|
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: 776.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAG 82
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMVGRP 242
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 243 LSDLFNKeRDIPLGKARLNVHHLTDGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIH 322
Cdd:COG1129 241 LEDLFPK-RAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 323 SPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERDARWGMLNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGN 402
Cdd:COG1129 320 SPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 403 QQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGK 482
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDRE 479
|
490
....*....|....*...
gi 13364550 483 NITQENIMTLATGVNDAH 500
Cdd:COG1129 480 EATEEAIMAAATGGAAAA 497
|
|
| 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: 552.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAG 82
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS------LTRDnlnagELVR 236
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfddmaqVDRD-----QLVQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 237 MMVGRPLSDLFN-KERdiPLGKARLNVHHLTDGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVD 315
Cdd:PRK11288 236 AMVGREIGDIYGyRPR--PLGEVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 316 GEPVVIHSPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERDARWGM-LNRKKAQTISDDAIKLLNIRVPHAQVR 394
Cdd:PRK11288 314 GKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGClINNRWEAENADRFIRSLNIKTPSREQL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 395 AGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGS 474
Cdd:PRK11288 394 IMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
490
....*....|....*....
gi 13364550 475 IAGELNGKNITQENIMTLA 493
Cdd:PRK11288 474 IAGELAREQATERQALSLA 492
|
|
| 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: 550.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSA 81
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNS 161
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 162 RILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMVGR 241
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 242 PLSDLFNKErDIPLGKARLNVHHLT---DGG--KVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDG 316
Cdd:COG3845 241 EVLLRVEKA-PAEPGEVVLEVENLSvrdDRGvpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 317 EPVVIHSPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERD--ARWGMLNRKKAQTISDDAIKLLNIRVPHAQVR 394
Cdd:COG3845 320 EDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPpfSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 395 AGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGS 474
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
490
....*....|....*
gi 13364550 475 IAGELNGKNITQENI 489
Cdd:COG3845 480 IVGEVPAAEATREEI 494
|
|
| 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: 547.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYT--ATSGEILIDGKPFHIRTPKDALS 80
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 AGITLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRN 160
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 161 SRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMVG 240
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 241 RPLSDLFNKE-RDIplGKARLNVHHLTDGGKVQPS-------SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRK-ATGGM 311
Cdd:PRK13549 242 RELTALYPREpHTI--GEVILEVRNLTAWDPVNPHikrvddvSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 312 IEVDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERDARWGMLNRKKAQTISDDAIKLLNIRVPHA 391
Cdd:PRK13549 320 IFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 392 QVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMR 471
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMH 479
|
490 500
....*....|....*....|....
gi 13364550 472 EGSIAGELNGKNITQENIMTLATG 495
Cdd:PRK13549 480 EGKLKGDLINHNLTQEQVMEAALR 503
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-503 |
3.62e-179 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 512.63 E-value: 3.62e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGI 83
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLGSELSHG-GLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMVGRP 242
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 243 LSDLFNKeRDIPLGKARLNVHHLTdGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIH 322
Cdd:PRK10762 242 LEDQYPR-LDKAPGEVRLKVDNLS-GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 323 SPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERDAR-WGMLNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGG 401
Cdd:PRK10762 320 SPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRaGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 402 NQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNG 481
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTR 479
|
490 500
....*....|....*....|..
gi 13364550 482 KNITQENIMTLATGVNDAHSQA 503
Cdd:PRK10762 480 EQATQEKLMAAAVGKLNRVNQE 501
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-492 |
2.00e-173 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 497.78 E-value: 2.00e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATS--GEILIDGKPFHIRTPKDALSAGI 83
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLT--RDNLNAGELVRMMVGR 241
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDcrADEVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 242 PLSDLFnKERDIPLGKARL-----NVHHLTDGGK--VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGV---RKATGgM 311
Cdd:NF040905 241 DLEDRY-PERTPKIGEVVFevknwTVYHPLHPERkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygRNISG-T 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 312 IEVDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERDARWGMLNRKKAQTISDDAIKLLNIRVPHA 391
Cdd:NF040905 319 VFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 392 QVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMR 471
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
490 500
....*....|....*....|.
gi 13364550 472 EGSIAGELNGKNITQENIMTL 492
Cdd:NF040905 479 EGRITGELPREEASQERIMRL 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-494 |
1.42e-163 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 473.12 E-value: 1.42e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSA 81
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQEMQLAPNLSVAENIFLGSELSHG----GLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARAL 157
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 158 HRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRM 237
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 238 MVGRPLSDLFNKERDI---PLGKARLNVHHLT--DGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMI 312
Cdd:PRK09700 241 MVGRELQNRFNAMKENvsnLAHETVFEVRNVTsrDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 313 EVDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERDAR----WGMLNRKKAQTISDDAIKLLNIRV 388
Cdd:PRK09700 321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGykgaMGLFHEVDEQRTAENQRELLALKC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 389 PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVY 468
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
|
490 500
....*....|....*....|....*..
gi 13364550 469 VMREGSIAGEL-NGKNITQENIMTLAT 494
Cdd:PRK09700 481 VFCEGRLTQILtNRDDMSEEEIMAWAL 507
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-495 |
1.49e-150 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 439.87 E-value: 1.49e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALS 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 AGITLIYQEMQLAPNLSVAENIFLGSElSHGGLVQRKEMLVQAqkvidrLGAQFNASDKVMTLTIAEQQQVEIARALHRN 160
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENILFGLP-KRQASMQKMKQLLAA------LGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 161 SRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMV- 239
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 240 ---GRPLSD-------LFNKERDIPLGKARLNVHHLTDGGKVQpSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATG 309
Cdd:PRK15439 239 aarEKSLSAsqklwleLPGNRRQQAAGAPVLTVEDLTGEGFRN-ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 310 GMIEVDGEPVVIHSPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERDARWgmLNRKKAQTISDDAIKLLNIRVP 389
Cdd:PRK15439 318 GRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCALTHNRRGFW--IKPARENAVLERYRRALNIKFN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 390 HAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYV 469
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLV 475
|
490 500
....*....|....*....|....*.
gi 13364550 470 MREGSIAGELNGKNITQENIMTLATG 495
Cdd:PRK15439 476 MHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-493 |
3.08e-148 |
|
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: 433.87 E-value: 3.08e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYT--ATSGEILIDGKPFHIRTPKDALSAGI 83
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLGSELSH-GGLVQRKEMLVQAQKVIDRLGAQ-FNASDKVMTLTIAEQQQVEIARALHRNS 161
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLpGGRMAYNAMYLRAKNLLRELQLDaDNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 162 RILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMVGR 241
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 242 PLSDLFNKE----RDIPLGKARLNVHHLTDG--GKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRK-ATGGMIEV 314
Cdd:TIGR02633 241 EITSLYPHEpheiGDVILEARNLTCWDVINPhrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 315 DGEPVVIHSPREAIDLGIGFLTENRKEQGLFLEMAAAENITMATLERDARWGMLNRKKAQTISDDAIKLLNIRVPHAQVR 394
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 395 AGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGS 474
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
490
....*....|....*....
gi 13364550 475 IAGELNGKNITQENIMTLA 493
Cdd:TIGR02633 481 LKGDFVNHALTQEQVLAAA 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-494 |
1.18e-146 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 429.15 E-value: 1.18e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 9 MRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGITLIYQ 88
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 89 EMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDE 168
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 169 PTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMVGRPLSDLFN 248
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 249 KERDIPlGKARLNVHHLTDggKVQPS----SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSP 324
Cdd:PRK10982 241 DKENKP-GEVILEVRNLTS--LRQPSirdvSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 325 REAIDLGIGFLTENRKEQGLFLEMAAAENITMATLER-DARWGMLNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQ 403
Cdd:PRK10982 318 NEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNyKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 404 QKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKN 483
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKT 477
|
490
....*....|.
gi 13364550 484 ITQENIMTLAT 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 |
7.17e-85 |
|
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: 259.67 E-value: 7.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 256 GKARLNVHHLTDGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFL 335
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 336 TENRKEQGLFLEMAAAENITMATLerdarwgmlnrkkaqtisddaikllnirvphaqvraggLSGGNQQKLLISRWVAIG 415
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 416 PRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 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 |
3.56e-84 |
|
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: 257.36 E-value: 3.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGITLI 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQemqlapnlsvaeniflgselshgglvqrkemlvqaqkvidrlgaqfnasdkvmtLTIAEQQQVEIARALHRNSRILVM 166
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 167 DEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-475 |
7.21e-61 |
|
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: 208.22 E-value: 7.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAF--GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTAT---SGEILIDGKPFhIRTPKDA 78
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 LSAGITLIYQE--MQLAPnLSVAENIFLGSELshgGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARA 156
Cdd:COG1123 81 RGRRIGMVFQDpmTQLNP-VTVGDQIAEALEN---LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 157 LHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELV 235
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 236 RMMVGRPLSDLFNKERDIPLGKARLNVHHLT---DGGKVQPS------SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRK 306
Cdd:COG1123 237 LAAVPRLGAARGRAAPAAAAAEPLLEVRNLSkryPVRGKGGVravddvSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 307 ATGGMIEVDGEPVVIHSPREaidlgigfLTENRKEQG---------LFLEMAAAENITMATLERdarwGMLNRKKAQTIS 377
Cdd:COG1123 317 PTSGSILFDGKDLTKLSRRS--------LRELRRRVQmvfqdpyssLNPRMTVGDIIAEPLRLH----GLLSRAERRERV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 378 DDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSE 456
Cdd:COG1123 385 AELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD 464
|
490
....*....|....*....
gi 13364550 457 LPEIVGMSDRVYVMREGSI 475
Cdd:COG1123 465 LAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-219 |
3.51e-56 |
|
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: 187.26 E-value: 3.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGITLI 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHGGLV-------QRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHR 159
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-219 |
1.16e-54 |
|
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: 184.09 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAG 82
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGSELSHGGLV------------QRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQ 150
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-234 |
1.45e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.95 E-value: 1.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPKDALSAGITLI 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED--VARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHGGLVQRKEmlvQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVM 166
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARE---RIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 167 DEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGEL 234
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-219 |
7.05e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 163.34 E-value: 7.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPKDALSAGITLI 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--IKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIflgsELSHGglvqrkemlvqaQKvidrlgaqfnasdkvmtltiaeqQQVEIARALHRNSRILVM 166
Cdd:cd03230 79 PEEPSLYENLTVRENL----KLSGG------------MK-----------------------QRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 167 DEPTAAL--SSRetHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03230 120 DEPTSGLdpESR--REFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-231 |
4.64e-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: 157.60 E-value: 4.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGITLI 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHGGLVQRKemlvqaqkvIDRLGAQF-----NASDKVMTLTIAEQQQVEIARALHRNS 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKAR---------LERVYELFprlkeRRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 162 RILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNA 231
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-219 |
9.63e-45 |
|
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: 156.50 E-value: 9.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFG----KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSA- 81
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS-KLSEKELAAf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 ---GITLIYQEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALH 158
Cdd:cd03255 80 rrrHIGFVFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 159 RNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMaEVYELSDRVSVLRDGQ 219
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-224 |
1.33e-44 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 156.94 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKdaLSAGITL 85
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILV 165
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 166 MDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ--YVGSL 224
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKvvAQGSL 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-219 |
9.42e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 9.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAFG----KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDAL 79
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS-SLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 80 SA------GItlIYQEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEI 153
Cdd:COG1136 81 ARlrrrhiGF--VFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 154 ARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMaEVYELSDRVSVLRDGQ 219
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-219 |
5.06e-42 |
|
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: 149.15 E-value: 5.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAFGKF--YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAGITL 85
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQ--EMQLApNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:cd03225 80 VFQnpDDQFF-GPTVEEEVAFGLENLG---LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-219 |
1.15e-41 |
|
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: 147.19 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAfgkfYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGIT 84
Cdd:cd03215 3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LI---YQEMQLAPNLSVAENIFLGSELShGGlvqrkemlvqaqkvidrlgaqfNasdkvmtltiaeQQQVEIARALHRNS 161
Cdd:cd03215 79 YVpedRKREGLVLDLSVAENIALSSLLS-GG----------------------N------------QQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 162 RILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-229 |
3.29e-41 |
|
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: 154.68 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAF-----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPK 76
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 77 D--ALSAGITLIYQ--EMQLAPNLSVAENIFLGseLSHGGLVQRKEMLVQAQKVIDR--LGAQFnASDKVMTLTIAEQQQ 150
Cdd:COG1123 336 SlrELRRRVQMVFQdpYSSLNPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERvgLPPDL-ADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNL 229
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-219 |
4.84e-41 |
|
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: 146.51 E-value: 4.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDalsAGITLI 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELshgGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVM 166
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKL---RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 167 DEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-236 |
8.46e-41 |
|
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: 146.67 E-value: 8.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGI 83
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMlvqaQKVID---RLGAQFNAsdKVMTLTIAEQQQVEIARALHRN 160
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADL----ERVYElfpRLKERRRQ--RAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 161 SRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVR 236
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-171 |
3.26e-40 |
|
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: 142.02 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKdALSAGITLIYQEMQLAPNLSVAEN 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 102 IFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVM----TLTIAEQQQVEIARALHRNSRILVMDEPTA 171
Cdd:pfam00005 80 LRLGLLLKG---LSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-219 |
4.38e-40 |
|
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: 142.00 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALsagitliy 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 88 qemqlapnlsvaENIFLGSELSHGglvqrkemlvqaqkvidrlgaqfnasdkvmtltiaEQQQVEIARALHRNSRILVMD 167
Cdd:cd00267 73 ------------RRIGYVPQLSGG-----------------------------------QRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 168 EPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
1.73e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.31 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKdals 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 agITLIYQEMQLAPN--LSVAENIFLGSeLSHGGLVQR--KEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARA 156
Cdd:COG1121 77 --IGYVPQRAEVDWDfpITVRDVVLMGR-YGRRGLFRRpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 157 LHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ-YVGS----LTRDNLNA 231
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLvAHGPpeevLTPENLSR 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-219 |
2.90e-39 |
|
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: 142.09 E-value: 2.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAGITL 85
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQ--EMQL-APnlSVAENIFLGSE---LShgglvqRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHR 159
Cdd:COG1122 80 VFQnpDDQLfAP--TVEEDVAFGPEnlgLP------REEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-219 |
1.33e-38 |
|
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: 138.86 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFH-IRTPKDALSAGITL 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQEMQLAPNLSVAENIFLGseLShGGlvqrkemlvqaqkvidrlgaqfnasdkvmtltiaEQQQVEIARALHRNSRILV 165
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--LS-GG----------------------------------QQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 166 MDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-240 |
1.83e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 146.71 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNI-AKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGI 83
Cdd:COG3845 256 VVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQE---MQLAPNLSVAENIFLGS----ELSHGGLVQRKEMLVQAQKVIDRlgaqF-----NASDKVMTLTIAEQQQV 151
Cdd:COG3845 336 AYIPEDrlgRGLVPDMSVAENLILGRyrrpPFSRGGFLDRKAIRAFAEELIEE----FdvrtpGPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 152 EIARALHRNSRILVMDEPTAAL---SSRETHRLfelIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDN 228
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLdvgAIEFIHQR---LLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
250
....*....|..
gi 13364550 229 LNAGELVRMMVG 240
Cdd:COG3845 489 ATREEIGLLMAG 500
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
3.58e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 140.22 E-value: 3.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNST-PVLEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHirtp 75
Cdd:COG1116 1 MSAAaPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 76 kdALSAGITLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEmlvQAQKVIDRLG-AQFnASDKVMTLTIAEQQQVEIA 154
Cdd:COG1116 77 --GPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRE---RARELLELVGlAGF-EDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 155 RALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAE-VYeLSDRVSVLRDG 218
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEaVF-LADRVVVLSAR 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-219 |
1.02e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFhirtpkDALSA- 81
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV------TGLPPe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 --GITLIYQEMQLAPNLSVAENI-FlgselshgGLVQRK----EMLVQAQKVIDRLG-AQFnASDKVMTLTIAEQQQVEI 153
Cdd:COG3842 76 krNVGMVFQDYALFPHLTVAENVaF--------GLRMRGvpkaEIRARVAELLELVGlEGL-ADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 154 ARALHRNSRILVMDEPTAAL--SSRETHRlFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALdaKLREEMR-EELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-234 |
2.98e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 137.50 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKD--ALSA 81
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQEMQLAPNLSVAENIFLGSeLSHGGLVQ------RKEMLVQAQKVIDRLG-AQFnASDKVMTLTIAEQQQVEIA 154
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGR-LGRTSTWRsllglfPPEDRERALEALERVGlADK-AYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 155 RALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGE 233
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAV 238
|
.
gi 13364550 234 L 234
Cdd:COG3638 239 L 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-229 |
3.46e-37 |
|
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: 137.48 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAGITL 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQEMQLAPNLSVAENIFLGsELSHGGLVQR--KEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALG-RYPHLGLFGRpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS------LTRDNL 229
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQgppeevLTPELL 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-223 |
8.68e-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: 135.83 E-value: 8.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHirtPKDALSAGITLI 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---NLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIdRLGAQfnASDKVMTLTIAEQQQVEIARALHRNSRILVM 166
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLV-QLEGY--ANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 167 DEPTAALSSR-ETHRLFELiMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDG--QYVGS 223
Cdd:cd03300 155 DEPLGALDLKlRKDMQLEL-KRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGkiQQIGT 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-227 |
9.76e-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: 135.29 E-value: 9.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFG----KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPkdalSAG 82
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP--VTGP----GPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGaqfnasdkvmtLTIAE-----------QQQV 151
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVG-----------LSGFEnayphqlsggmRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 152 EIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVL--RDGQYVGSLTRD 227
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-223 |
1.41e-36 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 134.27 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFhIRTPKDALSAGITLI 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEmqLAPNLSVAENIFLGSELsHGGLVQRkemlvqAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVM 166
Cdd:cd03268 80 APG--FYPNLTARENLRLLARL-LGIRKKR------IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 167 DEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-227 |
4.17e-36 |
|
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: 133.85 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG-----AYTATSGEILIDGKP-FHIRTPKDALS 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 AGITLIYQEmqlaPNL---SVAENIFLGseLSHGGLVQRKEMLVQAQKVIDR--LGAQFNASDKVMTLTIAEQQQVEIAR 155
Cdd:cd03260 81 RRVGMVFQK----PNPfpgSIYDNVAYG--LRLHGIKLKEELDERVEEALRKaaLWDEVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 156 ALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRD 227
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-219 |
4.52e-36 |
|
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: 131.74 E-value: 4.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFG--KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRT-PKDALSAGI 83
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD--LRDlDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLApNLSVAENIflgseLSHGglvqrkemlvqaqkvidrlgaqfnasdkvmtltiaEQQQVEIARALHRNSRI 163
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI-----LSGG-----------------------------------QRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRLRDeGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-219 |
9.87e-36 |
|
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: 132.27 E-value: 9.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPK-DALSAGITL 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQEMQLAPNLSVAENIFLGSELSHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILV 165
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 166 MDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-221 |
2.16e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 131.25 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDalsagITLI 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAEN-IFLGSelSHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILV 165
Cdd:cd03269 76 PEERGLYPKMKVIDQlVYLAQ--LKG--LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 166 MDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-218 |
2.55e-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: 131.34 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGK----FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpFHIRTPKDALSAG 82
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGSELsHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGL-YG--LKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-219 |
4.91e-35 |
|
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: 130.70 E-value: 4.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGK--FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPKDALSAGIT 84
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS--IRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENIFLGSELsHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRIL 164
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARL-KG--LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 165 VMDEPTAALSSRETHRLFELIMRLRdEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-221 |
5.32e-35 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 130.70 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSA 81
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 G--ITLIYQEMQLA--PNLSVAENIflgSE--LSHGGLVQRKEmlvqAQKVIDRLGAQFNASDKVMTLTIAE-----QQQ 150
Cdd:cd03257 81 RkeIQMVFQDPMSSlnPRMTIGEQI---AEplRIHGKLSKKEA----RKEAVLLLLVGVGLPEEVLNRYPHElsggqRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-224 |
7.89e-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: 7.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFhirTPKDALSAGitl 85
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 iY--QEMQLAPNLSVAENI-FLGsELsHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:COG4152 75 -YlpEERGLYPKMKVGEQLvYLA-RL-KG--LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV--GSL 224
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsGSV 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-219 |
1.05e-34 |
|
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: 129.30 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDalsAGITLI 86
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVM 166
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRK---VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 167 DEPTAALSS--RETHRLfELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03301 155 DEPLSNLDAklRVQMRA-ELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-218 |
1.39e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 130.50 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSA 81
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQ------EMQLAPNLSVAENIFLGSELSHGGL----VQRKEM--LVQAQKVIDRLGAQFNASDKVMTLTIAEQQ 149
Cdd:PRK11300 81 GVVRTFQhvrlfrEMTVIENLLVAQHQQLKTGLFSGLLktpaFRRAESeaLDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 150 QVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-229 |
2.17e-34 |
|
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: 129.33 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFH--IRTPKDALS 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 AGITLIYQEMQLAPNLSVAENIFLG----SELShgglvqRKEMLVQAQKVIDRLGAQfNASDKvMTltiAE-----QQQV 151
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPlrehTDLS------EAEIRELVLEKLELVGLP-GAADK-MP---SElsggmRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 152 EIARALHRNSRILVMDEPTAAL---SSREthrLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRD 227
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLdpiTSAV---IDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
..
