KRAR-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 331 GIGFLTEnrkEQGLFLELAAQENItMATLERdanwGMLNRRKAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQQKLLISR 410
Cdd:COG1137 79 GIGYLPQ---EASIFRKLTVEDNI-LAVLEL----RKLSKKEREERLEELLEEFGI-THLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 411 WVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
260-482 |
1.26e-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: 87.19 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLT----DGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAidlGIGFL 335
Cdd:cd03259 1 LELKGLSktygSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 TENRkeqGLFLELAAQENITMAtLERdanwGMLNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIG 415
Cdd:cd03259 78 FQDY---ALFPHLTVAENIAFG-LKL----RGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 416 PRILILDEPTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREGAIageLQAG 482
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI---VQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
271-425 |
1.46e-19 |
|
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: 85.39 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAIDLGIGFLTENRkeqGLFLELAA 350
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDP---QLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 351 QENITMATLERDanwgmLNRRKAQTISDDAIQLLNIRVPHAQV---RAGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:pfam00005 77 RENLRLGLLLKG-----LSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-221 |
1.75e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 9 MRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITLIYQ 88
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 89 EMQLAPNLTVAENIFLGSELARGGLVQRKAMLSQAqAVIDRLGA----QFKAsdrvmtLTIAEQQQVEIARALHRQSRIL 164
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQV-AEVLQLAHlldrKPKA------LSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 165 VMDEP----TAALS-------SRETQRLfelilrlrdeGMAIIYISHRMAEVYELSDRVSVLrDGQYV 221
Cdd:PRK11000 156 LLDEPlsnlDAALRvqmrieiSRLHKRL----------GRTMIYVTHDQVEAMTLADKIVVL-DAGRV 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-219 |
2.35e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.15 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 20 YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQEmqlaPN---- 95
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVFQN----PDnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 96 -LTVAENIFLGSElARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALS 174
Cdd:PRK13635 96 gATVQDDVAFGLE-NIG--VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496082746 175 SRETQRLFELILRLRDEGMA-IIYISHRMAEVYElSDRVSVLRDGQ 219
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGItVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
271-473 |
2.51e-19 |
|
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: 86.75 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPreaiDLGIGFltenrKEQGLFLELAA 350
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP----DRMVVF-----QNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENITMATlerDANWGMLNRRKAQTISDDAIQLLNIRvpHAQ-VRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:TIGR01184 72 RENIALAV---DRVLPDLSKSERRAIVEEHIALVGLT--EAAdKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 430 VGAKSEIY-RIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:TIGR01184 147 ALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-200 |
2.60e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.38 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTA---TSGEILIDGKPQTirgPKDALAAGITLIYQEMQLAPNLTV 98
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT---ALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGseLARG-GLVQRKAmlsQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRE 177
Cdd:COG4136 94 GENLAFA--LPPTiGRAQRRA---RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180
....*....|....*....|....
gi 496082746 178 TQRLFELIL-RLRDEGMAIIYISH 200
Cdd:COG4136 169 RAQFREFVFeQIRQRGIPALLVTH 192
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-254 |
3.36e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.35 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 20 YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpqTI-RGPKDALAAGITLIYQEmqlaPN--- 95
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI--TIsKENLKEIRKKIGIIFQN----PDnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 96 --LTVAENIFLGSELARgglVQRKAMlsqaQAVIDRLGAQF---KASDR-VMTLTIAEQQQVEIARALHRQSRILVMDEP 169
Cdd:PRK13632 97 igATVEDDIAFGLENKK---VPPKKM----KDIIDDLAKKVgmeDYLDKePQNLSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 170 TAALSSRETQRLFELILRLRDEGM-AIIYISHRMAEVYeLSDRVSVLRDGqyvgslvrdklnapELVRmmVGRPLSDLFN 248
Cdd:PRK13632 170 TSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEG--------------KLIA--QGKPKEILNN 232
|
250
....*....|..
gi 496082746 249 KER------DIP 254
Cdd:PRK13632 233 KEIlekakiDSP 244
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
271-484 |
3.87e-19 |
|
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: 86.78 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAidlgigflteNRKEQGLF----L 346
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF----------RRRVQMVFqdpyA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 347 ELAAQENITMATLERDANWGMLNRRkaqtisDDAIQLLNI---------RVPHAqvraggLSGGNQQKLLISRWVAIGPR 417
Cdd:COG1124 91 SLHPRHTVDRILAEPLRIHGLPDRE------ERIAELLEQvglppsfldRYPHQ------LSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 418 ILILDEPTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDI 484
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-243 |
6.53e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 87.55 E-value: 6.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGA----YTATSGEIL---IDGKPQTIR 73
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRfddIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 74 GPKDALAAGITLIYQEMQ--LAPNLTVAENI--------FLGSELARGGLVQRKAMlsqaqAVIDRLGaqFKASDRVM-- 141
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQscLDPSERVGRQLmqnipgwtYKGRWWQRFGWRKRRAI-----ELLHRVG--IKDHKDAMrs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 142 ---TLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRD 217
Cdd:PRK15093 155 fpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250 260 270
....*....|....*....|....*....|....*
gi 496082746 218 GQYVGSLVRDKL-NAPE------LVRMM--VGRPL 243
Cdd:PRK15093 235 GQTVETAPSKELvTTPHhpytqaLIRAIpdFGSAM 269
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
275-493 |
7.42e-19 |
|
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: 87.86 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEpvVIHSPREAIDLGigflTENRK------EQGLFLEL 348
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR--TLFDSRKGIFLP----PEKRRigyvfqEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 349 AAQENItmatlerdaNWGMLNRRKAQT-ISDDAI-QLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTR 426
Cdd:TIGR02142 91 SVRGNL---------RYGMKRARPSERrISFERViELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 427 GVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQESIMTLA 493
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-266 |
7.90e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.45 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGK-PQTIRgpkDALAAGITLIY-QEMQLAPNLTV 98
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKRR---KEFARRIGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AEN------IFlgsELARGGLVQRKAMLsqaqavIDRLGAQFKASDRVMTLTIAEQQQVEIARAL-HRqSRILVMDEPTA 171
Cdd:COG4586 114 IDSfrllkaIY---RIPDAEYKKRLDEL------VELLDLGELLDTPVRQLSLGQRMRCELAAALlHR-PKILFLDEPTI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 172 AL--SSRETQRlfELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ--YVGSL--VRDKLNAPELVRMMVGRPLS 244
Cdd:COG4586 184 GLdvVSKEAIR--EFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRiiYDGSLeeLKERFGPYKTIVLELAEPVP 261
|
250 260
....*....|....*....|..
gi 496082746 245 DLfnkerDIPRGQPRLRVEDLT 266
Cdd:COG4586 262 PL-----ELPRGGEVIEREGNR 278
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
275-475 |
8.44e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 86.20 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAID-LGIGFltENRKEQglFLELAAQEN 353
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKkIGIIF--QNPDNQ--FIGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 354 ITMAtLERDanwgMLNRRKAQTISDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGV 428
Cdd:PRK13632 105 IAFG-LENK----KVPPKKMKDIIDDLAKKVGMedyldKEPQN------LSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 429 DVGAKSEIYRIMNDMARQGV-AILMISSELPEVVgMSDRVYVMREGAI 475
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
260-484 |
9.31e-19 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 85.47 E-value: 9.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLT-DGG--KVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAidlGIGFLT 336
Cdd:cd03299 1 LKVENLSkDWKefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 337 ENrkeQGLFLELAAQENITMATLERDANWGMLNRRKAQTISDDAI-QLLNiRVPhaqvraGGLSGGNQQKLLISRWVAIG 415
Cdd:cd03299 78 QN---YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIdHLLN-RKP------ETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 416 PRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIageLQAGDI 484
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL---IQVGKP 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-218 |
1.06e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITLI 86
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLG-SELAR-----GGLVQRKAM--LSQAQavIDRLGAQFKASdrvmtLTIAEQQQVEIARALH 158
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGlTVLPRrerpnAAAIKAKVTqlLEMVQ--LAHLADRYPAQ-----LSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 159 RQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-219 |
1.13e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.83 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP--QTIRGPKdALAAGITLIYQ--EMQL----- 92
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRGLL-ALRQQVATVFQdpEQQIfytdi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 93 -------APNLTVAEniflgSELARgglvqrkaMLSQAQAVIDrlgAQFKASDRVMTLTIAEQQQVEIARALHRQSRILV 165
Cdd:PRK13638 96 dsdiafsLRNLGVPE-----AEITR--------RVDEALTLVD---AQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 166 MDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
271-478 |
1.23e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 84.73 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVihspREAIDL--GIGFLTENRKEQGlflEL 348
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVrrRIGIVFQDLSVDD---EL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 349 AAQENITMATLERDANWGMLNRRKAQTIsdDAIQLLNIRvpHAQVRAggLSGGNQQKLLISRWVAIGPRILILDEPTRGV 428
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELL--DFVGLLEAA--DRLVKT--YSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496082746 429 DVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:cd03265 163 DPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-88 |
1.95e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 84.69 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAG--AYTATSGEILIDGKPQTIRGPKDA 78
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEER 81
|
90
....*....|
gi 496082746 79 LAAGITLIYQ 88
Cdd:CHL00131 82 AHLGIFLAFQ 91
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
275-484 |
1.98e-18 |
|
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: 84.48 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPRE--AIDLGIGFLTenrkeQG--LFLELAA 350
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMGMLF-----QSgaLFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENITMATLERdanwGMLNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDV 430
Cdd:cd03261 95 FENVAFPLREH----TRLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 431 GAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDI 484
Cdd:cd03261 170 IASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
271-495 |
2.21e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTEnrkEQGLFLELAA 350
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQ---ELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENITMATLERDANWG--MLNRRKAQTISDDAIQLLNIRVpHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGV 428
Cdd:PRK09700 98 LENLYIGRHLTKKVCGvnIIDWREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 429 DVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQESIMTLATG 495
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-224 |
3.74e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEIlidgkpqtIRGPKDALAagit 84
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETVKIG---- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 liY--QEM-QLAPNLTVAENIflgSELARGGlvqrkamlsQAQAVIDRLGA-QFKASD---RVMTLTIAEQQQVEIARAL 157
Cdd:COG0488 382 --YfdQHQeELDPDKTVLDEL---RDGAPGG---------TEQEVRGYLGRfLFSGDDafkPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 158 HRQSRILVMDEPTAAL--SSREtqrlfELILRLRD-EGmAIIYISHRMAEVYELSDRVSVLRDGQ---YVGSL 224
Cdd:COG0488 448 LSPPNVLLLDEPTNHLdiETLE-----ALEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGvreYPGGY 514
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
275-475 |
4.36e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 82.96 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEpvVIHSPREAIDlgigfltENRKEQG-------LFLE 347
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGL--KLTDDKKNIN-------ELRQKVGmvfqqfnLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 LAAQENITMATLERdanWGMlNRRKAQTIsddAIQLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEP 424
Cdd:cd03262 91 LTVLENITLAPIKV---KGM-SKAEAEER---ALELLE-KVglaDKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 425 TRGVD---VGaksEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03262 163 TSALDpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-221 |
4.48e-18 |
|
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: 87.18 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRG-PKDALAAGITLIYQEMQLApNLTVAE 100
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG--QDIRDvTQASLRAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSReT 178
Cdd:COG5265 451 NIAYGRPDASEEEVEAAARAAQIHDFIESLpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR-T 529
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 179 QRLFELILRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:COG5265 530 ERAIQAALREVARGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-222 |
5.14e-18 |
|
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: 81.91 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTA--TSGEILIDGKPqtirgPKDALAAGITLIYQEMQLAPNLTVA 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRP-----LDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLgSELARG-GLVQRKamlsqaqavidrlgaqfkasdrvmTLTIAeqqqVEIAralhrqSR--ILVMDEPTAALSSR 176
Cdd:cd03232 98 EALRF-SALLRGlSVEQRK------------------------RLTIG----VELA------AKpsILFLDEPTSGLDSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 177 ETQRLFELILRLRDEGMAII-YISHRMAEVYELSDRVSVL-RDGQ--YVG 222
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLkRGGKtvYFG 192
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-225 |
5.83e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.35 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMK-----ILAGAYTATSGEILIDGKpqTIRGPK-DALA 80
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGR--NIYSPDvDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 A--GITLIYQEMQLAPNLTVAENIFLGSELarGGLVQRKAMLSQA-----------QAVIDRLgaqfkaSDRVMTLTIAE 147
Cdd:PRK14267 83 VrrEVGMVFQYPNPFPHLTIYDNVAIGVKL--NGLVKSKKELDERvewalkkaalwDEVKDRL------NDYPSNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 148 QQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEgMAIIYISHRMAEVYELSDRVSVLrdgqYVGSLV 225
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFL----YLGKLI 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-234 |
6.21e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.76 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAA--GITLIYQE--MQLAPNL 96
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 97 TVAENI-----FLGSELARGGLVQR-KAMLSQA---QAVIDRLGAQFKAsdrvmtltiAEQQQVEIARALHRQSRILVMD 167
Cdd:PRK15079 116 TIGEIIaeplrTYHPKLSRQEVKDRvKAMMLKVgllPNLINRYPHEFSG---------GQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 168 EPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLrdgqYVGslvrdklNAPEL 234
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM----YLG-------HAVEL 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
275-478 |
7.61e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.40 E-value: 7.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidlgigfLTENRKE------QGLFL-- 346
Cdd:COG1136 28 SLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE--------LARLRRRhigfvfQFFNLlp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 347 ELAAQENITMATLERDanwgmLNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTR 426
Cdd:COG1136 100 ELTALENVALPLLLAG-----VSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 427 GVDVGAKSEIYRIMNDMARQ-GVAILMISSElPEVVGMSDRVYVMREGAIAGE 478
Cdd:COG1136 174 NLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-221 |
7.84e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.17 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGK-----PQTIRGPKDALAAGITLIYQEMQLAPNL 96
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 97 TVAENIflGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMT----LTIAEQQQVEIARALHRQSRILVMDEPTAA 172
Cdd:PRK14246 106 SIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 173 LSSRETQRLFELILRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-243 |
7.85e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKdALAAGITLIYQEMQLAPNLTVAEN 101
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLG-----SELARGGLVQRKamlsQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSR 176
Cdd:PRK10575 106 VAIGrypwhGALGRFGAADRE----KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 177 ETQRLFELILRL-RDEGMAIIYISH--RMAEVYelSDRVSVLRDGQYVGSLVRDKLNAPELVRMMVGRPL 243
Cdd:PRK10575 182 HQVDVLALVHRLsQERGLTVIAVLHdiNMAARY--CDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPM 249
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-221 |
7.94e-18 |
|
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: 82.16 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP-QTIrgPKDALAAGITLIYQEmqlaPNL--- 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiSKI--GLHDLRSRISIIPQD----PVLfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 97 TVAENI--F-------LGSELARGGLVQR-KAMLSQAQAVIDRLGAQFKASDRvmtltiaeqQQVEIARALHRQSRILVM 166
Cdd:cd03244 93 TIRSNLdpFgeysdeeLWQALERVGLKEFvESLPGGLDTVVEEGGENLSVGQR---------QLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 167 DEPTAALSSrETQRLFELILRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:cd03244 164 DEATASVDP-ETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-221 |
8.09e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 83.34 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTAT--------SGEILIDGKP-QTIRGPKdaLAAGITLIYQEMQL 92
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPlAAIDAPR--LARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 93 APNLTVAENIFLG--SELARGGLVQRKAMlSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARAL---------HRQS 161
Cdd:PRK13547 95 AFAFSAREIVLLGryPHARRAGALTHRDG-EIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-236 |
8.14e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKdALAAGITLI 86
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR-QLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGselaR-------GGLVQR-KAMLSQA--QAVIDRLgaqfkASDRVMTLTIAEQQQVEIARA 156
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYG----RspwlslwGRLSAEdNARVNQAmeQTRINHL-----ADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVR 236
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLR 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
275-475 |
9.46e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 82.39 E-value: 9.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAidlGIGFLTENrkeQGLFLELAAQENI 354
Cdd:cd03296 22 SLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFVFQH---YALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANwgmlNRRKAQTISDDAIQLLNI--------RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPTR 426
Cdd:cd03296 96 AFGLRVKPRS----ERPPEAEIRAKVHELLKLvqldwladRYPAQ------LSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 427 GVDVGAKSEIYRIMNDMA-RQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
275-475 |
1.04e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 81.69 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAI-----DLGIGFlTENRkeqgLFLELA 349
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIpylrrKIGVVF-QDFR----LLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENITMATLERDANWGMLNRRKAqtisdDAIQLLNIRVPHAQVrAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:cd03292 95 VYENVAFALEVTGVPPREIRKRVP-----AALELVGLSHKHRAL-PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496082746 430 VGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
275-476 |
1.54e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVihspreaiDLGIGfLTENRKEQGLFLELAaQENI 354
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--------DKKVK-LSDIRKKVGLVFQYP-EYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMLNRrkaqTISDDAIqllNIRVPHAQVRAG------------GLSGGNQQKLLISRWVAIGPRILILD 422
Cdd:PRK13637 97 FEETIEKDIAFGPINL----GLSEEEI---ENRVKRAMNIVGldyedykdkspfELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 423 EPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-205 |
1.60e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPkDALA 80
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 AGITLIYQemqlAPNL---TVAENIFLGSELaRGGLVQRKAMLsqaqaviDRLgAQFKASDRVMTLTIA-----EQQQVE 152
Cdd:PRK10247 81 QQVSYCAQ----TPTLfgdTVYDNLIFPWQI-RNQQPDPAIFL-------DDL-ERFALPDTILTKNIAelsggEKQRIS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 153 IARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEV 205
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEI 201
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-219 |
1.63e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG--------KPQTIRGpkdalAAGITLIYQEMQL 92
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRK-----KVGLVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 93 APNlTVAENIFLGseLARGGLVQ-------RKAMlsqaQAV-IDRLGAQFKASdrvMTLTIAEQQQVEIARALHRQSRIL 164
Cdd:PRK13637 97 FEE-TIEKDIAFG--PINLGLSEeeienrvKRAM----NIVgLDYEDYKDKSP---FELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 165 VMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-218 |
1.64e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDA-------- 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 79 ----LAAGITLIYQEMQLAPNLTVAENIfLGSELARGGLVQRKAMlSQAQAVIDRLGAQFKASDRV-MTLTIAEQQQVEI 153
Cdd:PRK10619 86 qlrlLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQEAR-ERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 154 ARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-221 |
1.86e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF----GKFY-----ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIrGPK 76
Cdd:PRK15112 4 LLEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF-GDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 77 DALAAGITLIYQE--MQLAPNLTVAE----NIFLGSELARGGLVQR-KAMLSQAQAVIDRlgaqfkASDRVMTLTIAEQQ 149
Cdd:PRK15112 83 SYRSQRIRMIFQDpsTSLNPRQRISQildfPLRLNTDLEPEQREKQiIETLRQVGLLPDH------ASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 150 QVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
259-476 |
2.07e-17 |
|
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: 82.01 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 259 RLRVEDLT---DGGKV-KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLgIGF 334
Cdd:COG1120 1 MLEAENLSvgyGGRPVlDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 335 LTenrkeQglflELAAQENIT------MATLERDANWGMLNRRKAQTIsDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLI 408
Cdd:COG1120 80 VP-----Q----EPPAPFGLTvrelvaLGRYPHLGLFGRPSAEDREAV-EEALERTGLE-HLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 409 SRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMAR-QGVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
275-495 |
2.32e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.49 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRK--ATGGVIEIDGEPVVIHSPREAIDLGIGFLtenRKEQGLFLELAAQE 352
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIVII---HQELTLVPELSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 353 NITMATlERDANWGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGA 432
Cdd:TIGR02633 98 NIFLGN-EITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 433 KSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQESIMTLATG 495
Cdd:TIGR02633 177 TEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-247 |
2.44e-17 |
|
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: 85.84 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 29 VWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpqtirgpkdALAAGITLIYQEMQLAPNLTVAENIFLGSE- 107
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---------SILTNISDVHQNMGYCPQFDAIDDLLTGREh 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 108 ---LARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFEL 184
Cdd:TIGR01257 2033 lylYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 185 ILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG--QYVGSL--VRDKLNAPELVRMMVGRPLSDLF 247
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafQCLGTIqhLKSKFGDGYIVTMKIKSPKDDLL 2179
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-223 |
3.53e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.33 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTA---TSGEILIDGKPQTirgpKDALAAGITLIYQEMQLAPNLTV 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID----AKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGSEL---ARGGLVQRKAMLSQaqaVIDRLGAQfKASD-------RVMTLTIAEQQQVEIARALHRQSRILVMDE 168
Cdd:TIGR00955 117 REHLMFQAHLrmpRRVTKKEKRERVDE---VLQALGLR-KCANtrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 169 PTAALSSRETQRLFELILRLRDEGMAIIYISHR-MAEVYELSDRVSVLRDGQ--YVGS 223
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRvaYLGS 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-221 |
4.17e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFG-----------KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP-QTI 72
Cdd:PRK10261 312 PILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRiDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 73 RGPK-DALAAGITLIYQE--MQLAPNLTVAENIFlgSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRV-MTLTIAEQ 148
Cdd:PRK10261 392 SPGKlQALRRDIQFIFQDpyASLDPRQTVGDSIM--EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQR 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 149 QQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-221 |
4.20e-17 |
|
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: 80.39 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAG---AYTATSGEILIDGKPQTIRGPKDALAagitLIYQEMQLAPNLTV 98
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQKCVA----YVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGSELaRGGLVQRKAMLSQ--AQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSR 176
Cdd:cd03234 99 RETLTYTAIL-RLPRKSSDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496082746 177 ETQRLFELILRLRDEGMAIIYISHR-MAEVYELSDRVSVLRDGQYV 221
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-223 |
4.90e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.33 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGP-KD--ALAAGITLIYQ--EMQLAPN 95
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDikQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 96 lTVAENIFLGSE-----------LARGGLvqrkAMLSQAQAVIDRlgAQFKASDRVMtltiaeqQQVEIARALHRQSRIL 164
Cdd:PRK13649 102 -TVLKDVAFGPQnfgvsqeeaeaLAREKL----ALVGISESLFEK--NPFELSGGQM-------RRVAIAGILAMEPKIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 165 VMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
271-473 |
4.99e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTEnrkEQGLFLELAA 350
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQ---EASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENItMATLERDANwgmLNRRKAQTISDDAIQLLNIRvpHAQVRAG-GLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:PRK10895 96 YDNL-MAVLQIRDD---LSAEQREDRANELMEEFHIE--HLRDSMGqSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496082746 430 VGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-219 |
1.11e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.16 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 20 YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQ--EMQLApNLT 97
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQnpDNQFV-GAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 98 VAENIFLGSElARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRE 177
Cdd:PRK13650 99 VEDDVAFGLE-NKG--IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 178 TQRLFELILRLRDE-GMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:PRK13650 176 RLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
275-475 |
1.17e-16 |
|
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: 77.86 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLgIGFLTENRKEQGLfLELAaqeni 354
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVPQALELLGL-AHLA----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 tmatlERDANwgmlnrrkaqtisddaiqllnirvphaqvragGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:cd03214 92 -----DRPFN--------------------------------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496082746 435 EIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03214 135 ELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-478 |
1.71e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.74 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvihspreaIDLGIGFLTENRKEQGLFLElAAQENI 354
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP---------IKYDKKSLLEVRKTVGIVFQ-NPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMLN----RRKAQTISDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:PRK13639 92 FAPTVEEDVAFGPLNlglsKEEVEKRVKEALKAVGMegfenKPPHH------LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 426 RGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-221 |
2.10e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKIL------AGAYTaTSGEILIDGKpqTIRGPK 76
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYR-YSGDVLLGGR--SIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 77 DALA--AGITLIYQEMQLAPnLTVAENIFLGSELARggLVQRKAMLSQAQAVIDRLG----AQFKASDRVMTLTIAEQQQ 150
Cdd:PRK14271 95 DVLEfrRRVGMLFQRPNPFP-MSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 151 VEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
275-483 |
2.76e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 78.69 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPreaidlgigfltENRKEQGLFLELAAQENI 354
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR------------KQRRAFRRDVQLVFQDSP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGM-----------LNRRKAQTIsdDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDE 423
Cdd:TIGR02769 99 SAVNPRMTVRQIIgeplrhltsldESEQKARIA--ELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 424 PTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGD 483
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-219 |
2.99e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAAGITLIYQEMQLApNLTVAE 100
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAALRQAISVVSQRVHLF-SATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NIFLGSELAR-------------GGLVQRKAMLSqaqAVIDRLGAQfkasdrvmtLTIAEQQQVEIARALHRQSRILVMD 167
Cdd:PRK11160 433 NLLLAAPNASdealievlqqvglEKLLEDDKGLN---AWLGEGGRQ---------LSGGEQRRLGIARALLHDAPLLLLD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496082746 168 EPTAALSSRETQRLFELILRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:PRK11160 501 EPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGL-EQFDRICVMDNGQ 550
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
291-491 |
3.56e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.69 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 291 GAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDLGIGFLTENRKEQglflelaaqenITMATLERDANWGMLNR 370
Cdd:PRK13652 40 GAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVFQNPDDQ-----------IFSPTVEQDIAFGPINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 371 -RKAQTIS---DDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMN 441
Cdd:PRK13652 108 gLDEETVAhrvSSALHMLGLeelrdRVPHH------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496082746 442 DMA-RQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDI-SQESIMT 491
Cdd:PRK13652 182 DLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLA 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
243-476 |
4.04e-16 |
|
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: 81.42 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 243 LSDLFNKERD---------IPRGQPRLRVEDLT-----DGGKV-KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKA 307
Cdd:COG2274 448 LDDILDLPPEreegrsklsLPRLKGDIELENVSfrypgDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 308 TGGVIEIDGEPVvihsprEAIDLG-----IGFLTEnrkEQGLF---LElaaqENITMAtlerdanwgmlnrrkAQTISDD 379
Cdd:COG2274 528 TSGRILIDGIDL------RQIDPAslrrqIGVVLQ---DVFLFsgtIR----ENITLG---------------DPDATDE 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 380 ----AIQLLNI-----RVP---HAQVRAGG--LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMAr 445
Cdd:COG2274 580 eiieAARLAGLhdfieALPmgyDTVVGEGGsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL- 658
|
250 260 270
....*....|....*....|....*....|.
gi 496082746 446 QGVAILMISSELpEVVGMSDRVYVMREGAIA 476
Cdd:COG2274 659 KGRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-258 |
4.64e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.08 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG---KPQTIRGPKDALAAGI 83
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLGSELARGGLVQRKamlSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERR---EKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 164 LVMDEPTAALSSR-ETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDK-LNAP--ELVRMMV 239
Cdd:PRK10070 186 LLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEiLNNPanDYVRTFF 265
|
250 260
....*....|....*....|
gi 496082746 240 -GRPLSDLFNKeRDIPRGQP 258
Cdd:PRK10070 266 rGVDISQVFSA-KDIARRTP 284
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
4.70e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.35 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGK-FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP-QTIRGPKDALAAGI 83
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQ--EMQLApNLTVAENIFLGselARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQS 161
Cdd:PRK13636 85 GMVFQdpDNQLF-SASVYQDVSFG---AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-236 |
5.33e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGIT 84
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LIYQ---EMQLAPnlTVAENIFLGSelARGGLvQRKAMLSQAQAVIDRLGAQfKASDRV-MTLTIAEQQQVEIARALHRQ 160
Cdd:PRK13652 82 LVFQnpdDQIFSP--TVEQDIAFGP--INLGL-DEETVAHRVSSALHMLGLE-ELRDRVpHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGS-LVRDKLNAPELVR 236
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYgTVEEIFLQPDLLA 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-196 |
6.45e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIR---------GPKDAlaagitliyqemqL 92
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvaeachylGHRNA-------------M 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 93 APNLTVAENI-----FLGSElargglvqrkamLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMD 167
Cdd:PRK13539 85 KPALTVAENLefwaaFLGGE------------ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|.
gi 496082746 168 EPTAALSSReTQRLF-ELIL-RLRDEGMAII 196
Cdd:PRK13539 153 EPTAALDAA-AVALFaELIRaHLAQGGIVIA 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
260-478 |
6.52e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 6.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTDGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDLGIGFLTENR 339
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 340 KEQglflelaaqenITMATLERDANWGMLN----RRKAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIG 415
Cdd:PRK13642 91 DNQ-----------FVGATVEDDVAFGMENqgipREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 416 PRILILDEPTRGVDVGAKSEIYRIMNDMA-RQGVAILMISSELPEVVGmSDRVYVMREGAIAGE 478
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-430 |
7.78e-16 |
|
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: 79.98 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILidgkpqtirgpkdaLAAGIT 84
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------------PQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 85 LIY--QEMQLAPNLTVAENIFLGselargglvqrkamLSQAQAVIDRL---GAQFKASDRVMTLTIAEQ----------- 148
Cdd:TIGR03719 70 VGYlpQEPQLDPTKTVRENVEEG--------------VAEIKDALDRFneiSAKYAEPDADFDKLAAEQaelqeiidaad 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 149 -----QQVEIA---------------------------RALHRQSRILVMDEPTAALSSrETQRLFELILRlRDEGmAII 196
Cdd:TIGR03719 136 awdldSQLEIAmdalrcppwdadvtklsggerrrvalcRLLLSKPDMLLLDEPTNHLDA-ESVAWLERHLQ-EYPG-TVV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 197 YISH------RMAE-VYELsDR-VSVLRDGQYVGSLV---------------RDKLNAPEL--VRMMV-GR--------- 241
Cdd:TIGR03719 213 AVTHdryfldNVAGwILEL-DRgRGIPWEGNYSSWLEqkqkrleqeekeesaRQKTLKRELewVRQSPkGRqakskarla 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 242 PLSDLFNKERD---------IPRGqPRL-----RVEDLTD--GGKV--KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFG 303
Cdd:TIGR03719 292 RYEELLSQEFQkrnetaeiyIPPG-PRLgdkviEAENLTKafGDKLliDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 304 VRKATGGVIEIdGEPVVihspreaidlgIGFLTENRKeqglflELAAQENItmatlerdanWgmlnrrkaQTISD--DAI 381
Cdd:TIGR03719 371 QEQPDSGTIEI-GETVK-----------LAYVDQSRD------ALDPNKTV----------W--------EEISGglDII 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 382 QLLNIRVPH-------------AQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDV 430
Cdd:TIGR03719 415 KLGKREIPSrayvgrfnfkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-238 |
8.43e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.83 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTL-MKILAGAY-TATSGEILIDGKPQTIRGPKDALAAGITLIYQEM-QLAPNL-- 96
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRkGYGLNLid 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 97 TVAENIFLGS--ELARGGLVQRKAMLSQAQAVIDRLgaQFKASD---RVMTLTIAEQQQVEIARALHRQSRILVMDEPTA 171
Cdd:NF040905 356 DIKRNITLANlgKVSRRGVIDENEEIKVAEEYRKKM--NIKTPSvfqKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTR 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 172 ALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMM 238
Cdd:NF040905 434 GIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-215 |
1.15e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILidgKPQTIRgpkdalaagI 83
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGKLR---------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLAPNLTVAENIFLgseLARGGlVQRKAMLsqaqAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFL---RLRPG-TKKEDIL----PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 164 LVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVL 215
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
275-483 |
1.16e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVihspreaidlgigflTENRKEQGLF---LELAAQ 351
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA---------------KLNRAQRKAFrrdIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ENITMATLERDANWGM---------LNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILD 422
Cdd:PRK10419 97 DSISAVNPRKTVREIIreplrhllsLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 423 EPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGD 483
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-201 |
1.19e-15 |
|
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: 79.33 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAAGI 83
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIYQEMQLApNLTVAENIFLGSELARGGLVQrkAMLSQAQ--AVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHR 159
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENLRLARPDATDEELW--AALERVGlaDWLRALpdGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496082746 160 QSRILVMDEPTAALSSRETQRLFELILRLrDEGMAIIYISHR 201
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-221 |
1.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 36 ALMGENGAGKSTLMKILAGAYTATSGEILIDGK---PQTIRGPKDALAAGITLIYQ--EMQLAPNlTVAENIFLGSElaR 110
Cdd:PRK13641 37 ALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitPETGNKNLKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPK--N 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 111 GGLVQRKAMlSQAQAVIDRLGAqfkaSDRVMT-----LTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELI 185
Cdd:PRK13641 114 FGFSEDEAK-EKALKWLKKVGL----SEDLISkspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLF 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 496082746 186 LRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13641 189 KDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-224 |
1.27e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATS--GEILIDGkpqtiRGPKDALAAGITLIYQEMQLAPNLTVA 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN-----RKPTKQILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQfKASDRVMTLTI------AEQQQVEIARALHRQSRILVMDEPTAAL 173
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELGLT-KCENTIIGNSFirgisgGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 174 SSRETQRLFELILRLRDEGMAIIYISHR-MAEVYELSDRVSVLRDGQ--YVGSL 224
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRclFFGKG 291
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
271-475 |
1.33e-15 |
|
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: 76.12 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAidlGIGFLTENrkeQGLFLELAA 350
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTVFQN---YALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENI----TMATLERDAnwgmLNRRKAQTIsdDAIQLLNirvpHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTR 426
Cdd:cd03300 90 FENIafglRLKKLPKAE----IKERVAEAL--DLVQLEG----YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 427 GVDVGAKSEI-YRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03300 160 ALDLKLRKDMqLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
276-487 |
1.38e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.08 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 276 LVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIdGEPVVIHSPREAidlgigFLTENRKEQGLFLELAaQENIT 355
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQK------EIKPVRKKVGVVFQFP-ESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 356 MATLERDANWGMLN----RRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVG 431
Cdd:PRK13643 99 EETVLKDVAFGPQNfgipKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 432 AKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQE 487
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-236 |
1.53e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITL 85
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLGSELaRGGLVQRkamlsQAQAVIDRLGAQFKAS----DRVMTLTIAEQQQVEIARALHRQS 161
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQI-RDDLSAE-----QREDRANELMEEFHIEhlrdSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVR 236
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
1.87e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.20 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 18 KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILI---------DGKPQTI----RGPKDA--LAAG 82
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITnpysKKIKNFkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 83 ITLIYQ--EMQLAPNlTVAENIFLGSeLARGglVQRKAMLSQAQAVIDRLGAQFKASDRV-MTLTIAEQQQVEIARALHR 159
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGP-VALG--VKKSEAKKLAKFYLNKMGLDDSYLERSpFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 160 QSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
275-467 |
2.16e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.58 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGepvvihspreaiDLGIGFLTEnRKEQGLFLELAAQENI 354
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQ-RSEVPDSLPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMLNRRKAQTISD--DAIQLLNIRvpHAQVRAggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGA 432
Cdd:NF040873 79 AMGRWARRGLWRRLTRDDRAAVDDalERVGLADLA--GRQLGE--LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*
gi 496082746 433 KSEIYRIMNDMARQGVAILMISSElPEVVGMSDRV 467
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHD-LELVRRADPC 188
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
275-473 |
2.20e-15 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 73.96 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLgIGFLTenrkeqglflelaaQENI 354
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVP--------------QDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATlerdanwgmlnrrkaqTISDdaiqllNIrvphaqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:cd03228 87 LFSG----------------TIRE------NI-----------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 496082746 435 EIYRIMNDMaRQGVAILMISSELpEVVGMSDRVYVMREG 473
Cdd:cd03228 134 LILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
275-476 |
2.46e-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: 75.60 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGepvvihspreaIDLGIGFLTENRKEQGLFLelaaQENI 354
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG-----------HDLALADPAWLRRQVGVVL----QENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERD----ANWGMLNRR--KAQTISDDAIQLLNIRVPHAQV---RAGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:cd03252 87 LFNRSIRDnialADPGMSMERviEAAKLAGAHDFISELPEGYDTIvgeQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496082746 426 RGVDVGAKSEIYRIMNDMArQGVAILMISSELpEVVGMSDRVYVMREGAIA 476
Cdd:cd03252 167 SALDYESEHAIMRNMHDIC-AGRTVIIIAHRL-STVKNADRIIVMEKGRIV 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-219 |
2.58e-15 |
|
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: 79.22 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQE---------MQL 92
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDpvlfsgslrMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 93 APNLTVA-ENIFLGSELArgglvQRKAMLSQAQAVIDrlgaqFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTA 171
Cdd:TIGR00957 1381 DPFSQYSdEEVWWALELA-----HLKTFVSALPDKLD-----HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 172 ALsSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSdRVSVLRDGQ 219
Cdd:TIGR00957 1451 AV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE 1496
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
260-470 |
2.99e-15 |
|
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: 76.63 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDL-----TDGGKVKPS---SLVVHAGEIVGLAGLVGAGRSELAQLIFGV---RKATGGVIEIDGEPVVIHSPREAI 328
Cdd:COG0444 2 LEVRNLkvyfpTRRGVVKAVdgvSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 329 DLGigflteNRKEQGLFlelaaQE------------NITMATLERdanWGMLNRRKAQTISDDAIQLLNIRVPHAQVRA- 395
Cdd:COG0444 82 KIR------GREIQMIF-----QDpmtslnpvmtvgDQIAEPLRI---HGGLSKAEARERAIELLERVGLPDPERRLDRy 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 396 -GGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVM 470
Cdd:COG0444 148 pHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-478 |
3.70e-15 |
|
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: 74.93 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidlgigfLTENRKEQG-------LFLE 347
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKE--------LRKARRRIGmifqhfnLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 LAAQENITMAtLERdANWGMLNRRKAqtiSDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRG 427
Cdd:cd03258 97 RTVFENVALP-LEI-AGVPKAEIEER---VLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496082746 428 VDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:cd03258 171 LDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-475 |
3.76e-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: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVvihsPREAIDlGIGFLTEnrkEQGLFLELAAQENI 354
Cdd:COG4152 21 SFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRR-RIGYLPE---ERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 T-MATLerdanWGMlNRRKAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQQKL-----LISRwvaigPRILILDEPTRGV 428
Cdd:COG4152 93 VyLARL-----KGL-SKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVqliaaLLHD-----PELLILDEPFSGL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 429 DVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
275-478 |
4.46e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTENRKeqgLFLELAAQENI 354
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTVEENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDanwgmlnRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:PRK11614 102 AMGGFFAE-------RDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496082746 435 EIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
275-475 |
5.75e-15 |
|
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: 72.63 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLgIGFLTENRKeqgLFlelaaqeni 354
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VGYLPQDDE---LF--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 tmatlerdanwgmlnrrkAQTISDdaiqllNIrvphaqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:cd03246 89 ------------------SGSIAE------NI-----------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 435 EIYRIMNDMARQGVAILMISSElPEVVGMSDRVYVMREGAI 475
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-221 |
6.33e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.20 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 18 KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG-------KPQTIRGPKDALaaGITLIYQEM 90
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPVRKRI--GMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 91 QLAPNlTVAENIFLGSElargglvQRKAMLSQAQAVIDRLGAQFKASDRVMTLTI-----AEQQQVEIARALHRQSRILV 165
Cdd:PRK13646 97 QLFED-TVEREIIFGPK-------NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfqmsgGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 166 MDEPTAALSSRETQRLFELILRLR-DEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-201 |
6.79e-15 |
|
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: 72.19 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEIlidGKPQtirgpkdalAAGITLIYQEmqlapnltvaen 101
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPE---------GEDLLFLPQR------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 iflgSELARGGLvqrkamlsqAQAVIdrlgaqfKASDRVmtLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRL 181
Cdd:cd03223 73 ----PYLPLGTL---------REQLI-------YPWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170 180
....*....|....*....|
gi 496082746 182 FELilrLRDEGMAIIYISHR 201
Cdd:cd03223 131 YQL---LKELGITVISVGHR 147
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
260-473 |
7.36e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.53 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTDGGKVKPS---SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGgviEIDGEpvVIHSPREAIDLGIGFLT 336
Cdd:PRK09473 18 LRVTFSTPDGDVTAVndlNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGS--ATFNGREILNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 337 ENRKEQ--GLFLELAAQENITMATLERDANWGMLNRR--KAQTIsDDAIQLLN-IRVPHAQVRAG----GLSGGNQQKLL 407
Cdd:PRK09473 93 KLRAEQisMIFQDPMTSLNPYMRVGEQLMEVLMLHKGmsKAEAF-EESVRMLDaVKMPEARKRMKmyphEFSGGMRQRVM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 408 ISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-240 |
7.43e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPV-LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpQTIRGPKDAL 79
Cdd:PRK10253 1 MTESVArLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-HIQHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 80 AAGITLIYQEMQLAPNLTVAENIFLGSELARGGLVQ-RKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALH 158
Cdd:PRK10253 80 ARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 159 RQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRM 237
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
|
...
gi 496082746 238 MVG 240
Cdd:PRK10253 240 IYG 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-225 |
7.55e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.39 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAF----GKFY------ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpQTI 72
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ-DLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 73 RGPKDALAA---GITLIYQE--MQLAPNLTV----AENIFLGSELARGglvQRKAmlsQAQAVIDRLGAQFKASDRV--M 141
Cdd:PRK11308 81 KADPEAQKLlrqKIQIVFQNpyGSLNPRKKVgqilEEPLLINTSLSAA---ERRE---KALAMMAKVGLRPEHYDRYphM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 142 tLTIAEQQQVEIARALHRQSRILVMDEPTAALS-SRETQRLfELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLrdgq 219
Cdd:PRK11308 155 -FSGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVL-NLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM---- 228
|
....*.