gi 13364550 228 NL 229
Cdd:COG1127 228 EL 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-221 |
2.09e-33 |
|
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: 126.54 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFG----KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKD--AL 79
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 80 SAGITLIYQEMQLAPNLSVAENIFLGSELSHgglVQRKEmlvQAQKViDRLGAQFNASDKV----MTLTIAEQQQVEIAR 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAG---VPKAE---IEERV-LELLELVGLEDKAdaypAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 156 ALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-219 |
2.47e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.50 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPkdALSAGITLI 86
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP--PRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGseLSHGGL----VQRK--EML--VQAQKVIDRLGAQfnasdkvmtLTIAEQQQVEIARALH 158
Cdd:COG1118 81 FQHYALFPHMTVAENIAFG--LRVRPPskaeIRARveELLelVQLEGLADRYPSQ---------LSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 159 RNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-221 |
3.03e-33 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 126.30 E-value: 3.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYaLKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFhirTPKDALSAGITLI 86
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---TNLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGselshggLVQRKEMLVQAQKVIDRLGAQFNASD----KVMTLTIAEQQQVEIARALHRNSR 162
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYG-------LKKRKVDKKEIERKVLEIAEMLGIDHllnrKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-229 |
3.75e-33 |
|
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: 125.69 E-value: 3.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFH--IRTPKDALSAGIT 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENI-FLGSElsHGGLVQRkemlVQAQKVIDRLGA-QFNASDKVMTltiAE-----QQQVEIARAL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVaFPLRE--HTRLSEE----EIREIVLEKLEAvGLRGAEDLYP---AElsggmKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 158 HRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNL 229
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-236 |
3.88e-33 |
|
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: 126.14 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFG-KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKD--ALSAGI 83
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLGSeLSHGGLVQ------RKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARAL 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGR-LGRRSTWRslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 158 HRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVR 236
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-236 |
9.26e-33 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 124.58 E-value: 9.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDG-----KPFHIRTpkdalSA 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditkLPMHKRA-----RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQaqkVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNS 161
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEE---LLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 162 RILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVR 236
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-221 |
9.80e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 125.83 E-value: 9.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 12 IAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSA----GITLIY 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRElrrkKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 88 QEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMD 167
Cdd:cd03294 109 QSFALLPHRTVLENVAFGLEVQG---VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 168 EPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-200 |
8.14e-32 |
|
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: 121.43 E-value: 8.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPKDALSAGIT 84
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP--IRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENIFLGSELsHGGLVQRkemlVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRIL 164
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAAL-YGLRADR----EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 13364550 165 VMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH 200
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-237 |
1.75e-31 |
|
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: 121.09 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGITLI 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHGGLvqrkemlvqaQKVIDRLGAQFNASDKVMT-----LTIAEQQQVEIARALHRNS 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS----------RKIPDEIYELFPVLKEMLGrrggdLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 162 RILVMDEPTAALSS---RETHRlfeLIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAgELVRM 237
Cdd:TIGR03410 151 KLLLLDEPTEGIQPsiiKDIGR---VIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDE-DKVRR 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-219 |
2.63e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.54 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSA--- 81
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 --GItlIYQEMQLAPNLSVAENIFLGSELsHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHR 159
Cdd:COG2884 80 riGV--VFQDFRLLPDRTVYENVALPLRV-TG--KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-219 |
5.60e-31 |
|
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: 119.28 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKD--ALSAG 82
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRG---KKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-223 |
6.72e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.49 E-value: 6.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDalsAGITLI 86
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENI-FlgselshgGLVQRK--------------EMLvQAQKVIDRlgaqfnasdKVMTLTIAEQQQV 151
Cdd:COG3839 81 FQSYALYPHMTVYENIaF--------PLKLRKvpkaeidrrvreaaELL-GLEDLLDR---------KPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 152 EIARALHRNSRILVMDEPTAAL--SSRETHRLFelIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDG--QYVGS 223
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLdaKLRVEMRAE--IKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGriQQVGT 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-215 |
7.82e-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: 118.79 E-value: 7.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGITLIY 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 88 QEMqlapNLSVAENIFLGSeLSHGGLVQR-----KEMLVQAqkvIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:cd03235 81 RDF----PISVRDVVLMGL-YGHKGLFRRlskadKAKVDEA---LERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVL 215
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-223 |
1.32e-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: 118.98 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDAlsaGITLI 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHGG------LVQRKEM----LVQAQKVIDRLGAQfnasdkvmtLTIAEQQQVEIARA 156
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSerppeaEIRAKVHellkLVQLDWLADRYPAQ---------LSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 157 LHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQY--VGS 223
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIeqVGT 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-219 |
1.85e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 118.56 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHI-RTPKDALSAGIT 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDsKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENIFLGSELSHGglVQRKEMLVQAQKVIDRLGaqfnasdkvmtltIAE------------QQQ-V 151
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKK--MSKAEAEERAMELLERVG-------------LADkadaypaqlsggQQQrV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 152 EIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-223 |
2.02e-30 |
|
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: 117.78 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 12 IAKAFGKFyALKgVDLTVyPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSA---GITLIYQ 88
Cdd:cd03297 6 IEKRLPDF-TLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 89 EMQLAPNLSVAENIFLGSELShgglvQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDE 168
Cdd:cd03297 83 QYALFPHLNVRENLAFGLKRK-----RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 169 PTAAL--SSRETHRLfELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:cd03297 158 PFSALdrALRLQLLP-ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-219 |
2.45e-30 |
|
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: 117.92 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDA 78
Cdd:COG4181 5 SAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF-ALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 L----SAGITLIYQEMQLAPNLSVAENIFLGSElshggLVQRKEMLVQAQKVIDR--LGAQFNASDKvmTLTIAEQQQVE 152
Cdd:COG4181 84 RarlrARHVGFVFQSFQLLPTLTALENVMLPLE-----LAGRRDARARARALLERvgLGHRLDHYPA--QLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 153 IARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAeVYELSDRVSVLRDGQ 219
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPA-LAARCDRVLRLRAGR 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-221 |
2.51e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.48 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKV---LAGAYTA--TSGEILIDGKPFhIRTPKDALS 80
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQDI-FKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 AGITLIYQEMQLAPNLSVAENIFLGSEL-----SHGGLVQR-KEMLVQAQ---KVIDRLGAqfnasdKVMTLTIAEQQQV 151
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLnrlvkSKKELQERvRWALEKAQlwdEVKDRLDA------PAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 152 EIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-229 |
5.27e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.91 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLI 86
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA-AWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSeLSHGGLVQRKEMLVQAqkVIDRLGAQFNASDKVMTLTIAEQQQVEIARAL-------HR 159
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGR-APHGSSAAQDRQIVRE--ALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH--RMAEVYelSDRVSVLRDGQYVGS------LTRDNL 229
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlNLAAQY--ADRILLLHQGRLVAQgtpeevLTDELL 233
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-212 |
6.94e-30 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 115.79 E-value: 6.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 9 MRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK---PFHIRTPKDALSAGITL 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAqkvIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILV 165
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEA---LEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 166 MDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMaEVYELSDRV 212
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRV 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-219 |
7.24e-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: 115.23 E-value: 7.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKdalsagitliy 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 88 qemQLAPNLSVaeniflgselshgglvqrkemLVQAqkvIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMD 167
Cdd:cd03214 70 ---ELARKIAY---------------------VPQA---LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 168 EPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-229 |
1.02e-29 |
|
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: 115.93 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpFHIRTPKDALSAGITLI 86
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLgselsHGGL--VQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRIL 164
Cdd:cd03265 79 FQDLSVDDELTGWENLYI-----HARLygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 165 VMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNL 229
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-218 |
1.20e-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: 115.58 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFY-ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPF-HIR---TPKdaLSA 81
Cdd:cd03292 1 IEFINVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRgraIPY--LRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNS 161
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTG---VPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 162 RILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
275-475 |
1.65e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.93 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAIDLgIGFLTEnrkEQGLFLEMAAAENI 354
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRR-IGYVPQ---EPALYPDLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAtlerdARWGMLNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:COG1131 95 RFF-----ARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13364550 435 EIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG1131 169 ELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-231 |
2.78e-29 |
|
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: 121.86 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKF--YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRT-PKDALSAGI 83
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID--LRQiDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEmqlaPNL---SVAENIFLGSElshggLVQRKEM-----LVQAQKVIDRLGAQFNA--SDKVMTLTIAEQQQVEI 153
Cdd:COG2274 552 GVVLQD----VFLfsgTIRENITLGDP-----DATDEEIieaarLAGLHDFIEALPMGYDTvvGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 154 ARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQYVGSLTRDNLNA 231
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-221 |
3.29e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.40 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPkdaLSAGI 83
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLG---SELSHGGLVQR-KEML--VQAQKVIDRlgaqfnasdKVMTLTIAEQQQVEIARAL 157
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGlkqDKLPKAEIASRvNEMLglVHMQEFAKR---------KPHQLSGGQRQRVALARSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 158 HRNSRILVMDEPTAALSSRETHRL-FELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-221 |
6.07e-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: 113.51 E-value: 6.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 11 NIAKAFGKFY-ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHirtPKDALSAgITLIYQE 89
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKS-IGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 90 M--QLAPNlSVAENIFLGSELSHGGlvqrkemLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMD 167
Cdd:cd03226 80 VdyQLFTD-SVREELLLGLKELDAG-------NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 168 EPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-475 |
8.30e-29 |
|
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: 119.40 E-value: 8.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGK----FYALKGVDLTVYPGEIHALMGENGAGKS----TLMKVLAGAYTATSGEILIDGKPFhI 72
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 73 RTPKDALSA----GITLIYQE-M-QLAPNLSV----AENIFLgselsHGGLvQRKEMLVQAQKVIDRLG---AQFNASDK 139
Cdd:COG4172 80 GLSERELRRirgnRIAMIFQEpMtSLNPLHTIgkqiAEVLRL-----HRGL-SGAAARARALELLERVGipdPERRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 140 VMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 219 QYV--GSL-----------TRDNLNA---GELVRM-MVGRPLSDLFNKERDIPLGKARLN--VHHLTdggKVQPSSLLVR 279
Cdd:COG4172 234 EIVeqGPTaelfaapqhpyTRKLLAAeprGDPRPVpPDAPPLLEARDLKVWFPIKRGLFRrtVGHVK---AVDGVSLTLR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 280 SGEIVGLAGLVGAGRSELAQ----LIfgvrkATGGMIEVDGEPVVIH-----------------------SPR----EAI 328
Cdd:COG4172 311 RGETLGLVGESGSGKSTLGLallrLI-----PSEGEIRFDGQDLDGLsrralrplrrrmqvvfqdpfgslSPRmtvgQII 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 329 D--LGIGFLTENRKEQglflEMAAAENITMATLERDARWgmlnrkkaqtisddaikllniRVPHAqvraggLSGGNQQKL 406
Cdd:COG4172 386 AegLRVHGPGLSAAER----RARVAEALEEVGLDPAARH---------------------RYPHE------FSGGQRQRI 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 407 LISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-475 |
1.59e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 118.75 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG--AYTATSGEILID----------GKPFHIRT 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyvERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 75 P----------------------KDALSAGITLIYQE-MQLAPNLSVAENIFLG-SELSHGGlvqrKEMLVQAQKVIDrl 130
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRtFALYGDDTVLDNVLEAlEEIGYEG----KEAVGRAVDLIE-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 131 gaQFNASDKVM----TLTIAEQQQVEIARALHRNSRILVMDEPTAALSSrETHRLFE--LIMRLRDEGMAIIYISHRMAE 204
Cdd:TIGR03269 155 --MVQLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP-QTAKLVHnaLEEAVKASGISMVLTSHWPEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 205 VYELSDRVSVLRDGQYVGSLTRDNLNAgelvRMMVGRPLsdlFNKERDIPLGKARLNVHHLT------DGGKVQPS---S 275
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEVVA----VFMEGVSE---VEKECEVEVGEPIIKVRNVSkryisvDRGVVKAVdnvS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 276 LLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVD-GEPVVIHSPREAIDLG-----IGFLtenRKEQGLFLEMA 349
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRGrakryIGIL---HQEYDLYPHRT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 350 AAENITMA-TLERDARWGMlnRKKAQTI------SDDAIKLLNiRVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:TIGR03269 382 VLDNLTEAiGLELPDELAR--MKAVITLkmvgfdEEKAEEILD-KYPDE------LSEGERHRVALAQVLIKEPRIVILD 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 423 EPARGVDVGAKSEIYR-IMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
275-475 |
1.76e-28 |
|
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: 113.02 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTEnrkEQGLFLEMAAAENI 354
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQ---EASIFRKLTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tMATLERDArwgmLNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03218 97 -LAVLEIRG----LSKKEREEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13364550 435 EIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03218 171 DIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-242 |
2.59e-28 |
|
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: 112.78 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGK-FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIR-TPKDALSAGIT 84
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED--IReQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFnASDKVMTLTIAEQQQVEIARALHRNSRIL 164
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEF-ADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 165 VMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNL---NAGELVRMMVG 240
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrsPANDFVAEFVG 237
|
..
gi 13364550 241 RP 242
Cdd:cd03295 238 AD 239
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-229 |
3.44e-28 |
|
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: 117.94 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIYQEMQLaPNLSVAE 100
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRRQIAWVPQNPYL-FAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASdkvmtltIAEQ---------QQVEIARALHRNSRILVMDEPTA 171
Cdd:COG4988 430 NLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTP-------LGEGgrglsggqaQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 172 ALSSRETHRLFELIMRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQYVGSLTRDNL 229
Cdd:COG4988 503 HLDAETEAEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-229 |
5.86e-28 |
|
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: 111.16 E-value: 5.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRT-PKDALSAGITLIYQEMQLAPNlSVA 99
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID--IRDiSRKSLRSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHGGLVQRKEMLVQAQKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRE 177
Cdd:cd03254 95 ENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 178 THRLFELIMRLRDEGMAIIyISHRMAEVYElSDRVSVLRDGQYVGSLTRDNL 229
Cdd:cd03254 175 EKLIQEALEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
275-476 |
6.48e-28 |
|
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: 110.99 E-value: 6.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTENRkeqGLFLEMAAAENI 354
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPELTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAtlerdarWGMLNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03224 97 LLG-------AYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13364550 435 EIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:cd03224 170 EIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-236 |
7.22e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 111.51 E-value: 7.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGIT 84
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENiflgseLSHGGLVQRKEmlvQAQKVIDRLGAQF-----NASDKVMTLTIAEQQQVEIARALHR 159
Cdd:PRK11614 84 IVPEGRRVFSRMTVEEN------LAMGGFFAERD---QFQERIKWVYELFprlheRRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVR 236
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-223 |
1.04e-27 |
|
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: 113.66 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 11 NIAKAFGKFyALKgVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSA---GITLIY 87
Cdd:COG4148 6 DFRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPhrrRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 88 QEMQLAPNLSVAENIFLGseLSHGGLVQRKemlVQAQKVIDRLG-----AQfnasdKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:COG4148 84 QEARLFPHLSVRGNLLYG--RKRAPRAERR---ISFDEVVELLGighllDR-----RPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-221 |
1.67e-27 |
|
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: 109.60 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAGITLIYQEMQLApNLSVAE 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFN--ASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRET 178
Cdd:cd03245 97 NITLGAPLADDERILRAAELAGVTDFVNKHPNGLDlqIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 179 HRLFELIMRLRdEGMAIIYISHRMAeVYELSDRVSVLRDGQYV 221
Cdd:cd03245 177 ERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-231 |
2.25e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.63 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGIT 84
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENIFLGSeLSHGGLVQRKEMLVQAqkVIDRLGAQFNASDKVMTLTIAEQQQVEIARAL---HRNS 161
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAMGR-APHGLSRAEDDALVAA--ALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlWEPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 162 ---RILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISH--RMAEVYelSDRVSVLRDGQYV--GS----LTRDNL 229
Cdd:PRK13548 157 gppRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHdlNLAARY--ADRIVLLHQGRLVadGTpaevLTPETL 234
|
..
gi 13364550 230 NA 231
Cdd:PRK13548 235 RR 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
275-475 |
3.74e-27 |
|
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: 109.06 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGfltenRKEQ--GLFLEMAAAE 352
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG-----RTFQipRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NITMATLERDARWGMLNR-----KKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARG 427
Cdd:cd03219 95 NVMVAAQARTGSGLLLARarreeREARERAEELLERVGLA-DLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13364550 428 VDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03219 174 LNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-219 |
5.79e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.49 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 20 YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRT-PKDALSAGITLIYQEMQLApNLSV 98
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD--IRDlTLESLRRQIGVVPQDTFLF-SGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNA--SDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSR 176
Cdd:COG1132 431 RENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTvvGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 177 ETHRLFELIMRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:COG1132 511 TEALIQEALERLM-KGRTTIVIAHRLSTI-RNADRILVLDDGR 551
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-221 |
8.62e-27 |
|
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: 107.58 E-value: 8.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 26 DLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDalsAGITLIYQEMQLAPNLSVAENIFLG 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 106 -SELSHGGLVQRKEMlvqaQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFEL 184
Cdd:cd03298 95 lSPGLKLTAEDRQAI----EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 13364550 185 IMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03298 171 VLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
275-478 |
8.75e-27 |
|
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: 105.97 E-value: 8.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTEnrkeqglflemaaaeni 354
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tmatlerdarwgmlnrkkaqtisddaikllnirvphaqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 435 EIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:cd03216 120 RLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-219 |
1.71e-26 |
|
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: 105.38 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIYQEMQLAPNlSVAEN 101
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-QWDPNELGDHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IflgseLSHGglvQRkemlvqaqkvidrlgaqfnasdkvmtltiaeqQQVEIARALHRNSRILVMDEPTAALSSRETHRL 181
Cdd:cd03246 96 I-----LSGG---QR--------------------------------QRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 13364550 182 FELIMRLRDEGMAIIYISHRMaEVYELSDRVSVLRDGQ 219
Cdd:cd03246 136 NQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-203 |
2.72e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.10 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpFHIRTPKDA-----LS 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDerlirQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 AGitLIYQEMQLAPNLSVAENIFLGSELSHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRN 160
Cdd:PRK09493 79 AG--MVFQQFYLFPHLTALENVMFGPLRVRG--ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 161 SRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMA 203
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-240 |
2.80e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.70 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKdALSAGIT 84
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQA-QKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS------LTRDNLNAGELVRM 237
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAgppadvLTADTLRAAFDART 240
|
...
gi 13364550 238 MVG 240
Cdd:PRK09536 241 AVG 243
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-231 |
2.88e-26 |
|
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: 112.17 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAF--GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRT-PKDA 78
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD--LRDlDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 LSAGITLIYQEmqlaPNL---SVAENIFLGS-ELSHGGLVQrkeMLVQAQ--KVIDRLGAQFNAS--DKVMTLTIAEQQQ 150
Cdd:COG4987 407 LRRRIAVVPQR----PHLfdtTLRENLRLARpDATDEELWA---ALERVGlgDWLAALPDGLDTWlgEGGRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLrDEGMAIIYISHRMAEVyELSDRVSVLRDGQYVGSLTRDNLN 230
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEELL 557
|
.
gi 13364550 231 A 231
Cdd:COG4987 558 A 558
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
275-475 |
2.99e-26 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 104.79 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvIHSPREAIDLGIGFLTEnrkEQGLFLEMAAAENI 354
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--IKKEPEEVKRRIGYLPE---EPSLYENLTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TmatlerdarwgmlnrkkaqtisddaikllnirvphaqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03230 95 K------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13364550 435 EIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03230 133 EFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
9-219 |
3.17e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 106.70 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 9 MRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK---PFhirtpkdALSAGitl 85
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLL-------ELGAG--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 iyqemqLAPNLSVAENIFLGSELsHGglVQRKEMLVQAQKVID--RLGAQFNAsdKVMTLTIAEQqqveiAR-----ALH 158
Cdd:COG1134 99 ------FHPELTGRENIYLNGRL-LG--LSRKEIDEKFDEIVEfaELGDFIDQ--PVKTYSSGMR-----ARlafavATA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 159 RNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-221 |
5.89e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 105.35 E-value: 5.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGeIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPKDALSAGITLI 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--VLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAEniFLG-----SELSHGGLVQRKEMLVQAQKVIDRlgaqfnASDKVMTLTIAEQQQVEIARALHRNS 161
Cdd:cd03264 78 PQEFGVYPNFTVRE--FLDyiawlKGIPSKEVKARVDEVLELVNLGDR------AKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 162 RILVMDEPTAALSSRETHRLFELIMRLrDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-221 |
1.81e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.09 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKD--ALS 80
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 AGITLIYQEMQLAPNLSVAENIFLGSELSHgglVQRKEMLVQAQKVIDRLGaqfnASDKvmtltiAE---------QQQ- 150
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAG---VPKAEIRKRVAELLELVG----LSDK------ADaypsqlsggQKQr 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-215 |
2.04e-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: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAY---TATSGEILIDGKPFHIRTPKDA 78
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 LS---AGITLIYQE-MQ-LAPNLSVAENIflgSE--LSHGGLvQRKEMLVQAQKVIDRLGaqfnasdkvmtLTIAEQ--- 148
Cdd:COG0444 81 RKirgREIQMIFQDpMTsLNPVMTVGDQI---AEplRIHGGL-SKAEARERAIELLERVG-----------LPDPERrld 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 149 -----------QQVEIARALHRNSRILVMDEPTAAL--SSRetHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSV 214
Cdd:COG0444 146 ryphelsggmrQRVMIARALALEPKLLIADEPTTALdvTIQ--AQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAV 223
|
.
gi 13364550 215 L 215
Cdd:COG0444 224 M 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-221 |
2.15e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.32 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDA-----LSA 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEkairlLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQEMQLAPNLSVAENIF------LGselshgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIAR 155
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapckvLG--------LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 156 ALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
275-476 |
3.05e-25 |
|
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: 103.57 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLgIGFLTENrkeqglflemaaAEN- 353
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQN------------PDDq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 ITMATLERDARWGMLN----RKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:COG1122 88 LFAPTVEEDVAFGPENlglpREEIRERVEEALELVGLehladRPPHE------LSGGQKQRVAIAGVLAMEPEVLVLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 425 ARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:COG1122 162 TAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
275-478 |
5.40e-25 |
|
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: 103.14 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTENRkeqGLFLEMAAAENI 354
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGR---RIFPSLTVEENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARwgmlnRKKAQTIsDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARG-----VD 429
Cdd:COG0410 100 LLGAYARRDR-----AEVRADL-ERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGlapliVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 430 vgaksEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:COG0410 174 -----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-219 |
7.34e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.80 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfHIRTPKDALS 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-ITHVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 agITLIYQEMQLAPNLSVAENIFLG---SELSHGGLVQR-KEML--VQAQKVIDRlgaqfnasdKVMTLTIAEQQQVEIA 154
Cdd:PRK09452 88 --VNTVFQSYALFPHMTVFENVAFGlrmQKTPAAEITPRvMEALrmVQLEEFAQR---------KPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 155 RALHRNSRILVMDEPTAALSsretHRL-----FELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALD----YKLrkqmqNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-215 |
7.65e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.40 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPkdalSAGITLIYQEMQLAPNLSVAE 100
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP--VTGP----GADRGVVFQKDALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGSELSHGGLVQRKEmlvQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS--REt 178
Cdd:COG4525 96 NVAFGLRLRGVPKAERRA---RAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltRE- 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 13364550 179 hRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVL 215
Cdd:COG4525 172 -QMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-475 |
7.85e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.02 E-value: 7.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKS----TLMKVL--AGAyTATSGEIL------ 64
Cdd:PRK10261 7 LDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGG-LVQCDKMLlrrrsr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 65 --IDGKPFHIRTPKDALSAGITLIYQE--MQLAPNLSVAENIFLGSELSHGglVQRKEMLVQAQKVIDRL---GAQFNAS 137
Cdd:PRK10261 86 qvIELSEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQG--ASREEAMVEAKRMLDQVripEAQTILS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 138 DKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLR 216
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 217 DGQYV--GSL-----------TRDNLNAGELVRMMVGR------PLSDLFNKERDIPL--------GKARLNVHHLTD-- 267
Cdd:PRK10261 244 QGEAVetGSVeqifhapqhpyTRALLAAVPQLGAMKGLdyprrfPLISLEHPAKQEPPieqdtvvdGEPILQVRNLVTrf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 268 ---GG----------KVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPR--EAIDLGI 332
Cdd:PRK10261 324 plrSGllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 333 GFLTenrkeQGLFLEMAAAENITMATLERDARWGMLNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWV 412
Cdd:PRK10261 404 QFIF-----QDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARAL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 413 AIGPRILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-247 |
8.00e-25 |
|
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: 103.24 E-value: 8.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSG-EILIDGKP------FHIRTPk 76
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedvWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 77 dalsagITLIYQEMQLA--PNLSVAENI---FLGSElshgGLVQR--KEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQ 149
Cdd:COG1119 80 ------IGLVSPALQLRfpRDETVLDVVlsgFFDSI----GLYREptDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 150 QVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEG-MAIIYISHRMAEVYELSDRVSVLRDGQYVGsltrdn 228
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVA------ 223
|
250
....*....|....*....
gi 13364550 229 lnAGELVRMMVGRPLSDLF 247
Cdd:COG1119 224 --AGPKEEVLTSENLSEAF 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-222 |
1.45e-24 |
|
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: 100.70 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG--AYTATSGEILIDGKPFHIRTPKDAlsagITLIYQEMQLAPNLSVA 99
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELS--HGGlvQRKemlvqaqkvidrlgaqfnasdkvmtltiaeqqQVEIARALHRNSRILVMDEPTAALSSRE 177
Cdd:cd03213 101 ETLMFAAKLRglSGG--ERK--------------------------------RVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13364550 178 THRLFELIMRLRDEGMAIIYISHRM-AEVYELSDRVSVLRDGQ--YVG 222
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRviYFG 194
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-262 |
4.80e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.61 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFG--KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKP------FHIR 73
Cdd:PRK13632 3 NKSVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 74 TpkdalsaGITLIYQEmqlaPN-----LSVAENIFLGSElshGGLVQRKEMlvqaQKVIDRLGAQFNASDKV----MTLT 144
Cdd:PRK13632 83 K-------KIGIIFQN----PDnqfigATVEDDIAFGLE---NKKVPPKKM----KDIIDDLAKKVGMEDYLdkepQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 145 IAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGM-AIIYISHRMAEVYeLSDRVSVlrdgqyvgs 223
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIV--------- 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 13364550 224 ltrdnLNAGELVRmmVGRPLSDLFNKERdipLGKARLNV 262
Cdd:PRK13632 215 -----FSEGKLIA--QGKPKEILNNKEI---LEKAKIDS 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-478 |
6.16e-24 |
|
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: 99.75 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAiDLGIGFLTENRkeqGLFLEMAAAENi 354
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEA-RRRLGFVSDST---GLYDRLTAREN- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tmatLERDARWGMLNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03266 99 ----LEYFAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 435 EIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:cd03266 174 ALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-225 |
9.92e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.50 E-value: 9.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAF--GKFYA--LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFhirtpkD 77
Cdd:PRK11629 1 MNKILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM------S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 78 ALSAG---------ITLIYQEMQLAPNLSVAENIFLgsELSHGGlVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQ 148
Cdd:PRK11629 75 KLSSAakaelrnqkLGFIYQFHHLLPDFTALENVAM--PLLIGK-KKPAEINSRALEMLAAVGLEHRANHRPSELSGGER 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 149 QQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSvLRDGQYVGSLT 225
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAELS 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-229 |
1.27e-23 |
|
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: 99.54 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfHIRT-PKDALSAGITLIYQEMQLAPNlSVAE 100
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV--DIRDlNLRWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFN--ASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRET 178
Cdd:cd03249 96 NIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13364550 179 HRLFELIMRLRdEGMAIIYISHRMAEVYElSDRVSVLRDGQYVGSLTRDNL 229
Cdd:cd03249 176 KLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
275-473 |
1.28e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 98.69 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTENRKEQglflemaaaenI 354
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGLVFQNPDDQ-----------F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLN----RKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:cd03225 89 FGPTVEEEVAFGLENlglpEEEIEERVEEALELVGLeglrdRSPFT------LSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13364550 426 RGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-224 |
1.28e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.73 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVL-------AGAytATSGEILIDGKPfhIRT 74
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGA--RVEGEILLDGED--IYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 75 PK---DALSAGITLIYQEmqlaPN---LSVAENIFLGSELShgGLVQRKEM-------LVQA---QKVIDRLgaqfnaSD 138
Cdd:COG1117 83 PDvdvVELRRRVGMVFQK----PNpfpKSIYDNVAYGLRLH--GIKSKSELdeiveesLRKAalwDEVKDRL------KK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 139 KVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEgMAIIYISHRMAEVYELSDRVSVLrdg 218
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFF--- 226
|
....*.