gi 496082746 220 YVGSLV 225
Cdd:PRK11308 229 YLGRCV 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
275-475 |
1.01e-14 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 73.39 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDLGIGFLTEnrkEQGLFLElAAQENI 354
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQ---DVTLFYG-TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMlnrrKAQTISdDAIQLLNiRVPHA---QVRAGG--LSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:cd03245 99 TLGAPLADDERIL----RAAELA-GVTDFVN-KHPNGldlQIGERGrgLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496082746 430 VGAKSEIYRIMNDMARQgvAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03245 173 MNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
260-476 |
1.11e-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: 73.76 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLT----DGGKV-KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVvihspreaIDLGIGF 334
Cdd:cd03256 1 IEVENLSktypNGKKAlKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI--------NKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 335 LTENRKEQG-------LFLELAAQENITMATLERDANW-GMLNRRKAQTISDdAIQLLNiRV---PHAQVRAGGLSGGNQ 403
Cdd:cd03256 73 LRQLRRQIGmifqqfnLIERLSVLENVLSGRLGRRSTWrSLFGLFPKEEKQR-ALAALE-RVgllDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 404 QKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-235 |
1.61e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.62 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQEmqlaPN----- 95
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW-VRSKVGLVFQD----PDdqvfs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 96 LTVAENIFLGSELARgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSS 175
Cdd:PRK13647 95 STVWDDVAFGPVNMG---LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 176 RETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELV 235
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-221 |
2.13e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAF-----------GKFYALKGVDLTVWPGEIHALMGENGAGKST----LMKILAgaytaTSGEILIDG 67
Cdd:PRK15134 272 ASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 68 KPQTIRGPKDALA--AGITLIYQE--MQLAPNLTVAENIFLGSELARGGL--VQRKAMLSQAQAVI-------DRLGAQF 134
Cdd:PRK15134 347 QPLHNLNRRQLLPvrHRIQVVFQDpnSSLNPRLNVLQIIEEGLRVHQPTLsaAQREQQVIAVMEEVgldpetrHRYPAEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 135 KASDRvmtltiaeqQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVS 213
Cdd:PRK15134 427 SGGQR---------QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVI 497
|
....*...
gi 496082746 214 VLRDGQYV 221
Cdd:PRK15134 498 VLRQGEVV 505
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-221 |
2.25e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRGPK-DALAAGITLIYQEMQLApNLTVA 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDLRDYTlASLRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIflgsELARGGLVQRK-----AMLSQAQAVIDRLGAQFkasDRVM-----TLTIAEQQQVEIARALHRQSRILVMDEP 169
Cdd:PRK11176 435 NNI----AYARTEQYSREqieeaARMAYAMDFINKMDNGL---DTVIgengvLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496082746 170 TAALSSrETQRLFELILRLRDEGMAIIYISHRMAEVyELSDRVSVLRDGQYV 221
Cdd:PRK11176 508 TSALDT-ESERAIQAALDELQKNRTSLVIAHRLSTI-EKADEILVVEDGEIV 557
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
268-489 |
2.34e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 268 GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVvihsPREA--IDLGIGFLTENrkeQG 343
Cdd:PRK13536 52 GDKavVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARArlARARIGVVPQF---DN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 344 LFLELAAQENITMatlerdanWGMLNRRKAQTISDDAIQLLNI-RVPH-AQVRAGGLSGGNQQKLLISRWVAIGPRILIL 421
Cdd:PRK13536 125 LDLEFTVRENLLV--------FGRYFGMSTREIEAVIPSLLEFaRLESkADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 422 DEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQESI 489
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-219 |
2.46e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.11 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAF-GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDalaAGITL 85
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLTVAENIFLG--------SELARggLVQRKAMLSQAQAVIDRLGAQFKASDRvmtltiaeqQQVEIARAL 157
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGlkirgmpkAEIEE--RVAEAARILELEPLLDRKPRELSGGQR---------QRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 158 HRQSRILVMDEPtaaLSS-----RETQRLfElILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK11650 150 VREPAVFLFDEP---LSNldaklRVQMRL-E-IQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
3.09e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAF--GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDa 78
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 79 LAAGITLIYQEmqlapnltvAENIFLGS----ELARG---GLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQV 151
Cdd:PRK13648 81 LRKHIGIVFQN---------PDNQFVGSivkyDVAFGlenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 152 EIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYElSDRVSVLRDG 218
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
257-479 |
4.20e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.04 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDL-----TDGGKV---KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPreai 328
Cdd:COG1116 5 APALELRGVskrfpTGGGGVtalDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 329 DLGIGFltenrkeQ--GLFLELAAQENITMATLERDanwgmLNRRKAQTISDDAIQLLNI-----RVPHAqvraggLSGG 401
Cdd:COG1116 81 DRGVVF-------QepALLPWLTVLDNVALGLELRG-----VPKAERRERARELLELVGLagfedAYPHQ------LSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 402 NQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVM--REGAIAGE 478
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEE 222
|
.
gi 496082746 479 L 479
Cdd:COG1116 223 I 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
253-473 |
4.98e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 253 IPRGQ--------PRLRVEDLT---DG-GKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVV 320
Cdd:PRK11607 5 IPRPQaktrkaltPLLEIRNLTksfDGqHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 321 iHSPREAIDLGIGFltenrKEQGLFLELAAQENITMATLERDANWGMLNRRKAQTISDDAIQLLNIRVPHAqvraggLSG 400
Cdd:PRK11607 85 -HVPPYQRPINMMF-----QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ------LSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 401 GNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEI-YRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-219 |
5.26e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKF-YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPkDALAAGITL 85
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP-EDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQLAPNLtvaenifLGSElargGLVQRKAmlsQAQAVIDRLGAQFKAS---DRVMTLTIAEQQQVEIAR--ALHRQ 160
Cdd:PRK10522 402 VFTDFHLFDQL-------LGPE----GKPANPA---LVEKWLERLKMAHKLEledGRISNLKLSKGQKKRLALllALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 161 SRILVMDEpTAALSSRETQRLF--ELILRLRDEGMAIIYISHRMAeVYELSDRVSVLRDGQ 219
Cdd:PRK10522 468 RDILLLDE-WAADQDPHFRREFyqVLLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNGQ 526
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-210 |
5.38e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILaGAYTATSGEILIDGK----PQTI---RGPKD 77
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRveffNQNIyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 78 ALAAGITLIYQEMQLAPnLTVAENIFLG-------SELARGGLVQRKAmlsQAQAVIDRLGAQFKASdrVMTLTIAEQQQ 150
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGvkivgwrPKLEIDDIVESAL---KDADLWDEIKHKIHKS--ALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 151 VEIARALHRQSRILVMDEPTAALSSRETQRLFELI--LRLRDEgMAIIYISHRMAEVYELSD 210
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-219 |
5.55e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.37 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 25 VDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpqtiRGPKDAlAAGITL---------IYQEMQLAPN 95
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-----RVLFDA-EKGICLppekrrigyVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 96 LTVAENIFLGselargglvQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSS 175
Cdd:PRK11144 91 YKVRGNLRYG---------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 176 RETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK11144 162 PRKRELLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-224 |
7.02e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.76 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTA---TSGEILIDGkpqtirGPKDALAAGITLIYQEMQL-APNLT 97
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNG------RPLDSSFQRSIGYVQQQDLhLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 98 VAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMT----LTIAEQQQVEIARALHRQSRILV-MDEPTAA 172
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 173 LSSRETQRLFELILRLRDEGMAIIYISHR-MAEVYELSDRVSVLRDGQ---YVGSL 224
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHGQAILCTIHQpSAILFEEFDRLLLLQKGGqtvYFGDL 988
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
256-478 |
7.12e-14 |
|
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: 74.02 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 256 GQPRLRVEDLT---DGGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAIDL 330
Cdd:COG4988 333 GPPSIELEDVSfsyPGGRpaLDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 331 GIGFLTENrkeQGLF---LElaaqENITMATleRDANWGMLNR--RKAQtISDDAIQL---LNIRVphaQVRAGGLSGGN 402
Cdd:COG4988 412 QIAWVPQN---PYLFagtIR----ENLRLGR--PDASDEELEAalEAAG-LDEFVAALpdgLDTPL---GEGGRGLSGGQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 403 QQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARqGVAILMISSELpEVVGMSDRVYVMREGAIAGE 478
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRIVEQ 552
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-196 |
8.70e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 70.08 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDALAAGITLI 86
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP--LAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENIFLGSELARGGlvQRkaMLSQAQAVIDRLGaqfkASDR-VMTLTIAEQQQVEIARALHRQSRILV 165
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHGGA--QR--TIEDALAAVGLTG----FEDLpAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|...
gi 496082746 166 MDEPTAALsSRETQRLFELILR--LRDEGMAII 196
Cdd:TIGR01189 151 LDEPTTAL-DKAGVALLAGLLRahLARGGIVLL 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-221 |
8.84e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP--QTIRGPKDALAAGITLIYQEMQLA--PNLT 97
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaKLNRAQRKAFRRDIQMVFQDSISAvnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 98 VAENI-----FLGSELARGGLVQRKAMLSQ---AQAVIDRLGAQfkasdrvmtLTIAEQQQVEIARALHRQSRILVMDEP 169
Cdd:PRK10419 108 VREIIreplrHLLSLDKAERLARASEMLRAvdlDDSVLDKRPPQ---------LSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 170 TAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-225 |
9.27e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 9.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMK-------ILAGAytATSGEILIDGKpqTIRGPK-D 77
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGK--NLYAPDvD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 78 ALAA--GITLIYQEMQLAPNlTVAENIFLGSELA--RGG---LVQRKamLSQAqAVIDRLGAQFKASDrvMTLTIAEQQQ 150
Cdd:PRK14243 86 PVEVrrRIGMVFQKPNPFPK-SIYDNIAYGARINgyKGDmdeLVERS--LRQA-ALWDEVKDKLKQSG--LSLSGGQQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 151 VEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRdEGMAIIYISHRMAEVYELSD-----RVSVLRDGQYVGSLV 225
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDmtaffNVELTEGGGRYGYLV 238
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
275-482 |
9.37e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.47 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAI-----DLGIGFltenrKEQGLFLELA 349
Cdd:COG2884 22 SLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIpylrrRIGVVF-----QDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENITMATLERDANWGMLNRRkaqtiSDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEP 424
Cdd:COG2884 96 VYENVALPLRVTGKSRKEIRRR-----VREVLDLVGLsdkakALPHE------LSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 425 TRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAG 482
Cdd:COG2884 165 TGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARG 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
257-474 |
9.57e-14 |
|
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: 70.54 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDLTD-------GGKVKPS----SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEI--DGEPVVIH- 322
Cdd:COG4778 2 TTLLEVENLSKtftlhlqGGKRLPVldgvSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 323 -SPREAIDL---GIGFLTEnrkeqglFL---------ELAAQENITMATLERDAnwgmlnRRKAQtisdDAIQLLNIRVP 389
Cdd:COG4778 82 aSPREILALrrrTIGYVSQ-------FLrviprvsalDVVAEPLLERGVDREEA------RARAR----ELLARLNLPER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 390 HAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYV 469
Cdd:COG4778 145 LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVD 224
|
....*
gi 496082746 470 MREGA 474
Cdd:COG4778 225 VTPFS 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
275-476 |
1.04e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.89 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVviHSPREAIdlgigflTENRKEQG-------LFLE 347
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDE-------RLIRQEAGmvfqqfyLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 LAAQENITMATLE-RDANwgmlnRRKAQTIsddAIQLLNiRVPHAQvRAGG----LSGGNQQKLLISRWVAIGPRILILD 422
Cdd:PRK09493 92 LTALENVMFGPLRvRGAS-----KEEAEKQ---ARELLA-KVGLAE-RAHHypseLSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 423 EPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-221 |
1.06e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.60 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGpKDALAAGITLIYQE-MQLAPnlTVAE 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQDpVVLAD--TFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NIFLGSELARGGLVQRKAMLSQAQAVID-------RLGAQFKasdrvmTLTIAEQQQVEIARALHRQSRILVMDEPTAAL 173
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSlpdglytPLGEQGN------NLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 174 SSrETQRLFELILRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:PRK10790 508 DS-GTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
260-476 |
1.10e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 69.86 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLT--DGGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVR--KATGGVIEIDGEPVVIHSPREAIDLGIg 333
Cdd:cd03217 1 LEIKDLHvsVGGKeiLKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 334 FLTenrkeqglFLELAAQENITMATLERDANWGmlnrrkaqtisddaiqllnirvphaqvraggLSGGNQQKLLISRWVA 413
Cdd:cd03217 80 FLA--------FQYPPEIPGVKNADFLRYVNEG-------------------------------FSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 414 IGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMIS--SELPEVVgMSDRVYVMREGAIA 476
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYI-KPDRVHVLYDGRIV 184
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-221 |
1.31e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.34 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 25 VDLTVWPGEIHALMGENGAGKSTLMKILAG--AYTatsGEILIDGKPQTIRGPKDALAAgITLIYQEMQLaPNLTVAENI 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGflPYQ---GSLKINGIELRELDPESWRKH-LSWVGQNPQL-PHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 103 FLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQR 180
Cdd:PRK11174 444 LLGNPDASDEQLQQALENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 181 LFELILRLRDEGMAIIyISHRMAEVYELsDRVSVLRDGQYV 221
Cdd:PRK11174 524 VMQALNAASRRQTTLM-VTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
260-475 |
1.35e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDL----TDGGK-VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvihspreaIDLGIGF 334
Cdd:PRK13636 6 LKVEELnynySDGTHaLKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP---------IDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 335 LTENRKEQGLFLElAAQENITMATLERDANWGMLNRRkaqtISDDAIQLlniRVPHAQVRAG----------GLSGGNQQ 404
Cdd:PRK13636 77 LMKLRESVGMVFQ-DPDNQLFSASVYQDVSFGAVNLK----LPEDEVRK---RVDNALKRTGiehlkdkpthCLSFGQKK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 405 KLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
257-478 |
1.92e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDL------TDGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDL 330
Cdd:PRK13635 3 EEIIRVEHIsfrypdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 331 GIGFLTENRKEQglFLElaaqenitmATLERDANWGMLN----RRKAQTISDDAIQLLNI-----RVPHAqvraggLSGG 401
Cdd:PRK13635 82 QVGMVFQNPDNQ--FVG---------ATVQDDVAFGLENigvpREEMVERVDQALRQVGMedflnREPHR------LSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 402 NQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEvVGMSDRVYVMREGAIAGE 478
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDE-AAQADRVIVMNKGEILEE 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-267 |
2.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.43 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDgkPQTIRGPKDAL-------AAGITLIYQEMQLA 93
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG--ERVITAGKKNKklkplrkKVGIVFQFPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 94 PNlTVAENIFLGSElaRGGLVQRKAmLSQAQAVIDRLGAQFKASDRV-MTLTIAEQQQVEIARALHRQSRILVMDEPTAA 172
Cdd:PRK13634 100 EE-TVEKDICFGPM--NFGVSEEDA-KQKAREMIELVGLPEELLARSpFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 173 LSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKL--NAPELVRMMVGRPLSDLFNK 249
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfaDPDELEAIGLDLPETVKFKR 255
|
250 260
....*....|....*....|..
gi 496082746 250 ERDIPRG----QPRLRVEDLTD 267
Cdd:PRK13634 256 ALEEKFGisfpKPCLTLEELAH 277
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
275-478 |
2.46e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGepVVIHSPREAidlgiGFLTENRKEQGLFLELAaQENI 354
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD--ITITHKTKD-----KYIRPVRKRIGMVFQFP-ESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMLN-RRKAQTISDDAIQLL-------NIrvphAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTR 426
Cdd:PRK13646 99 FEDTVEREIIFGPKNfKMNLDEVKNYAHRLLmdlgfsrDV----MSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 427 GVDVGAKSEIYRIMNDMA-RQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-210 |
2.73e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqTIRGPKDALAAgitLIYQEMQLAPNLTV-A 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVA---YVPQSEEVDWSFPVlV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELARGGLVQR-----KAMLSQAQAVIDRLGAQFKasdRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALS 174
Cdd:PRK15056 98 EDVVMMGRYGHMGWLRRakkrdRQIVTAALARVDMVEFRHR---QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 496082746 175 SRETQRLFELILRLRDEGMAIIYISHRMAEVYELSD 210
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
271-475 |
3.12e-13 |
|
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: 69.98 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidlgigfLTENRKEQ-------- 342
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE--------LRELRRKKismvfqsf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 343 GLFLELAAQENIT-------MATLERdanwgmlnRRKAQtisdDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIG 415
Cdd:cd03294 112 ALLPHRTVLENVAfglevqgVPRAER--------EERAA----EALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 416 PRILILDEPTRGVDvgakSEIYRIMND-----MARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03294 179 PDILLMDEAFSALD----PLIRREMQDellrlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-234 |
3.51e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.48 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTAtSGEILIDGKPqtIRG-PKDALAAGITLIYQEMQLAPNLTVAE 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRP--LSDwSAAELARHRAYLSQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 NIFLGselargglVQRKAMLSQAQAVIDRLGAQFKASDR----VMTLTIAEQQQVEIARAL-------HRQSRILVMDEP 169
Cdd:COG4138 89 YLALH--------QPAGASSEAVEQLLAQLAEALGLEDKlsrpLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 170 TAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPEL 234
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-249 |
3.69e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 18 KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILI-DGK-PQTIRGPKDA--LAAGITLIYQ--EMQ 91
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAiPANLKKIKEVkrLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 92 LAPNlTVAENIFLGSeLARGGlvQRKAMLSQAQAVIDRLGAQFKASDRV-MTLTIAEQQQVEIARALHRQSRILVMDEPT 170
Cdd:PRK13645 103 LFQE-TIEKDIAFGP-VNLGE--NKQEAYKKVPELLKLVQLPEDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 171 AALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV--GS----------LVRDKLNAPELVRM 237
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIsiGSpfeifsnqelLTKIEIDPPKLYQL 258
|
250
....*....|....
gi 496082746 238 M--VGRPLSDLFNK 249
Cdd:PRK13645 259 MykLKNKGIDLLNK 272
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
275-475 |
3.84e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.50 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVvihSPREAIDLGIGFLTENrkeQGLFLELAAQENI 354
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQH---YALFRHMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATlerdanwGMLNRRK---AQTISDDAIQLLN-IRVPH-AQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:PRK10851 96 AFGL-------TVLPRRErpnAAAIKAKVTQLLEmVQLAHlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 430 VGAKSEIYR----IMNDMARQGVAILMISSELPEVvgmSDRVYVMREGAI 475
Cdd:PRK10851 169 AQVRKELRRwlrqLHEELKFTSVFVTHDQEEAMEV---ADRVVVMSQGNI 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-475 |
3.85e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 68.87 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvIHSPREAIDlgigfltENRKEQG-------LFLE 347
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED--LTDSKKDIN-------KLRRKVGmvfqqfnLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 LAAQENITMATLErdanwgMLNRRKAQTIsDDAIQLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEP 424
Cdd:COG1126 92 LTVLENVTLAPIK------VKKMSKAEAE-ERAMELLE-RVglaDKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 425 TRGVD---VGaksEIYRIMNDMARQGVAILMISSELP---EVvgmSDRVYVMREGAI 475
Cdd:COG1126 164 TSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGfarEV---ADRVVFMDGGRI 214
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-221 |
4.34e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.63 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG-------KPQTIRGpkdalAAGITLIYQEMQLA 93
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRK-----LVGIVFQNPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 94 pNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIdRLGAQFKASDRvmTLTIAEQQQVEIARALHRQSRILVMDEPTAAL 173
Cdd:PRK13644 92 -GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-GLEKYRHRSPK--TLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 174 SSRETQRLFELILRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-218 |
4.81e-13 |
|
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: 68.51 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAG---ITLIYQEMQLApNLTV 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGSELARgglvQRKAMLSQA---QAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAAL 173
Cdd:cd03290 96 EENITFGSPFNK----QRYKAVTDAcslQPDIDLLpfGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 174 SSRETQRLF-ELILR-LRDEGMAIIYISHRMAEVYElSDRVSVLRDG 218
Cdd:cd03290 172 DIHLSDHLMqEGILKfLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-233 |
5.17e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 28 TVWPGEIHALMGENGAGKSTLMKILAGAyTATSGEILIDGKP-QTIRGPKDALAAGitliYQEMQLAPNLTVAenIFLGS 106
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPlEAWSAAELARHRA----YLSQQQTPPFAMP--VFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 107 ELARGGLVQrkamLSQAQAVIDRLGAQFKASDR----VMTLTIAEQQQVEIA-------RALHRQSRILVMDEPTAALSS 175
Cdd:PRK03695 91 TLHQPDKTR----TEAVASALNEVAEALGLDDKlgrsVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 176 RETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPE 233
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-240 |
6.89e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 60 SGEILIDGKPQTIRGPKDaLAAGITLIYQEMQLApNLTVAENIFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKAS-- 137
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNvg 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 138 DRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEG-MAIIYISHRMAEVyELSDRVSVLR 216
Cdd:PTZ00265 1354 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKIVVFN 1432
|
170 180
....*....|....*....|....
gi 496082746 217 DGQYVGSLVRDKLNAPELVRMMVG 240
Cdd:PTZ00265 1433 NPDRTGSFVQAHGTHEELLSVQDG 1456
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-219 |
7.50e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQEMQLAPNlTVAEN 101
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-LRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLGSELARGGLVQrkaMLSQA--QAVIDR--LGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRe 177
Cdd:PLN03232 1330 IDPFSEHNDADLWE---ALERAhiKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR- 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496082746 178 TQRLFELILRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQ 219
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
275-487 |
7.78e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIdlgigflTENRKEQGLFLELAaQENI 354
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDI-------KQIRKKVGLVFQFP-ESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMLN----RRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDV 430
Cdd:PRK13649 99 FEETVLKDVAFGPQNfgvsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 431 GAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQE 487
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-200 |
8.13e-13 |
|
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: 70.73 E-value: 8.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDgkpQTIRgpkdalaagitL 85
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---ETVK-----------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQ---LAPNLTVAENIFLGSELARGGLVQrkamlSQAQAVIDRLGaqFKASD---RVMTLTIAEQQQVEIARALHR 159
Cdd:TIGR03719 388 AYVDQSrdaLDPNKTVWEEISGGLDIIKLGKRE-----IPSRAYVGRFN--FKGSDqqkKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 160 QSRILVMDEPTAALSSrETQRLFELILrLRDEGMAIIyISH 200
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDV-ETLRALEEAL-LNFAGCAVV-ISH 498
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
32-201 |
8.42e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 32 GEIHaLMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRGPKDALAAGITLIYQEMQLAPNLTVAENIFLGSELARG 111
Cdd:PRK13540 28 GLLH-LKGSNGAGKTTLLKLIAGLLNPEKGEILFER--QSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 112 GLvqrkamlsqaqaVIDRLGAQFKASDRV----MTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILR 187
Cdd:PRK13540 105 AV------------GITELCRLFSLEHLIdypcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....
gi 496082746 188 LRDEGMAIIYISHR 201
Cdd:PRK13540 173 HRAKGGAVLLTSHQ 186
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-221 |
8.95e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.19 E-value: 8.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 23 KGVDLTVWPGEIHALMGENGAGKS----TLMKILAGAYTATSGEILIDGKP---QTIRGPKdalaagITLIYQEMQLA-- 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPvapCALRGRK------IATIMQNPRSAfn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 94 PNLTVAENiflGSE--LARGGLVQRKAMLSQAQAVidrlgaQFKASDRVMTLTIAEQ-----QQVEIARALHRQSRILVM 166
Cdd:PRK10418 94 PLHTMHTH---AREtcLALGKPADDATLTAALEAV------GLENAARVLKLYPFEMsggmlQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 167 DEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
275-476 |
1.16e-12 |
|
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: 67.22 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGeIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHspREAIDLGIGFLTEnrkEQGLFLELAAQENI 354
Cdd:cd03264 20 SLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ--PQKLRRRIGYLPQ---EFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 -TMATLErdanwGMLNRRKAQTIsDDAIQLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGak 433
Cdd:cd03264 94 dYIAWLK-----GIPSKEVKARV-DEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE-- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 434 sEIYRIMNDMARQGV-AILMISSELPE-VVGMSDRVYVMREGAIA 476
Cdd:cd03264 165 -ERIRFRNLLSELGEdRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
281-473 |
1.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.32 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 281 GEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAidlgigfLTENRKEQGL---FLELAAQENitma 357
Cdd:PRK13641 33 GSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKN-------LKKLRKKVSLvfqFPEAQLFEN---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 358 TLERDANWGMLN----RRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAK 433
Cdd:PRK13641 102 TVLKDVEFGPKNfgfsEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496082746 434 SEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
275-476 |
1.46e-12 |
|
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: 66.91 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFG-VR--KATGGVIEIDGEPVVIHSPREAIdlgiGFLTENrkeqGLFL-ELAA 350
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGrVEggGTTSGQILFNGQPRKPDQFQKCV----AYVRQD----DILLpGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENITMATLERDANwGMLNRRKAQTISDDAIQLLNI-RVPHAQVRagGLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:cd03234 99 RETLTYTAILRLPR-KSSDAIRKKRVEDVLLRDLALtRIGGNLVK--GISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 430 VGAKSEIYRIMNDMARQGVAILM-ISSELPEVVGMSDRVYVMREGAIA 476
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
271-475 |
1.51e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 66.89 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAiDLGIGFltenrKEQGLFLELAA 350
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-DIAMVF-----QNYALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENITMATLERDANWGMLNRRkaqtiSDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:cd03301 90 YDNIAFGLKLRKVPKDEIDER-----VREVAELLQIehlldRKPKQ------LSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 426 RGVD----VGAKSEIYRImndMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03301 159 SNLDaklrVQMRAELKRL---QQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-219 |
1.54e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.42 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 8 EMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKDALAAGITLIY 87
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 88 QEMQLAPNLTVAENIFLG----SelaRGGLVQR-KAMLSQAqavIDRLG-AQFKasDRVM-TLTIAEQQQVEIARALHRQ 160
Cdd:COG4604 82 QENHINSRLTVRELVAFGrfpyS---KGRLTAEdREIIDEA---IAYLDlEDLA--DRYLdELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 161 SRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISH--RMAEVYelSDRVSVLRDGQ 219
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHdiNFASCY--ADHIVAMKDGR 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
260-474 |
1.80e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.43 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTD--GGKVKPS----SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLG-- 331
Cdd:TIGR01257 1938 LRLNELTKvySGTSSPAvdrlCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGyc 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 332 -----IGFLTENRKEQGLFLELaaqENITMATLERDANWGmlnrrkaqtisddaIQLLNIRVpHAQVRAGGLSGGNQQKL 406
Cdd:TIGR01257 2018 pqfdaIDDLLTGREHLYLYARL---RGVPAEEIEKVANWS--------------IQSLGLSL-YADRLAGTYSGGNKRKL 2079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 407 LISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGA 474
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
274-475 |
1.87e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 274 SSLVVHAGEIVGLAGLVGAGRSELAQLIFG-VRKATGGVIEIDGE-PVVIHSPREAIDLgigfltenRKEQGLFLELAaQ 351
Cdd:PRK13645 30 TSLTFKKNKVTCVIGTTGSGKSTMIQLTNGlIISETGQTIVGDYAiPANLKKIKEVKRL--------RKEIGLVFQFP-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ENITMATLERDANWGML----NRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRG 427
Cdd:PRK13645 101 YQLFQETIEKDIAFGPVnlgeNKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 428 VDVGAKSEIYRIMNDMAR-QGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
275-475 |
2.17e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.45 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDLGIGFLTENRKEQglflelaaqenI 354
Cdd:PRK13650 27 SFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNPDNQ-----------F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMLNR----RKAQTISDDAIQLLNI-----RVPhaqvraGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:PRK13650 95 VGATVEDDVAFGLENKgiphEEMKERVNEALELVGMqdfkeREP------ARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496082746 426 RGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEvVGMSDRVYVMREGAI 475
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-223 |
2.27e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 67.12 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGA--YTATSGEILIDGKPQTIRGPKDALAAGITLIYQEMQLAPNltVA 99
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIPG--VS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELARGGLVQRKAMLSQ--AQAVIDRLGAQFKASDRVMTLTI------AEQQQVEIARALHRQSRILVMDEPTA 171
Cdd:PRK09580 95 NQFFLQTALNAVRSYRGQEPLDRfdFQDLMEEKIALLKMPEDLLTRSVnvgfsgGEKKRNDILQMAVLEPELCILDESDS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 172 ALSSRETQRLFELILRLRDEGMAIIYISH--RMAEvYELSDRVSVLRDGQYVGS 223
Cdd:PRK09580 175 GLDIDALKIVADGVNSLRDGKRSFIIVTHyqRILD-YIKPDYVHVLYQGRIVKS 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
270-495 |
2.76e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.60 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 270 KVKPSSlvVHAgeivgLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLtenRKEQGLFLELA 349
Cdd:PRK10982 20 KVRPHS--IHA-----LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMV---HQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENITmatLERDANWGML-----NRRKAQTISDDaiqlLNIRVpHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEP 424
Cdd:PRK10982 90 VMDNMW---LGRYPTKGMFvdqdkMYRDTKAIFDE----LDIDI-DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 425 TRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQESIMTLATG 495
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
271-470 |
2.98e-12 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 68.85 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVvIHSPREAIDLGIGFLTEnrkeQGLFLELAA 350
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL-ADADADSWRDQIAWVPQ----HPFLFAGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENITMATleRDANWGMLNRRKAQTISDDAIQLLNiRVPHAQV--RAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGV 428
Cdd:TIGR02857 413 AENIRLAR--PDASDAEIREALERAGLDEFVAALP-QGLDTPIgeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496082746 429 DVGAKSEIYRIMNDMArQGVAILMISSElPEVVGMSDRVYVM 470
Cdd:TIGR02857 490 DAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
281-479 |
3.03e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.05 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 281 GEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDL--GIGFLTENRKeqgLFLELAAQENITMAT 358
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQIGMIFQDHH---LLMDRTVYDNVAIPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 359 LERDANWGMLNRRKAQTIsdDAIQLLNirvpHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYR 438
Cdd:PRK10908 105 IIAGASGDDIRRRVSAAL--DKVGLLD----KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 439 IMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGEL 479
Cdd:PRK10908 179 LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-219 |
3.40e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 65.51 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpQTIRG-PKDALAAGITLIYQEmqlaPNLtva 99
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--IDISTiPLEDLRSSLTIIPQD----PTL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 eniFLGSelARGGLvQRKAMLSQAQavidrLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSrETQ 179
Cdd:cd03369 94 ---FSGT--IRSNL-DPFDEYSDEE-----IYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY-ATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496082746 180 RLFELILRLRDEGMAIIYISHRMAEVYELsDRVSVLRDGQ 219
Cdd:cd03369 162 ALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGE 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-219 |
3.96e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQT-IRgpKDALAAGITLIYQEMQLAPNlTVA 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTkLQ--LDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELARGGLVQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSR- 176
Cdd:PRK10789 407 NNIALGRPDATQQEIEHVARLASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRt 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 177 ETQRLFEliLRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQ 219
Cdd:PRK10789 487 EHQILHN--LRQWGEGRTVIISAHRLSALTE-ASEILVMQHGH 526
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-227 |
6.92e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.26 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGK-----FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEI---LIDGKPQTIRGPKDA 78
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 79 LAAGITL--------------------IYQ--EMQLAPNlTVAENIFLGselARGGLVQRKAMLSQAQAVIDRLGAQFKA 136
Cdd:PRK13651 83 VLEKLVIqktrfkkikkikeirrrvgvVFQfaEYQLFEQ-TIEKDIIFG---PVSMGVSKEEAKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 137 SDRV-MTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVL 215
Cdd:PRK13651 159 LQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|..
gi 496082746 216 RDGQyvgsLVRD 227
Cdd:PRK13651 239 KDGK----IIKD 246
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
271-476 |
7.02e-12 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 65.40 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDLGIGFLTEnrkEQGLFLELAA 350
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE-LRRKIGYVIQ---QIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENI-TMATLERdanWGmlnRRKAQTISDDAIQLLNI-------RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILD 422
Cdd:cd03295 93 EENIaLVPKLLK---WP---KEKIRERADELLALVGLdpaefadRYPHE------LSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 423 EPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-221 |
8.22e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILI-------DGKPQTIRGPKDALaaGITLIYQEMQLA 93
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKPVRKKV--GVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 94 PNlTVAENIFLGSElaRGGLVQRKAMLSQAQAvIDRLGAQFKASDRV-MTLTIAEQQQVEIARALHRQSRILVMDEPTAA 172
Cdd:PRK13643 99 EE-TVLKDVAFGPQ--NFGIPKEKAEKIAAEK-LEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 173 LSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
260-470 |
9.28e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.08 E-value: 9.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTDGGKVKP---SSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRK----ATGGVIEIDGEPVVIHSPRE-----A 327
Cdd:COG4170 9 LTIEIDTPQGRVKAvdrVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRErrkiiG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 328 IDLGIGF------LTENRK--EQglfLElaaqENITMATLERDAnWGMLNRRKAQtisddAIQLLNiRV----------- 388
Cdd:COG4170 89 REIAMIFqepsscLDPSAKigDQ---LI----EAIPSWTFKGKW-WQRFKWRKKR-----AIELLH-RVgikdhkdimns 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 389 -PHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMAR-QGVAILMISSELPEVVGMSDR 466
Cdd:COG4170 155 yPHE------LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADT 228
|
....
gi 496082746 467 VYVM 470
Cdd:COG4170 229 ITVL 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-200 |
9.30e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.05 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDALAAGITLI 86
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP--LDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 87 YQEMQLAPNLTVAENI-FLGSELARgglvqrkamlSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILV 165
Cdd:cd03231 79 GHAPGIKTTLSVLENLrFWHADHSD----------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 496082746 166 MDEPTAALSSRETQRLFELILRLRDEGMAIIYISH 200
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
275-484 |
1.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.16 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDLGIGFLTENRKEQglflelaaqenI 354
Cdd:PRK13648 29 SFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK-LRKHIGIVFQNPDNQ-----------F 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDANWGMLN---------RRKAQTISDdaIQLLNIR--VPHAqvraggLSGGNQQKLLISRWVAIGPRILILDE 423
Cdd:PRK13648 97 VGSIVKYDVAFGLENhavpydemhRRVSEALKQ--VDMLERAdyEPNA------LSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 424 PTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGmSDRVYVMREGAIAGELQAGDI 484
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
397-494 |
1.25e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.64 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 397 GLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIa 476
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI- 254
|
90 100
....*....|....*....|..
gi 496082746 477 geLQAGD----ISQESIMTLAT 494
Cdd:PRK13631 255 --LKTGTpyeiFTDQHIINSTS 274
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
275-476 |
1.30e-11 |
|
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: 65.89 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVV-----IHSPREAIDLGIGFltenrKEQGLFLELA 349
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargIFLPPHRRRIGYVF-----QEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENItmatlerdaNWGMLNRRKAQTIS--DDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRG 427
Cdd:COG4148 94 VRGNL---------LYGRKRAPRAERRIsfDEVVELLGIG-HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 428 VDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:COG4148 164 LDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-68 |
1.43e-11 |
|
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: 62.08 E-value: 1.43e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGK 68
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST 62
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
275-476 |
1.46e-11 |
|
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: 64.17 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEP---VVIHSPREAIdlgiGFLTENRKeqgLFlelaaq 351
Cdd:cd03253 21 SFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDireVTLDSLRRAI----GVVPQDTV---LF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 eNITMATLERDANWG-----MLNRRKAQTIsDDAIqllnIRVPHA---QV--RAGGLSGGNQQKLLISRWVAIGPRILIL 421
Cdd:cd03253 88 -NDTIGYNIRYGRPDatdeeVIEAAKAAQI-HDKI----MRFPDGydtIVgeRGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 422 DEPTRGVDVGAKSEIYRIMNDMARqGVAILMISSELPEVVGmSDRVYVMREGAIA 476
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
260-475 |
1.57e-11 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 63.68 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDL--TDGGKV--KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPreaidlgigfl 335
Cdd:COG4619 1 LELEGLsfRVGGKPilSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 336 TENRK-------EQGLFLELAAqENITMAtlerdanWGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLI 408
Cdd:COG4619 70 PEWRRqvayvpqEPALWGGTVR-DNLPFP-------FQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 409 SRWVAIGPRILILDEPTRGVDVGAKSEIYRIMND-MARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-201 |
1.69e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.37 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILI-DGK-----PQTIRGPKDALAAgiTLIYQEMQLAPN 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGArvlflPQRPYLPLGTLRE--ALLYPATAEAFS 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 96 LTVAENIflgseLARGGLvqrkamlsqaQAVIDRLGAQfkaSDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSS 175
Cdd:COG4178 457 DAELREA-----LEAVGL----------GHLAERLDEE---ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....*.
gi 496082746 176 RETQRLFELiLRLRDEGMAIIYISHR 201
Cdd:COG4178 519 ENEAALYQL-LREELPGTTVISVGHR 543
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-221 |
3.14e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.95 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 20 YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQ-------TIRGpkdalAAGITLIYQEMQL 92
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdeenlwDIRN-----KAGMVFQNPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 93 APNLtVAENIFLGSE-LArgglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTA 171
Cdd:PRK13633 99 VATI-VEEDVAFGPEnLG----IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496082746 172 ALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
275-479 |
3.15e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDL---GIGFLTENRKeqgLFLELAAQ 351
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqKLGFIYQFHH---LLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ENITMATLerdanWGMLNRRKAQTISDDAIQL--LNIRVPHaqvRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:PRK11629 106 ENVAMPLL-----IGKKKPAEINSRALEMLAAvgLEHRANH---RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496082746 430 VGAKSEIYRIMNDM-ARQGVAILMISSELpEVVGMSDRVYVMREGAIAGEL 479
Cdd:PRK11629 178 ARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAEL 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-221 |
3.43e-11 |
|
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: 62.67 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 9 MRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGA---YTATSGEILIDGKPqtirGPKDALAAGITL 85
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIP----YKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IY--QEMQLAPNLTVAENIflgselargglvqrkamlsqaqavidRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRI 163
Cdd:cd03233 86 IYvsEEDVHFPTLTVRETL--------------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 164 LVMDEPTAALSSRETqrlFELILRLRD-----EGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03233 140 LCWDNSTRGLDSSTA---LEILKCIRTmadvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-264 |
4.37e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.20 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 32 GEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG-----KPQTIR----GPKDALAAGITLIyqemqlapnltVAENI 102
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsyKPQYIKadyeGTVRDLLSSITKD-----------FYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 103 FLGSELArgglvqrKAMlsQAQAVIDRlgaqfkasdRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLF 182
Cdd:cd03237 94 YFKTEIA-------KPL--QIEQILDR---------EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 183 ELILRLRDEGMAIIY-ISHRMAEVYELSDRVSVLrDGQyvgSLVRDKLNAPELVRMMVGRPLSDL---FnkERDIPRGQP 258
Cdd:cd03237 156 KVIRRFAENNEKTAFvVEHDIIMIDYLADRLIVF-EGE---PSVNGVANPPQSLRSGMNRFLKNLditF--RRDPETGRP 229
|
....*.
gi 496082746 259 RLRVED 264
Cdd:cd03237 230 RINKLG 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-219 |
4.46e-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: 62.10 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 19 FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGkpqtirgpkdalaaGITLIYQEMQLaPNLTV 98
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWI-QNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGSELargglvqRKAMLsqaQAVIDRLG-----AQFKASDRVM------TLTIAEQQQVEIARALHRQSRILVMD 167
Cdd:cd03250 83 RENILFGKPF-------DEERY---EKVIKACAlepdlEILPDGDLTEigekgiNLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 168 EPTAALSSRETQRLFE-LILRLRDEGMAIIYISHRMaEVYELSDRVSVLRDGQ 219
Cdd:cd03250 153 DPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-207 |
4.58e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 8 EMRHIAKAFG------KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIrGPKDALAA 81
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF-GREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 gitliyqemQLAPNLTVAENIFLgseLARGGLVQRKAMLSqaqavidrlgaqfkasdRVMTLTIAEQQQVEIARALHRQS 161
Cdd:COG2401 105 ---------AIGRKGDFKDAVEL---LNAVGLSDAVLWLR-----------------RFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 162 RILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRmAEVYE 207
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHH-YDVID 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
275-491 |
4.77e-11 |
|
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: 63.18 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFG-VRKATGGVIEIDGEPVVIHSPREaIDLGIGFLTenrkeQGLFLELAAQEN 353
Cdd:COG1119 23 SWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWE-LRKRIGLVS-----PALQLRFPRDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 354 -----IT--MATLERDANWGMLNRRKAqtisDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTR 426
Cdd:COG1119 97 vldvvLSgfFDSIGLYREPTDEQRERA----RELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 427 GVDVGAKSEIYRIMNDMARQG-VAILMIS---SELPEVVgmsDRVYVMREGAIageLQAGDIsqESIMT 491
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGaPTLVLVThhvEEIPPGI---THVLLLKDGRV---VAAGPK--EEVLT 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
260-473 |
5.04e-11 |
|
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: 62.58 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLT--DGGK--VKPSSLVVHAGEIVGLAGLVGAGRS-------ELAQLIFGVRkaTGGVIEIDGEPVVihspreAI 328
Cdd:cd03260 1 IELRDLNvyYGDKhaLKDISLDIPKGEITALIGPSGCGKStllrllnRLNDLIPGAP--DEGEVLLDGKDIY------DL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 329 DLGIgflTENRKEQG-LF-----LELAAQENITMATLERdanwGMLNRRKAQTISDDAIQL--LNIRVpHAQVRAGGLSG 400
Cdd:cd03260 73 DVDV---LELRRRVGmVFqkpnpFPGSIYDNVAYGLRLH----GIKLKEELDERVEEALRKaaLWDEV-KDRLHALGLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 401 GNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQgVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
275-475 |
5.54e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 64.01 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIH-SPREaidLGIGFLTENrkeQGLFLELAAQEN 353
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRE---RRVGFVFQH---YALFPHMTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 354 ItMATLErdanwgMLNRRKAQtISDDAIQLLN-IRVPH-AQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVG 431
Cdd:COG1118 96 I-AFGLR------VRPPSKAE-IRARVEELLElVQLEGlADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 432 AKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG1118 168 VRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
254-476 |
6.01e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 64.77 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 254 PRGQPRLRVEDLT---DGGK---VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREa 327
Cdd:COG4618 325 PRPKGRLSVENLTvvpPGSKrpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 328 idLG--IGFLTENrkeqglfLELAA---QENItmatlerdANWGMLNRRK----AQTIS-DDAIQLLnirvPHA---QVR 394
Cdd:COG4618 404 --LGrhIGYLPQD-------VELFDgtiAENI--------ARFGDADPEKvvaaAKLAGvHEMILRL----PDGydtRIG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 395 AGG--LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMIsSELPEVVGMSDRVYVMRE 472
Cdd:COG4618 463 EGGarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVI-THRPSLLAAVDKLLVLRD 541
|
....