gi 13364550 219 qYVGSL 224
Cdd:COG1117 227 -YLGEL 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-219 |
1.58e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.65 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAG 82
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ItlIYQEMQLAPNLSVAENIFLGSE---LSHGGLVQRKEMLVQAQKVIDRlgaqfnASDKVMTLTIAEQQQVEIARALHR 159
Cdd:PRK13537 84 V--VPQFDNLDPDFTVRENLLVFGRyfgLSAAAARALVPPLLEFAKLENK------ADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-219 |
1.87e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 101.33 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFhirTPKDALSAGITLI 86
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVmtlTIAEQQQVEIARALHRNSRILVM 166
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI---SGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 167 DEPTAAL------SSRETHRlfELIMRLrdeGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK11432 161 DEPLSNLdanlrrSMREKIR--ELQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-219 |
1.88e-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: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFyaLKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfHIRTPKDAlsAGITLI 86
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-LTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGselSHGGL----VQRKEMLVQAQKV-----IDRLGAQfnasdkvmtLTIAEQQQVEIARAL 157
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLG---LRPGLkltaEQRAQVEQALERVglaglLDRLPGQ---------LSGGQRQRVALARCL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 158 HRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-221 |
1.96e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.04 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPkDAL 79
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA-DAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 80 SA----GITLIYQEMQLAPNLSVAEN-----IFLGSElshgglvqRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQ 150
Cdd:PRK10535 81 AQlrreHFGFIFQRYHLLSHLTAAQNvevpaVYAGLE--------RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRmAEVYELSDRVSVLRDGQYV 221
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-223 |
2.51e-23 |
|
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: 97.60 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG--AYTATSGEILIDGKPFHIRTPKDALSAGIT 84
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLAPNLSVAENI-FLGSELShGGlvqrkemlvqaqkvidrlgaqfnasdkvmtltiaEQQQVEIARALHRNSRI 163
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLrYVNEGFS-GG----------------------------------EKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH--RMAEvYELSDRVSVLRDGQYVGS 223
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqRLLD-YIKPDRVHVLYDGRIVKS 186
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-221 |
2.62e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.60 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG--AYTATSGEILIDGkpfhirtpKDALS--------AGITLIYQEMQ 91
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDG--------EDILElspderarAGIFLAFQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 92 LAPNLSVAEniFLGSELS--HGGLVQRKEMLVQAQKVIDRLGaqfnasdkvMTLTIA-----------EQQQVEIARALH 158
Cdd:COG0396 88 EIPGVSVSN--FLRTALNarRGEELSAREFLKLLKEKMKELG---------LDEDFLdryvnegfsggEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 159 RNSRILVMDEPTA-----ALSsrethRLFELIMRLRDEGMAIIYISH--RMAEvYELSDRVSVLRDGQYV 221
Cdd:COG0396 157 LEPKLAILDETDSgldidALR-----IVAEGVNKLRSPDRGILIITHyqRILD-YIKPDFVHVLVDGRIV 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-215 |
4.09e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 102.36 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPkDALSAGI 83
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNlSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNS 161
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 162 RILVMDEPTAALsSRETHRLFELIMRLRDEGMAIIYISHRMAeVYELSDRVSVL 215
Cdd:TIGR02857 478 PLLLLDEPTAHL-DAETEAEVLEALRALAQGRTVLLVTHRLA-LAALADRIVVL 529
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-236 |
4.73e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.79 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK-----PFHIRtpkdAL 79
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlPMHKR----AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 80 sAGITLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLvqaqkviDRLGAQFN----ASDKVMTLTIAEQQQVEIAR 155
Cdd:COG1137 78 -LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERL-------EELLEEFGithlRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 156 ALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELV 235
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLV 229
|
.
gi 13364550 236 R 236
Cdd:COG1137 230 R 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-219 |
5.27e-23 |
|
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: 95.84 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPKDALSAGITLIYQEMQLApNLSVAE 100
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP--VSDLEKALSSLISVLNQRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NifLGSELSHGglvqrkemlvqaqkvidrlgaqfnasdkvmtltiaEQQQVEIARALHRNSRILVMDEPTAALSSRETHR 180
Cdd:cd03247 94 N--LGRRFSGG-----------------------------------ERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 13364550 181 LFELIMRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:cd03247 137 LLSLIFEVL-KDKTLIWITHHLTGI-EHMDKILFLENGK 173
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-219 |
6.95e-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: 97.12 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAF------GK-FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDgkpfHIRTPK 76
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR----HDGGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 77 DALSAG-ITLIY----------QEMQLAPNLS----VAENIflgseLSHGglVQRKEMLVQAQKVIDRLgaqfNASDKVM 141
Cdd:COG4778 78 DLAQASpREILAlrrrtigyvsQFLRVIPRVSaldvVAEPL-----LERG--VDREEARARARELLARL----NLPERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 142 TLTIA-----EQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLR 216
Cdd:COG4778 147 DLPPAtfsggEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 13364550 217 DGQ 219
Cdd:COG4778 227 PFS 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-219 |
8.33e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.77 E-value: 8.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFG----KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHI--RT 74
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 75 PKDALSA-GITLIYQEMQLAPNLSVAENI----FLGSELSHGGLVQRKEMLVQA--QKVIDRLGAQfnasdkvmtLTIAE 147
Cdd:PRK10584 81 ARAKLRAkHVGFVFQSFMLIPTLNALENVelpaLLRGESSRQSRNGAKALLEQLglGKRLDHLPAQ---------LSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 148 QQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRmAEVYELSDRVSVLRDGQ 219
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
275-475 |
8.51e-23 |
|
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: 97.42 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGfltenRKEQ--GLFLEMAAAE 352
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIA-----RTFQnpRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NITMATLERDAR--WGMLNR--------KKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:COG0411 99 NVLVAAHARLGRglLAALLRlprarreeREARERAEELLERVGLA-DRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 423 EPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
9.44e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.44 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLeMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDgkpfhiRTPKDALSAGI 83
Cdd:PRK11247 11 TPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG------TAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLGselshgglvQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLG---------LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
275-470 |
1.22e-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: 96.06 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPReaidlgIGFLTENRKEQGLFleMAAAENI 354
Cdd:cd03235 19 SFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVPQRRSIDRDF--PISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLNRKKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03235 91 VLMGLYGHKGLFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 13364550 435 EIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVM 470
Cdd:cd03235 170 DIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-219 |
2.21e-22 |
|
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: 95.62 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKdALSAGITLIYQEMQLAPNlSVAEN 101
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK-YLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGSELSHGGLVQRKEMLVQAQKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSrETH 179
Cdd:cd03248 108 IAYGLQSCSFECVKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA-ESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13364550 180 RLFELIMRLRDEGMAIIYISHRMAEVyELSDRVSVLRDGQ 219
Cdd:cd03248 187 QQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-475 |
2.81e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFGKFYALK----GVDLTVYPGEIHALMGENGAGKS-TLMKVL----AGAYTATSGEILIDGKPF-- 70
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRtvvnDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESLlh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 71 -------HIRTPKdalsagITLIYQE--MQLAPNLSVAENifLGSELS-HGGLVQ---RKEMLvqaqKVIDRLG---AQF 134
Cdd:PRK15134 81 aseqtlrGVRGNK------IAMIFQEpmVSLNPLHTLEKQ--LYEVLSlHRGMRReaaRGEIL----NCLDRVGirqAAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 135 NASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVS 213
Cdd:PRK15134 149 RLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 214 VLRDGQYV-------------GSLTRDNLNA---GELVRMMVGR-PLSDLFNKERDIPLGK---ARLNVHHLTdggkVQP 273
Cdd:PRK15134 229 VMQNGRCVeqnraatlfsaptHPYTQKLLNSepsGDPVPLPEPAsPLLDVEQLQVAFPIRKgilKRTVDHNVV----VKN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 274 SSLLVRSGEIVGLAGLVGAGRS----ELAQLIfgvrkATGGMIEVDGEPVVIHSPREaidlgigFLTENRKEQGLFLEMA 349
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSttglALLRLI-----NSQGEIWFDGQPLHNLNRRQ-------LLPVRHRIQVVFQDPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 350 AAENITMATLERDARWGMLNRKK--AQTISDDAIKLLNIRVPHAQVR---AGGLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:PRK15134 373 SSLNPRLNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLDPETRhryPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 425 ARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-221 |
2.97e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVL-----AGAYTATSGEILIDGKPFHI-RTPK 76
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSpRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 77 DALSAGITLIYQEmqlaPN---LSVAENIFLGSELSHgglVQRKEMLVQA-----------QKVIDRLgaqfnaSDKVMT 142
Cdd:PRK14239 82 VDLRKEIGMVFQQ----PNpfpMSIYENVVYGLRLKG---IKDKQVLDEAvekslkgasiwDEVKDRL------HDSALG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 143 LTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-233 |
3.56e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.18 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPF----HirtpkDALSAGITLIYQEMQLApNLS 97
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqydH-----HYLHRQVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 98 VAENIFLGSELSHGGLVQRKEMLVQAQKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS 175
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 176 RETHRLFELIMRlrdEGMAIIYISHRMAEVyELSDRVSVLRDGQYVGSLTRDNLNAGE 233
Cdd:TIGR00958 651 ECEQLLQESRSR---ASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-221 |
4.04e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 99.49 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAF-----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILID-GKPFHIRTPKDA 78
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 LSAG-----ITLIYQEMQLAPNLSVAENIF--LGSELSHgGLVQRKEMLV---------QAQKVIDRLGAQfnasdkvmt 142
Cdd:TIGR03269 358 DGRGrakryIGILHQEYDLYPHRTVLDNLTeaIGLELPD-ELARMKAVITlkmvgfdeeKAEEILDKYPDE--------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 143 LTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
275-476 |
4.22e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 95.16 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPReaidlgIGFLtenrkEQglFLEMAAAENI 354
Cdd:COG1121 26 SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------IGYV-----PQ--RAEVDWDFPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 T---MATLERDARWGMLNR--KKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:COG1121 93 TvrdVVLMGRYGRRGLFRRpsRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 430 VGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:COG1121 172 AATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-219 |
4.94e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 94.52 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 17 GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhirTPKDALSAGitliyqemqLAPNL 96
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV----SSLLGLGGG---------FNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 97 SVAENIFLGSELsHGglVQRKEMlvqaQKVIDR------LGAQFNasDKVMTLTIAEQQQVEIARALHRNSRILVMDEPT 170
Cdd:cd03220 100 TGRENIYLNGRL-LG--LSRKEI----DEKIDEiiefseLGDFID--LPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 171 AALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-218 |
7.82e-22 |
|
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: 94.32 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK-PFhirTPKDALSAGITLIY-QEMQLAPNLSV 98
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPW---KRRKKFLRRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENIFLGSE---LSHGGLVQRKEMLVQAQKVIDRLGAQfnasdkVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS 175
Cdd:cd03267 113 IDSFYLLAAiydLPPARFKKRLDELSELLDLEELLDTP------VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 176 RETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:cd03267 187 VAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
280-477 |
9.44e-22 |
|
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: 93.51 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 280 SGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGepVVIHSPREAIDL-----GIGFLTENrkeQGLFLEMAAAENI 354
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKINLppqqrKIGLVFQQ---YALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAtLERDARWGMLNRKKAQTISDDAIKLLNIRVphaqvraGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03297 97 AFG-LKRKRNREDRISVDELLDLLGLDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 435 EIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVMREGSIAG 477
Cdd:cd03297 169 QLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
275-473 |
1.04e-21 |
|
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: 93.11 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIhSPREAIdlgiGFLTEnrkEQGLFLEMAAAEN- 353
Cdd:cd03269 20 SFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-AARNRI----GYLPE---ERGLYPKMKVIDQl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 ITMATLErdarwGMlNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAK 433
Cdd:cd03269 92 VYLAQLK-----GL-KKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13364550 434 SEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:cd03269 165 ELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-214 |
1.20e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 95.57 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAF-----------GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKP 69
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 70 FHIRTPKD--ALSAGITLIYQEMQ--LAPNLSVAENIflGSELSHGGLVQRKEMLVQAQKVIDRLG----------AQFN 135
Cdd:COG4608 82 ITGLSGRElrPLRRRMQMVFQDPYasLNPRMTVGDII--AEPLRIHGLASKAERRERVAELLELVGlrpehadrypHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 136 AsdkvmtltiAEQQQVEIARALHRNSRILVMDEPTAALS-SRETHRLfELIMRLRDE-GMAIIYISHRMAEVYELSDRVS 213
Cdd:COG4608 160 G---------GQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQVL-NLLEDLQDElGLTYLFISHDLSVVRHISDRVA 229
|
.
gi 13364550 214 V 214
Cdd:COG4608 230 V 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-219 |
1.24e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.49 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 26 DLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfHIRTPKDalSAGITLIYQEMQLAPNLSVAENIFLG 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPS--RRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 106 selSHGGL----VQRKEMLVQAQKV-----IDRLGAQfnasdkvmtLTIAEQQQVEIARALHRNSRILVMDEPTAALSSR 176
Cdd:PRK10771 96 ---LNPGLklnaAQREKLHAIARQMgiedlLARLPGQ---------LSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 177 ETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK10771 164 LRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-221 |
1.27e-21 |
|
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: 93.45 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpFHIRTPK-DALSAGITLIYQEMQLApNLSVA 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDVRDYTlASLRRQIGLVSQDVFLF-NDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHGGLVQRKEMLVQAQKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRE 177
Cdd:cd03251 94 ENIAYGRPGATREEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 178 THRLFELIMRLRdEGMAIIYISHRMAEVyELSDRVSVLRDGQYV 221
Cdd:cd03251 174 ERLVQAALERLM-KNRTTFVIAHRLSTI-ENADRIVVLEDGKIV 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-221 |
1.35e-21 |
|
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: 93.45 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFG-KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPK-DALSAGIT 84
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD--IREVTlDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQEMQLApNLSVAENIflgselSHGGLVQRKEMLVQAQKVidrlgAQFNasDKVMTL-----TI----------AEQQ 149
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNI------RYGRPDATDEEVIEAAKA-----AQIH--DKIMRFpdgydTIvgerglklsgGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 150 QVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRdEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-271 |
1.38e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.70 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 20 YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAGITLIYQEmqlaPN---- 95
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVFQN----PDnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 96 -LSVAENIFLGSElSHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALS 174
Cdd:PRK13635 96 gATVQDDVAFGLE-NIG--VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 175 SRETHRLFELIMRLRDEGMA-IIYISHRMAEVYElSDRVSVLRDGQYVGSLTRDNL--NAGELVRMMVGRP----LSDLF 247
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGItVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfkSGHMLQEIGLDVPfsvkLKELL 251
|
250 260
....*....|....*....|....
gi 13364550 248 nKERDIPLGKArlnvhHLTDGGKV 271
Cdd:PRK13635 252 -KRNGILLPNT-----YLTMESLV 269
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-200 |
1.59e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDA-----LSA 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDkaireLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQEMQLAPNLSVAENIF------LGselshgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIAR 155
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIeapcrvLG--------LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 156 ALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH 200
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-221 |
1.65e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.64 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpfhirtpKD--ALSA 81
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG--------QDltALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 G--------ITLIYQEMQLAPNLSVAENIFLGSELSHgglVQRKEMlvqAQKV---IDRLGaqfnASDKVMT----LTIA 146
Cdd:PRK11153 75 KelrkarrqIGMIFQHFNLLSSRTVFDNVALPLELAG---TPKAEI---KARVtelLELVG----LSDKADRypaqLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 147 EQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-221 |
1.67e-21 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 94.12 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTAT--------SGEILIDGKPFHiRTPKDALSAGITLIYQEMQLA 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLA-AIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 94 PNLSVAENIFLG--SELSHGGLVQRKEMLVqAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARAL---------HRNSR 162
Cdd:PRK13547 96 FAFSAREIVLLGryPHARRAGALTHRDGEI-AWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
275-475 |
2.11e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 92.32 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIdlgiGFLTENRKEQgLFlemaaaeni 354
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI----GYVMQDVDYQ-LF--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tMATLERDARWGMLNRKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:cd03226 86 -TDSVREELLLGLKELDAGNEQAETVLKDLDLyalkeRHPLS------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13364550 430 VGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-218 |
2.21e-21 |
|
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: 92.91 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDalsagiTLIYQEMQLAPNLSVAEN 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR------MVVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLG--SELSHGGLVQRKEMLVQAqkvIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETH 179
Cdd:TIGR01184 75 IALAvdRVLPDLSKSERRAIVEEH---IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13364550 180 RLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:TIGR01184 152 NLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
275-479 |
2.27e-21 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 92.53 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPreaiDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:cd03293 24 SLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRGYVF-----QQDALLPWLTVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAtLERdARWGmlnRKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:cd03293 95 ALG-LEL-QGVP---KAEARERAEELLELVGLsgfenAYPHQ------LSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 430 VGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVM--REGSIAGEL 479
Cdd:cd03293 164 ALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEV 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-236 |
2.48e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKdALSAGITLI 86
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR-QLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSE--LSH-GGLVQRKEMLVQ---AQKVIDRLgaqfnASDKVMTLTIAEQQQVEIARALHRN 160
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSpwLSLwGRLSAEDNARVNqamEQTRINHL-----ADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 161 SRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVR 236
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLR 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-221 |
3.21e-21 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 92.78 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG--AYTATSGEILIDGKPFHIRTPKDA 78
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 LSAGITLIYQEMQLAPNLSVAEniFL----GSELSHGGLVQRK-----EMLVQAQKVIDrLGAQFNASDKVMTLTIAEQQ 149
Cdd:CHL00131 82 AHLGIFLAFQYPIEIPGVSNAD--FLrlayNSKRKFQGLPELDpleflEIINEKLKLVG-MDPSFLSRNVNEGFSGGEKK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 150 QVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH--RMAEvYELSDRVSVLRDGQYV 221
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLD-YIKPDYVHVMQNGKII 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-221 |
3.32e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 93.07 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKP----------- 69
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 70 ----FHIRT--------PKDALsagitliyqEMQLAPNLSVAENIFLGSELSHGGLvqRKEMLVQAQKV------IDRLG 131
Cdd:PRK11701 81 aerrRLLRTewgfvhqhPRDGL---------RMQVSAGGNIGERLMAVGARHYGDI--RATAGDWLERVeidaarIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 132 AQFNASdkvMtltiaeQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSD 210
Cdd:PRK11701 150 TTFSGG---M------QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAH 220
|
250
....*....|.
gi 13364550 211 RVSVLRDGQYV 221
Cdd:PRK11701 221 RLLVMKQGRVV 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
275-475 |
4.63e-21 |
|
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: 92.02 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlGIGFLTENrkeQGLFLEMAAAENI 354
Cdd:cd03296 22 SLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFVFQH---YALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TmatlerdarWGMLNRKKAQTISDDAIK-----LLNI--------RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLL 421
Cdd:cd03296 96 A---------FGLRVKPRSERPPEAEIRakvheLLKLvqldwladRYPAQ------LSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 422 DEPARGVDVGAKSEIYRIMNEMA-RKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-231 |
5.01e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpFHIRT-PKDALSAGITL 85
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTvTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQEMQLApNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDR--LGAQFNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRLRdEGMAIIYISHRMAEVYElSDRVSVLRDGQYVGSLTRDNLNA 231
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVA 558
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
275-476 |
5.81e-21 |
|
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: 91.04 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlGIGFLTENRkeqGLFLEMAAAENI 354
Cdd:cd03259 20 SLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMVFQDY---ALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAtLERdarwGMLNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03259 94 AFG-LKL----RGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLRE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 435 EIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:cd03259 168 ELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
260-475 |
8.19e-21 |
|
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: 91.03 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 260 LNVHHLTDGGK---VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGigflt 336
Cdd:cd03257 7 LSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 337 enRKEQGLFLEMAAAENITM----ATLERDARWGMLNRKKAQTIsddAIKLLNIRVPHAQVRAG----GLSGGNQQKLLI 408
Cdd:cd03257 82 --KEIQMVFQDPMSSLNPRMtigeQIAEPLRIHGKLSKKEARKE---AVLLLLVGVGLPEEVLNryphELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 409 SRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-229 |
8.59e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 91.39 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 20 YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPkDALSAGITLIYQEMQLApNLSVA 99
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNA--SDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSrE 177
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY-E 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 178 THRLFELIMRLRDEGMAIIYISHRMAEVyELSDRVSVLRDGQYVGSLTRDNL 229
Cdd:cd03252 173 SEHAIMRNMHDICAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-256 |
8.96e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 8.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFY-ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPKDAL----- 79
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP--IKYDKKSLlevrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 80 SAGITLIYQEMQL-APnlSVAENIFLGSeLSHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALH 158
Cdd:PRK13639 79 TVGIVFQNPDDQLfAP--TVEEDVAFGP-LNLG--LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 159 RNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLT-RDNLNAGELVRM 237
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTpKEVFSDIETIRK 233
|
250 260
....*....|....*....|....
gi 13364550 238 MVGR-----PLSDLFNKERDIPLG 256
Cdd:PRK13639 234 ANLRlprvaHLIEILNKEDNLPIK 257
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-219 |
9.07e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.00 E-value: 9.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSG-----EILIDGKPFHIRTPKDALS 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 --AGITLIYQEMQLAPNLSVAENIFLGSE---------LSHGGLVQRKEMLvqaqKVIDRLGAQFNASDKVMTLTIAEQQ 149
Cdd:PRK09984 84 srANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRAL----QALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 150 QVEIARALHRNSRILVMDEPTAALSSrETHRLfeLIMRLRD----EGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDP-ESARI--VMDTLRDinqnDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
275-475 |
9.91e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.24 E-value: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVV---IHspREAIdLGIGFLTEnrkEQGLFLEMAAA 351
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpMH--KRAR-LGIGYLPQ---EASIFRKLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 ENItMATLERdarwGMLNRKKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:COG1137 97 DNI-LAVLEL----RKLSKKEREERLEELLEEFGI-THLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 432 AKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG1137 171 AVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-218 |
1.01e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhirTPKDALSA- 81
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP----VPARARLAr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 -GITLIYQEMQLAPNLSVAENIFLGSElsHGGLVQRK-EMLVQAQKVIDRLGAQFNAsdKVMTLTIAEQQQVEIARALHR 159
Cdd:PRK13536 114 aRIGVVPQFDNLDLEFTVRENLLVFGR--YFGMSTREiEAVIPSLLEFARLESKADA--RVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-226 |
1.27e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.46 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK-PFHIRTpkdALSAGITLIY-QEMQLAPNLSV 98
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKRRK---EFARRIGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENIFLGSELsHGglVQRKEmlvqAQKVIDRLGAQFNASDK----VMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL- 173
Cdd:COG4586 114 IDSFRLLKAI-YR--IPDAE----YKKRLDELVELLDLGELldtpVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLd 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 174 -SSRETHRlfELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ--YVGSLTR 226
Cdd:COG4586 187 vVSKEAIR--EFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRiiYDGSLEE 241
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-219 |
1.36e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 94.81 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIYQEMQLAPNlSVAEN 101
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS-QWDREELGRHIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 I--FLGselshgglvqrkemlVQAQKVID--------------------RLGAQfnasdkVMTLTIAEQQQVEIARALHR 159
Cdd:COG4618 426 IarFGD---------------ADPEKVVAaaklagvhemilrlpdgydtRIGEG------GARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAeVYELSDRVSVLRDGQ 219
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGR 543
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-225 |
1.37e-20 |
|
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: 95.85 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKF--YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfHIRTPKDALSAG 82
Cdd:TIGR01257 927 PGVCVKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGSELSHGglvQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGR---SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLRdEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLT 225
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-236 |
2.21e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.34 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK-----PFHIRTPKdals 80
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 aGITLIYQEMQLAPNLSVAENIFlgselshgGLVQRKEMLVQAQKV--IDRLGAQFNAS---DKV-MTLTIAEQQQVEIA 154
Cdd:PRK10895 79 -GIGYLPQEASIFRRLSVYDNLM--------AVLQIRDDLSAEQREdrANELMEEFHIEhlrDSMgQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 155 RALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGEL 234
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
..