gi 496082746 473 GAIA 476
Cdd:COG4618 542 GRVQ 545
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
275-470 |
6.81e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.60 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLgigflteNRKEQGLFlelaaQ--- 351
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPL-------RRRMQMVF-----Qdpy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ---------ENITMATLErdaNWGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILD 422
Cdd:COG4608 106 aslnprmtvGDIIAEPLR---IHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 423 EPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVM 470
Cdd:COG4608 183 EPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
250-478 |
7.29e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.42 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 250 ERDIPRGQPRLRVEDLT---DGGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVvihsp 324
Cdd:COG1132 330 AVPLPPVRGEIEFENVSfsyPGDRpvLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI----- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 325 REaIDLG-----IGFLTenrkeQGLFL-ELAAQENI-------TMATLERDAnwgmlnrRKAQTisDDAIQLLnirvPH- 390
Cdd:COG1132 405 RD-LTLEslrrqIGVVP-----QDTFLfSGTIRENIrygrpdaTDEEVEEAA-------KAAQA--HEFIEAL----PDg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 391 --AQVRAGG--LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMaRQGVAILMISSELPEVVGMsDR 466
Cdd:COG1132 466 ydTVVGERGvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNA-DR 543
|
250
....*....|..
gi 496082746 467 VYVMREGAIAGE 478
Cdd:COG1132 544 ILVLDDGRIVEQ 555
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
275-467 |
9.19e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEidgepvviHSPReaidLGIGFLTenrkeQGLFLElaaqeni 354
Cdd:PRK09544 24 SLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGK----LRIGYVP-----QKLYLD------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 tmATLERDANWGMlnRRKAQTISDDAIQLLNiRVPHAQVRAG---GLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVG 431
Cdd:PRK09544 80 --TTLPLTVNRFL--RLRPGTKKEDILPALK-RVQAGHLIDApmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 496082746 432 AKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRV 467
Cdd:PRK09544 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
257-475 |
9.53e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDLTD--GGKV--KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEI---DGEPVVIHSPREAID 329
Cdd:PRK11701 4 QPLLSVRGLTKlyGPRKgcRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 330 LGI-----GFLTENrKEQGLFLELAAQENI---TMATLERdaNWGMLNRRKAQTISDDAIQLLNI-RVPHAqvraggLSG 400
Cdd:PRK11701 84 RRLlrtewGFVHQH-PRDGLRMQVSAGGNIgerLMAVGAR--HYGDIRATAGDWLERVEIDAARIdDLPTT------FSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 401 GNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
269-476 |
1.01e-10 |
|
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: 61.03 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 269 GKVKPsslvvhaGEIVGLAGLVGAGRSELAQLIFGVRKATG--GVIEIDGEPVVIHSPREAIdlgiGFLtenRKEQGLFL 346
Cdd:cd03213 30 GKAKP-------GELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKII----GYV---PQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 347 ELAAQENITMAtlerdanwgmlnrrkaqtisddaiqllnirvphAQVRagGLSGGNQQKLLISRWVAIGPRILILDEPTR 426
Cdd:cd03213 96 TLTVRETLMFA---------------------------------AKLR--GLSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 427 GVDVGAKSEIYRIMNDMARQGVAILMI----SSelpEVVGMSDRVYVMREGAIA 476
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGRVI 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
271-478 |
1.01e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIH---------SPREAIDLGIGFLTENRKE 341
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 342 QGLFLELAAQENITMATLErdanwgMLNRRKAQTiSDDAIQLLN---IRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRI 418
Cdd:PRK10619 101 FNLWSHMTVLENVMEAPIQ------VLGLSKQEA-RERAVKYLAkvgIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 419 LILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
275-475 |
1.44e-10 |
|
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: 60.02 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVviHSPREAIDLGIGFLTEnrkEQGLFlelaaqeni 354
Cdd:cd03247 22 SLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLISVLNQ---RPYLF--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 tmatlerdanwgmlnrrkAQTISDDaiqlLNIRvphaqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:cd03247 88 ------------------DTTLRNN----LGRR----------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 435 EIYRIMNDMARqGVAILMISSELPEVVGMsDRVYVMREGAI 475
Cdd:cd03247 136 QLLSLIFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
275-470 |
1.51e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.29 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDL--GIGFLTEN-------RKEQGLF 345
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQNpygslnpRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 346 LELAAQENITMATLERdanwgmlnRRKAQTIsddaIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:PRK11308 115 LEEPLLINTSLSAAER--------REKALAM----MAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496082746 426 RGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVM 470
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-69 |
1.59e-10 |
|
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: 63.28 E-value: 1.59e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 496082746 25 VDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKP 69
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP 395
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
271-475 |
2.07e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 60.81 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEpvVIHSPREAIDLGIGFLTENRKEqgLFLELAA 350
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL--VPWKRRKKFLRRIGVVFGQKTQ--LWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QEniTMATLERDANwgmLNRRKAQTISDDAIQLLNI-RVPHAQVRAggLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:cd03267 113 ID--SFYLLAAIYD---LPPARFKKRLDELSELLDLeELLDTPVRQ--LSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 430 VGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:cd03267 186 VVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-429 |
2.14e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 26 DLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEiLIDGKPQTIRGPKDALAagiTLIYQEMQ------LAPN---- 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFSHITRLSFEQLQ---KLVSDEWQrnntdmLSPGeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 96 -LTVAENIFLGSELArgGLVQRKAMLSQAQAVIDRlgaqfkasdRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALS 174
Cdd:PRK10938 99 gRTTAEIIQDEVKDP--ARCEQLAQQFGITALLDR---------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 175 SRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNAPELVRMM--------VGRPLSDL 246
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLahseqlegVQLPEPDE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 247 FNKERDIPRGQPRLRVEDLTDGGKVKPS----SLVVHAGEIVGLAGLVGAGRSELAQLI--------------FGVRKAT 308
Cdd:PRK10938 248 PSARHALPANEPRIVLNNGVVSYNDRPIlhnlSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndltlFGRRRGS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 309 GGVI------------EIDGEPVVIHSPREAIDLG----IGfltenrkeqglflelaaqenITMATLERdanwgmlNRRK 372
Cdd:PRK10938 328 GETIwdikkhigyvssSLHLDYRVSTSVRNVILSGffdsIG--------------------IYQAVSDR-------QQKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 373 AQTISDdaiqLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:PRK10938 381 AQQWLD----ILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
237-475 |
2.34e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 237 MMVGRPLSDLFNKERdiprgqprlRVEDLTDGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDG 316
Cdd:PRK14246 1 MEAGKSAEDVFNISR---------LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 317 EPVVIHSPREAIDLgigflTENRKEQGL-------FLELAAQENITMATlerdANWGMLNRRKAQTISDDAIQLLNI-RV 388
Cdd:PRK14246 72 KVLYFGKDIFQIDA-----IKLRKEVGMvfqqpnpFPHLSIYDNIAYPL----KSHGIKEKREIKKIVEECLRKVGLwKE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 389 PHAQVR--AGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQgVAILMISSELPEVVGMSDR 466
Cdd:PRK14246 143 VYDRLNspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADY 221
|
....*....
gi 496082746 467 VYVMREGAI 475
Cdd:PRK14246 222 VAFLYNGEL 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
275-475 |
2.43e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.04 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAIDLGIGFltenrKEQGLFLELAAQENI 354
Cdd:PRK11432 26 NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-HRSIQQRDICMVF-----QSYALFPHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 tmatlerdaNWG--MLNRRKAQTIS--DDAIQLLNIrvphaqvrAG-------GLSGGNQQKLLISRWVAIGPRILILDE 423
Cdd:PRK11432 100 ---------GYGlkMLGVPKEERKQrvKEALELVDL--------AGfedryvdQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 424 PTRGVDvgakSEIYRIMNDMARQ-----GVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK11432 163 PLSNLD----ANLRRSMREKIRElqqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
275-475 |
2.64e-10 |
|
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: 60.32 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEP---VVIHSPREaidlGIGFLTEnrkEQGLFlELAAQ 351
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdISRKSLRS----MIGVVLQ---DTFLF-SGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ENITMATLE-RDANWgmlNRRKAQTISDDAIqllnIRVP---HAQV--RAGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:cd03254 95 ENIRLGRPNaTDEEV---IEAAKEAGAHDFI----MKLPngyDTVLgeNGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496082746 426 RGVDVGAKSeiyRIMNDMAR--QGVAILMISSELPEVVGmSDRVYVMREGAI 475
Cdd:cd03254 168 SNIDTETEK---LIQEALEKlmKGRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
8-227 |
2.93e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 8 EMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTA--TSGEILIDGKPQtirgpKDALAAGITL 85
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPK-----KQETFARISG 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQL-APNLTVAENIFLGSELARGGLVQRKAMLSQAQAV-----IDRLGAQFKASDRVMTLTIAEQQQVEIARALHR 159
Cdd:PLN03140 957 YCEQNDIhSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVmelveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVA 1036
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 160 QSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMA-EVYELSDRVSVL-RDGQ--YVGSLVRD 227
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQviYSGPLGRN 1108
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-223 |
3.12e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.97 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAF--GKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAG---AYTATSGEILIDG---KPQTIRGPKD 77
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGitlTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 78 ALaaGITLIYQEMQLApNLTVAENIFLGSElARGglVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARAL 157
Cdd:PRK13640 85 KV--GIVFQNPDNQFV-GATVGDDVAFGLE-NRA--VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 158 HRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVyELSDRVSVLRDGQYVGS 223
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQ 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
274-475 |
3.34e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.67 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 274 SSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVvihspREAIDLG-IGFLTENRKEQGLFLELAaqE 352
Cdd:PRK15056 26 ASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-----RQALQKNlVAYVPQSEEVDWSFPVLV--E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 353 NITMatLERDANWGMLNRRKA--QTISDDA---IQLLNIRvpHAQVraGGLSGGNQQKLLISRWVAIGPRILILDEPTRG 427
Cdd:PRK15056 99 DVVM--MGRYGHMGWLRRAKKrdRQIVTAAlarVDMVEFR--HRQI--GELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 428 VDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVyVMREGAI 475
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTV 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-254 |
3.35e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.88 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQ--EMQLApNLTVA 99
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQnpDNQFV-GATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSE---LARGGLVQRkamLSQAQAVIDRLGAQFKASDRvmtLTIAEQQQVEIARALHRQSRILVMDEPTAALSSR 176
Cdd:PRK13642 101 DDVAFGMEnqgIPREEMIKR---VDEALLAVNMLDFKTREPAR---LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 177 ETQRLFELILRLRDE-GMAIIYISHRMAEVYElSDRVSVLRDGQYVGSLVRDKL--NAPELVRMMVGRPLS-----DLFN 248
Cdd:PRK13642 175 GRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELfaTSEDMVEIGLDVPFSsnlmkDLRK 253
|
....*.
gi 496082746 249 KERDIP 254
Cdd:PRK13642 254 NGFDLP 259
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-152 |
3.40e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFG-KFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILidgkpqtirgpkdaL 79
Cdd:PRK11819 1 MMAQYIYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--------------P 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 80 AAGITLIY--QEMQLAPNLTVAENIFLGselargglvqrkamLSQAQAVIDRL---GAQFKASDRVMTLTIAEQQQVE 152
Cdd:PRK11819 67 APGIKVGYlpQEPQLDPEKTVRENVEEG--------------VAEVKAALDRFneiYAAYAEPDADFDALAAEQGELQ 130
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
271-470 |
3.40e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.26 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidlgigfLTENRKE-QGLFLELA 349
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDE--------WRAVRSDiQMIFQDPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENITMAT--------------LERDANwgmlnRRKAQTISDDAIQLLNI--RVPHAqvraggLSGGNQQKLLISRWVA 413
Cdd:PRK15079 109 ASLNPRMTIgeiiaeplrtyhpkLSRQEV-----KDRVKAMMLKVGLLPNLinRYPHE------FSGGQCQRIGIARALI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 414 IGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVM 470
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
275-476 |
3.82e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 59.85 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEpvvIHSPreaIDLGIGFLtenrkeqglfLELAAQENI 354
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---VSSL---LGLGGGFN----------PELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TM-ATLerdanWGMlNRRKAQTISDDAIQLLNI-RVPHAQVRAggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGA 432
Cdd:cd03220 106 YLnGRL-----LGL-SRKEIDEKIDEIIEFSELgDFIDLPVKT--YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496082746 433 KSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
271-475 |
4.46e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.58 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGV---RKATGGVIEIDGepvvihspreaIDLGIGFLTENRKEQGLFLE 347
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG-----------ITLTAKTVWDIREKVGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 lAAQENITMATLERDANWGMLNRR----KAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDE 423
Cdd:PRK13640 92 -NPDNQFVGATVGDDVAFGLENRAvprpEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 424 PTRGVDVGAKSEIYRIMND-MARQGVAILMISSELPEVVgMSDRVYVMREGAI 475
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
283-484 |
4.85e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 283 IVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPReaidlgiGFLTENRKEQGLFLElaAQENITMATLERD 362
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKR-------GLLALRQQVATVFQD--PEQQIFYTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 363 A-----NWGMLNRRKAQTIsDDAIQLLNI-RVPHAQVRAggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEI 436
Cdd:PRK13638 99 IafslrNLGVPEAEITRRV-DEALTLVDAqHFRHQPIQC--LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496082746 437 YRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDI 484
Cdd:PRK13638 176 IAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
242-475 |
6.19e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 242 PLSDLFNKERDIPRGQPRLRVedltdggkVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVi 321
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEV--------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 322 hspreaiDLGIGFLTENRKEQGLFL--------ELAAQENItmatlERDANWGMLNRRKAQTISDDAIQLLNI--RVPHa 391
Cdd:PRK10535 74 -------TLDADALAQLRREHFGFIfqryhllsHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLedRVEY- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 392 qvRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSElPEVVGMSDRVYVMR 471
Cdd:PRK10535 141 --QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIR 217
|
....
gi 496082746 472 EGAI 475
Cdd:PRK10535 218 DGEI 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
260-473 |
9.17e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTDGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIeIDGEPVVIHSPREaidlgigfLTENR 339
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQ-FAGQPLEAWSAAE--------LARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 340 KEqglfleLAAQEN--ITMATlerdanWGMLNR-RKAQTISDDAIQLLNIRVPHAQVR------AGGLSGGNQQKL---- 406
Cdd:PRK03695 72 AY------LSQQQTppFAMPV------FQYLTLhQPDKTRTEAVASALNEVAEALGLDdklgrsVNQLSGGEWQRVrlaa 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 407 -LISRWVAIGP--RILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK03695 140 vVLQVWPDINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
275-473 |
9.88e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.82 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTENrkeqgLFLELAAQENI 354
Cdd:PRK13537 27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDN-----LDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMatlerdanWGMLNRRKAQTISDDAIQLLNI-RVPH-AQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGA 432
Cdd:PRK13537 102 LV--------FGRYFGLSAAAARALVPPLLEFaKLENkADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 433 KSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK13537 174 RHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
274-475 |
1.07e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 274 SSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEI-------DGEPVVIHSPREAIDLG------IGFLTENRK 340
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknKKKTKEKEKVLEKLVIQktrfkkIKKIKEIRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 341 EQGLFLELAaQENITMATLERDANWGMLN----RRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGP 416
Cdd:PRK13651 106 RVGVVFQFA-EYQLFEQTIEKDIIFGPVSmgvsKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEP 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 417 RILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK13651 185 DFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
275-460 |
1.40e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.29 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIhspreAIDLGIgflteNRKEQGLflelaaqENI 354
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI-----AISSGL-----NGQLTGI-------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDanwgmLNRRKAQTISDDAIQLLNI-RVPHAQVRAggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAK 433
Cdd:PRK13545 107 ELKGLMMG-----LTKEKIKEIIPEIIEFADIgKFIYQPVKT--YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180
....*....|....*....|....*..
gi 496082746 434 SEIYRIMNDMARQGVAILMISSELPEV 460
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-221 |
1.52e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGK--PQTIRGPKDA 78
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 79 LAAGITLIYQEMQLAPNLTVAENIF--LGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDrvmtLTIAEQQQVEIARA 156
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAypLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSE----LSGGMARRAALARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 157 LHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
275-475 |
1.62e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVV------IHspREAIDLGigfltenrKEQGLFlEL 348
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhyLH--RQVALVG--------QEPVLF-SG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 349 AAQENITMAtLERDANWGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGV 428
Cdd:TIGR00958 570 SVRENIAYG-LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 429 DVGAKSEIYrimNDMARQGVAILMISSELPeVVGMSDRVYVMREGAI 475
Cdd:TIGR00958 649 DAECEQLLQ---ESRSRASRTVLLIAHRLS-TVERADQILVLKKGSV 691
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-465 |
1.68e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.51 E-value: 1.68e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEI-YRIMNDMARQGVAILMISSELPEVVGMSD 465
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVeSLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-214 |
1.72e-09 |
|
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: 60.18 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAFGKFyalkgvDLTVWPGEIH-----ALMGENGAGKSTLMKILAGAYTATSGEIL----IDGKPQTI 72
Cdd:COG1245 337 EEETLVEYPDLTKSYGGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkISYKPQYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 73 RGPKDAlaagitliyqemqlapnlTVAEniFLGSelARGGLVQRKAMLSQaqaVIDRLGAQFKASDRVMTLTIAEQQQVE 152
Cdd:COG1245 411 SPDYDG------------------TVEE--FLRS--ANTDDFGSSYYKTE---IIKPLGLEKLLDKNVKDLSGGELQRVA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082746 153 IARALHRQSRILVMDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSV 214
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-214 |
1.81e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAFGKFyalkgvDLTVWPGEIHA-----LMGENGAGKSTLMKILAGAYTATSGEILID----GKPQTI 72
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDF------SLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisYKPQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 73 R----GPKDALAAGITLIYqemqlapnltvaENIFLGSELARGGLVQRkamlsqaqaVIDRlgaqfkasdRVMTLTIAEQ 148
Cdd:PRK13409 410 KpdydGTVEDLLRSITDDL------------GSSYYKSEIIKPLQLER---------LLDK---------NVKDLSGGEL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 149 QQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSV 214
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMV 526
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-223 |
1.99e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 19 FYALKGVDLTVWPGEIHALMGENGAGKS----TLMKILAGAYTATSGEILIDGKPQTIRGPKDA---LAAGITLIYQE-- 89
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERrnlVGAEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 90 MQLAPNLTVAENIFLGSELARGGlvQRKAMLSQAQAVIDRLGAQFKASdRV----MTLTIAEQQQVEIARALHRQSRILV 165
Cdd:PRK11022 100 TSLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVGIPDPAS-RLdvypHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496082746 166 MDEPTAALSSRETQRLFELILRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
275-460 |
2.09e-09 |
|
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: 57.37 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPV--VIHSPREAIdLGIGFLTenrkeqGLFLELAAQE 352
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeQRDEPHENI-LYLGHLP------GLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 353 NITMatlerdanWGMLNRRKAQTIsDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGA 432
Cdd:TIGR01189 93 NLHF--------WAAIHGGAQRTI-EDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....*....
gi 496082746 433 KSEIYRIMND-MARQGVAILMISSELPEV 460
Cdd:TIGR01189 163 VALLAGLLRAhLARGGIVLLTTHQDLGLV 191
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
260-470 |
2.47e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.66 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTDGGKVKPS---SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRK----ATGGVIEIDGEPVVIHSPREaidlgi 332
Cdd:PRK15093 9 LTIEFKTSDGWVKAVdrvSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRE------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 333 gflteNRKEQG-----LFLE----LAAQENITMATLERDANWGMLNR-------RKAQtisddAIQLLN---IRVPHAQV 393
Cdd:PRK15093 83 -----RRKLVGhnvsmIFQEpqscLDPSERVGRQLMQNIPGWTYKGRwwqrfgwRKRR-----AIELLHrvgIKDHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 394 RAGG--LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMAR-QGVAILMISSELPEVVGMSDRVYVM 470
Cdd:PRK15093 153 RSFPyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-196 |
2.47e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 24 GVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPqtIRGPKDAL---------AAGITliyqemqlaP 94
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEYhqdllylghQPGIK---------T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 95 NLTVAENI-FLgselargglvQRKAMLSQAQAVIDRLgAQFKASDR----VMTLTIAEQQQVEIARALHRQSRILVMDEP 169
Cdd:PRK13538 88 ELTALENLrFY----------QRLHGPGDDEALWEAL-AQVGLAGFedvpVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180
....*....|....*....|....*...
gi 496082746 170 TAALSSRETQRLFELILR-LRDEGMAII 196
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQhAEQGGMVIL 184
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
275-476 |
2.54e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.19 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEpVVIHSPREAIDLGIGFltenrKEQGLFLELAAQENI 354
Cdd:PRK09452 34 DLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ-DITHVPAENRHVNTVF-----QSYALFPHMTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TmatlerdanWGM-LNRRKAQTISD---DAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDv 430
Cdd:PRK09452 108 A---------FGLrMQKTPAAEITPrvmEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 431 gakseiYRIMNDM-------ARQ-GVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:PRK09452 177 ------YKLRKQMqnelkalQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
252-457 |
2.93e-09 |
|
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: 59.30 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 252 DIPRGQPRLRVEDLT---DGGKVKPS--SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPRE 326
Cdd:TIGR02868 327 AVGLGKPTLELRDLSagyPGAPPVLDgvSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 327 aIDLGIGFLTENRKeqgLFlELAAQENITMATLE--RDANWGMLNRRKAQTISDDAIQLLNIRVphaQVRAGGLSGGNQQ 404
Cdd:TIGR02868 407 -VRRRVSVCAQDAH---LF-DTTVRENLRLARPDatDEELWAALERVGLADWLRALPDGLDTVL---GEGGARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496082746 405 KLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDmARQGVAILMISSEL 457
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-219 |
3.23e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 4 TPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEIlidgkpqtirgpkdALAAGI 83
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------------GLAKGI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 TLIY-QEMQLApnltvaeniFLGSELARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTI----AEQQQVEIARALH 158
Cdd:PRK10636 376 KLGYfAQHQLE---------FLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrfsgGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 159 RQSRILVMDEPTAALSSRETQRLFELILRLrdEGmAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
275-476 |
3.49e-09 |
|
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: 56.65 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGepvvihspreaIDLGIGFLTENRKEqglfLELAAQE-N 353
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG-----------IDISTIPLEDLRSS----LTIIPQDpT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 354 ITMATLErdANWGMLNRRkaqtiSDDAIqllnirVPHAQVRAGG--LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVG 431
Cdd:cd03369 93 LFSGTIR--SNLDPFDEY-----SDEEI------YGALRVSEGGlnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 432 AKSEIYRIMNDMArQGVAILMISSELPEVVGMsDRVYVMREGAIA 476
Cdd:cd03369 160 TDALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-219 |
5.80e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.81 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 2 TATPVLEMRHIAKAF----GKFYALKGVDLTVWPGEIHALMGENGAGKS----TLMKILAgAYTATSGEILIDGKpQTIR 73
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-ANGRIGGSATFNGR-EILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 74 GPKDAL----AAGITLIYQE--MQLAPNLTVAENIFlgsELarggLVQRKAMlSQAQAV---IDRLGA-QFKASDRVMTL 143
Cdd:PRK09473 86 LPEKELnklrAEQISMIFQDpmTSLNPYMRVGEQLM---EV----LMLHKGM-SKAEAFeesVRMLDAvKMPEARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 144 TIAE-----QQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDE-GMAIIYISHRMAEVYELSDRVSVLRD 217
Cdd:PRK09473 158 YPHEfsggmRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYA 237
|
..
gi 496082746 218 GQ 219
Cdd:PRK09473 238 GR 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-221 |
6.39e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDaLAAGITLIYQemqlAPNL---TV 98
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD-LRKVLGIIPQ----APVLfsgTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLGSELARGGLVQ--RKAMLSQaqaVIDR--LGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALS 174
Cdd:PLN03130 1330 RFNLDPFNEHNDADLWEslERAHLKD---VIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 175 SReTQRLFELILRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:PLN03130 1407 VR-TDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-430 |
6.55e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 15 AFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGK----------PQTIRGPK-DALAAGI 83
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpPRNVEGTVyDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 84 tliyQEmqlapnltVAENIFLGSELARggLVQRKAM------LSQAQAVIDRLGA-QFK-------------ASDRVMTL 143
Cdd:PRK11147 92 ----EE--------QAEYLKRYHDISH--LVETDPSeknlneLAKLQEQLDHHNLwQLEnrinevlaqlgldPDAALSSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 144 TIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELilrLRDEGMAIIYISH------RMA-------------- 203
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGF---LKTFQGSIIFISHdrsfirNMAtrivdldrgklvsy 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 204 ----EVYELSD----RVSVLRDGQYvgslvrDKLNAPELVRMMVG------------RPLSDLFN--KERDIPRGQPRLR 261
Cdd:PRK11147 235 pgnyDQYLLEKeealRVEELQNAEF------DRKLAQEEVWIRQGikarrtrnegrvRALKALRRerSERREVMGTAKMQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 262 VEDLTDGGK-----------------VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIeidgepvvihsp 324
Cdd:PRK11147 309 VEEASRSGKivfemenvnyqidgkqlVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 325 REAIDLGIGFLTENRKEqgLFLELAAQENITMATLERdanwgMLNRRKAQTIS---DDAIQLLNIRVPhaqVRAggLSGG 401
Cdd:PRK11147 377 HCGTKLEVAYFDQHRAE--LDPEKTVMDNLAEGKQEV-----MVNGRPRHVLGylqDFLFHPKRAMTP---VKA--LSGG 444
|
490 500
....*....|....*....|....*....
gi 496082746 402 NQQKLLISRWVAIGPRILILDEPTRGVDV 430
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
275-490 |
7.50e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.13 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAiDLGIGFltenrKEQGLFLELAAQENI 354
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR-PVSMLF-----QENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATlerdaNWGM-LNRRKAQTISDDAIQ-----LLNiRVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGV 428
Cdd:PRK10771 93 GLGL-----NPGLkLNAAQREKLHAIARQmgiedLLA-RLPGQ------LSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 429 DVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIA-----GELQAGDISQESIM 490
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAwdgptDELLSGKASASALL 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
271-475 |
7.59e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPV--------------VIHSPREAIDlgigflt 336
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyrsqrirmIFQDPSTSLN------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 337 eNRKEQGLFLELAAQENITMATLERDanwgmlnRRKAQTIsddaiQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGP 416
Cdd:PRK15112 102 -PRQRISQILDFPLRLNTDLEPEQRE-------KQIIETL-----RQVGLLPDHASYYPHMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 417 RILILDEPTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
275-478 |
8.22e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.53 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTENRKEQ--GLFLE--LA- 349
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQfvGRTVEedLAf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENITMATLErdanwgmLNRRKAQTISDDAIQLLNIRVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:PRK13644 102 GPENLCLPPIE-------IRKRVDRALAEIGLEKYRHRSPKT------LSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 430 VGAKSEIYRIMNDMARQGVAILMISSELPEvVGMSDRVYVMREGAIAGE 478
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLE 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
273-496 |
8.88e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 273 PSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPReAIDLGIGFLTEnrkeqglflELAAQE 352
Cdd:PRK10575 29 PLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQ---------QLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 353 NITMATLERDANW---GMLNRRKAQTIS--DDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRG 427
Cdd:PRK10575 99 GMTVRELVAIGRYpwhGALGRFGAADREkvEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 428 VDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQESIMTLATGV 496
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGI 247
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
257-476 |
9.09e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 57.03 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDLTD--GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAIDLGI 332
Cdd:COG3842 3 MPALELENVSKryGDVtaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 333 GFltenrkeQ--GLFLELAAQENIT----MATLERDAnwgmlnrRKAQTisDDAIQLLNIRvPHAQVRAGGLSGGNQQKL 406
Cdd:COG3842 82 VF-------QdyALFPHLTVAENVAfglrMRGVPKAE-------IRARV--AELLELVGLE-GLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 407 LISRWVAIGPRILILDEPTRGVDVGAK----SEIYRIMndmARQGVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLReemrEELRRLQ---RELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-63 |
1.28e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 7 LEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEI 63
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
257-473 |
1.31e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDLT----DGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLI-----FGVRKATGGVIEIDGEPvvIHSPR-E 326
Cdd:PRK14239 3 EPILQVSDLSvyynKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHN--IYSPRtD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 327 AIDLgigfltenRKEQGLFLElaaQENITMATLERDANWGM-LNRRKAQTISDDAIQ--LLNIRV-----PHAQVRAGGL 398
Cdd:PRK14239 81 TVDL--------RKEIGMVFQ---QPNPFPMSIYENVVYGLrLKGIKDKQVLDEAVEksLKGASIwdevkDRLHDSALGL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 399 SGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMaRQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-200 |
1.62e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 27 LTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpQTIRGPKDALaagiTLIYQEMQLAPNLTVAENIFLGS 106
Cdd:PRK13541 21 ITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNC-NINNIAKPYC----TYIGHNLGLKLEMTVFENLKFWS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 107 ELARGglvqrkamLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELIL 186
Cdd:PRK13541 96 EIYNS--------AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
170
....*....|....
gi 496082746 187 RLRDEGMAIIYISH 200
Cdd:PRK13541 168 MKANSGGIVLLSSH 181
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-219 |
1.65e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 19 FYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIrgpkdALAAGitliyqemqLAPNLTV 98
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI-----AISAG---------LSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 AENIFLgSELARGglVQRKAMLSQAQAVID--RLGaQFkASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSR 176
Cdd:PRK13546 103 IENIEF-KMLCMG--FKRKEIKAMTPKIIEfsELG-EF-IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 177 ETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
275-477 |
1.84e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIdGEPVvIHSPREAIDL-------GIGFlteNRKEQGLFLE 347
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERV-ITAGKKNKKLkplrkkvGIVF---QFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 laaqenitmaTLERDANWGMLN----RRKAQTISDDAIQLLNI------RVPHAqvraggLSGGNQQKLLISRWVAIGPR 417
Cdd:PRK13634 102 ----------TVEKDICFGPMNfgvsEEDAKQKAREMIELVGLpeellaRSPFE------LSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 418 ILILDEPTRGVDVGAKSEI----YRIMNdmaRQGVAILMISSELPEVVGMSDRVYVMREGAIAG 477
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMmemfYKLHK---EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
271-475 |
2.01e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.20 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLgigfltENRKEQGLFLELAA 350
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREV------RRKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENITMATlerDANWGM----LNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTR 426
Cdd:PRK10070 118 MPHMTVLD---NTAFGMelagINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 427 GVDVGAKSEIY-RIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK10070 194 ALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
258-452 |
2.20e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.49 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 258 PRLRVEDLT--DGGKV--KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAID-LGi 332
Cdd:PRK13539 1 MMLEGEDLAcvRGGRVlfSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 333 gfltenrKEQGLFLELAAQENITMatlerdanWGMLNRRKAQTIsDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWV 412
Cdd:PRK13539 80 -------HRNAMKPALTVAENLEF--------WAAFLGGEELDI-AAALEAVGLA-PLAHLPFGYLSAGQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496082746 413 AIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILM 452
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
275-475 |
2.80e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.70 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEpvvIHSPreaIDLGIGFltenrkeQGlflELAAQENI 354
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---VSAL---LELGAGF-------HP---ELTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMatlerdaNWGMLNRRKAQT------ISD-----DAIqllnirvpHAQVRAggLSGGNQQKLLISRWVAIGPRILILDE 423
Cdd:COG1134 110 YL-------NGRLLGLSRKEIdekfdeIVEfaelgDFI--------DQPVKT--YSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 424 ptrGVDVG-----AKSeiYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG1134 173 ---VLAVGdaafqKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-225 |
2.96e-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: 53.48 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 21 ALKGVDLTVWPGEIHALMGENGAGKSTLmkILAGAYTatSGEILIDGKPQTirgpkdalaagitliyqemqLAPNLTVae 100
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA--SGKARLISFLPK--------------------FSRNKLI-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 101 niflgselargglvqrkaMLSQAQAVIDrLGAQFKASDRVM-TLTIAEQQQVEIARAL--HRQSRILVMDEPTAALSSRE 177
Cdd:cd03238 64 ------------------FIDQLQFLID-VGLGYLTLGQKLsTLSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 178 TQRLFELILRLRDEGMAIIYISHRMaEVYELSDRVSVL--RDGQYVGSLV 225
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWIIDFgpGSGKSGGKVV 173
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
281-473 |
3.10e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 281 GEIVGLAGLVGAGRSELAQLIFGVRKA---TGGVIEIDGEPVvihsprEAIDLGIGFLTEnrkEQGLFLELAAQENITMA 357
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnfTGTILANNRKPT------KQILKRTGFVTQ---DDILYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 358 TLERDANwgMLNRRKAQTISDDAIQLL------NIRVPHAQVRagGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVG 431
Cdd:PLN03211 165 SLLRLPK--SLTKQEKILVAESVISELgltkceNTIIGNSFIR--GISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496082746 432 AKSEIYRIMNDMARQGVAILM-ISSELPEVVGMSDRVYVMREG 473
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEG 283
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-213 |
3.19e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 5 PVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTirgPKDaLAA--- 81
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGD-IATrrr 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 82 ------GITLiYQEmqlapnLTVAENIFLGselARggLVQRKAmlSQAQAVIDRLGAQFKASDrVM-----TLTIAEQQQ 150
Cdd:NF033858 341 vgymsqAFSL-YGE------LTVRQNLELH---AR--LFHLPA--AEIAARVAEMLERFDLAD-VAdalpdSLPLGIRQR 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 151 VEIARA-LHRqSRILVMDEPT-----AAlssREtqRLFELILRL-RDEGMAiIYIS-HRMAEVyELSDRVS 213
Cdd:NF033858 406 LSLAVAvIHK-PELLILDEPTsgvdpVA---RD--MFWRLLIELsREDGVT-IFIStHFMNEA-ERCDRIS 468
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
259-475 |
3.28e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.40 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 259 RLRVEDLTDGGKVKPSSLVV-------HAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPV------VIHSPR 325
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLVLqdvsftlHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqyehkYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 326 EAIDlgigfltenrKEQGLFLElAAQENITMATleRDANWGMLNRRKAQTISDDAIQLLNIRVPHAQVRAGG-LSGGNQQ 404
Cdd:cd03248 91 SLVG----------QEPVLFAR-SLQDNIAYGL--QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSqLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 405 KLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDmARQGVAILMISSELpEVVGMSDRVYVMREGAI 475
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
275-481 |
3.58e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.98 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvIHS----PREAI---DLGIGFltenRKEQgLFLE 347
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFAldedARARLrarHVGFVF----QSFQ-LLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 LAAQENItMATLERDanwgmlNRRKAQTISDDAIQL--LNIRVPHaqvRAGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:COG4181 105 LTALENV-MLPLELA------GRRDARARARALLERvgLGHRLDH---YPAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 426 RGVDvGAKSEiyRIMNDM----ARQGVAILMISSElPEVVGMSDRVYVMREGAIAGELQA 481
Cdd:COG4181 175 GNLD-AATGE--QIIDLLfelnRERGTTLVLVTHD-PALAARCDRVLRLRAGRLVEDTAA 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
262-485 |
3.96e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 54.74 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 262 VEDLT----DGGK-VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAidlgigflt 336
Cdd:PRK13647 7 VEDLHfrykDGTKaLKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 337 enRKEQGLFLElAAQENITMATLERDANWGMLNRRKAQTISD----DAIQLLNI-----RVPHAqvraggLSGGNQQKLL 407
Cdd:PRK13647 78 --RSKVGLVFQ-DPDDQVFSSTVWDDVAFGPVNMGLDKDEVErrveEALKAVRMwdfrdKPPYH------LSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 408 ISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIageLQAGDIS 485
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV---LAEGDKS 223
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-170 |
4.16e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 6 VLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIdGkpQTIRgpkdalaagitL 85
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G--ETVK-----------L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 86 IYQEMQ---LAPNLTVAENIFLGSELARGGLVQrkaMLSqaQAVIDRLGaqFKASD---RVMTLTIAEQQQVEIARALHR 159
Cdd:PRK11819 390 AYVDQSrdaLDPNKTVWEEISGGLDIIKVGNRE---IPS--RAYVGRFN--FKGGDqqkKVGVLSGGERNRLHLAKTLKQ 462
|
170
....*....|.
gi 496082746 160 QSRILVMDEPT 170
Cdd:PRK11819 463 GGNVLLLDEPT 473
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
398-484 |
6.43e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
....*...
gi 496082746 477 GELQAGDI 484
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
271-475 |
8.26e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.04 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidlgigfLTENRKEQGL----FL 346
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE--------LRKARRQIGMifqhFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 347 ELAAQ---ENITMAtLERDanwgmlNRRKAQtISDDAIQLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILI 420
Cdd:PRK11153 93 LLSSRtvfDNVALP-LELA------GTPKAE-IKARVTELLE-LVglsDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 421 LDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELpEVV-GMSDRVYVMREGAI 475
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRElGLTIVLITHEM-DVVkRICDRVAVIDAGRL 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
250-473 |
8.77e-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: 55.02 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 250 ERDIPRGQPRLRVEDLTD----GGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvIHS 323
Cdd:TIGR01257 919 ERELPGLVPGVCVKNLVKifepSGRpaVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD--IET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 324 PREAIDLGIGFLTENRKeqgLFLELAAQENITMATLERDANWGMLNRRKAQTISDDAIQllNIRVPHAQvragGLSGGNQ 403
Cdd:TIGR01257 997 NLDAVRQSLGMCPQHNI---LFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLH--HKRNEEAQ----DLSGGMQ 1067
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 404 QKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMaRQGVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:TIGR01257 1068 RKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
275-475 |
1.02e-07 |
|
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: 54.75 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVV---IHSPREAID-------LGIGFLTENrkeqgl 344
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidRHTLRQFINylpqepyIFSGSILEN------ 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 345 fLELAAQENITMATLERDANWGmlnrrkaqTISDDAIQLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEP 424
Cdd:TIGR01193 568 -LLLGAKENVSQDEIWAACEIA--------EIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496082746 425 TRGVDVGAKSEIyrIMNDMARQGVAILMISSELpEVVGMSDRVYVMREGAI 475
Cdd:TIGR01193 639 TSNLDTITEKKI--VNNLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
271-478 |
1.06e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGepvvihspreaID-LGIGFLTENRKEQGLFLEla 349
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-----------LDtSDEENLWDIRNKAGMVFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 350 AQENITMATL-ERDANWGMLN----RRKAQTISDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRIL 419
Cdd:PRK13633 93 NPDNQIVATIvEEDVAFGPENlgipPEEIRERVDESLKKVGMyeyrrHAPHL------LSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 420 ILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAILMISSELPEVVgMSDRVYVMREGAIAGE 478
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAV-EADRIIVMDSGKVVME 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-205 |
1.07e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 20 YALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIrgpkdALAAGitliyqemqLAPNLTVA 99
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI-----AISSG---------LNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 100 ENIFLGSELArgGLVQRKAMLSQAQaVIDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQ 179
Cdd:PRK13545 104 ENIELKGLMM--GLTKEKIKEIIPE-IIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180
....*....|....*....|....*.