gi 13364550 235 VR 236
Cdd:PRK10895 230 VK 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
275-473 |
2.96e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 88.01 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSP-REAIDLGIGFLTEnrkEQGLFLEMAAAEN 353
Cdd:cd03229 20 SLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDeLPPLRRRIGMVFQ---DFALFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 ITMatlerdarwgmlnrkkaqtisddaikllnirvphaqvragGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAK 433
Cdd:cd03229 97 IAL----------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13364550 434 SEIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:cd03229 137 REVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-221 |
3.15e-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: 93.60 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAF-----------GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAyTATSGEILIDGKPF 70
Cdd:COG4172 271 DAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 71 HIRTPKDALSagitlIYQEMQ---------LAPNLSVAENIFLGSELSHGGL--VQRKEMLVQA-QKV------IDRL-- 130
Cdd:COG4172 350 DGLSRRALRP-----LRRRMQvvfqdpfgsLSPRMTVGQIIAEGLRVHGPGLsaAERRARVAEAlEEVgldpaaRHRYph 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 131 ---GAQfnasdkvmtltiaeQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVY 206
Cdd:COG4172 425 efsGGQ--------------RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVR 490
|
250
....*....|....*
gi 13364550 207 ELSDRVSVLRDGQYV 221
Cdd:COG4172 491 ALAHRVMVMKDGKVV 505
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-243 |
7.44e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 9 MRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDalsAGITLIYQ 88
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 89 EMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIdRLGAQFNASDKvmTLTIAEQQQVEIARALHRNSRILVMDE 168
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVL-QLAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 169 P----TAALSSRETHRLFELIMRLrdeGMAIIYISHRMAEVYELSDRVSVlrdgqyvgsltrdnLNAGELVRmmVGRPL 243
Cdd:PRK11000 160 PlsnlDAALRVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVV--------------LDAGRVAQ--VGKPL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
275-475 |
8.35e-20 |
|
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: 87.95 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvIHSPREAIDLGIGFLTENRkeqGLFLEMAAAENI 354
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS--IRTDRKAARQSLGYCPQFD---ALFDELTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 T-MATLerdarWGmLNRKKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKLLisrwVAI----GPRILLLDEPARGVD 429
Cdd:cd03263 97 RfYARL-----KG-LPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLS----LAIaligGPSVLLLDEPTSGLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13364550 430 VGAKSEIYRIMNEMaRKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03263 166 PASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-243 |
1.05e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKdALSAGITLIYQEMQLAPNLSVAEN 101
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGSELSHGGLVQ-RKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHR 180
Cdd:PRK10575 106 VAIGRYPWHGALGRfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 181 LFELIMRL-RDEGMAIIYISH--RMAEVYelSDRVSVLRDGQYVGSLTRDNLNAGELVRMMVGRPL 243
Cdd:PRK10575 186 VLALVHRLsQERGLTVIAVLHdiNMAARY--CDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPM 249
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
261-473 |
1.23e-19 |
|
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: 85.76 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 261 NVHHLTDGGKV-QPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDlGIGFLTEnr 339
Cdd:cd00267 4 NLSFRYGGRTAlDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 340 keqglflemaaaenitmatlerdarwgmlnrkkaqtisddaikllnirvphaqvraggLSGGNQQKLLISRWVAIGPRIL 419
Cdd:cd00267 81 ----------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 420 LLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-219 |
1.29e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.60 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGK-----FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK-----PFHIRtpk 76
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklPEYKR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 77 dalSAGITLIYQEMQL--APNLSVAENIFLGSE------LSHGGLVQRKEMLVQAQKVI-----DRLGaqfnasDKVMTL 143
Cdd:COG1101 79 ---AKYIGRVFQDPMMgtAPSMTIEENLALAYRrgkrrgLRRGLTKKRRELFRELLATLglgleNRLD------TKVGLL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 144 TIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-229 |
1.53e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.58 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRN----IAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGA----YTATSGEILIDGKPFHIRTPK 76
Cdd:COG4170 2 PLLDIRNltieIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 77 D---ALSAGITLIYQEMQ--LAPNLSV----AENI----FLGSELSHggLVQRKEmlvQAQKVIDRLGAQfnASDKVMT- 142
Cdd:COG4170 82 ErrkIIGREIAMIFQEPSscLDPSAKIgdqlIEAIpswtFKGKWWQR--FKWRKK---RAIELLHRVGIK--DHKDIMNs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 143 ----LTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRD 217
Cdd:COG4170 155 ypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYC 234
|
250
....*....|..
gi 13364550 218 GQYVGSLTRDNL 229
Cdd:COG4170 235 GQTVESGPTEQI 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
275-476 |
1.92e-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: 87.14 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPreaiDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP----DRMVVF-----QNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATlerDARWGMLNRKKAQTISDDAIKLLNIRvpHAQ-VRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAK 433
Cdd:TIGR01184 76 ALAV---DRVLPDLSKSERRAIVEEHIALVGLT--EAAdKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 434 SEIY-RIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:TIGR01184 151 GNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAA 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-170 |
2.18e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 9 MRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpfhirtpkdalsaGITLIY- 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLRIGYl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 88 -QEMQLAPNLSVAENIFLG-SELSHggLVQRKEMLVQA-------QKVIDRLGAQFNASD---------KVMT---LTIA 146
Cdd:COG0488 67 pQEPPLDDDLTVLDTVLDGdAELRA--LEAELEELEAKlaepdedLERLAELQEEFEALGgweaearaeEILSglgFPEE 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 13364550 147 EQQQ------------VEIARALHRNSRILVMDEPT 170
Cdd:COG0488 145 DLDRpvselsggwrrrVALARALLSEPDLLLLDEPT 180
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-221 |
3.24e-19 |
|
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: 86.56 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG---AYTATSGEILIDGKPFHIRTPKDALSagitLIYQEMQLAPNLSV 98
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQKCVA----YVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AE-----NIFLGSELSHGGlvqRKEMLVqAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:cd03234 99 REtltytAILRLPRKSSDA---IRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 174 SSRETHRLFELIMRLRDEGMAIIYISHR-MAEVYELSDRVSVLRDGQYV 221
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
275-475 |
3.97e-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: 86.24 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlGIGFLTENrkeQGLFLEMAAAENI 354
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYVPQN---YALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERdarwgMLNRKKAQTISDDAIKLLNIRvpHAQVR-AGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAK 433
Cdd:cd03299 93 AYGLKKR-----KVDKKEIERKVLEIAEMLGID--HLLNRkPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 434 SEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03299 166 EKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-221 |
4.45e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATS-----GEILIDG-KPFH-----IRtp 75
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTaRSLSqqkglIR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 76 kdALSAGITLIYQEMQLAPNLSVAENIFLGSELSHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIAR 155
Cdd:PRK11264 82 --QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 156 ALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-204 |
5.20e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPkdalSAGITLI 86
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGP----GAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQfnaSDKVMTLTIAEQQQVEIARALHRNSRILVM 166
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAE---KRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 13364550 167 DEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAE 204
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEE 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-219 |
6.98e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpFHIRTPKDALS-----AGITLIYQEMQLAPN 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKLSdirkkVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 96 lSVAENIFLGseLSHGGLVQrKEMLVQAQKVIDRLGAQFNA-SDKV-MTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:PRK13637 100 -TIEKDIAFG--PINLGLSE-EEIENRVKRAMNIVGLDYEDyKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 174 SSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-218 |
8.38e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 8.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDA-------- 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 ----LSAGITLIYQEMQLAPNLSVAENIfLGSELSHGGLvQRKEMLVQAQKVIDRLGAQFNASDKV-MTLTIAEQQQVEI 153
Cdd:PRK10619 86 qlrlLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGL-SKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 154 ARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
275-473 |
1.11e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.43 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTENRKeqgLFLEMAAAENI 354
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVR---LFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAT---LERDARWGMLN----RKKAQTISDDAIKLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:PRK11300 102 LVAQhqqLKTGLFSGLLKtpafRRAESEALDRAATWLE-RVgllEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 425 ARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-221 |
1.36e-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: 84.47 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRT-PKDALSAGITLIYQEmqlaPNL--- 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVD--ISKiGLHDLRSRISIIPQD----PVLfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 97 SVAENIFLGSELShgglvqrKEMLVQA-QKV--IDRLGAQFNASDKVMT-----LTIAEQQQVEIARALHRNSRILVMDE 168
Cdd:cd03244 93 TIRSNLDPFGEYS-------DEELWQAlERVglKEFVESLPGGLDTVVEeggenLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 169 PTAALSSRETHRLFELImRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:cd03244 166 ATASVDPETDALIQKTI-REAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-218 |
1.41e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKP---FHIRTPKdalsagI 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDvsrLHARDRK------V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLG------SELSHGGLVQRKEM----LVQAQKVIDRLGAQFNASDKvmtltiaeqQQVEI 153
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGltvlprRERPNAAAIKAKVTqlleMVQLAHLADRYPAQLSGGQK---------QRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 154 ARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDG 218
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-221 |
1.57e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHI-----RTPKDALSAGITLIYQEMQLAPNL 96
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 97 SVAENIflGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMT----LTIAEQQQVEIARALHRNSRILVMDEPTAA 172
Cdd:PRK14246 106 SIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 173 LSSRETHRLFELIMRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-173 |
1.72e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTA---TSGEILIDGKPfhiRTPKDALSAGITLIYQEMQLAPNLSV 98
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRR---LTALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 99 AENIFLGseLSHGglVQRKEMLVQAQKVIDRLG-AQFNASDkVMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:COG4136 94 GENLAFA--LPPT--IGRAQRRARVEQALEEAGlAGFADRD-PATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
282-478 |
2.06e-18 |
|
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: 86.70 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 282 EIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEpvVIHSPREAIDLGigflTENRK------EQGLFLEMAAAENIt 355
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR--TLFDSRKGIFLP----PEKRRigyvfqEARLFPHLSVRGNL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 356 matlerdaRWGMLN-RKKAQTISDDAI-KLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAK 433
Cdd:TIGR02142 97 --------RYGMKRaRPSERRISFERViELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13364550 434 SEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:TIGR02142 168 YEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-219 |
2.19e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.06 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPF-HIRTPKDALSAGITLIYQEmqlaPNlsvaE 100
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdYSKRGLLALRQQVATVFQD----PE----Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIF-------LGSELSHGGlVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:PRK13638 89 QIFytdidsdIAFSLRNLG-VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13364550 174 SSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-238 |
2.79e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.54 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTL-MKVLAGAY-TATSGEILIDGKPFHIRTPKDALSAGITLIYQE-MQLAPNL-- 96
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDrKGYGLNLid 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 97 SVAENIFLGS--ELSHGGLV-QRKEMLVqAQKVIDRLGAQ-FNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAA 172
Cdd:NF040905 356 DIKRNITLANlgKVSRRGVIdENEEIKV-AEEYRKKMNIKtPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRG 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 173 LSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMM 238
Cdd:NF040905 435 IDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-224 |
3.08e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.12 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVL-----AGAYTATSGEILIDGKpfHIRTPK-DALS 80
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGR--NIYSPDvDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 A--GITLIYQEMQLAPNLSVAENIFLGSELShgGLVQRKEMLVQA-----------QKVIDRLgaqfnaSDKVMTLTIAE 147
Cdd:PRK14267 83 VrrEVGMVFQYPNPFPHLTIYDNVAIGVKLN--GLVKSKKELDERvewalkkaalwDEVKDRL------NDYPSNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 148 QQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEgMAIIYISHRMAEVYELSDRVSVLrdgqYVGSL 224
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFL----YLGKL 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
275-475 |
3.76e-18 |
|
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: 83.31 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfLTENRKEQ--------GLFL 346
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE--------LAAFRRRHigfvfqsfNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 347 EMAAAENITMAtlerdarwGMLNRKKAQTISDDAIKLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:cd03255 96 DLTALENVELP--------LLLAGVPKKERRERAEELLE-RVglgDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 424 PARGVDVGAKSEIYRIMNEMARK-GVAILMISSElPEIVGMSDRVYVMREGSI 475
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
258-475 |
4.20e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.79 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 258 ARLNVHHLTDGGK----VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIG 333
Cdd:PRK10895 2 ATLTAKNLAKAYKgrrvVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 334 FLTEnrkEQGLFLEMAAAENItMATLE-RDArwgmLNRKKAQTISDDAIKLLNIRvpHAQVRAG-GLSGGNQQKLLISRW 411
Cdd:PRK10895 82 YLPQ---EASIFRRLSVYDNL-MAVLQiRDD----LSAEQREDRANELMEEFHIE--HLRDSMGqSLSGGERRRVEIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 412 VAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
271-424 |
4.74e-18 |
|
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: 80.77 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAIDLGIGFLTENRkeqGLFLEMAA 350
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDP---QLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 351 AENITMATLErdarWGMLNRKKAQTIsDDAIKLLNIRVPHAQV---RAGGLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:pfam00005 77 RENLRLGLLL----KGLSKREKDARA-EEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-221 |
4.77e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.07 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAF----GKFY-----ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIrTPK 76
Cdd:PRK15112 4 LLEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF-GDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 77 DALSAGITLIYQE--MQLAPNLSVAE----NIFLGSELSHgglVQRKEMLVQAQKVIDRLGAqfNASDKVMTLTIAEQQQ 150
Cdd:PRK15112 83 SYRSQRIRMIFQDpsTSLNPRQRISQildfPLRLNTDLEP---EQREKQIIETLRQVGLLPD--HASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-247 |
4.85e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.15 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFGKFY--ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfhirtpkdAL 79
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK---------SI 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 80 SAGITLIYQEMQLAPNLSVAENIFLGSElsHGGLVQR------KEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEI 153
Cdd:TIGR01257 2004 LTNISDVHQNMGYCPQFDAIDDLLTGRE--HLYLYARlrgvpaEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLST 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 154 ARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDG--QYVGSLT--RDNL 229
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafQCLGTIQhlKSKF 2161
|
250
....*....|....*...
gi 13364550 230 NAGELVRMMVGRPLSDLF 247
Cdd:TIGR01257 2162 GDGYIVTMKIKSPKDDLL 2179
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-225 |
6.17e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEIlidgkpfhirtpkdALSAGIT 84
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------------KLGETVK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIY--QEM-QLAPNLSVAENIflgSELSHGGlvqrkemlvQAQKVIDRLGAqFN-----ASDKVMTLTIAEQQQVEIARA 156
Cdd:COG0488 380 IGYfdQHQeELDPDKTVLDEL---RDGAPGG---------TEQEVRGYLGR-FLfsgddAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 157 LHRNSRILVMDEPTAAL--SSREthrlfELIMRLRD-EGmAIIYISHRMAEVYELSDRVSVLRDGQ---YVGSLT 225
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLdiETLE-----ALEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGvreYPGGYD 515
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
275-478 |
6.27e-18 |
|
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: 82.26 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVihspREAIDLG-IGFLTEnrkEQGLFLEMAAAEN 353
Cdd:cd03268 20 SLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEALRrIGALIE---APGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 itmatLERDARWGMLNRKKAqtisDDAIKLLNIRVpHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAK 433
Cdd:cd03268 93 -----LRLLARLLGIRKKRI----DEVLDVVGLKD-SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 434 SEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:cd03268 163 KELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-222 |
8.08e-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: 81.52 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTA--TSGEILIDGKPfhirtPKDALSAGITLIYQEMQLAPNLSVA 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRP-----LDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHGGLVQRKEmlvqaqkvidrlgaqfnasdkvmtLTIAeqqqVEIAralhRNSRILVMDEPTAALSSRETH 179
Cdd:cd03232 98 EALRFSALLRGLSVEQRKR------------------------LTIG----VELA----AKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 180 RLFELIMRLRDEGMAII-YISHRMAEVYELSDRVSVL-RDGQ--YVG 222
Cdd:cd03232 146 NIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLkRGGKtvYFG 192
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
275-478 |
8.65e-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: 82.03 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVihspREAIDLgigfltenRKEQGLFLEMAAAENI 354
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREV--------RRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAT--LERDAR-WGMLNRKKAQTISD--DAIKLLNIRvpHAQVRAggLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:cd03265 88 LTGWenLYIHARlYGVPGAERRERIDEllDFVGLLEAA--DRLVKT--YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 430 VGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-221 |
9.24e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAF-----------GKFYALKGVDLTVYPGEIHALMGENGAGKST----LMKVLagaytATSGEILID 66
Cdd:PRK15134 271 PASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 67 GKPFHIRTPKDAL--SAGITLIYQE--MQLAPNLSVAENIFLGSELSHGGL--VQRKEMLVQAQKVI-------DRLGAQ 133
Cdd:PRK15134 346 GQPLHNLNRRQLLpvRHRIQVVFQDpnSSLNPRLNVLQIIEEGLRVHQPTLsaAQREQQVIAVMEEVgldpetrHRYPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 134 FNAsdkvmtltiAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRV 212
Cdd:PRK15134 426 FSG---------GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQV 496
|
....*....
gi 13364550 213 SVLRDGQYV 221
Cdd:PRK15134 497 IVLRQGEVV 505
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-234 |
1.33e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.99 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKD--ALSAGITLIYQE--MQLAPNL 96
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 97 SVAENI-----FLGSELSHGGLVQR-KEMLVQA---QKVIDRLGAQFNAsdkvmtltiAEQQQVEIARALHRNSRILVMD 167
Cdd:PRK15079 116 TIGEIIaeplrTYHPKLSRQEVKDRvKAMMLKVgllPNLINRYPHEFSG---------GQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 168 EPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLrdgqYVGsltrdnlNAGEL 234
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM----YLG-------HAVEL 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-223 |
1.60e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTA---TSGEILIDGKPFHirtpKDALSAGITLIYQEMQLAPNLSV 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID----AKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQ------FNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAA 172
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcantrIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 173 LSSRETHRLFELIMRLRDEGMAIIYISHR-MAEVYELSDRVSVLRDGQ--YVGS 223
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRvaYLGS 250
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-205 |
1.89e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPkDALS 80
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 AGITLIYQemqlAPNL---SVAENIFLGSELSHgglvQRKEMlvqaQKVIDRLgAQFNASDKVMTLTIA-----EQQQVE 152
Cdd:PRK10247 81 QQVSYCAQ----TPTLfgdTVYDNLIFPWQIRN----QQPDP----AIFLDDL-ERFALPDTILTKNIAelsggEKQRIS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 153 IARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEV 205
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEI 201
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-479 |
2.42e-17 |
|
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: 81.39 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlgigflteNRKEQGLFLEMAAAEN- 353
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF----------RRRVQMVFQDPYASLHp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 -ITMATLERDARWGMLNRKKAQTIsDDAIKLLNI------RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPAR 426
Cdd:COG1124 95 rHTVDRILAEPLRIHGLPDREERI-AELLEQVGLppsfldRYPHQ------LSGGQRQRVAIARALILEPELLLLDEPTS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 427 GVDVGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVMREGSIAGEL 479
Cdd:COG1124 168 ALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
275-495 |
2.95e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTEnrkEQGLFLEMAAAENI 354
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQ---ELSVIDELTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWG--MLNRKKAQTISDDAIKLLNIRVpHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGA 432
Cdd:PRK09700 102 YIGRHLTKKVCGvnIIDWREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 433 KSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQENIMTLATG 495
Cdd:PRK09700 181 VDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
3.18e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 20 YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPF-HIRTPKDALSAGITLIYQ--EMQLApNL 96
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdYSRKGLMKLRESVGMVFQdpDNQLF-SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 97 SVAENIflgselSHGGL---VQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:PRK13636 99 SVYQDV------SFGAVnlkLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 174 SSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
275-475 |
3.88e-17 |
|
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: 80.27 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEpvVIHSPREAIDlgigfltENRKEQG-------LFLE 347
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGL--KLTDDKKNIN-------ELRQKVGmvfqqfnLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENITMATLERdarWGMlNRKKAQTIsddAIKLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:cd03262 91 LTVLENITLAPIKV---KGM-SKAEAEER---ALELLE-KVglaDKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 425 ARGVD---VGaksEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03262 163 TSALDpelVG---EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-229 |
5.38e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.16 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAyTATSGEILIDGKPFH--------I 72
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDdidllrlsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 73 RTPKDALSAGITLIYQEMQ--LAPNLSVAENI--------FLGSELSHGGLVQRKemlvqAQKVIDRLGaqFNASDKVM- 141
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQscLDPSERVGRQLmqnipgwtYKGRWWQRFGWRKRR-----AIELLHRVG--IKDHKDAMr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 142 ----TLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLR 216
Cdd:PRK15093 154 sfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLY 233
|
250
....*....|...
gi 13364550 217 DGQYVGSLTRDNL 229
Cdd:PRK15093 234 CGQTVETAPSKEL 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-229 |
5.68e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 18 KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDG-------KPFHIRTPKDALsaGITLIYQEM 90
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPVRKRI--GMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 91 QLAPNlSVAENIFLGSelshgglvqrKEMLVQAQKVID---RLGAQFNASDKVMTLTI-----AEQQQVEIARALHRNSR 162
Cdd:PRK13646 97 QLFED-TVEREIIFGP----------KNFKMNLDEVKNyahRLLMDLGFSRDVMSQSPfqmsgGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRLR-DEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNL 229
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-221 |
6.07e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVL------AGAYTaTSGEILIDGKPfhIRTPK 76
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYR-YSGDVLLGGRS--IFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 77 DALS--AGITLIYQEMQLAPnLSVAENIFLGSElSHGgLVQRKEMLVQAQKVIDRLG----AQFNASDKVMTLTIAEQQQ 150
Cdd:PRK14271 95 DVLEfrRRVGMLFQRPNPFP-MSIMDNVLAGVR-AHK-LVPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEgMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-229 |
6.36e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDG---KPFHIRTPKDALSAGI 83
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLGSELSHGGLVQRKEmlvQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERRE---KALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 164 LVMDEPTAALSSR-ETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNL 229
Cdd:PRK10070 186 LLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
269-482 |
6.37e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.92 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 269 GKVQP---SSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTENRKeqgLF 345
Cdd:PRK11614 16 GKIQAlheVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 346 LEMAAAENITMATLERDarwgmlnRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:PRK11614 93 SRMTVEENLAMGGFFAE-------RDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 426 RGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGK 482
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGD 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-224 |
6.55e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 6.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDA--LSAG 82
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGSELSHGGLvqrKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSR 162
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASG---DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 163 ILVMDEPTAALS---SRETHRLFELIMRLrdeGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSL 224
Cdd:PRK10908 158 VLLADEPTGNLDdalSEGILRLFEEFNRV---GVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-210 |
6.65e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLaGAYTATSGEILIDGKP-------FHIRTPKD 77
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVeffnqniYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 78 ALSAGITLIYQEMQLAPnLSVAENIFLG-------SELSHGGLVqrkEMLVQAQKVIDRLGAQFNASdkVMTLTIAEQQQ 150
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGvkivgwrPKLEIDDIV---ESALKDADLWDEIKHKIHKS--ALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELI--MRLRDEgMAIIYISHRMAEVYELSD 210
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
275-478 |
8.18e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 79.85 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPRE--AIDLGIGFLTenrkeQG--LFLEMAA 350
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMGMLF-----QSgaLFDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITMATLERdarwGMLNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDV 430
Cdd:cd03261 95 FENVAFPLREH----TRLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 431 GAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:cd03261 170 IASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-231 |
9.61e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIYQEMQLApNLSVAE 100
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAALRQAISVVSQRVHLF-SATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGSE----------LSHGGLvqrkEMLVQAQKVID----RLGAQfnasdkvmtLTIAEQQQVEIARALHRNSRILVM 166
Cdd:PRK11160 433 NLLLAAPnasdealievLQQVGL----EKLLEDDKGLNawlgEGGRQ---------LSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 167 DEPTAALsSRETHRlfeLIMRLRDEGMA---IIYISHRMAEVyELSDRVSVLRDGQYVGSLTRDNLNA 231
Cdd:PRK11160 500 DEPTEGL-DAETER---QILELLAEHAQnktVLMITHRLTGL-EQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
271-475 |
1.26e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.20 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlGIGFLTENrkeQGLFLEMAA 350
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTVFQN---YALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENI----TMATLERDArwgmLNRKKAQTIsdDAIKLLNirvpHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPAR 426
Cdd:cd03300 90 FENIafglRLKKLPKAE----IKERVAEAL--DLVQLEG----YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 427 GVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-224 |
2.42e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.85 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATS--GEILIDGkpfhiRTPKDALSAGITLIYQEMQLAPNLSVA 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN-----RKPTKQILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTI-----AEQQQVEIARALHRNSRILVMDEPTAALS 174
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIrgisgGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 175 SRETHRLFELIMRLRDEGMAIIYISHR-MAEVYELSDRVSVLRDGQ--YVGSL 224
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRclFFGKG 291
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
275-495 |
2.75e-16 |
|
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: 81.41 E-value: 2.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRK--ATGGMIEVDGEPVVIHSPREAIDLGIGFLtenRKEQGLFLEMAAAE 352
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIVII---HQELTLVPELSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NITMATlERDARWGMLNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGA 432
Cdd:TIGR02633 98 NIFLGN-EITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 433 KSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQENIMTLATG 495
Cdd:TIGR02633 177 TEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-244 |
2.82e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 20 YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAGITLIYQEmqlapnlsvA 99
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQN---------P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHG---GL----VQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAA 172
Cdd:PRK13650 91 DNQFVGATVEDDvafGLenkgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 173 LSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVyELSDRVSVLRDGQYVGSLTRDNLNA--GELVRMMVGRPLS 244
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSrgNDLLQLGLDIPFT 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
275-482 |
3.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.94 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVihspreaiDLGIGfLTENRKEQGLFLEMAAAEnI 354
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--------DKKVK-LSDIRKKVGLVFQYPEYQ-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLNRKkaqtISDDAIkllNIRVPHAQVRAG------------GLSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:PRK13637 97 FEETIEKDIAFGPINLG----LSEEEI---ENRVKRAMNIVGldyedykdkspfELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 423 EPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIagELNGK 482
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKC--ELQGT 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-215 |
4.34e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfhIRtpkdalsagI 83
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---LR---------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAENIFLgsELSHGglVQRKEML-----VQAQKVIDRlgaqfnasdKVMTLTIAEQQQVEIARALH 158
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFL--RLRPG--TKKEDILpalkrVQAGHLIDA---------PMQKLSGGETQRVLLARALL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 159 RNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVL 215
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
275-475 |
4.43e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.49 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAID-LGIGFltENRKEQglFLEmaaaen 353
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKkIGIIF--QNPDNQ--FIG------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 itmATLERDARWG----MLNRKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:PRK13632 99 ---ATVEDDIAFGlenkKVPPKKMKDIIDDLAKKVGMedyldKEPQN------LSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 425 ARGVDVGAKSEIYRIMNEMARKGV-AILMISSELPEIVgMSDRVYVMREGSI 475
Cdd:PRK13632 170 TSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-221 |
4.62e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFG-----------KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIR 73
Cdd:PRK10261 312 PILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 74 TPK--DALSAGITLIYQE--MQLAPNLSVAENIFlgSELSHGGLVQRKEMLVQAQKVIDRLGAQ-FNASDKVMTLTIAEQ 148
Cdd:PRK10261 392 SPGklQALRRDIQFIFQDpyASLDPRQTVGDSIM--EPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQR 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 149 QQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-229 |
5.40e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.24 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAgITLIYQEmqlaPN----- 95
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVFQD----PDdqvfs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 96 LSVAENIFLGSElsHGGLvQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS 175
Cdd:PRK13647 95 STVWDDVAFGPV--NMGL-DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 176 RETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS-----LTRDNL 229
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEgdkslLTDEDI 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
275-475 |
6.14e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.97 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVvihSPREAIDLGIGFLTENrkeQGLFLEMAAAENI 354
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQH---YALFRHMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 T--MATLERDarwgmlNRKKAQTISDDAIKLLN-IRVPH-AQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDV 430
Cdd:PRK10851 96 AfgLTVLPRR------ERPNAAAIKAKVTQLLEmVQLAHlADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 431 GAKSEIYR----IMNEMARKGVAILMISSELPEIvgmSDRVYVMREGSI 475
Cdd:PRK10851 170 QVRKELRRwlrqLHEELKFTSVFVTHDQEEAMEV---ADRVVVMSQGNI 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-221 |
7.50e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.15 E-value: 7.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIYQE-MQLAPnlSVAE 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQDpVVLAD--TFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGSELSHGGLVQRKEMLVQAQKVID-------RLGAQFNasdkvmTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSlpdglytPLGEQGN------NLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13364550 174 SSrETHRLFELIMRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:PRK10790 508 DS-GTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
275-478 |
1.00e-15 |
|
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: 77.15 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLgigflteNRKEQGLFLEMAAAENI 354
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAF-------RRDVQLVFQDSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAtlerdARWGM---------LNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:TIGR02769 104 RMT-----VRQIIgeplrhltsLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 426 RGVDVGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-221 |
1.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 36 ALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSA---GITLIYQ--EMQLAPNlSVAENIFLGSeLSH 110
Cdd:PRK13641 37 ALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKlrkKVSLVFQfpEAQLFEN-TVLKDVEFGP-KNF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 111 GglVQRKEMLVQAQKVIDRLGAQFNASDKV-MTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLR 189
Cdd:PRK13641 115 G--FSEDEAKEKALKWLKKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ 192
|
170 180 190
....*....|....*....|....*....|..
gi 13364550 190 DEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13641 193 KAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
275-475 |
1.04e-15 |
|
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: 75.91 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAI-----DLGIGFlTENRkeqgLFLEMA 349
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIpylrrKIGVVF-QDFR----LLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 350 AAENITMAtLERDARWGMLNRKKAQtisdDAIKLLNIRVPHAQVrAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:cd03292 95 VYENVAFA-LEVTGVPPREIRKRVP----AALELVGLSHKHRAL-PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 430 VGAKSEIYRIMNEMARKGVAILMiSSELPEIVG-MSDRVYVMREGSI 475
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVV-ATHAKELVDtTRHRVIALERGKL 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-219 |
1.12e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.38 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 25 VDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpfhiRTPKDAlSAGITL---------IYQEMQLAPN 95
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-----RVLFDA-EKGICLppekrrigyVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 96 LSVAENIFLGselshgglvQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS 175
Cdd:PRK11144 91 YKVRGNLRYG---------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 176 RETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK11144 162 PRKRELLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-223 |
1.17e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.09 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTP-KDALS----AGITLIYQEMQLAPN 95
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQirkkVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 96 lSVAENIFLGSElSHGglVQRKEMLVQAQKVIDRLGAQFNASDK-VMTLTIAEQQQVEIARALHRNSRILVMDEPTAALS 174
Cdd:PRK13649 102 -TVLKDVAFGPQ-NFG--VSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 175 SRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-219 |
1.56e-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: 79.99 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpfhIRTPK---DALSAGITLIYQE--------- 89
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG----LNIAKiglHDLRFKITIIPQDpvlfsgslr 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 90 MQLAPNLSVA-ENIFLGSELSHgglvqrKEMLVQAQKviDRLgaQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDE 168
Cdd:TIGR00957 1378 MNLDPFSQYSdEEVWWALELAH------LKTFVSALP--DKL--DHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13364550 169 PTAALsSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSdRVSVLRDGQ 219
Cdd:TIGR00957 1448 ATAAV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE 1496
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-201 |
1.63e-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: 74.11 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEIlidGKPFHirtpkdalsAGITLIYQEMQLaPNLSVAEN 101
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEG---------EDLLFLPQRPYL-PLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFL--GSELSHGglvqrkemlvqaqkvidrlgaqfnasdkvmtltiaEQQQVEIARALHRNSRILVMDEPTAALSSRETH 179
Cdd:cd03223 84 LIYpwDDVLSGG-----------------------------------EQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|..
gi 13364550 180 RLFELimrLRDEGMAIIYISHR 201
Cdd:cd03223 129 RLYQL---LKELGITVISVGHR 147
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
275-476 |
1.65e-15 |
|
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: 76.24 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidLG--IGFLTenrkeQglflEMAAAE 352
Cdd:COG1120 21 SLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LArrIAYVP-----Q----EPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NIT------MATLERDARWGMLNRKKAQTIsDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPAR 426
Cdd:COG1120 89 GLTvrelvaLGRYPHLGLFGRPSAEDREAV-EEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13364550 427 GVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:COG1120 167 HLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
275-478 |
2.17e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.47 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfLTENRKE------QGLFL-- 346
Cdd:COG1136 28 SLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE--------LARLRRRhigfvfQFFNLlp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 347 EMAAAENITMAtlerdARWGMLNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPAR 426
Cdd:COG1136 100 ELTALENVALP-----LLLAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 427 GVDVGAKSEIYRIMNEMARK-GVAILMISSElPEIVGMSDRVYVMREGSIAGE 478
Cdd:COG1136 174 NLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
275-475 |
2.22e-15 |
|
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: 74.01 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLgIGFLtenrkEQGLflemaaaeni 354
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYV-----PQAL---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tmatlerdARWGMLNrKKAQTISDdaikllnirvphaqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03214 83 --------ELLGLAH-LADRPFNE-------------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13364550 435 EIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03214 135 ELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
266-478 |
3.97e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.51 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 266 TDGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTENRKEQglf 345
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNPDNQ--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 346 lemaaaenITMATLERDARWGMLN----RKKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLL 421
Cdd:PRK13642 94 --------FVGATVEDDVAFGMENqgipREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 422 DEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEiVGMSDRVYVMREGSIAGE 478
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDE-AASSDRILVMKAGEIIKE 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
291-491 |
4.14e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 291 GAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTENRKEQglflemaaaenITMATLERDARWGMLNR 370
Cdd:PRK13652 40 GAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVFQNPDDQ-----------IFSPTVEQDIAFGPINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 371 K-KAQTIS---DDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMN 441
Cdd:PRK13652 108 GlDEETVAhrvSSALHMLGLeelrdRVPHH------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 442 EMA-RKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNI-TQENIMT 491
Cdd:PRK13652 182 DLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLA 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
4.90e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAF--GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDa 78
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 LSAGITLIYQEmqlapnlsvAENIFLGSELSHG---GL----VQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQV 151
Cdd:PRK13648 81 LRKHIGIVFQN---------PDNQFVGSIVKYDvafGLenhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 152 EIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYElSDRVSVLRDG 218
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
275-467 |
4.97e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.42 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGepvvihspreaiDLGIGFLTEnRKEQGLFLEMAAAENI 354
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQ-RSEVPDSLPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLNRKKAQTIsDDAIKLLNI-RVPHAQVRAggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAK 433
Cdd:NF040873 79 AMGRWARRGLWRRLTRDDRAAV-DDALERVGLaDLAGRQLGE--LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....
gi 13364550 434 SEIYRIMNEMARKGVAILMISSElPEIVGMSDRV 467
Cdd:NF040873 156 ERIIALLAEEHARGATVVVVTHD-LELVRRADPC 188
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-478 |
5.89e-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: 74.15 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfLTENRKEQG-------LFLE 347
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKE--------LRKARRRIGmifqhfnLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENITMAtLERdARWGMLNRKKAqtiSDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARG 427
Cdd:cd03258 97 RTVFENVALP-LEI-AGVPKAEIEER---VLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 428 VDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:cd03258 171 LDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-221 |
5.92e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.11 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHI--RTPKDALSAGITLIYQEMQLA--PNLS 97
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKAFRRDIQMVFQDSISAvnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 98 VAENIflGSELSH-------GGLVQRKEMLVQ---AQKVIDRLGAQfnasdkvmtLTIAEQQQVEIARALHRNSRILVMD 167
Cdd:PRK10419 108 VREII--REPLRHllsldkaERLARASEMLRAvdlDDSVLDKRPPQ---------LSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 168 EptaALSSRETH---RLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK10419 177 E---AVSNLDLVlqaGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-223 |
6.00e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.77 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAF----GKFY------ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPF-- 70
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 71 HIRTPKDALSAGITLIYQE--MQLAPNLSV----AENIFLGSELSHGglvQRKEmlvQAQKVIDRLGAQFNASDKV--Mt 142
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQNpyGSLNPRKKVgqilEEPLLINTSLSAA---ERRE---KALAMMAKVGLRPEHYDRYphM- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 143 LTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLrdgqYV 221
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM----YL 230
|
..
gi 13364550 222 GS 223
Cdd:PRK11308 231 GR 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-228 |
6.16e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 6.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 28 TVYPGEIHALMGENGAGKSTLMKVLAGAyTATSGEILIDGKPF-HIRTPKDALSAGitliYQEMQLAPNLSVAenIFLGS 106
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeAWSAAELARHRA----YLSQQQTPPFAMP--VFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 107 ELSHGGLVQrkemLVQAQKVIDRLGAQFNASDK----VMTLTIAEQQQVEIA-------RALHRNSRILVMDEPTAALSS 175
Cdd:PRK03695 91 TLHQPDKTR----TEAVASALNEVAEALGLDDKlgrsVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 176 RETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDN 228
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-201 |
6.63e-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: 77.02 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIYQEMQLApNLSVAE 100
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVRRRVSVCAQDAHLF-DTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGSelshgGLVQRKEMLVQAQKV-----IDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:TIGR02868 428 NLRLAR-----PDATDEELWAALERVgladwLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*...
gi 13364550 174 SSRETHRLFELiMRLRDEGMAIIYISHR 201
Cdd:TIGR02868 503 DAETADELLED-LLAALSGRTVVLITHH 529
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-196 |
6.69e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTP--------- 75
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 76 KDALSagitliyqemqlaPNLSVAENI-----FLGSELSHgglvqrkemlvqAQKVIDRLGAQFNASDKVMTLTIAEQQQ 150
Cdd:PRK13539 81 RNAMK-------------PALTVAENLefwaaFLGGEELD------------IAAALEAVGLAPLAHLPFGYLSAGQKRR 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 151 VEIARALHRNSRILVMDEPTAALSSRETHRLFELIM-RLRDEGMAII 196
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAVALFAELIRaHLAQGGIVIA 182
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
275-476 |
8.30e-15 |
|
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: 77.18 E-value: 8.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVvihsprEAIDLG-----IGFLTENrkeqGLFLEMA 349
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL------RQIDPAslrrqIGVVLQD----VFLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 350 AAENITMAtlerdarwgmlnrkkAQTISDD----AIKLLNI-----RVP---HAQVRAGG--LSGGNQQKLLISRWVAIG 415
Cdd:COG2274 565 IRENITLG---------------DPDATDEeiieAARLAGLhdfieALPmgyDTVVGEGGsnLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 416 PRILLLDEPARGVDVGAKSEIYRIMNEMArKGVAILMISSELpEIVGMSDRVYVMREGSIA 476
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-484 |
1.43e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.96 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvihspreaIDLGIGFLTENRKEQGLFLEmAAAENI 354
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP---------IKYDKKSLLEVRKTVGIVFQ-NPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLN----RKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:PRK13639 92 FAPTVEEDVAFGPLNlglsKEEVEKRVKEALKAVGMegfenKPPHH------LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 426 RGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNI 484
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-240 |
1.63e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 3 STPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAG 82
Cdd:PRK10253 4 SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQEMQLAPNLSVAENIFLGsELSHGGLVQ--RKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRN 160
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARG-RYPHQPLFTrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 161 SRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMV 239
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
.
gi 13364550 240 G 240
Cdd:PRK10253 242 G 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
275-487 |
1.63e-14 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 72.99 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVvihspreaIDLGIGFLTENRKEQG-------LFLE 347
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI--------NKLKGKALRQLRRQIGmifqqfnLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENITMATLERDARW-GMLNRKKAQTISDdAIKLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:cd03256 93 LSVLENVLSGRLGRRSTWrSLFGLFPKEEKQR-ALAALE-RVgllDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 424 PARGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQE 487
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINReEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
276-487 |
1.66e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 276 LLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVdGEPVVIHSPREAIdlgigfLTENRKEQGLFLEMAAAEnIT 355
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKE------IKPVRKKVGVVFQFPESQ-LF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 356 MATLERDARWGMLN----RKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:PRK13643 99 EETVLKDVAFGPQNfgipKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 432 AKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQE 487
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-224 |
1.73e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.69 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTA---TSGEILIDGKpfhirtPKDALSAGITLIYQEMQL-APNLS 97
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGR------PLDSSFQRSIGYVQQQDLhLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 98 VAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQFNASDKVMT----LTIAEQQQVEIARALHRNSRILV-MDEPTAA 172
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 173 LSSRETHRLFELIMRLRDEGMAIIYISHR-MAEVYELSDRVSVLRDGQ---YVGSL 224
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHGQAILCTIHQpSAILFEEFDRLLLLQKGGqtvYFGDL 988
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-221 |
2.00e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 75.63 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRT-PKDALSAGITLIYQEMQLApNLSVAE 100
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD--IRDvTQASLRAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGS-ELSHgglvqrkEMLVQAQKV------IDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTA 171
Cdd:COG5265 451 NIAYGRpDASE-------EEVEAAARAaqihdfIESLpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 172 ALSSRETHRLFELIMRLRdEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:COG5265 524 ALDSRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-482 |
2.05e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.60 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVvihsPREAIDlGIGFLTEnrkEQGLFLEMAAAENI 354
Cdd:COG4152 21 SFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRR-RIGYLPE---ERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 T-MATLerdarWGMlNRKKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKL-----LISRwvaigPRILLLDEPARGV 428
Cdd:COG4152 93 VyLARL-----KGL-SKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVqliaaLLHD-----PELLILDEPFSGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 429 DVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAgeLNGK 482
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV--LSGS 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
2.91e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAGIT 84
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIYQ---EMQLAPnlSVAENIFLGSelSHGGLvQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNS 161
Cdd:PRK13652 82 LVFQnpdDQIFSP--TVEQDIAFGP--INLGL-DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 162 RILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLT 225
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
268-482 |
3.46e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.83 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 268 GGK--VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDL--GIGFLTENRKeqg 343
Cdd:PRK10908 13 GGRqaLQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQIGMIFQDHH--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 344 LFLEMAAAENITMATLERDARWGMLNRKKAQTIsdDAIKLLNirvpHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:PRK10908 90 LLMDRTVYDNVAIPLIIAGASGDDIRRRVSAAL--DKVGLLD----KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 424 PARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGK 482
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
271-475 |
3.52e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 72.68 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfLTENRKEQ-------- 342
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE--------LRELRRKKismvfqsf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 343 GLFLEMAAAENIT----MATLERDARwgmlnRKKAQtisdDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRI 418
Cdd:cd03294 112 ALLPHRTVLENVAfgleVQGVPRAER-----EERAA----EALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 419 LLLDEPARGVD----VGAKSEIYRIMNEMARkgvAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03294 182 LLMDEAFSALDplirREMQDELLRLQAELQK---TIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
275-484 |
4.33e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlgigfLTENRKEQGL---FLEMAAA 351
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKN-------LKKLRKKVSLvfqFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 ENitmaTLERDARWGMLN----RKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARG 427
Cdd:PRK13641 100 EN----TVLKDVEFGPKNfgfsEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 428 VDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNI 484
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-219 |
4.33e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 73.72 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDalsAGITL 85
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQEMQLAPNLSVAENIFLGseLSHGGL--------VQRKEMLVQAQKVIDRLGAQfnasdkvmtLTIAEQQQVEIARAL 157
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYG--LKIRGMpkaeieerVAEAARILELEPLLDRKPRE---------LSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 158 HRNSRILVMDEPtaaLSS-----RETHRLfElIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK11650 150 VREPAVFLFDEP---LSNldaklRVQMRL-E-IQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-196 |
5.94e-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: 70.47 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHirTPKDALSAGITLI 86
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA--EQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENIFLGSELsHGGlvqrkemlvqAQKVIDRLGAQFNASDK----VMTLTIAEQQQVEIARALHRNSR 162
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAI-HGG----------AQRTIEDALAAVGLTGFedlpAAQLSAGQQRRLALARLWLSRRP 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 13364550 163 ILVMDEPTAALsSRETHRLFELIMR--LRDEGMAII 196
Cdd:TIGR01189 148 LWILDEPTTAL-DKAGVALLAGLLRahLARGGIVLL 182
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-229 |
6.36e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTAtSGEILIDGKPF---------HIRT--PKDALSAGITLIYQEM 90
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLsdwsaaelaRHRAylSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 91 QLapnlsvaeniFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQfnasdkVMTLTIAEQQQVEIARAL-------HRNSRI 163
Cdd:COG4138 91 AL----------HQPAGASSEAVEQLLAQLAEALGLEDKLSRP------LTQLSGGEWQRVRLAAVLlqvwptiNPEGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 164 LVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS------LTRDNL 229
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASgetaevMTPENL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
275-480 |
6.58e-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: 71.66 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPreaiDLGIGFltenrkeQ--GLFLEMAAAE 352
Cdd:COG1116 31 SLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP----DRGVVF-------QepALLPWLTVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NITMAtlerdARWGMLNRKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARG 427
Cdd:COG1116 100 NVALG-----LELRGVPKAERRERARELLELVGLagfedAYPHQ------LSGGMRQRVAIARALANDPEVLLMDEPFGA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 428 VDVGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVM--REGSIAGELN 480
Cdd:COG1116 169 LDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEID 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
271-476 |
6.92e-14 |
|
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: 71.18 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTEnrkEQGLFLEMAA 350
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE-LRRKIGYVIQ---QIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENI-TMATLERdarWGmlnRKKAQTISDDAIKLLNI-------RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:cd03295 93 EENIaLVPKLLK---WP---KEKIRERADELLALVGLdpaefadRYPHE------LSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 423 EPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-219 |
7.29e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKF-YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTP---------- 75
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedyrklfsav 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 76 ---------------KDALSAGITLIYQEMQLAPNLSVAENIFLGSELSHGglvQRKemlvqaqkvidRLGaqfnasdkv 140
Cdd:PRK10522 403 ftdfhlfdqllgpegKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKG---QKK-----------RLA--------- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 141 MTLTIAEQQQveiaralhrnsrILVMDEpTAALSSRETHRLF--ELIMRLRDEGMAIIYISHRMAeVYELSDRVSVLRDG 218
Cdd:PRK10522 460 LLLALAEERD------------ILLLDE-WAADQDPHFRREFyqVLLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNG 525
|
.
gi 13364550 219 Q 219
Cdd:PRK10522 526 Q 526
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-267 |
8.62e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.97 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSA-----GITLIYQEMQLAPN 95
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPlrkkvGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 96 lSVAENIFLGSeLSHGglVQRKEMLVQAQKVIDRLGaqfnASDKVMT-----LTIAEQQQVEIARALHRNSRILVMDEPT 170
Cdd:PRK13634 102 -TVEKDICFGP-MNFG--VSEEDAKQKAREMIELVG----LPEELLArspfeLSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 171 AALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNL--NAGELVRMMVGRPLSDLF 247
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfaDPDELEAIGLDLPETVKF 253
|
250 260
....*....|....*....|....
gi 13364550 248 NKERDIPLG----KARLNVHHLTD 267
Cdd:PRK13634 254 KRALEEKFGisfpKPCLTLEELAH 277
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
8.96e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.19 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFG-----KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIdgKPFHI-------- 72
Cdd:PRK13631 21 ILRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIgdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 73 -------RTPKDA--LSAGITLIYQ--EMQLAPNlSVAENIFLGSElshgGLVQRKEMLVQ-AQKVIDRLGAQFNASDKV 140
Cdd:PRK13631 99 litnpysKKIKNFkeLRRRVSMVFQfpEYQLFKD-TIEKDIMFGPV----ALGVKKSEAKKlAKFYLNKMGLDDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 141 -MTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13631 174 pFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
....*.