gi 496082746 180 RLFELILRLRDEGMAIIYISHRMAEV 205
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
275-475 |
1.25e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.69 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLgigfLTENRKEQGLFLELAAQENI 354
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR----VASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMAT---LERDANWGMLNRRKAqtisDDAIQllniRVPHAQVRA---GGLSGGNQQKLLISRWVAIGPRILILDEPTRGV 428
Cdd:PRK09536 99 EMGRtphRSRFDTWTETDRAAV----ERAME----RTGVAQFADrpvTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 429 DVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-219 |
1.38e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.57 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIrgPKDALAAgitliyqemqlapNLTVAEN 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYV--PQQAWIQ-------------NDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLGSELARgglvQRKAMLSQAQAVIDRL-----GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSR 176
Cdd:TIGR00957 719 ILFGKALNE----KYYQQVLEACALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496082746 177 ETQRLFELIlrLRDEGM----AIIYISHRMAEVYELsDRVSVLRDGQ 219
Cdd:TIGR00957 795 VGKHIFEHV--IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGK 838
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
276-485 |
1.40e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.72 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 276 LVVHAGEIVGLAGLVGAGRSELAQLIFG--VRKATGGVIEIDGEPVVIHSPreaidlgigfltENRKEQGLFLelAAQEN 353
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEP------------EERAHLGIFL--AFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 354 ITMATLErDANWGML---NRRKAQTISD-DAIQLLNIRVP------------HAQVRAGgLSGGNQQKLLISRWVAIGPR 417
Cdd:CHL00131 94 IEIPGVS-NADFLRLaynSKRKFQGLPElDPLEFLEIINEklklvgmdpsflSRNVNEG-FSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 418 ILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMIS--SELPEVVgMSDRVYVMREGAIageLQAGDIS 485
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyQRLLDYI-KPDYVHVMQNGKI---IKTGDAE 237
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
271-475 |
1.46e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.54 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPReaiDLGIGFLTENrkeQGLFLELAA 350
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK---DRNIAMVFQS---YALYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENITmatlerdanWGMLNRR-KAQTIS---DDAIQLLNIRvPHAQVRAGGLSGGNQQKllisrwVAIG------PRILI 420
Cdd:COG3839 93 YENIA---------FPLKLRKvPKAEIDrrvREAAELLGLE-DLLDRKPKQLSGGQRQR------VALGralvrePKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 421 LDEPTRGVDvgAK------SEIYRImndMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG3839 157 LDEPLSNLD--AKlrvemrAEIKRL---HRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
260-490 |
1.49e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 52.71 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 260 LRVEDLTDG-GK---VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidLG--IG 333
Cdd:PRK11231 3 LRTENLTVGyGTkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LArrLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 334 FLTEnrkeqglflELAAQENITMATL---ERD---ANWGMLNRRKAQTIsDDAIQLLNIrVPHAQVRAGGLSGGNQQKLL 407
Cdd:PRK11231 80 LLPQ---------HHLTPEGITVRELvayGRSpwlSLWGRLSAEDNARV-NQAMEQTRI-NHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 408 ISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQAGDISQE 487
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
...
gi 496082746 488 SIM 490
Cdd:PRK11231 229 GLL 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
257-475 |
1.74e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.71 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 257 QPRLRVEDLT----DGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGV---RKATGGVIEIDGEpVVIHSPREAID 329
Cdd:PRK09984 2 QTIIRVEKLAktfnQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGR-TVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 330 LgigflTENRKEQGLFLE-------LAAQENITMATLERDANWGMLNRRKAQTISDDAIQLLN-IRVPH-AQVRAGGLSG 400
Cdd:PRK09984 81 I-----RKSRANTGYIFQqfnlvnrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTrVGMVHfAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 401 GNQQKLLISRWVAIGPRILILDEPTRGVDvgakSEIYRIMNDMAR-----QGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLD----PESARIVMDTLRdinqnDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-475 |
2.48e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.84 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 395 AGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQgVAILMISSELPEVVGMSDRVYVMREGA 474
Cdd:PRK14247 144 AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
.
gi 496082746 475 I 475
Cdd:PRK14247 223 I 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-478 |
2.56e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQgVAILMISSELPEVVGMSDRVYVMREGAIAG 477
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
.
gi 496082746 478 E 478
Cdd:PRK14271 243 E 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
275-475 |
2.59e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGE---PVVIHSPREAIdlGIGFltenrKEQGLFlELAAQ 351
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirTVTRASLRRNI--AVVF-----QDAGLF-NRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ENITM----ATLE--RDAnwgmLNRRKAQTISDDAIQLLNIRVPHaqvRAGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:PRK13657 427 DNIRVgrpdATDEemRAA----AERAQAHDFIERKPDGYDTVVGE---RGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 426 RGVDVGAKSEIYRIMnDMARQGVAILMISSELpEVVGMSDRVYVMREGAI 475
Cdd:PRK13657 500 SALDVETEAKVKAAL-DELMKGRTTFIIAHRL-STVRNADRILVFDNGRV 547
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-173 |
2.61e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 1 MTATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTiRGPKdalA 80
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDR---S 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 81 AGITLIYQEMQLAPNLTVAENI-FLGSELARgglvQRKAMLSQAQAVIdrlGAQFKASDRVMTLTIAEQQQVEIARALHR 159
Cdd:PRK13543 82 RFMAYLGHLPGLKADLSTLENLhFLCGLHGR----RAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLS 154
|
170
....*....|....
gi 496082746 160 QSRILVMDEPTAAL 173
Cdd:PRK13543 155 PAPLWLLDEPYANL 168
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
258-476 |
3.46e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 51.70 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 258 PRLRVEDLT--DGGK--VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPRE------- 326
Cdd:PRK13548 1 AMLEARNLSvrLGGRtlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 327 ---AIDLGIGFLtenrkeqglflelaAQENITMATlerdANWGmLNRRKAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQ 403
Cdd:PRK13548 81 lpqHSSLSFPFT--------------VEEVVAMGR----APHG-LSRAEDDALVAAALAQVDL-AHLAGRDYPQLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 404 QKLLISR-----W-VAIGPRILILDEPTRGVDVGAKSEIYRIMNDMAR-QGVAILMISSELPEVVGMSDRVYVMREGAIA 476
Cdd:PRK13548 141 QRVQLARvlaqlWePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHeRGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
275-475 |
4.31e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 52.00 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidlgigfLTENRKEQG-------LFLE 347
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE--------LRAARRKIGmifqhfnLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 LAAQENITMAtLERdanWGMlNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRG 427
Cdd:COG1135 97 RTVAENVALP-LEI---AGV-PKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 428 VDVGAKSEIYRIMNDMARQ-GVAILMISSELpEVV-GMSDRVYVMREGAI 475
Cdd:COG1135 171 LDPETTRSILDLLKDINRElGLTIVLITHEM-DVVrRICDRVAVLENGRI 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
275-495 |
7.96e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGepvvihspreaIDLGIGFLTENRK------EQGLFLEL 348
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-----------CDVAKFGLTDLRRvlsiipQSPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 349 AAQENITMATLERDAN-WGMLNRRKAQTISDDAIQLLNirvphAQVRAGG--LSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:PLN03232 1325 TVRFNIDPFSEHNDADlWEALERAHIKDVIDRNPFGLD-----AEVSEGGenFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 426 RGVDVGAKSEIYRIMNDMARQgVAILMISSELPEVVGmSDRVYVMREGAI-----AGELQAGDISQESIMTLATG 495
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVleydsPQELLSRDTSAFFRMVHSTG 1472
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
275-429 |
9.07e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTenrkeQGL----FLELAA 350
Cdd:NF033858 21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMP-----QGLgknlYPTLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 351 QENIT-MATL------ERDANWGMLNRrkaqtisddAIQLLnirvPHAQVRAGGLSGGNQQKL-----LISrwvaiGPRI 418
Cdd:NF033858 96 FENLDfFGRLfgqdaaERRRRIDELLR---------ATGLA----PFADRPAGKLSGGMKQKLglccaLIH-----DPDL 157
|
170
....*....|.
gi 496082746 419 LILDEPTRGVD 429
Cdd:NF033858 158 LILDEPTTGVD 168
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-473 |
9.49e-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: 51.32 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 31 PGEIHALMGENGAGKSTLMKILAGAYTATSGEilIDGKP------QTIRGPK-----DALAAG-ITLIY--QEMQLAPNL 96
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGD--YDEEPswdevlKRFRGTElqdyfKKLANGeIKVAHkpQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 97 ---TVaeniflgSELARGglVQRKAMLSQaqaVIDRLGAQfKASDR-VMTLTIAEQQQVEIARALHRQSRILVMDEPTAA 172
Cdd:COG1245 176 fkgTV-------RELLEK--VDERGKLDE---LAEKLGLE-NILDRdISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 173 LSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVL--RDGQY-VGSL---VRDKLNA-------PELVRMmv 239
Cdd:COG1245 243 LDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILygEPGVYgVVSKpksVRVGINQyldgylpEENVRI-- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 240 gRPLSDLFNK--ERDIPRGQPRLRVEDLT---DGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEi 314
Cdd:COG1245 321 -RDEPIEFEVhaPRREKEEETLVEYPDLTksyGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 315 dgepvvihspreaIDLGIGFltenrKEQglflELAAQENITMATLERDANWGMLNRRKAQTisdDAIQLLNI-RVPHAQV 393
Cdd:COG1245 399 -------------EDLKISY-----KPQ----YISPDYDGTVEEFLRSANTDDFGSSYYKT---EIIKPLGLeKLLDKNV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 394 RagGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMAR-QGVAIL----------MISSEL----- 457
Cdd:COG1245 454 K--DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEnRGKTAMvvdhdiylidYISDRLmvfeg 531
|
490
....*....|....*..
gi 496082746 458 -PEVVGMSDRVYVMREG 473
Cdd:COG1245 532 ePGVHGHASGPMDMREG 548
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
280-485 |
1.06e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 50.01 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 280 AGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIH---SPREAIDL----GIGFLTENrkeqgLFLELAAQE 352
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqkpSEKAIRLLrqkvGMVFQQYN-----LWPHLTVME 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 353 NITMATLErdanwgMLNRRKAQTIsDDAIQLLN-IRV-PHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDV 430
Cdd:COG4161 102 NLIEAPCK------VLGLSKEQAR-EKAMKLLArLRLtDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 431 GAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIageLQAGDIS 485
Cdd:COG4161 175 EITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI---IEQGDAS 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
394-486 |
1.11e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.00 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 394 RAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDvgAKSEiYRIMNDM--ARQGVAILMISSELPEVVGMsDRVYVMR 471
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSE-QLVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQ 557
|
90
....*....|....*
gi 496082746 472 EGAIAgelQAGDISQ 486
Cdd:PRK11174 558 DGQIV---QQGDYAE 569
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
254-480 |
1.13e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 49.86 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 254 PRGQPRLRVEDLtdggkvkpsSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVviHSPreAIDLGIG 333
Cdd:COG4525 15 GGGQPQPALQDV---------SLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGP--GADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 334 FltenrKEQGLFLELAAQENIT----MATLERDAnwgmlnRRKaqtISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLIS 409
Cdd:COG4525 82 F-----QKDALLPWLNVLDNVAfglrLRGVPKAE------RRA---RAEELLALVGLA-DFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 410 RWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVM--REGAIAGELQ 480
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLE 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
275-476 |
1.15e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 49.41 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEP---VVIHSPREAIDLgI--------GFLTENrkeqg 343
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskIGLHDLRSRISI-IpqdpvlfsGTIRSN----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 344 L-FLELAAQENItMATLERDANWGMLnrrKAQTISDDaiqllnirvphAQVRAGG--LSGGNQQKLLISRWVAIGPRILI 420
Cdd:cd03244 98 LdPFGEYSDEEL-WQALERVGLKEFV---ESLPGGLD-----------TVVEEGGenLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 421 LDEPTRGVDVGAKSEIYR-IMNDMArqGVAILMISSELPEVVGmSDRVYVMREGAIA 476
Cdd:cd03244 163 LDEATASVDPETDALIQKtIREAFK--DCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
247-475 |
1.23e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.98 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 247 FNKERDIPRGQPRLRVEDLTDGGKVKPS------SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvv 320
Cdd:PRK11160 326 FPTTSTAAADQVSLTLNNVSFTYPDQPQpvlkglSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 321 IHSPREA------------IDLGIGFLTENrkeqglfLELAAqENITMATLErdanwGMLNRRKAQTISDDAiQLLNirv 388
Cdd:PRK11160 404 IADYSEAalrqaisvvsqrVHLFSATLRDN-------LLLAA-PNASDEALI-----EVLQQVGLEKLLEDD-KGLN--- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 389 phAQVRAGG--LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMArQGVAILMISSELPEVVGMsDR 466
Cdd:PRK11160 467 --AWLGEGGrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DR 542
|
....*....
gi 496082746 467 VYVMREGAI 475
Cdd:PRK11160 543 ICVMDNGQI 551
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
259-478 |
1.44e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.60 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 259 RLRVEDLT--DGGKVKPSSLVVHA--GEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaIDLGIGF 334
Cdd:PRK10253 7 RLRGEQLTlgYGKYTVAENLTVEIpdGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 335 LTENRKEQGlflELAAQENIT--------MATLERDANWGMLNR-RKAQTISDDAIQLLNIrvphaqvraggLSGGNQQK 405
Cdd:PRK10253 86 LAQNATTPG---DITVQELVArgryphqpLFTRWRKEDEEAVTKaMQATGITHLADQSVDT-----------LSGGQRQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 406 LLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMAR-QGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
275-475 |
1.51e-06 |
|
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: 49.15 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPV---VIHSPREAIdlgiGFLTEnrkEQGLFLELAAq 351
Cdd:cd03251 22 SLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASLRRQI----GLVSQ---DVFLFNDTVA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ENITMATLERDanwgmlnrrKAQTIsdDAIQLLN-----IRVP---HAQV--RAGGLSGGNQQKLLISRWVAIGPRILIL 421
Cdd:cd03251 94 ENIAYGRPGAT---------REEVE--EAARAANahefiMELPegyDTVIgeRGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 422 DEPTRGVDVGAKSEIYRIMNDMArQGVAILMISSELPEVVGmSDRVYVMREGAI 475
Cdd:cd03251 163 DEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
276-480 |
1.79e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.29 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 276 LVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvIHSPREAIDLgigfltenrkeqgLFLE---LAAQE 352
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP--LAEAREDTRL-------------MFQDarlLPWKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 353 NITMATLERDANWgmlnrRKAQTISDDAIQLLNirvpHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPtrgvdVGA 432
Cdd:PRK11247 98 VIDNVGLGLKGQW-----RDAALQALAAVGLAD----RANEWPAALSGGQKQRVALARALIHRPGLLLLDEP-----LGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 433 KSEIYRI-MNDM-----ARQGVAILMISSELPEVVGMSDRVYVMREGAIAGELQ 480
Cdd:PRK11247 164 LDALTRIeMQDLieslwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
275-475 |
2.15e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 49.08 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPV---VIHSPREAIdlgiGFLTEnrkEQGLFlELAAQ 351
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlNLRWLRSQI----GLVSQ---EPVLF-DGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ENITM----ATLE------RDANwgmlnrrkaqtiSDDAIQLLnirvPHA---QVRAGG--LSGGNQQKLLISRWVAIGP 416
Cdd:cd03249 95 ENIRYgkpdATDEeveeaaKKAN------------IHDFIMSL----PDGydtLVGERGsqLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 417 RILILDEPTRGVDvgAKSEiYRIMN--DMARQGVAILMISSELPEVVGmSDRVYVMREGAI 475
Cdd:cd03249 159 KILLLDEATSALD--AESE-KLVQEalDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-200 |
2.54e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.41 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLM--KILA----------GAYTAT----------------SGEILIDGKpqTIR 73
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdTIYAegqrryveslSAYARQflgqmdkpdvdsieglSPAIAIDQK--TTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 74 GPKDALAAGITLIYQemqlapnltvaeniFLGSELARGGLVQRKAMLsqaqaviDRLGAQFKASDR-VMTLTIAEQQQVE 152
Cdd:cd03270 89 RNPRSTVGTVTEIYD--------------YLRLLFARVGIRERLGFL-------VDVGLGYLTLSRsAPTLSGGEAQRIR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 153 IARALHRQ--SRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISH 200
Cdd:cd03270 148 LATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
276-478 |
2.54e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.62 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 276 LVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREAIDL---GIGFLTENRKeqgLFLELAAQE 352
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFM---LIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 353 NITMATLERdanwGMLNRRKAQTISDDAIQL-LNIRVPH--AQvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVD 429
Cdd:PRK10584 108 NVELPALLR----GESSRQSRNGAKALLEQLgLGKRLDHlpAQ-----LSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496082746 430 VGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
259-475 |
2.55e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 259 RLRVEDL---TDGGKVKPSSLVVHAGEIVGLAGLVGAGRS-----ELAQLIFGVRKaTGGVIEIDGEPV----------- 319
Cdd:PRK10418 4 QIELRNIalqAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVapcalrgrkia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 320 -VIHSPREAIDlGIGFLTENRKEQGLFLELAAQENITMATLErdanwgmlnrrkAQTISDDAiqllniRVPhaQVRAGGL 398
Cdd:PRK10418 83 tIMQNPRSAFN-PLHTMHTHARETCLALGKPADDATLTAALE------------AVGLENAA------RVL--KLYPFEM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 399 SGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYR-IMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDlLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
251-475 |
2.77e-06 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 49.72 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 251 RDIPRGQPRLRVEDLT-----DGGKVKPS-SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSP 324
Cdd:TIGR02203 322 RAIERARGDVEFRNVTfrypgRDRPALDSiSLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 325 ReaiDL--GIGFLTENRKeqgLF-------LELAAQENITMATLER---DANwgmlnrrkAQTISDDAIQLLNIRVphaQ 392
Cdd:TIGR02203 402 A---SLrrQVALVSQDVV---LFndtiannIAYGRTEQADRAEIERalaAAY--------AQDFVDKLPLGLDTPI---G 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 393 VRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIY----RIMndmarQGVAILMISSELPEVVGmSDRVY 468
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQaaleRLM-----QGRTTLVIAHRLSTIEK-ADRIV 538
|
....*..
gi 496082746 469 VMREGAI 475
Cdd:TIGR02203 539 VMDDGRI 545
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
348-478 |
2.99e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 LAAQENITMATLERDanwgmLNRRKAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRG 427
Cdd:NF000106 101 FSGRENLYMIGR*LD-----LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 496082746 428 VDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
271-473 |
3.12e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGV---IEIDGEPVVI---HSPREAIdlgigfltenrkeqgl 344
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVegdIHYNGIPYKEfaeKYPGEII---------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 345 fleLAAQENITMATLErdanwgmlnrrKAQTIsDDAIQLLNirvpHAQVRagGLSGGNQQKLLISRWVAIGPRILILDEP 424
Cdd:cd03233 87 ---YVSEEDVHFPTLT-----------VRETL-DFALRCKG----NEFVR--GISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496082746 425 TRGVDVGAKSEIYRIMNDMARQ--GVAILMISSELPEVVGMSDRVYVMREG 473
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
252-475 |
3.13e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.72 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 252 DIPRGQPRLRVEDLT----DGGKV-KPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPRe 326
Cdd:PRK10790 333 DRPLQSGRIDIDNVSfayrDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 327 AIDLGIGFLtenrKEQGLFLELAAQENITMA-TLERDANWGMLnrrkaqtisdDAIQL--LNIRVP---HAQVRAGG--L 398
Cdd:PRK10790 412 VLRQGVAMV----QQDPVVLADTFLANVTLGrDISEEQVWQAL----------ETVQLaeLARSLPdglYTPLGEQGnnL 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 399 SGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNdMARQGVAILMISSELPEVVGmSDRVYVMREGAI 475
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA-AVREHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-315 |
3.36e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 31 PGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTI----RGPK-----DALAAG-ITLIY--QEMQLAPNLtv 98
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVlkrfRGTElqnyfKKLYNGeIKVVHkpQYVDLIPKV-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 99 aeniFLG--SELARGglVQRKAMLSQaqaVIDRLGAQfKASDR-VMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSS 175
Cdd:PRK13409 176 ----FKGkvRELLKK--VDERGKLDE---VVERLGLE-NILDRdISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 176 RETQRLFELILRLRdEGMAIIYISHRMAEVYELSDRVSVL--RDGQY-VGSL---VRDKLNA-------PELVRMmvgRP 242
Cdd:PRK13409 246 RQRLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHIAygEPGAYgVVSKpkgVRVGINEylkgylpEENMRI---RP 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 243 LSDLFNK--ERDIPRGQPRLRVEDLT---DGGKVKPSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEID 315
Cdd:PRK13409 322 EPIEFEErpPRDESERETLVEYPDLTkklGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE 399
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
112-212 |
3.75e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 112 GLVQRKAMLsqaqavIDrLGAQFKASDRVM-TLTIAEQQQVEIARALHRQ-SRIL-VMDEPTAALSSRETQRLFELILRL 188
Cdd:PRK00635 452 GLKSRLSIL------ID-LGLPYLTPERALaTLSGGEQERTALAKHLGAElIGITyILDEPSIGLHPQDTHKLINVIKKL 524
|
90 100
....*....|....*....|....