gi 13364550 220 YVGSLT 225
Cdd:PRK13631 254 ILKTGT 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-430 |
9.42e-14 |
|
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: 73.43 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAF-GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILidgkpfhirtpkdaLSAGIT 84
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------------PQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIY--QEMQLAPNLSVAENIFLGselshgglVQRKemlVQAQKVIDRLGAQFNASDKVMTLTIAEQ-------------- 148
Cdd:TIGR03719 70 VGYlpQEPQLDPTKTVRENVEEG--------VAEI---KDALDRFNEISAKYAEPDADFDKLAAEQaelqeiidaadawd 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 149 --QQVEIA---------------------------RALHRNSRILVMDEPTAALSSRE------------------TH-R 180
Cdd:TIGR03719 139 ldSQLEIAmdalrcppwdadvtklsggerrrvalcRLLLSKPDMLLLDEPTNHLDAESvawlerhlqeypgtvvavTHdR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 181 LF-----ELIMRLrDEGMAIIYISH----------RMA-EVYELSDRVSVL-RDGQYVGSLT--RDNLNAGELVRmmvgr 241
Cdd:TIGR03719 219 YFldnvaGWILEL-DRGRGIPWEGNysswleqkqkRLEqEEKEESARQKTLkRELEWVRQSPkgRQAKSKARLAR----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 242 pLSDLFNKERD---------IP----LGKARLNVHHLTD--GGKV--QPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGV 304
Cdd:TIGR03719 293 -YEELLSQEFQkrnetaeiyIPpgprLGDKVIEAENLTKafGDKLliDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 305 RKATGGMIEVdGEPVVIHS---PREAIDlgigfltenrkeqglflemaAAENItmatlerdarWgmlnrkkaQTISD--D 379
Cdd:TIGR03719 372 EQPDSGTIEI-GETVKLAYvdqSRDALD--------------------PNKTV----------W--------EEISGglD 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 380 AIKLLNIRVPH-------------AQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDV 430
Cdd:TIGR03719 413 IIKLGKREIPSrayvgrfnfkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-229 |
9.71e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 9.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALsagITLIYQEMQLAPNLSV-A 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-QALQKNL---VAYVPQSEEVDWSFPVlV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHGGLVQRKEmlVQAQKVIDRLGAQFNASD----KVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS 175
Cdd:PRK15056 98 EDVVMMGRYGHMGWLRRAK--KRDRQIVTAALARVDMVEfrhrQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 176 RETHRLFELIMRLRDEGMAIIYISHRMAEVYELSD-----RVSVLRDGQYVGSLTRDNL 229
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDytvmvKGTVLASGPTETTFTAENL 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
275-475 |
1.07e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVihspreaidlgigflTENRKEQGLF---LEMAAA 351
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA---------------KLNRAQRKAFrrdIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 ENITMATLERDARWGM---------LNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:PRK10419 97 DSISAVNPRKTVREIIreplrhllsLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 423 EPARGVDVGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-219 |
1.41e-13 |
|
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: 69.42 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 19 FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpfhirtpkdalsaGITLIYQEMQLaPNLSV 98
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWI-QNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENIFLGSELSHgglvQRKEMLVQA---QKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:cd03250 83 RENILFGKPFDE----ERYEKVIKAcalEPDLEILpdGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 174 SSRETHRLFE-LIMRLRDEGMAIIYISHRMaEVYELSDRVSVLRDGQ 219
Cdd:cd03250 159 DAHVGRHIFEnCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
271-470 |
1.69e-13 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 72.70 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVvIHSPREAIDLGIGFLTEnrkeQGLFLEMAA 350
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL-ADADADSWRDQIAWVPQ----HPFLFAGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITMATleRDARWGMLNRKKAQTISDDAIKLLNiRVPHAQV--RAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGV 428
Cdd:TIGR02857 413 AENIRLAR--PDASDAEIREALERAGLDEFVAALP-QGLDTPIgeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13364550 429 DVGAKSEIYRIMNEMARkGVAILMISSElPEIVGMSDRVYVM 470
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ-GRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-221 |
1.81e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 72.74 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpFHIRTPK-DALSAGITLIYQEMQLApNLSVA 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDLRDYTlASLRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSElshgGLVQRKEM-----LVQAQKVIDRLGaqfNASDKVM-----TLTIAEQQQVEIARALHRNSRILVMDEP 169
Cdd:PRK11176 435 NNIAYART----EQYSREQIeeaarMAYAMDFINKMD---NGLDTVIgengvLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 170 TAALSSRETHRLFELIMRLRDEGMAIIyISHRMAEVyELSDRVSVLRDGQYV 221
Cdd:PRK11176 508 TSALDTESERAIQAALDELQKNRTSLV-IAHRLSTI-EKADEILVVEDGEIV 557
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
275-476 |
1.81e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.12 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVviHSPREAIdlgigflTENRKEQG-------LFLE 347
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDE-------RLIRQEAGmvfqqfyLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENITMATLE-RDArwgmlnrKKAQTiSDDAIKLLNiRVPHAQvRAGG----LSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:PRK09493 92 LTALENVMFGPLRvRGA-------SKEEA-EKQARELLA-KVGLAE-RAHHypseLSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 423 EPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-221 |
1.84e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGK-----FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILI---------DGKPFHI 72
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 73 RTPKDALS----------------AGITLIYQEMQLAPNlSVAENIFLGSeLSHGglVQRKEMLVQAQKVIDRLGAQFNA 136
Cdd:PRK13651 83 VLEKLVIQktrfkkikkikeirrrVGVVFQFAEYQLFEQ-TIEKDIIFGP-VSMG--VSKEEAKKRAAKYIELVGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 137 SDKV-MTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVL 215
Cdd:PRK13651 159 LQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*.
gi 13364550 216 RDGQYV 221
Cdd:PRK13651 239 KDGKII 244
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
275-475 |
1.92e-13 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 69.54 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTEnrkEQGLF---LEmaaa 351
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQ---DVTLFygtLR---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 ENITMATLE-RDARwgMLNRKKAQTISDdaikLLNiRVPHA---QVRAGG--LSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:cd03245 96 DNITLGAPLaDDER--ILRAAELAGVTD----FVN-KHPNGldlQIGERGrgLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 426 RGVDVGAKSEIYRIMNEMARKgvAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-210 |
2.03e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMK-------VLAGAytATSGEILIDGK--------PF 70
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGKnlyapdvdPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 71 HIRTPkdalsagITLIYQEMQLAPNlSVAENIFLGSELS-HGG----LVQRKemLVQA---QKVIDRLgaqfnaSDKVMT 142
Cdd:PRK14243 88 EVRRR-------IGMVFQKPNPFPK-SIYDNIAYGARINgYKGdmdeLVERS--LRQAalwDEVKDKL------KQSGLS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 143 LTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRdEGMAIIYISHRMAEVYELSD 210
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSD 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
263-474 |
2.84e-13 |
|
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: 69.00 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 263 HHLtdGGKVQPS----SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEV--DGEPVVIH--SPREAIDL---G 331
Cdd:COG4778 17 HLQ--GGKRLPVldgvSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAqaSPREILALrrrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 332 IGFLTEnrkeqglFLEM---AAAENITMATLerdARWGMlNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLI 408
Cdd:COG4778 95 IGYVSQ-------FLRViprVSALDVVAEPL---LERGV-DREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 409 SRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGS 474
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
268-473 |
2.98e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 268 GGK--VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVvihsPREA--IDLGIGFLTENrkeQG 343
Cdd:PRK13536 52 GDKavVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARArlARARIGVVPQF---DN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 344 LFLEMAAAENITMatlerdarWGMLNRKKAQTISDDAIKLLNI-RVPH-AQVRAGGLSGGNQQKLLISRWVAIGPRILLL 421
Cdd:PRK13536 125 LDLEFTVRENLLV--------FGRYFGMSTREIEAVIPSLLEFaRLESkADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 422 DEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-219 |
3.15e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGkpfhirtpKDALSAGITLIYQEMQLAPNL----- 96
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--------CDVAKFGLTDLRRVLSIIPQSpvlfs 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 97 -SVAENIFLGSELSHGGLVQRKEMlVQAQKVIDR--LGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:PLN03232 1324 gTVRFNIDPFSEHNDADLWEALER-AHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13364550 174 SSReTHRLFELIMRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQ 219
Cdd:PLN03232 1403 DVR-TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-219 |
3.22e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 71.75 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAF-----GKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKP------------ 69
Cdd:COG4615 328 LELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPvtadnreayrql 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 70 -------FH-----IRTPKDALSAGITLIYQEMQLAPNLSVAENIFLGSELSHGglvQRKemlvqaqkvidRLGaqfnas 137
Cdd:COG4615 408 fsavfsdFHlfdrlLGLDGEADPARARELLERLELDHKVSVEDGRFSTTDLSQG---QRK-----------RLA------ 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 138 dkvMTLTIAEQQQveiaralhrnsrILVMDEpTAALSSRETHRLF--ELIMRLRDEGMAIIYISH--RMaevYELSDRVS 213
Cdd:COG4615 468 ---LLVALLEDRP------------ILVFDE-WAADQDPEFRRVFytELLPELKARGKTVIAISHddRY---FDLADRVL 528
|
....*.
gi 13364550 214 VLRDGQ 219
Cdd:COG4615 529 KMDYGK 534
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-221 |
3.36e-13 |
|
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: 68.44 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 9 MRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGA---YTATSGEILIDGKPFHirtpKDALSAGITL 85
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYK----EFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IY--QEMQLAPNLSVAENIflgselshgglvqrkemlvqaqkvidRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:cd03233 86 IYvsEEDVHFPTLTVRETL--------------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 164 LVMDEPTAALSSREThrlFELIMRLRD-----EGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:cd03233 140 LCWDNSTRGLDSSTA---LEILKCIRTmadvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
275-475 |
4.53e-13 |
|
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: 68.44 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAiDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:cd03301 20 NLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-DIAMVF-----QNYALYPHMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLNRKkaqtiSDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:cd03301 94 AFGLKLRKVPKDEIDER-----VREVAELLQIehlldRKPKQ------LSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 430 ----VGAKSEIYRIMNEMarkGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03301 163 aklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
275-478 |
4.57e-13 |
|
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: 68.85 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPRE--AIDLGIGFLTenrkeQG--LFLEMAA 350
Cdd:COG1127 25 SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyELRRRIGMLF-----QGgaLFDSLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITMATLERdarwGMLNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDV 430
Cdd:COG1127 100 FENVAFPLREH----TDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 431 GAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:COG1127 175 ITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
275-476 |
4.68e-13 |
|
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: 68.67 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGepvvihspreaIDLGIGFLTENRKEQGLFLEMAAAENI 354
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG-----------HDLALADPAWLRRQVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLNRK--KAQTISDDAIKLLNIRVPHAQV---RAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:cd03252 91 SIRDNIALADPGMSMERviEAAKLAGAHDFISELPEGYDTIvgeQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 430 VGAKSEIYRIMNEMArKGVAILMISSELpEIVGMSDRVYVMREGSIA 476
Cdd:cd03252 171 YESEHAIMRNMHDIC-AGRTVIIIAHRL-STVKNADRIIVMEKGRIV 215
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-223 |
5.73e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.66 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGA--YTATSGEILIDGKPFHIRTPKDALSAGITLIYQEMQLAPnlSVA 99
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIP--GVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHGGLVQRKEML--VQAQKVIDRLGAQFNASDKVMTLTI------AEQQQVEIARALHRNSRILVMDEPTA 171
Cdd:PRK09580 95 NQFFLQTALNAVRSYRGQEPLdrFDFQDLMEEKIALLKMPEDLLTRSVnvgfsgGEKKRNDILQMAVLEPELCILDESDS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 172 ALSSRETHRLFELIMRLRDEGMAIIYISH--RMAEvYELSDRVSVLRDGQYVGS 223
Cdd:PRK09580 175 GLDIDALKIVADGVNSLRDGKRSFIIVTHyqRILD-YIKPDYVHVLYQGRIVKS 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
275-475 |
6.87e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 66.86 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLgIGFLTENRKeqgLFlemaaaeni 354
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VGYLPQDDE---LF--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tmatlerdarwgmlnrkkAQTISDdaikllNIrvphaqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:cd03246 89 ------------------SGSIAE------NI-----------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13364550 435 EIYRIMNEMARKGVAILMISSElPEIVGMSDRVYVMREGSI 475
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
276-495 |
7.68e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 276 LLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLtenRKEQGLFLEMAAAENIT 355
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMV---HQELNLVLQRSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 356 matLERDARWGM-LNRKKAQTISDDAIKLLNIRVpHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKS 434
Cdd:PRK10982 96 ---LGRYPTKGMfVDQDKMYRDTKAIFDELDIDI-DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 435 EIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQENIMTLATG 495
Cdd:PRK10982 172 HLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
275-487 |
8.37e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIdlgigflTENRKEQGLFLEMAAAEnI 354
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDI-------KQIRKKVGLVFQFPESQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLN----RKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDV 430
Cdd:PRK13649 99 FEETVLKDVAFGPQNfgvsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 431 GAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQE 487
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
275-475 |
1.04e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.38 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAI-----DLGIGFltenrKEQGLFLEMA 349
Cdd:COG2884 22 SLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-RLKRREIpylrrRIGVVF-----QDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 350 AAENITMATLERdarwGMlNRKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:COG2884 96 VYENVALPLRVT----GK-SRKEIRRRVREVLDLVGLsdkakALPHE------LSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13364550 425 ARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG2884 165 TGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-221 |
1.08e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 25 VDLTVYPGEIHALMGENGAGKSTLMKVLAG--AYTatsGEILIDGKPFHIRTPKDALSAgITLIYQEMQLaPNLSVAENI 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGflPYQ---GSLKINGIELRELDPESWRKH-LSWVGQNPQL-PHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 103 FLGSELSHGGLVQRKEMLVQAQKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHR 180
Cdd:PRK11174 444 LLGNPDASDEQLQQALENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13364550 181 LFELIMRLRDEGMAIIyISHRMAEVYELsDRVSVLRDGQYV 221
Cdd:PRK11174 524 VMQALNAASRRQTTLM-VTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
275-475 |
1.25e-12 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 67.21 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRS-------ELAQLIFGVRkaTGGMIEVDGEPVVihspreaiDLGIGfLTENRKEQG-LF- 345
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKStllrllnRLNDLIPGAP--DEGEVLLDGKDIY--------DLDVD-VLELRRRVGmVFq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 346 ----LEMAAAENITMATLERdarwGMLNRKKAQTISDDAIKL--LNIRVpHAQVRAGGLSGGNQQKLLISRWVAIGPRIL 419
Cdd:cd03260 89 kpnpFPGSIYDNVAYGLRLH----GIKLKEELDERVEEALRKaaLWDEV-KDRLHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 420 LLDEPARGVDVGAKSEIYRIMNEMARKgVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
279-473 |
1.28e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 279 RSGEIVGLAGLVGAGRSELAQLIFGVRKATGgmiEVDGEpvVIHSPREAIDLGIGFLTENRKEQ--GLFLEMAAAENITM 356
Cdd:PRK09473 40 RAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGS--ATFNGREILNLPEKELNKLRAEQisMIFQDPMTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 357 ATLERDARWGMLNRK--KAQTIsDDAIKLLN-IRVPHAQVRAG----GLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:PRK09473 115 RVGEQLMEVLMLHKGmsKAEAF-EESVRMLDaVKMPEARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 430 VGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:PRK09473 194 VTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
275-475 |
1.49e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.63 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIH-SPREaidLGIGFLTENrkeQGLFLEMAAAEN 353
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRE---RRVGFVFQH---YALFPHMTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 ItMATLErdarwgMLNRKKAQtISDDAIKLLN-IRVPH-AQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:COG1118 96 I-AFGLR------VRPPSKAE-IRARVEELLElVQLEGlADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 432 AKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG1118 168 VRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-68 |
1.51e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.16 E-value: 1.51e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK 68
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST 62
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-249 |
1.69e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 18 KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILI-DGK-PFHIRTPKDA--LSAGITLIYQ--EMQ 91
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAiPANLKKIKEVkrLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 92 LAPNlSVAENIFLGSelSHGGlVQRKEMLVQAQKVID--RLGAQFnASDKVMTLTIAEQQQVEIARALHRNSRILVMDEP 169
Cdd:PRK13645 103 LFQE-TIEKDIAFGP--VNLG-ENKQEAYKKVPELLKlvQLPEDY-VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 170 TAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV--GS----------LTRDNLNAGELVR 236
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIsiGSpfeifsnqelLTKIEIDPPKLYQ 257
|
250
....*....|....*
gi 13364550 237 MM--VGRPLSDLFNK 249
Cdd:PRK13645 258 LMykLKNKGIDLLNK 272
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
8-228 |
1.91e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 70.26 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTA--TSGEILIDGKPfhirtPKDALSAGITL 85
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFP-----KKQETFARISG 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 IYQEMQL-APNLSVAENIFLGSELSHGGLVQRKEMLVQAQKV-----IDRLGAQFNASDKVMTLTIAEQQQVEIARALHR 159
Cdd:PLN03140 957 YCEQNDIhSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVmelveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVA 1036
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMA-EVYELSDRVSVL-RDGQ--YVGSLTRDN 228
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQviYSGPLGRNS 1109
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-100 |
1.92e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.03 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIY 87
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELAKRLAILR 81
|
90
....*....|...
gi 13364550 88 QEMQLAPNLSVAE 100
Cdd:COG4604 82 QENHINSRLTVRE 94
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
275-484 |
2.16e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGepVVIHSPREAidlgiGFLTENRKEQGLFLEMAAAEnI 354
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD--ITITHKTKD-----KYIRPVRKRIGMVFQFPESQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLNRK-KAQTISDDAIKLL-------NIrvphAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPAR 426
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKmNLDEVKNYAHRLLmdlgfsrDV----MSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 427 GVDVGAKSEIYRIMNEMA-RKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNI 484
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-218 |
2.74e-12 |
|
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: 66.20 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAG---ITLIYQEMQLApNLSV 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENIFLGSELSHgglvQRKEMLVQA---QKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAAL 173
Cdd:cd03290 96 EENITFGSPFNK----QRYKAVTDAcslQPDIDLLpfGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 174 SSR-ETHRLFELIMR-LRDEGMAIIYISHRMAEVYElSDRVSVLRDG 218
Cdd:cd03290 172 DIHlSDHLMQEGILKfLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-219 |
2.89e-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: 65.90 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfHIRT-PKDALSAGITLIYQEMQL-----AP 94
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI--DISTiPLEDLRSSLTIIPQDPTLfsgtiRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 95 NLSV-----AENIFLGSELSHGGLvqrkeMLVQAQKvidrlgaqfnasdkvmtltiaeqQQVEIARALHRNSRILVMDEP 169
Cdd:cd03369 101 NLDPfdeysDEEIYGALRVSEGGL-----NLSQGQR-----------------------QLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 170 TAALSSrETHRLFELIMRLRDEGMAIIYISHRMAEVYELsDRVSVLRDGQ 219
Cdd:cd03369 153 TASIDY-ATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGE 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
275-476 |
3.22e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.05 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEpVVIHSPREAIDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:PRK09452 34 DLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ-DITHVPAENRHVNTVF-----QSYALFPHMTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAtlerdarwgmLNRKK--AQTISD---DAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:PRK09452 108 AFG----------LRMQKtpAAEITPrvmEALRMVQLE-EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 430 vgakseiYRIMNEM-------ARK-GVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:PRK09452 177 -------YKLRKQMqnelkalQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-240 |
3.28e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 60 SGEILIDGKPFHIRTPKDaLSAGITLIYQEMQLApNLSVAENIFLGSELSHGGLVQRKEMLVQAQKVIDRLGAQF--NAS 137
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYdtNVG 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 138 DKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDEG-MAIIYISHRMAEVyELSDRVSVLR 216
Cdd:PTZ00265 1354 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKIVVFN 1432
|
170 180
....*....|....*....|....
gi 13364550 217 DGQYVGSLTRDNLNAGELVRMMVG 240
Cdd:PTZ00265 1433 NPDRTGSFVQAHGTHEELLSVQDG 1456
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
278-490 |
3.68e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.80 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 278 VRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvihspreaIDLGIGFLTENRKEQGLFLEmAAAENITMA 357
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP---------IDYSRKGLMKLRESVGMVFQ-DPDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 358 TLERDARWGMLNRKkaqtISDDAIKLlniRVPHAQVRAG----------GLSGGNQQKLLISRWVAIGPRILLLDEPARG 427
Cdd:PRK13636 99 SVYQDVSFGAVNLK----LPEDEVRK---RVDNALKRTGiehlkdkpthCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 428 VDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQENIM 490
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-221 |
3.69e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.65 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 20 YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDG-------KPFHIRTpkdalSAGITLIYQEMQL 92
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeeNLWDIRN-----KAGMVFQNPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 93 APNLsVAENIFLGSElSHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAA 172
Cdd:PRK13633 99 VATI-VEEDVAFGPE-NLG--IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 173 LSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
261-478 |
3.82e-12 |
|
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: 68.63 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 261 NVHHLTDGGK--VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAIDLGIGFLTEN 338
Cdd:COG4988 341 DVSFSYPGGRpaLDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRRQIAWVPQN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 339 rkeqGLFLEMAAAENITMATleRDArwgmlnrkkaqtiSDD----AIKLLNI-----RVPH---AQV--RAGGLSGGNQQ 404
Cdd:COG4988 420 ----PYLFAGTIRENLRLGR--PDA-------------SDEeleaALEAAGLdefvaALPDgldTPLgeGGRGLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 405 KLLISRwvAI--GPRILLLDEPARGVDVGAKSEIYRIMNEMArKGVAILMISSELPEIVGMsDRVYVMREGSIAGE 478
Cdd:COG4988 481 RLALAR--ALlrDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQA-DRILVLDDGRIVEQ 552
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-221 |
3.94e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILI-------DGKPFHIRTPKDALsaGITLIYQEMQLA 93
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKPVRKKV--GVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 94 PNlSVAENIFLGSElsHGGLVQRKEMLVQAQKvIDRLGAQFNASDKV-MTLTIAEQQQVEIARALHRNSRILVMDEPTAA 172
Cdd:PRK13643 99 EE-TVLKDVAFGPQ--NFGIPKEKAEKIAAEK-LEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 173 LSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
275-475 |
4.34e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.44 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAIDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:PRK11432 26 NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-HRSIQQRDICMVF-----QSYALFPHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TmatlerdarWG--MLNRKKAQTIS--DDAIKLLNIrvphaqvrAG-------GLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:PRK11432 100 G---------YGlkMLGVPKEERKQrvKEALELVDL--------AGfedryvdQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 424 PARGVDvgakSEIYRIMNEMARK-----GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK11432 163 PLSNLD----ANLRRSMREKIRElqqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
280-476 |
5.19e-12 |
|
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: 67.05 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 280 SGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVV-----IHSPREAIDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:COG4148 24 GRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargIFLPPHRRRIGYVF-----QEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tmatleRDARWGMlnRKKAQTIS-DDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAK 433
Cdd:COG4148 99 ------LYGRKRA--PRAERRISfDEVVELLGIG-HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 434 SEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:COG4148 170 AEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
275-476 |
5.26e-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: 65.37 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFG-VR--KATGGMIEVDGEPVVIHSPREAIdlgiGFLTENrkeqGLFL-EMAA 350
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGrVEggGTTSGQILFNGQPRKPDQFQKCV----AYVRQD----DILLpGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITMATLERDARwGMLNRKKAQTISDDAIKLLNI-RVPHAQVRagGLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:cd03234 99 RETLTYTAILRLPR-KSSDAIRKKRVEDVLLRDLALtRIGGNLVK--GISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13364550 430 VGAKSEIYRIMNEMARKGVAILM-ISSELPEIVGMSDRVYVMREGSIA 476
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
260-470 |
5.26e-12 |
|
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: 67.00 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 260 LNVHHLTDGGKVQPS---SLLVRSGEIVGLAGLVGAGRSELAQLIFGV---RKATGGMIEVDGEPVVIHSPREAIDL-Gi 332
Cdd:COG0444 7 LKVYFPTRRGVVKAVdgvSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKELRKIrG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 333 gfltenRKEQGLFLE-MAA-----------AENItmatlerdARWGMLNRKKAQTISDDAIKLLNIRVPHAQVRA--GGL 398
Cdd:COG0444 86 ------REIQMIFQDpMTSlnpvmtvgdqiAEPL--------RIHGGLSKAEARERAIELLERVGLPDPERRLDRypHEL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 399 SGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVM 470
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
260-473 |
5.29e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.17 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 260 LNVHHLT---DG-GKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAIDLGIGFl 335
Cdd:PRK11607 20 LEIRNLTksfDGqHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQRPINMMF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 336 tenrKEQGLFLEMAAAENITMATLERDARWGMLNRKKAQTISDDAIKLLNIRVPHAqvraggLSGGNQQKLLISRWVAIG 415
Cdd:PRK11607 98 ----QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ------LSGGQRQRVALARSLAKR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 416 PRILLLDEPARGVDVGAKSEI-YRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-200 |
5.47e-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: 64.82 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHirTPKDALSAGITLI 86
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 87 YQEMQLAPNLSVAENI-FLGSELSHGGLVQrkemlvqaqkVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILV 165
Cdd:cd03231 79 GHAPGIKTTLSVLENLrFWHADHSDEQVEE----------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 13364550 166 MDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH 200
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-475 |
5.50e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 65.40 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvIHSPREAIDlgigfltENRKEQG-------LFLE 347
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED--LTDSKKDIN-------KLRRKVGmvfqqfnLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENITMATLErdarwgMLNRKKAQTIsDDAIKLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:COG1126 92 LTVLENVTLAPIK------VKKMSKAEAE-ERAMELLE-RVglaDKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 425 ARGVD---VGaksEIYRIMNEMARKGVAILMISSElpeivgM------SDRVYVMREGSI 475
Cdd:COG1126 164 TSALDpelVG---EVLDVMRDLAKEGMTMVVVTHE------MgfarevADRVVFMDGGRI 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
261-473 |
6.77e-12 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 64.84 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 261 NVHHLTDGGKV-QPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVvihSPREAIDLgigfltenR 339
Cdd:COG4619 5 GLSFRVGGKPIlSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL---SAMPPPEW--------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 340 K-------EQGLFlEMAAAENITMATLERDARWgmlNRKKAQtisdDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWV 412
Cdd:COG4619 74 RqvayvpqEPALW-GGTVRDNLPFPFQLRERKF---DRERAL----ELLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 413 AIGPRILLLDEPARGVDVGAKSEIYRIMNE-MARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
275-476 |
1.13e-11 |
|
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: 63.70 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVR--KATGGMIEVDGEPVVIHSPREAIDLGIgFLTenrkeqglFLEMAAAE 352
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGI-FLA--------FQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NITMATLERDarwgmlnrkkaqtisddaiklLNIrvphaqvragGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGA 432
Cdd:cd03217 91 GVKNADFLRY---------------------VNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13364550 433 KSEIYRIMNEMARKGVAILMIS--SELPEIVgMSDRVYVMREGSIA 476
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIIThyQRLLDYI-KPDRVHVLYDGRIV 184
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-219 |
1.17e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.04 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIYQemqlAPNL---S 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQ----TPFLfsdT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 98 VAENIFLGSELSHGGLVQRKEMLVQAQKVIDRL--GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS 175
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVARLASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 176 RETHRLFELIMRLRdEGMAIIYISHRMAEVYElSDRVSVLRDGQ 219
Cdd:PRK10789 485 RTEHQILHNLRQWG-EGRTVIISAHRLSALTE-ASEILVMQHGH 526
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
274-475 |
1.25e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.41 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 274 SSLLVRSGEIVGLAGLVGAGRSELAQLIFG-VRKATGGMIEVDGE-PVVIHSPREAIDLgigfltenRKEQGLFLEMAAA 351
Cdd:PRK13645 30 TSLTFKKNKVTCVIGTTGSGKSTMIQLTNGlIISETGQTIVGDYAiPANLKKIKEVKRL--------RKEIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 EnITMATLERDARWGML----NRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARG 427
Cdd:PRK13645 102 Q-LFQETIEKDIAFGPVnlgeNKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 428 VDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
275-479 |
1.56e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDL---GIGFLTENRKeqgLFLEMAAA 351
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqKLGFIYQFHH---LLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 ENITMATLerdarWGMLNRKKAQTISDDAIKL--LNIRVPHaqvRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:PRK11629 106 ENVAMPLL-----IGKKKPAEINSRALEMLAAvgLEHRANH---RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13364550 430 VGAKSEIYRIMNEM-ARKGVAILMISSELpEIVGMSDRVYVMREGSIAGEL 479
Cdd:PRK11629 178 ARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAEL 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
275-476 |
1.97e-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: 63.79 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEP---VVIHSPREAIdlgiGFLTENRKeqgLFlemaaa 351
Cdd:cd03253 21 SFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDireVTLDSLRRAI----GVVPQDTV---LF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 eNitmATLERDARWGMLNRKKAQTIsdDAIKLLNI-----RVPHA---QV--RAGGLSGGNQQKLLISRWVAIGPRILLL 421
Cdd:cd03253 88 -N---DTIGYNIRYGRPDATDEEVI--EAAKAAQIhdkimRFPDGydtIVgeRGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 422 DEPARGVDVGAKSEIYRIMNEMArKGVAILMISSELPEIVGmSDRVYVMREGSIA 476
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
32-201 |
2.03e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 32 GEIHaLMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfHIRTPKDALSAGITLIYQEMQLAPNLSVAENIFLGSELSHG 111
Cdd:PRK13540 28 GLLH-LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ--SIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 112 GLvqrkemlvqaqkVIDRLGAQFNASDKV----MTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMR 187
Cdd:PRK13540 105 AV------------GITELCRLFSLEHLIdypcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....
gi 13364550 188 LRDEGMAIIYISHR 201
Cdd:PRK13540 173 HRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-221 |
2.25e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 64.24 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGITLIYQ--EMQLAPNlSV 98
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQnpETQFVGR-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENIFLGSElshgGLVQRKemlVQAQKVIDR------LGAQFNASDKvmTLTIAEQQQVEIARALHRNSRILVMDEPTAA 172
Cdd:PRK13644 96 EEDLAFGPE----NLCLPP---IEIRKRVDRalaeigLEKYRHRSPK--TLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 173 LSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYV 221
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
278-474 |
2.35e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 278 VRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLG-------IGFLTENRKEQGLFlemAA 350
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGycpqfdaIDDLLTGREHLYLY---AR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITMATLERDARWGmlnrkkaqtisddaIKLLNIRVpHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDV 430
Cdd:TIGR01257 2039 LRGVPAEEIEKVANWS--------------IQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13364550 431 GAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGS 474
Cdd:TIGR01257 2104 QARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
275-475 |
2.94e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.98 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTENRKEQglflemaaaenI 354
Cdd:PRK13650 27 SFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNPDNQ-----------F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLNR----KKAQTISDDAIKLLNI-----RVPhaqvraGGLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:PRK13650 95 VGATVEDDVAFGLENKgiphEEMKERVNEALELVGMqdfkeREP------ARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13364550 426 RGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEiVGMSDRVYVMREGSI 475
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
283-476 |
3.12e-11 |
|
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: 62.98 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 283 IVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHspREAIDLGIGFLTEnrkEQGLFLEMAAAENI-TMATLER 361
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ--PQKLRRRIGYLPQ---EFGVYPNFTVREFLdYIAWLKG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 362 darwgmLNRKKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMN 441
Cdd:cd03264 102 ------IPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLS 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 13364550 442 EMARKgvAILMISSELPE-IVGMSDRVYVMREGSIA 476
Cdd:cd03264 175 ELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
275-478 |
3.66e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIH---------SPREAIDLGIGFLTENRKEQGLF 345
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvADKNQLRLLRTRLTMVFQHFNLW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 346 LEMAAAENITMATLErdarwgMLNRKKAQTiSDDAIKLLN---IRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:PRK10619 105 SHMTVLENVMEAPIQ------VLGLSKQEA-RERAVKYLAkvgIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 423 EPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
274-496 |
3.89e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 274 SSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPV--------VIHSPR-EAIDLGIGFLTENRKEQGL 344
Cdd:PRK15056 26 ASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrqalqknlVAYVPQsEEVDWSFPVLVEDVVMMGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 345 FLEMaaaenitmatlerdarwGMLNRKKA--QTISDDA---IKLLNIRvpHAQVraGGLSGGNQQKLLISRWVAIGPRIL 419
Cdd:PRK15056 106 YGHM-----------------GWLRRAKKrdRQIVTAAlarVDMVEFR--HRQI--GELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 420 LLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQENIMTLATGV 496
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGV 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-207 |
4.54e-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: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 8 EMRNIAKAFG------KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDgkpfhirtpkdalsa 81
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 gitliYQEMQLAPNLSVAENIFlgselshgglvqRKEMLVQAQKVIDRLGaqfnASD------KVMTLTIAEQQQVEIAR 155
Cdd:COG2401 91 -----VPDNQFGREASLIDAIG------------RKGDFKDAVELLNAVG----LSDavlwlrRFKELSTGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 156 ALHRNSRILVMDEPTAALsSRETHRLFELIMR--LRDEGMAIIYISHRmAEVYE 207
Cdd:COG2401 150 LLAERPKLLVIDEFCSHL-DRQTAKRVARNLQklARRAGITLVVATHH-YDVID 201
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-221 |
4.75e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYaLKGVDLTVYPGEIHALMGENGAGKS----TLMKVLAGAYTATSGEILIDGKPFHirtPKDALSA 81
Cdd:PRK10418 4 QIELRNIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 82 GITLIYQEMQLAPNLsvaenifLGSELSHGglvqrKEMLVQAQK--VIDRLGAQFNA-----SDKVMTLTIAEQ-----Q 149
Cdd:PRK10418 80 KIATIMQNPRSAFNP-------LHTMHTHA-----RETCLALGKpaDDATLTAALEAvglenAARVLKLYPFEMsggmlQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 150 QVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYV 221
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-201 |
5.08e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.83 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEI----------------LIDGkpfhirTPKDALSagitl 85
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIarpagarvlflpqrpyLPLG------TLREALL----- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 86 iYqemqlaPNLSvaeniflgSELSHGGLvqrKEMLVQA--QKVIDRLGAQFNASDkvmTLTIAEQQQVEIARALHRNSRI 163
Cdd:COG4178 448 -Y------PATA--------EAFSDAEL---REALEAVglGHLAERLDEEADWDQ---VLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13364550 164 LVMDEPTAALSSRETHRLFELimrLRDE--GMAIIYISHR 201
Cdd:COG4178 507 LFLDEATSALDEENEAALYQL---LREElpGTTVISVGHR 543
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-219 |
6.35e-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: 62.43 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 28 TVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfhirtpkdalsagiTLIYQEMQLAPNLSVAENIFLGSE 107
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD---------------TVSYKPQYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 108 L-SHGGLVQ-RKEML--VQAQKVIDRLgaqfnasdkVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFE 183
Cdd:cd03237 86 TkDFYTHPYfKTEIAkpLQIEQILDRE---------VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 13364550 184 LIMRLRDEGMAIIY-ISHRMAEVYELSDRVSVLrDGQ 219
Cdd:cd03237 157 VIRRFAENNEKTAFvVEHDIIMIDYLADRLIVF-EGE 192
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
275-492 |
7.39e-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: 62.41 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFG-VRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTENRKEQglFLEMAAAEN 353
Cdd:COG1119 23 SWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWE-LRKRIGLVSPALQLR--FPRDETVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 ITM----ATLERDARWGMLNRKKAqtisDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:COG1119 100 VVLsgffDSIGLYREPTDEQRERA----RELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 430 VGAKSEIYRIMNEMARKG-VAILMISSELPEIVGMSDRVYVMREGSI--AGELNgKNITQENIMTL 492
Cdd:COG1119 175 LGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVvaAGPKE-EVLTSENLSEA 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
281-484 |
8.26e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.46 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 281 GEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTENRKEQglflemaaaenITMATLE 360
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK-LRKHIGIVFQNPDNQ-----------FVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 361 RDARWGMLN---------RKKAQTISDdaIKLLNIR--VPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:PRK13648 103 YDVAFGLENhavpydemhRRVSEALKQ--VDMLERAdyEPNA------LSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 430 VGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGmSDRVYVMREGSIAGELNGKNI 484
Cdd:PRK13648 175 PDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
237-475 |
1.12e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.99 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 237 MMVGRPLSDLFNKerdiplgkARLNVHhLTDGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDG 316
Cdd:PRK14246 1 MEAGKSAEDVFNI--------SRLYLY-INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 317 EPVVIHSPREAIDLgigflTENRKEQGL-------FLEMAAAENITMATLERdarwGMLNRKKAQTISDDAIKLLNI-RV 388
Cdd:PRK14246 72 KVLYFGKDIFQIDA-----IKLRKEVGMvfqqpnpFPHLSIYDNIAYPLKSH----GIKEKREIKKIVEECLRKVGLwKE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 389 PHAQVR--AGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMaRKGVAILMISSELPEIVGMSDR 466
Cdd:PRK14246 143 VYDRLNspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADY 221
|
....*....
gi 13364550 467 VYVMREGSI 475
Cdd:PRK14246 222 VAFLYNGEL 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-200 |
1.28e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIdgkpfhirtpkdalsaGIT- 84
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI----------------GETv 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 -LIYQEMQ---LAPNLSVAENIFLGSELSHGGLVQrkemlVQAQKVIDRLGaqFNASD---KVMTLTIAEQQQVEIARAL 157
Cdd:TIGR03719 386 kLAYVDQSrdaLDPNKTVWEEISGGLDIIKLGKRE-----IPSRAYVGRFN--FKGSDqqkKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 158 HRNSRILVMDEPTAALSSrETHRLFELIMrLRDEGMAIIyISH 200
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDV-ETLRALEEAL-LNFAGCAVV-ISH 498
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
275-476 |
1.58e-10 |
|
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: 60.97 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAIDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-AAPPADRPVSMLF-----QENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMatlerdarwGMLNRKKAQTISDDAIKLLNIRVPHAQV---RAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:cd03298 92 GL---------GLSPGLKLTAEDRQAIEVALARVGLAGLekrLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13364550 432 AKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:cd03298 163 LRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-203 |
1.77e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 15 AFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK----------PFHIR-TPKDALSAGI 83
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpPRNVEgTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 tliyQEmqlapnlsVAENIFLGSELSHggLVQRKEM------LVQAQKVIDRLGA-QF-------------NASDKVMTL 143
Cdd:PRK11147 92 ----EE--------QAEYLKRYHDISH--LVETDPSeknlneLAKLQEQLDHHNLwQLenrinevlaqlglDPDAALSSL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 144 TIAEQQQVEIARALHRNSRILVMDEPTAALSSrETHRLFELImrLRDEGMAIIYISH------RMA 203
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDI-ETIEWLEGF--LKTFQGSIIFISHdrsfirNMA 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-223 |
2.35e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG---AYTATSGEILIDGKPFHIRTPKDaLSAGITLIYQEmqlapnls 97
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTAKTVWD-IREKVGIVFQN-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 98 vAENIFLGSELSHG---GL----VQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPT 170
Cdd:PRK13640 93 -PDNQFVGATVGDDvafGLenraVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 171 AALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVyELSDRVSVLRDGQYVGS 223
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQ 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
275-476 |
2.60e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.04 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREAIDLGIGFltenrkeQ--GLFLEMAAAE 352
Cdd:COG3842 25 SLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEKRNVGMVF-------QdyALFPHLTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NIT----MATLERDARwgmlnRKKAqtisDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGV 428
Cdd:COG3842 97 NVAfglrMRGVPKAEI-----RARV----AELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 429 DVGAK----SEIYRIMNEMarkGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:COG3842 167 DAKLReemrEELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
275-476 |
4.23e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.77 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGE----------PVVI---------H-SPREAIDLGI-- 332
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerPVSMlfqennlfpHlTVAQNIGLGLrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 333 -GFLTENRKEQglfLEMAAAE-NITmatlerdarwGMLNRKKAQtisddaikllnirvphaqvraggLSGGNQQKLLISR 410
Cdd:COG3840 99 gLKLTAEQRAQ---VEQALERvGLA----------GLLDRLPGQ-----------------------LSGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 411 wVAIGPR-ILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:COG3840 143 -CLVRKRpILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-465 |
5.21e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 5.21e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 398 LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEI-YRIMNEMARKGVAILMISSELPEIVGMSD 465
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVeSLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
260-474 |
6.15e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 260 LNVHHLTDGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGmIEVDGEPVVIHSPREaidLGI--GFLTE 337
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGS-IQFAGQPLEAWSAAE---LARhrAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 338 NRKE-------QGLFLEMAA--AENITMATLERDARWGMLNRKKAQTISDdaikllnirvphaqvraggLSGGNQQKL-- 406
Cdd:PRK03695 77 QQTPpfampvfQYLTLHQPDktRTEAVASALNEVAEALGLDDKLGRSVNQ-------------------LSGGEWQRVrl 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 407 ---LISRWVAIGP--RILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGS 474
Cdd:PRK03695 138 aavVLQVWPDINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
275-478 |
6.99e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.03 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTENRKEQglFLEmaaaeni 354
Cdd:PRK13635 27 SFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVFQNPDNQ--FVG------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tmATLERDARWGMLN----RKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:PRK13635 97 --ATVQDDVAFGLENigvpREEMVERVDQALRQVGMedflnREPHR------LSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 426 RGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEiVGMSDRVYVMREGSIAGE 478
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEqKGITVLSITHDLDE-AAQADRVIVMNKGEILEE 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-219 |
7.25e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEIlidgkpfhirtpkdALSAGI 83
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------------GLAKGI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLIYQEMQLAPNLSVAEniflgSELSHGGLVQRKEMlvqAQKVIDRLGAQFNASDKVMTLTI----AEQQQVEIARALHR 159
Cdd:PRK10636 376 KLGYFAQHQLEFLRADE-----SPLQHLARLAPQEL---EQKLRDYLGGFGFQGDKVTEETRrfsgGEKARLVLALIVWQ 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 160 NSRILVMDEPTAALSSRETHRLFELIMRLrdEGmAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
271-475 |
8.38e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.47 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPReaiDLGIGFLTENrkeQGLFLEMAA 350
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK---DRNIAMVFQS---YALYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITmatlerdarWGMLNRK-KAQTIS---DDAIKLLNIRvPHAQVRAGGLSGGNQQKllisrwVAIG------PRILL 420
Cdd:COG3839 93 YENIA---------FPLKLRKvPKAEIDrrvREAAELLGLE-DLLDRKPKQLSGGQRQR------VALGralvrePKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 421 LDEPARGVDvgAK------SEIYRIMNEMarkGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG3839 157 LDEPLSNLD--AKlrvemrAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-254 |
8.40e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.72 E-value: 8.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGK---FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDaLSAG 82
Cdd:PRK13642 4 ILEVENLVFKYEKesdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 83 ITLIYQ--EMQLApNLSVAENIFLGSElSHGglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRN 160
Cdd:PRK13642 83 IGMVFQnpDNQFV-GATVEDDVAFGME-NQG--IPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 161 SRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYElSDRVSVLRDGQYVGSLTRDNLNAG--ELVRM 237
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATseDMVEI 237
|
250 260
....*....|....*....|..