gi 496082746 189 RDEGMAIIYISHRmAEVYELSDRV 212
Cdd:PRK00635 525 RDQGNTVLLVEHD-EQMISLADRI 547
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
389-450 |
3.86e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 3.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082746 389 PHAQVRAGGLSGGNQQKLliSRWVAI--GPRILILDEPTRGVDVGAKSEIYRIMNDMARQ-GVAI 450
Cdd:NF033858 389 DVADALPDSLPLGIRQRL--SLAVAVihKPELLILDEPTSGVDPVARDMFWRLLIELSREdGVTI 451
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-242 |
3.93e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 3 ATPVLEMRHIAKAFGKFYALKGVDLTVWPGEIHALMGENGAGKSTlmkilaGAYTATsgeilIDGkPQTIRGP------- 75
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAH-----V*G-PDAGRRPwrf*twc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 76 --KDALAAGITLiYQEMQLA--PNLTVAENIFLgseLARGGLVQRKAMLSQAQAVIDRLGAQFKASDRVMTLTIAEQQQV 151
Cdd:NF000106 78 anRRALRRTIG*-HRPVR*GrrESFSGRENLYM---IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 152 EIARALHRQSRILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLVRDKLNA 231
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
250
....*....|.
gi 496082746 232 PELVRMMVGRP 242
Cdd:NF000106 234 KVGGRTLQIRP 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
283-475 |
5.07e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.72 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 283 IVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVihspreAIDLGIGFLTENRK------EQGLFLELAAQENItm 356
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF------DAEKGICLPPEKRRigyvfqDARLFPHYKVRGNL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 357 atlerdaNWGMLNRRKAQTisDDAIQLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVG 431
Cdd:PRK11144 98 -------RYGMAKSMVAQF--DKIVALLGIeplldRYPGS------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496082746 432 AKSEIYRIMNDMARQ-GVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK11144 163 RKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-211 |
5.42e-06 |
|
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: 46.58 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMK----ILAGAYTATsgeilidgkpqtirGPKDALAAGITLIYQEMQLapnlt 97
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDaiglALGGAQSAT--------------RRRSGVKAGCIVAAVSAEL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 98 vaenIFLgselarggLVQrkamLSQAQavidrlgaqfkaSDRVMTLTIaeqqqveIARALHRQSRILVMDEPTAALSSRE 177
Cdd:cd03227 72 ----IFT--------RLQ----LSGGE------------KELSALALI-------LALASLKPRPLYILDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|....
gi 496082746 178 TQRLFELILRLRDEGMAIIYISHRmAEVYELSDR 211
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITHL-PELAELADK 149
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
275-452 |
7.69e-06 |
|
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: 46.72 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVviHSPREAIDLGIGFLTEnrkEQGLFLELAAQENI 354
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL--DFQRDSIARGLLYLGH---APGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMatlerdanWGMLNRRKAqtiSDDAIQLLNIR-VPHAQVraGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAK 433
Cdd:cd03231 95 RF--------WHADHSDEQ---VEEALARVGLNgFEDRPV--AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170
....*....|....*....
gi 496082746 434 SEIYRIMNDMARQGVAILM 452
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVL 180
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-221 |
7.97e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.60 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpQTIRGPKDALAAGITLIYQE---------MQL 92
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI-DISKLPLHTLRSRLSIILQDpilfsgsirFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 93 APNLTVAEN-IFLGSELARGGLVQrKAMLSQAQAVIDRLGAQFkasdrvmtlTIAEQQQVEIARALHRQSRILVMDEPTA 171
Cdd:cd03288 116 DPECKCTDDrLWEALEIAQLKNMV-KSLPGGLDAVVTEGGENF---------SVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 172 ALsSRETQRLFELILRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:cd03288 186 SI-DMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
398-454 |
1.20e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 45.61 E-value: 1.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMarqGVAILMIS 454
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVG 145
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
275-476 |
1.97e-05 |
|
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: 47.12 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEP---VVIHSPREAIdlGIgfltenrkeqglflelAAQ 351
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdVTQASLRAAI--GI----------------VPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 E----------NI-------TMATLERDAnwgmlnrRKAQTisDDAIQLLnirvP---HAQVRAGG--LSGGNQQKLLIS 409
Cdd:COG5265 440 DtvlfndtiayNIaygrpdaSEEEVEAAA-------RAAQI--HDFIESL----PdgyDTRVGERGlkLSGGEKQRVAIA 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082746 410 RWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARqGVAILMISSELPEVVGmSDRVYVMREGAIA 476
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-187 |
2.12e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIdgkpqtIRGpKDALAAGITLIYqemqlapNLTVAEN 101
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------IRG-TVAYVPQVSWIF-------NATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLGSELARGGLvQRKAMLSQAQAVIDRL--GAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQ 179
Cdd:PLN03130 699 ILFGSPFDPERY-ERAIDVTALQHDLDLLpgGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
....*...
gi 496082746 180 RLFELILR 187
Cdd:PLN03130 778 QVFDKCIK 785
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
37-66 |
2.40e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 2.40e-05
10 20 30
....*....|....*....|....*....|
gi 496082746 37 LMGENGAGKSTLMKILAGAYTATSGEILID 66
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-218 |
2.50e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIdgkpqtIRGPKdALAAGITLIYqemqlapNLTVAEN 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------IRGSV-AYVPQVSWIF-------NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLGS--ELARGGlvqRKAMLSQAQAVIDRLGAQ--FKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRE 177
Cdd:PLN03232 699 ILFGSdfESERYW---RAIDVTALQHDLDLLPGRdlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496082746 178 TQRLFELILRLRDEGMAIIYISHRMaEVYELSDRVSVLRDG 218
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEG 815
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
395-425 |
2.52e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.80 E-value: 2.52e-05
10 20 30
....*....|....*....|....*....|.
gi 496082746 395 AGGLSGGNQQKLLISRWVAIGPRILILDEPT 425
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
142-202 |
3.17e-05 |
|
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: 45.68 E-value: 3.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 142 TLTIAEQQQVEIARALHRQSR---ILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRM 202
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
275-485 |
3.70e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.39 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGE---------PVVIHSPREaiDLGIGFLTENrkeqgLF 345
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsDKAIRELRR--NVGMVFQQYN-----LW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 346 LELAAQENITMATLErdanwgMLNRRKAQTISDdAIQLLN-IRV-PHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDE 423
Cdd:PRK11124 95 PHLTVQQNLIEAPCR------VLGLSKDQALAR-AEKLLErLRLkPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 424 PTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIageLQAGDIS 485
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI---VEQGDAS 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-455 |
4.64e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.22 E-value: 4.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 395 AGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISS 455
Cdd:PRK14267 147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHS 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
398-475 |
5.61e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 44.74 E-value: 5.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
398-465 |
6.08e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.77 E-value: 6.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQgVAILMISSELPEVVGMSD 465
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
275-464 |
6.68e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 44.69 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVihSPreAIDLGIGFltenrKEQGLFLELAAQENI 354
Cdd:PRK11248 21 NLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GP--GAERGVVF-----QNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMAtLErdanWGMLNRRKAQTISDDAIQLLNIRVPHAQvRAGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKS 434
Cdd:PRK11248 92 AFG-LQ----LAGVEKMQRLEIAHQMLKKVGLEGAEKR-YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190
....*....|....*....|....*....|.
gi 496082746 435 EIYRIMNDM-ARQGVAILMISSELPEVVGMS 464
Cdd:PRK11248 166 QMQTLLLKLwQETGKQVLLITHDIEEAVFMA 196
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-475 |
8.48e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.69 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGepvviHSP---REAIDLGIGFLTENRkeQGLFLELAAQ 351
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPfkrRKEFARRIGVVFGQR--SQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 EnitmaTLErdanwgmLNRRKAQtISDDA--------IQLLNI----RVPhaqVRAggLSGGnqQKL-------LISRwv 412
Cdd:COG4586 115 D-----SFR-------LLKAIYR-IPDAEykkrldelVELLDLgellDTP---VRQ--LSLG--QRMrcelaaaLLHR-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 413 aigPRILILDEPTRGVDVGAKSEIYRIMNDM-ARQGVAILMISSELPEVVGMSDRVYVMREGAI 475
Cdd:COG4586 173 ---PKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
39-201 |
1.15e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.74 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 39 GENGAGKSTLMKILAGAYTATSGEILIDGK------PQ----TIRGPKDalaagiTLIY---QEMQLAPNLTVAENIFLG 105
Cdd:TIGR00954 485 GPNGCGKSSLFRILGELWPVYGGRLTKPAKgklfyvPQrpymTLGTLRD------QIIYpdsSEDMKRRGLSDKDLEQIL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 106 SELARGGLVQRKAMLSQAQAVIDrlgaqfkasdrvmTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELi 185
Cdd:TIGR00954 559 DNVQLTHILEREGGWSAVQDWMD-------------VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL- 624
|
170
....*....|....*.
gi 496082746 186 lrLRDEGMAIIYISHR 201
Cdd:TIGR00954 625 --CREFGITLFSVSHR 638
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
275-476 |
1.43e-04 |
|
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: 44.55 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVV---IHSPREAID-------LGIGFLTENRKEQGL 344
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkigLHDLRFKITiipqdpvLFSGSLRMNLDPFSQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 345 FlelaAQENITMAtLErdanwgmLNRRKaqtisdDAIQLLNIRVPHaQVRAGG--LSGGNQQKLLISRWVAIGPRILILD 422
Cdd:TIGR00957 1386 Y----SDEEVWWA-LE-------LAHLK------TFVSALPDKLDH-ECAEGGenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496082746 423 EPTRGVDVGAKSEIYRIMNDMArQGVAILMISSELPEVVGMSdRVYVMREGAIA 476
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQF-EDCTVLTIAHRLNTIMDYT-RVIVLDKGEVA 1498
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
227-475 |
1.46e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 227 DKLNAPELVrmmvgrPLSDLFNKERDIPRGQpRLRVEDLT----DGG-KVKPSSLVVHAGEIVGLAGLVGAGRSELAQLI 301
Cdd:PRK10522 297 NKLNKLALA------PYKAEFPRPQAFPDWQ-TLELRNVTfayqDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 302 FGVRKATGGVIEIDGEPVVIHSPREAIDLGIGFLTENRkeqgLFLELAAQENiTMATLERDANWgmLNRRKAQ---TISD 378
Cdd:PRK10522 370 TGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFH----LFDQLLGPEG-KPANPALVEKW--LERLKMAhklELED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 379 DaiQLLNIRvphaqvraggLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYR-IMNDMARQGVAILMISSEl 457
Cdd:PRK10522 443 G--RISNLK----------LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHD- 509
|
250
....*....|....*...
gi 496082746 458 PEVVGMSDRVYVMREGAI 475
Cdd:PRK10522 510 DHYFIHADRLLEMRNGQL 527
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
269-473 |
1.55e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 42.62 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 269 GKVKPsslvvhaGEIVGLAGLVGAGRSELAQLIFGvRKaTGGVIE----IDGEPVVIHSPREaidlgIGFLTENrkeqgl 344
Cdd:cd03232 28 GYVKP-------GTLTALMGESGAGKTTLLDVLAG-RK-TAGVITgeilINGRPLDKNFQRS-----TGYVEQQ------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 345 flelaaqenitmatlerDANWGMLNRRKAQTISddaiqllnirvphAQVRagGLSGGNQQKLLISRWVAIGPRILILDEP 424
Cdd:cd03232 88 -----------------DVHSPNLTVREALRFS-------------ALLR--GLSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496082746 425 TRGVDVGAKSEIYRIMNDMARQGVAIL-MISSELPEVVGMSDRVYVMREG 473
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-186 |
2.01e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpqtirgpkdaLAAGITLIYQEmQLAPNLTVAEN 101
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----------LEVAYFDQHRA-ELDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLG-SELARGGlvQRKAMLSQAQaviDRLGAQFKASDRVMTLTIAEQQQVEIARALHRQSRILVMDEPTAALSSrETQR 180
Cdd:PRK11147 404 LAEGkQEVMVNG--RPRHVLGYLQ---DFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV-ETLE 477
|
....*.
gi 496082746 181 LFELIL 186
Cdd:PRK11147 478 LLEELL 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-251 |
2.08e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 43.31 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 22 LKGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKpqtirgpkdalaagITLIYQEMQLAPNlTVAEN 101
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 102 IFLGSELARgglVQRKAMLSQAQAVIDRlgAQFKASDRV------MTLTIAEQQQVEIARALHRQSRILVMDEPTAALSS 175
Cdd:cd03291 118 IIFGVSYDE---YRYKSVVKACQLEEDI--TKFPEKDNTvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 176 RETQRLFELILRLRDEGMAIIYISHRMaEVYELSDRVSVLRDGQ--YVGSLVRDKLNAPELVRMMVGRPLSDLFNKER 251
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKM-EHLKKADKILILHEGSsyFYGTFSELQSLRPDFSSKLMGYDTFDQFSAER 269
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-215 |
2.20e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.17 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 32 GEIHALMGENGAGKSTLMKILAGAYTATSGEILIDG-----KPQTIRgpkdalaagitliyqemqlapnltvaeniflgs 106
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGitpvyKPQYID--------------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 107 elargglvqrkamlsqaqavidrlgaqfkasdrvmtLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELIL 186
Cdd:cd03222 72 ------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|
gi 496082746 187 RLRDEGM-AIIYISHRMAEVYELSDRVSVL 215
Cdd:cd03222 116 RLSEEGKkTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
275-478 |
2.94e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.83 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIHSPREaidlgigfLTENRKEQ-------GLFLE 347
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSR--------LYTVRKRMsmlfqsgALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 348 LAAQENITMATLERDAnwgmLNRRKAQTISDDAIQLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILILDEP--- 424
Cdd:PRK11831 99 MNVFDNVAYPLREHTQ----LPAPLLHSTVMMKLEAVGLR-GAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPfvg 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 425 ----TRGVDVGAKSEIYRIMndmarqGVAILMISSELPEVVGMSDRVYVMREGAIAGE 478
Cdd:PRK11831 174 qdpiTMGVLVKLISELNSAL------GVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
275-423 |
3.72e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVVIhspreAIDlgigfltenrkeQGLFLELAAQENI 354
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI-----AIS------------AGLSGQLTGIENI 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 355 TMATLERDanwgmLNRRKAQTISDDAIQLLNI-RVPHAQVRAggLSGGNQQKLLISRWVAIGPRILILDE 423
Cdd:PRK13546 107 EFKMLCMG-----FKRKEIKAMTPKIIEFSELgEFIYQPVKK--YSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-211 |
5.48e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 23 KGVDLTVWPGEIHALMGENGAGKSTLMKILAGAYTATSGEILIDGKPQTIRGPKDALAAGITLIYQEMQLAPNlTVAENI 102
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 103 -----------FLGSELARGG--------------------------------LVQRK-----------AMLSQAQAVID 128
Cdd:PTZ00265 481 kyslyslkdleALSNYYNEDGndsqenknkrnscrakcagdlndmsnttdsneLIEMRknyqtikdsevVDVSKKVLIHD 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 129 RLGAQFKASDRVM-----TLTIAEQQQVEIARALHRQSRILVMDEPTAALSSRETQRLFELILRLR-DEGMAIIYISHRM 202
Cdd:PTZ00265 561 FVSALPDKYETLVgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRL 640
|
250
....*....|....*
gi 496082746 203 A------EVYELSDR 211
Cdd:PTZ00265 641 StiryanTIFVLSNR 655
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
398-502 |
7.14e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVMREGAIAG 477
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTG 1438
|
90 100
....*....|....*....|....*
gi 496082746 478 ELQAGDISQESIMTLATGVNDSHLK 502
Cdd:PTZ00265 1439 SFVQAHGTHEELLSVQDGVYKKYVK 1463
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
398-462 |
8.84e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 8.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMIS---SELPEVVG 462
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLnrfDEIPDFVQ 203
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-202 |
9.75e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 9.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 142 TLTIAEQQQVEIARALHRQSR---ILVMDEPTAALSSRETQRLFELILRLRDEGMAIIYISHRM 202
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
271-473 |
1.01e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 271 VKPSSLVVHAGEIVGLAGLVGAGRSEL----AQLIFGVRKATGGVIEIDGepvviHSPREAIDLGIGFLTENRKEQGLFL 346
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDG-----ITPEEIKKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 347 ELAAQENI-TMATLERDANWGMLNRRK--AQTISDDAIQLL------NIRVPHAQVRagGLSGGNQQKLLISRWVAIGPR 417
Cdd:TIGR00956 152 HLTVGETLdFAARCKTPQNRPDGVSREeyAKHIADVYMATYglshtrNTKVGNDFVR--GVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082746 418 ILILDEPTRGVDVGAKSEIYRIMNDMARQG-----VAILMISselPEVVGMSDRVYVMREG 473
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSANILdttplVAIYQCS---QDAYELFDKVIVLYEG 287
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
273-452 |
1.08e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 273 PSSLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPVViHSPREAIDLGIGFLTenrkeqGLFLELAAQE 352
Cdd:PRK13543 29 PLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDRSRFMAYLGHLP------GLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 353 NITMATlerdanwgMLNRRKAQTISDDAIQLLNIrVPHAQVRAGGLSGGNQQKLLISR-WVAIGPrILILDEPTRGVDVG 431
Cdd:PRK13543 102 NLHFLC--------GLHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALARlWLSPAP-LWLLDEPYANLDLE 171
|
170 180
....*....|....*....|.
gi 496082746 432 AKSEIYRIMNDMARQGVAILM 452
Cdd:PRK13543 172 GITLVNRMISAHLRGGGAALV 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
395-470 |
1.12e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082746 395 AGGLSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMARQGVAILMISSELPEVVGMSDRVYVM 470
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
281-481 |
1.35e-03 |
|
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: 39.61 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 281 GEIVGLAGLVGAGRSELAQLIFgvrKATGGVIEIDGEP-------VVIHSPREAIDLGIGFLTENRKeqglflelaaqen 353
Cdd:cd03238 21 NVLVVVTGVSGSGKSTLVNEGL---YASGKARLISFLPkfsrnklIFIDQLQFLIDVGLGYLTLGQK------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 354 itMATLerdanwgmlnrrkaqtisddaiqllnirvphaqvragglSGGNQQKLLISRWVA--IGPRILILDEPTRGVDVG 431
Cdd:cd03238 85 --LSTL---------------------------------------SGGELQRVKLASELFsePPGTLFILDEPSTGLHQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496082746 432 AKSEIYRIMNDMARQGVAILMISSElPEVVGMSDRVYVM--REGAIAGELQA 481
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWIIDFgpGSGKSGGKVVF 174
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
275-451 |
1.61e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 39.79 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 275 SLVVHAGEIVGLAGLVGAGRSELAQLIFGVRKATGGVIEIDGEPvvIHSPREAID---LGIGFLTenrkeqGLFLELAAQ 351
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEYHqdlLYLGHQP------GIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 352 ENITMATlerdanwgmlnrRKAQTISDDAI-QLLnirvphAQVRAGG--------LSGGNQQKLLISRWVAIGPRILILD 422
Cdd:PRK13538 93 ENLRFYQ------------RLHGPGDDEALwEAL------AQVGLAGfedvpvrqLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|
gi 496082746 423 EPTRGVDVGAKSEIYRIMNDMARQ-GVAIL 451
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQgGMVIL 184
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
398-443 |
2.67e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 40.18 E-value: 2.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDM 443
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
165-200 |
3.91e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 3.91e-03
10 20 30
....*....|....*....|....*....|....*.
gi 496082746 165 VMDEPTAALSSRETQRLFELILRLRDEGMAIIYISH 200
Cdd:TIGR00630 513 VLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-201 |
5.64e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.35 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 31 PGEIHALMGENGAGKSTLMKILAGAYTATSGEILIdgkpqtirgpkdalAAGITLIYQEMQLAPNLTVAENIFLGSelar 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------IDGEDILEEVLDQLLLIIVGGKKASGS---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082746 111 GGLVQRKAmlsqaqavidrlgaqfkasdrvmtltiaeqqqveIARALHRQSRILVMDEPTAALSSRETQRLFE------L 184
Cdd:smart00382 63 GELRLRLA----------------------------------LALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170
....*....|....*..
gi 496082746 185 ILRLRDEGMAIIYISHR 201
Cdd:smart00382 109 LLLKSEKNLTVILTTND 125
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
398-430 |
7.92e-03 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 37.04 E-value: 7.92e-03
10 20 30
....*....|....*....|....*....|...
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDV 430
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
398-460 |
8.85e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 37.77 E-value: 8.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496082746 398 LSGGNQQKLLISRWVAIGPRILILDEPTRGVDVGAKSEIYRIMNDMAR-QGVAILMISSELPEV 460
Cdd:PRK10247 138 LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEI 201
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
142-200 |
9.13e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 9.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496082746 142 TLTIAEQQQVEIARALHRQS--RIL-VMDEPTAALSSRETQRLFELILRLRDEGMAIIYISH 200
Cdd:PRK00349 830 TLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEH 891
|
|
| |