gi 13364550 238 MVGRPLS-----DLFNKERDIP 254
Cdd:PRK13642 238 GLDVPFSsnlmkDLRKNGFDLP 259
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-239 |
8.74e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDG---KPFHIRTPKDALSagitLIYQemqlAPNL-- 96
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiSKFGLMDLRKVLG----IIPQ----APVLfs 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 97 -SVAENIFLGSELSHGGLVqrkEMLVQA--QKVIDR--LGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTA 171
Cdd:PLN03130 1327 gTVRFNLDPFNEHNDADLW---ESLERAhlKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 172 ALSSReTHRLFELIMRLRDEGMAIIYISHRMAEVYElSDRVSVLRDGQYVGSLTRDNL--NAGELVRMMV 239
Cdd:PLN03130 1404 AVDVR-TDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLlsNEGSAFSKMV 1471
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
275-475 |
1.05e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlgigflteNRKEQGLFLEMAAAENI 354
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA----------SRRVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLNRKKAQTISDDAIkllnirVPHAQVRAG----------GLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:PRK09536 93 DVRQVVEMGRTPHRSRFDTWTETDRAA------VERAMERTGvaqfadrpvtSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13364550 425 ARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
275-478 |
1.38e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 60.56 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVvihspREaIDLG-----IGFLTenrkeQGLFL-EM 348
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI-----RD-LTLEslrrqIGVVP-----QDTFLfSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 349 AAAENI-------TMATLERDARwgmlnrkKAQtISDDAIKLlnirvPH---AQVRAGG--LSGGNQQKLLISRWVAIGP 416
Cdd:COG1132 429 TIRENIrygrpdaTDEEVEEAAK-------AAQ-AHEFIEAL-----PDgydTVVGERGvnLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 417 RILLLDEPARGVDVGAKSEIYRIMNEMaRKGVAILMISSELPEIVGMsDRVYVMREGSIAGE 478
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQ 555
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
275-476 |
1.71e-09 |
|
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: 57.93 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEpvvIHSPreaIDLGIGFLtenrkeqglfLEMAAAENI 354
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---VSSL---LGLGGGFN----------PELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMatlerDARWGMLNRKKAQTISDDAI------KLLNIRVPHaqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGV 428
Cdd:cd03220 106 YL-----NGRLLGLSRKEIDEKIDEIIefselgDFIDLPVKT-------YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13364550 429 DVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
275-467 |
1.89e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEpvvihspreaidLGIGFLTenrkeQGLFLEmaaaeni 354
Cdd:PRK09544 24 SLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LRIGYVP-----QKLYLD------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tmATLERDARWGMlnRKKAQTISDDAIKLLNiRVPHAQVRAG---GLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:PRK09544 80 --TTLPLTVNRFL--RLRPGTKKEDILPALK-RVQAGHLIDApmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 13364550 432 AKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRV 467
Cdd:PRK09544 155 GQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
275-475 |
1.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.66 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGV---RKATGGMIEVDGEPV---VIHSPREAIdlGIGFLTENRKEQGlflem 348
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLtakTVWDIREKV--GIVFQNPDNQFVG----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 349 aaaenitmATLERDARWGMLNR----KKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:PRK13640 100 --------ATVGDDVAFGLENRavprPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 425 ARGVDVGAKSEIYRIMNE-MARKGVAILMISSELPEIVgMSDRVYVMREGSI 475
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
283-475 |
1.96e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.48 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 283 IVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPReaidlgiGFLTENRKEQGLFLEmaAAENITMATLERD 362
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKR-------GLLALRQQVATVFQD--PEQQIFYTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 363 ARWGMLNRKKAQT-IS---DDAIKLLNI-RVPHAQVRAggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIY 437
Cdd:PRK13638 99 IAFSLRNLGVPEAeITrrvDEALTLVDAqHFRHQPIQC--LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 13364550 438 RIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK13638 177 AIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-152 |
1.97e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFG-KFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILidgkpfhirtpkdaLSAGIT 84
Cdd:PRK11819 6 IYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--------------PAPGIK 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 85 LIY--QEMQLAPNLSVAENIFLGselshgglVQRKemlVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVE 152
Cdd:PRK11819 72 VGYlpQEPQLDPEKTVRENVEEG--------VAEV---KAALDRFNEIYAAYAEPDADFDALAAEQGELQ 130
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
271-496 |
2.16e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.26 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPReAIDLGIGFLTEnrkeqglflEMAA 350
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK-AFARKVAYLPQ---------QLPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITMATLERDARW---GMLNRKKAQTIS--DDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:PRK10575 97 AEGMTVRELVAIGRYpwhGALGRFGAADREkvEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 426 RGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQENIMTLATGV 496
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGI 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-219 |
2.36e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAF----GKFYALKGVDLTVYPGEIHALMGENGAGKS----TLMKVLAgAYTATSGEILIDGKPFhIR 73
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-ANGRIGGSATFNGREI-LN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 74 TPKDAL----SAGITLIYQE--MQLAPNLSVAENIFLGSELsHGGLvQRKEMLVQAQKVIDrlGAQFNASDKVMTLTIAE 147
Cdd:PRK09473 86 LPEKELnklrAEQISMIFQDpmTSLNPYMRVGEQLMEVLML-HKGM-SKAEAFEESVRMLD--AVKMPEARKRMKMYPHE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 148 -----QQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK09473 162 fsggmRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
271-475 |
2.55e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.28 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfLTENRKEQGLFLEMAA 350
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAE--------LREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITMATLERDArWGM----LNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPAR 426
Cdd:PRK10070 116 ALMPHMTVLDNTA-FGMelagINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 427 GVDVGAKSEIY-RIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK10070 194 ALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-63 |
2.57e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 2.57e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEI 63
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-213 |
2.97e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 5 PVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFhirTPKDA------ 78
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIatrrrv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 --LSAGITLiYQEmqlapnLSVAENIFLGSELSHgglVQRKEmlvqAQKVIDRLGAQFNASDkVM-----TLTIAEQQQV 151
Cdd:NF033858 342 gyMSQAFSL-YGE------LTVRQNLELHARLFH---LPAAE----IAARVAEMLERFDLAD-VAdalpdSLPLGIRQRL 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 152 EIARA-LHRnSRILVMDEPT-----AAlssREthRLFELIMRL-RDEGMAiIYIS-HRMAEVyELSDRVS 213
Cdd:NF033858 407 SLAVAvIHK-PELLILDEPTsgvdpVA---RD--MFWRLLIELsREDGVT-IFIStHFMNEA-ERCDRIS 468
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
275-473 |
3.36e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 58.28 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGI---------GF-LTENRKEQGL 344
Cdd:PRK13537 27 SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVvpqfdnldpDFtVRENLLVFGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 345 FLEMAAAEnitmatlERDARWGMLNRKKAQTISDdaikllnirvphAQVRAggLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:PRK13537 107 YFGLSAAA-------ARALVPPLLEFAKLENKAD------------AKVGE--LSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 425 ARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-231 |
3.41e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGK--PFHIRTPKDA 78
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 79 LSAGITLIYQEMQLAPNLSVAENI-FLGSElsHGGL---VQRKEMLVQAQKVIDRLGAQFNASDkvmtLTIAEQQQVEIA 154
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVaYPLRE--HTQLpapLLHSTVMMKLEAVGLRGAAKLMPSE----LSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 155 RALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNA 231
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-214 |
3.83e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFGKFyalkgvDLTVYPGEIHA-----LMGENGAGKSTLMKVLAGAYTATSGEILID----GKPFHI 72
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDF------SLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisYKPQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 73 RTPkdalsagitliyQEMQLAPNL-SVAENI---FLGSELSHGglvqrkemlVQAQKVIDRlgaqfnasdKVMTLTIAEQ 148
Cdd:PRK13409 410 KPD------------YDGTVEDLLrSITDDLgssYYKSEIIKP---------LQLERLLDK---------NVKDLSGGEL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 149 QQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE-GMAIIYISHRMAEVYELSDRVSV 214
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMV 526
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
275-470 |
3.92e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.99 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRK----ATGGMIEVDGEPVVIHSPRE-----AIDLGIGF------LTENR 339
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRErrkiiGREIAMIFqepsscLDPSA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 340 K--EQglfLEmaaaENITMATLE----RDARWgmlnRKKAqtisddAIKLLNiRV------------PHAqvraggLSGG 401
Cdd:COG4170 107 KigDQ---LI----EAIPSWTFKgkwwQRFKW----RKKR------AIELLH-RVgikdhkdimnsyPHE------LTEG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 402 NQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVM 470
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-219 |
4.58e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.13 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 19 FYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIrtpkdALSAGitliyqemqLAPNLSV 98
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI-----AISAG---------LSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENIFLgSELSHGglVQRKEMLVQAQKVID--RLGaQFnASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSR 176
Cdd:PRK13546 103 IENIEF-KMLCMG--FKRKEIKAMTPKIIEfsELG-EF-IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 177 ETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQ 219
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
275-484 |
5.06e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.30 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTENRKEQ--GLFLEMAAA- 351
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQfvGRTVEEDLAf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 --ENITMATLErdarwgmLNRKKAQTISDDAIKLLNIRVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:PRK13644 102 gpENLCLPPIE-------IRKRVDRALAEIGLEKYRHRSPKT------LSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 430 VGAKSEIYRIMNEMARKGVAILMISSELPEIvGMSDRVYVMREGSIAGELNGKNI 484
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENV 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-219 |
5.20e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIrtPKDALsagitliyqeMQlapNLSVAEN 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYV--PQQAW----------IQ---NDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGSELSHgglvQRKEMLVQAQKVIDRL-----GAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSR 176
Cdd:TIGR00957 719 ILFGKALNE----KYYQQVLEACALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 177 ETHRLFELImrLRDEGM----AIIYISHRMAEVYELsDRVSVLRDGQ 219
Cdd:TIGR00957 795 VGKHIFEHV--IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGK 838
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
279-476 |
5.39e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.52 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 279 RSGEIVGLAGLVGAGRSELAQLIFGvRKATG----GMIEVDGEPV------VIHSPREAIDLGIGFLTEnrKEQGLFlem 348
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMPIdakemrAISAYVQQDDLFIPTLTV--REHLMF--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 349 aaaenitMATLERDARwgmLNRKKAQTISDDAIKLLNIRvPHAQVRAG------GLSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:TIGR00955 123 -------QAHLRMPRR---VTKKEKRERVDEVLQALGLR-KCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 423 EPARGVDVGAKSEIYRIMNEMARKG-VAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
275-476 |
6.05e-09 |
|
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: 58.22 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVViHSPREaiDLG--IGFL---TEnrkeqglFLEMA 349
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS-QWDRE--ELGrhIGYLpqdVE-------LFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 350 AAENItmatlerdARWGMLNRKKAQtisdDAIKLLNI-----RVPHA---QVRAGG--LSGGNQQKLLISRWVAIGPRIL 419
Cdd:COG4618 422 IAENI--------ARFGDADPEKVV----AAAKLAGVhemilRLPDGydtRIGEGGarLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 420 LLDEPARGVDVGAKSEIYRIMNEMARKGVAILMIsSELPEIVGMSDRVYVMREGSIA 476
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKARGATVVVI-THRPSLLAAVDKLLVLRDGRVQ 545
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
248-479 |
6.46e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.41 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 248 NKERDIPLGKARLNVHHLTDGGKV---QPSSLL-------VR--SGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVD 315
Cdd:PRK15079 2 TEGKKVLLEVADLKVHFDIKDGKQwfwQPPKTLkavdgvtLRlyEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 316 GEPVVIHSPREaidlgigfLTENRKE-QGLFLEMAAAENITMAT--------------LERDARwgmlnRKKAQTISDDA 380
Cdd:PRK15079 82 GKDLLGMKDDE--------WRAVRSDiQMIFQDPLASLNPRMTIgeiiaeplrtyhpkLSRQEV-----KDRVKAMMLKV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 381 IKLLNI--RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSEL 457
Cdd:PRK15079 149 GLLPNLinRYPHE------FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDL 222
|
250 260
....*....|....*....|..
gi 13364550 458 PEIVGMSDRVYVMREGSiAGEL 479
Cdd:PRK15079 223 AVVKHISDRVLVMYLGH-AVEL 243
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-223 |
6.71e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 19 FYALKGVDLTVYPGEIHALMGENGAGKS----TLMKVLAGAYTATSGEILIDGKPFHIRTPKDA---LSAGITLIYQE-- 89
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERrnlVGAEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 90 MQLAPNLSVAENIFLGSELSHGGlvQRKEmlvQAQKVIDRLgAQFNASDKVMTLTI-------AEQQQVEIARALHRNSR 162
Cdd:PRK11022 100 TSLNPCYTVGFQIMEAIKVHQGG--NKKT---RRQRAIDLL-NQVGIPDPASRLDVyphqlsgGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 163 ILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGS 223
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
275-484 |
6.92e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.02 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGepvvihspreaID-LGIGFLTENRKEQGLFLEmaAAEN 353
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-----------LDtSDEENLWDIRNKAGMVFQ--NPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 354 ITMATL-ERDARWGMLN----RKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:PRK13633 97 QIVATIvEEDVAFGPENlgipPEEIRERVDESLKKVGMyeyrrHAPHL------LSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 424 PARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVgMSDRVYVMREGSIAGELNGKNI 484
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAV-EADRIIVMDSGKVVMEGTPKEI 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-205 |
7.21e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 20 YALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIrtpkdALSAGitliyqemqLAPNLSVA 99
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI-----AISSG---------LNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSeLSHGglVQRKEMLVQAQKVID--RLGAQFNasDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRE 177
Cdd:PRK13545 104 ENIELKG-LMMG--LTKEKIKEIIPEIIEfaDIGKFIY--QPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTF 178
|
170 180
....*....|....*....|....*...
gi 13364550 178 THRLFELIMRLRDEGMAIIYISHRMAEV 205
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
397-475 |
8.16e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 8.16e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 397 GLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
274-475 |
8.18e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 274 SSLLVRSGEIVGLAGLVGAGRSELAQ--------------LIFG--VRKATGGMIEVDGEPVVIHSPREAidlGIGFLTE 337
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEhlnalllpdtgtieWIFKdeKNKKKTKEKEKVLEKLVIQKTRFK---KIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 338 NRKEQGLFLEMAAAEnITMATLERDARWGMLN----RKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVA 413
Cdd:PRK13651 103 IRRRVGVVFQFAEYQ-LFEQTIEKDIIFGPVSmgvsKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 414 IGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
242-475 |
8.40e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 242 PLSDLFNKERDIPLGKARLNVhhltdggkVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVi 321
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEV--------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 322 hspreaiDLGIGFLTENRKEQGLFL--------EMAAAENITM----ATLERDARwgmlnRKKAQTIsddAIKL-LNIRV 388
Cdd:PRK10535 74 -------TLDADALAQLRREHFGFIfqryhllsHLTAAQNVEVpavyAGLERKQR-----LLRAQEL---LQRLgLEDRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 389 PHaqvRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSElPEIVGMSDRVY 468
Cdd:PRK10535 139 EY---QPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVI 214
|
....*..
gi 13364550 469 VMREGSI 475
Cdd:PRK10535 215 EIRDGEI 221
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
243-460 |
9.29e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.59 E-value: 9.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 243 LSDLFNKERDIPLGKARLNVhhltdggkvqpsSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIh 322
Cdd:PRK13545 24 LKDLFFRSKDGEYHYALNNI------------SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 323 spreAIDLGIgflteNRKEQGLflemaaaENITMATLERDarwgmLNRKKAQTISDDAIKLLNI-RVPHAQVRAggLSGG 401
Cdd:PRK13545 91 ----AISSGL-----NGQLTGI-------ENIELKGLMMG-----LTKEKIKEIIPEIIEFADIgKFIYQPVKT--YSSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 402 NQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEI 460
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
274-476 |
1.02e-08 |
|
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: 55.25 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 274 SSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATG--GMIEVDGEPVVIHSPREAIdlgiGFLtenRKEQGLFLEMAAA 351
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKII----GYV---PQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 ENITMAtlerdarwgmlnrkkaqtisddaikllnirvphAQVRagGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:cd03213 101 ETLMFA---------------------------------AKLR--GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13364550 432 AKSEIYRIMNEMARKGVAILMISSELP-EIVGMSDRVYVMREGSIA 476
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-214 |
1.37e-08 |
|
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: 57.10 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 2 NSTPVLEMRNIAKAFGKFyalkgvDLTVYPGEIH-----ALMGENGAGKSTLMKVLAGAYTATSGEIL----IDGKPFHI 72
Cdd:COG1245 337 EEETLVEYPDLTKSYGGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkISYKPQYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 73 RTPkdalsagitliyQEMQLAPNLSVAENIFLGSELSHGGLVQRkemlVQAQKVIDRlgaqfnasdKVMTLTIAEQQQVE 152
Cdd:COG1245 411 SPD------------YDGTVEEFLRSANTDDFGSSYYKTEIIKP----LGLEKLLDK---------NVKDLSGGELQRVA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 153 IARALHRNSRILVMDEPTAALSSRETHRLFELIMRL-RDEGMAIIYISHRMAEVYELSDRVSV 214
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
271-475 |
2.18e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPV--------------VIHSPREAIDlgigflt 336
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyrsqrirmIFQDPSTSLN------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 337 eNRKEQGLFLEMAAAENITMATLERDARwgmlnrkkaqtiSDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGP 416
Cdd:PRK15112 102 -PRQRISQILDFPLRLNTDLEPEQREKQ------------IIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 417 RILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
278-477 |
2.35e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.41 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 278 VRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVdGEPVvIHSPREAIDL-------GIGFlteNRKEQGLFLEmaa 350
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERV-ITAGKKNKKLkplrkkvGIVF---QFPEHQLFEE--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 aenitmaTLERDARWGMLN----RKKAQTISDDAIKLLNI------RVPHAqvraggLSGGNQQKLLISRWVAIGPRILL 420
Cdd:PRK13634 102 -------TVEKDICFGPMNfgvsEEDAKQKAREMIELVGLpeellaRSPFE------LSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 421 LDEPARGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSIAG 477
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
275-475 |
3.03e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 54.47 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPV---VIHSPREAidlgIGFLTEnrkEQGLFlEMAAA 351
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlNLRWLRSQ----IGLVSQ---EPVLF-DGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 ENItmatlerdaRWGMLNRKKAQTISddAIKLLNI-----RVPHA---QVRAGG--LSGGNQQKLLISRWVAIGPRILLL 421
Cdd:cd03249 95 ENI---------RYGKPDATDEEVEE--AAKKANIhdfimSLPDGydtLVGERGsqLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 422 DEPARGVDVGAKSEIYRIMNEmARKGVAILMISSELPEIVGmSDRVYVMREGSI 475
Cdd:cd03249 164 DEATSALDAESEKLVQEALDR-AMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
275-475 |
3.80e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVV------IHspREAIDLGigfltenrKEQGLFlEM 348
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhyLH--RQVALVG--------QEPVLF-SG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 349 AAAENITMAtLERDARWGMLNRKKAQTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGV 428
Cdd:TIGR00958 570 SVRENIAYG-LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 429 DVGAKSEIYRIMNemaRKGVAILMISSELPeIVGMSDRVYVMREGSI 475
Cdd:TIGR00958 649 DAECEQLLQESRS---RASRTVLLIAHRLS-TVERADQILVLKKGSV 691
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-196 |
3.86e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 24 GVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPfhIRTPKDALSAgiTLIYQEMQLA--PNLSVAEN 101
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEYHQ--DLLYLGHQPGikTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGSELSHgglVQRKEMLVQAqkvIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRL 181
Cdd:PRK13538 95 LRFYQRLHG---PGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170
....*....|....*.
gi 13364550 182 FELIMR-LRDEGMAII 196
Cdd:PRK13538 169 EALLAQhAEQGGMVIL 184
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-475 |
3.91e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 395 AGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMaRKGVAILMISSELPEIVGMSDRVYVMREGS 474
Cdd:PRK14247 144 AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
.
gi 13364550 475 I 475
Cdd:PRK14247 223 I 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
275-476 |
4.02e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 53.57 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGepvvihspreaIDLGIGFLTENRKEQGLfleMAAAENI 354
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG-----------IDISTIPLEDLRSSLTI---IPQDPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLErdarwgmLNRKKAQTISDDAI-KLLnirvphaQVRAGG--LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:cd03369 94 FSGTIR-------SNLDPFDEYSDEEIyGAL-------RVSEGGlnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 432 AKSEIYRIMNEMArKGVAILMISSELPEIVGMsDRVYVMREGSIA 476
Cdd:cd03369 160 TDALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
275-475 |
4.33e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEV---DGEPVVIHSPREAIDLGI-----GFLTENrKEQGLFL 346
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRRLlrtewGFVHQH-PRDGLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 347 EMAAAENI---TMATLERdaRWGMLNRKKAQTISDDAIKLLNI-RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLD 422
Cdd:PRK11701 105 QVSAGGNIgerLMAVGAR--HYGDIRATAGDWLERVEIDAARIdDLPTT------FSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 423 EPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-429 |
4.37e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 26 DLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDgkpFHiRTPKDALSAGITLIYQEMQ------LAPN---- 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ---FS-HITRLSFEQLQKLVSDEWQrnntdmLSPGeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 96 -LSVAENIFLGSELShgglvQRKEMLVQAQKVIDRLGAQFnasdkvMTLTIAEQQQVEIARALHRNSRILVMDEPTAALS 174
Cdd:PRK10938 99 gRTTAEIIQDEVKDP-----ARCEQLAQQFGITALLDRRF------KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 175 SRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMV-GRPLSDLFNKERDI 253
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAhSEQLEGVQLPEPDE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 254 PLGKARLN--------------------VHHLtdggkvqpsSLLVRSGEIVGLAGLVGAGRSELAQLI------------ 301
Cdd:PRK10938 248 PSARHALPaneprivlnngvvsyndrpiLHNL---------SWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndl 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 302 --FGVRKATGGMIevdgepvvihsprEAIDLGIGFLTENrkeqgLFLEM---AAAEN-----------ITMATLERdarw 365
Cdd:PRK10938 319 tlFGRRRGSGETI-------------WDIKKHIGYVSSS-----LHLDYrvsTSVRNvilsgffdsigIYQAVSDR---- 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 366 gmlNRKKAQTISDdaikLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:PRK10938 377 ---QQKLAQQWLD----ILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
218-457 |
5.13e-08 |
|
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: 55.44 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 218 GQYVGSLTRDNlnagELVRMMVGRPLSDlFNKERDIPLGKARLNVHHLTDGGKVQPS-----SLLVRSGEIVGLAGLVGA 292
Cdd:TIGR02868 298 TRVRAAAERIV----EVLDAAGPVAEGS-APAAGAVGLGKPTLELRDLSAGYPGAPPvldgvSLDLPPGERVAILGPSGS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 293 GRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIGFLTENRKeqgLFlEMAAAENITMATLE--RDARWGMLNR 370
Cdd:TIGR02868 373 GKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE-VRRRVSVCAQDAH---LF-DTTVRENLRLARPDatDEELWAALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 371 KKAQTISDDAIKLLNIRVphaQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEmARKGVAI 450
Cdd:TIGR02868 448 VGLADWLRALPDGLDTVL---GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTV 523
|
....*..
gi 13364550 451 LMISSEL 457
Cdd:TIGR02868 524 VLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-211 |
7.20e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 23 KGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfhiRTPKDA----LSAGITLIYQEMQLAPNlSV 98
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS----HNLKDInlkwWRSKIGVVSQDPLLFSN-SI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 99 AENI-----------FLGSELSHGGLVQRKEM-------------------------LVQAQKVIDRLGAQ--FNASDKV 140
Cdd:PTZ00265 477 KNNIkyslyslkdleALSNYYNEDGNDSQENKnkrnscrakcagdlndmsnttdsneLIEMRKNYQTIKDSevVDVSKKV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 141 M---------------------TLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLR-DEGMAIIYI 198
Cdd:PTZ00265 557 LihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIII 636
|
250
....*....|....*....
gi 13364550 199 SHRMA------EVYELSDR 211
Cdd:PTZ00265 637 AHRLStiryanTIFVLSNR 655
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
283-475 |
8.59e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 283 IVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVihspreAIDLGIGFLTENRK------EQGLFLEMAAAENItm 356
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF------DAEKGICLPPEKRRigyvfqDARLFPHYKVRGNL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 357 atlerdaRWGMLNRKKAQTisDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:PRK11144 98 -------RYGMAKSMVAQF--DKIVALLGIeplldRYPGS------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 432 AKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK11144 163 RKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-242 |
1.30e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 7 LEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTlmkvlaGAYTATSGEILIDGKPFHIRT---PKDALSAGI 83
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHV*GPDAGRRPWRF*TwcaNRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 84 TLiYQEMQLA--PNLSVAENIFL-GSELShgglVQRKEMLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRN 160
Cdd:NF000106 88 G*-HRPVR*GrrESFSGRENLYMiGR*LD----LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 161 SRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRMAEVYELSDRVSVLRDGQYVGSLTRDNLNAGELVRMMVG 240
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQI 242
|
..
gi 13364550 241 RP 242
Cdd:NF000106 243 RP 244
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
275-475 |
1.33e-07 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 52.62 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPV---VIHSPREAIDLgigfltenrKEQGLFL-EMAA 350
Cdd:cd03251 22 SLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASLRRQIGL---------VSQDVFLfNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENItmatlerdaRWGMLNRKKAQTIsdDAIKLLN-----IRVP---HAQV--RAGGLSGGNQQKLLISRWVAIGPRILL 420
Cdd:cd03251 93 AENI---------AYGRPGATREEVE--EAARAANahefiMELPegyDTVIgeRGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 421 LDEPARGVDVGAKSEIYRIMNEMArKGVAILMISSELPEIVGmSDRVYVMREGSI 475
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
275-488 |
1.51e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.82 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlgigfltenRKEQGLFLEmAAAENI 354
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-----------RSKVGLVFQ-DPDDQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDARWGMLN----RKKAQTISDDAIKLLNI-----RVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:PRK13647 93 FSSTVWDDVAFGPVNmgldKDEVERRVEEALKAVRMwdfrdKPPYH------LSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 426 RGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGE-----LNGKNITQEN 488
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEgdkslLTDEDIVEQA 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
271-475 |
1.81e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.88 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfLTENRKEQG------- 343
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE--------LRKARRQIGmifqhfn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 344 LFLEMAAAENITMAtLERDarwgmlNRKKAQtISDDAIKLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILL 420
Cdd:PRK11153 93 LLSSRTVFDNVALP-LELA------GTPKAE-IKARVTELLE-LVglsDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 421 LDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
275-475 |
1.89e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.01 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEpvvIHSPreaIDLGIGFltenrkeQGlflEMAAAENI 354
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---VSAL---LELGAGF-------HP---ELTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMAtlerdARwgMLNRKKAQT------ISD-----DAIkllnirvpHAQVRAggLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:COG1134 110 YLN-----GR--LLGLSRKEIdekfdeIVEfaelgDFI--------DQPVKT--YSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 424 parGVDVG-----AKSeiYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG1134 173 ---VLAVGdaafqKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-478 |
4.10e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 398 LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKgVAILMISSELPEIVGMSDRVYVMREGSIAG 477
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
.
gi 13364550 478 E 478
Cdd:PRK14271 243 E 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
260-473 |
4.15e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.17 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 260 LNVHHLTDG-GK---VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidLG--IG 333
Cdd:PRK11231 3 LRTENLTVGyGTkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LArrLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 334 FLTEnrkeqglflEMAAAENITMATLERDAR------WGMLNRKKAQTIsDDAIKLLNIrVPHAQVRAGGLSGGNQQKLL 407
Cdd:PRK11231 80 LLPQ---------HHLTPEGITVRELVAYGRspwlslWGRLSAEDNARV-NQAMEQTRI-NHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13364550 408 ISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
275-476 |
4.21e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 51.40 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVviHSPreAIDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:COG4525 27 SLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGP--GADRGVVF-----QKDALLPWLNVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 T----MATLERDARwgmlnrkkaQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPargvdV 430
Cdd:COG4525 98 AfglrLRGVPKAER---------RARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP-----F 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 431 GAKSEIYR-IMNEM-----ARKGVAILMISSELPEIVGMSDRVYVM--REGSIA 476
Cdd:COG4525 163 GALDALTReQMQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIV 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-65 |
4.35e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 4.35e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILI 65
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
253-470 |
4.90e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 253 IPLGKAR-LNVHHLTDGGKVQPS---SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRK----ATGGMIEVDGEPVVIHSP 324
Cdd:PRK15093 1 MPLLDIRnLTIEFKTSDGWVKAVdrvSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 325 REaidlgigflteNRKEQG-----LFLE----MAAAENITMATLERDARWGMLNR--KKAQTISDDAIKLLN---IRVPH 390
Cdd:PRK15093 81 RE-----------RRKLVGhnvsmIFQEpqscLDPSERVGRQLMQNIPGWTYKGRwwQRFGWRKRRAIELLHrvgIKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 391 AQVRAGG--LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRV 467
Cdd:PRK15093 150 DAMRSFPyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKI 229
|
...
gi 13364550 468 YVM 470
Cdd:PRK15093 230 NVL 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
271-473 |
6.03e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.95 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSelaQLIFGVRKATGGMIEVDGEpvvIHSPreaidlGIGFLTENRKEQGLFLeMAA 350
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCS---TLLKALANRTEGNVSVEGD---IHYN------GIPYKEFAEKYPGEII-YVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENITMATLerdarwgmlnrKKAQTIsDDAIKLLNirvpHAQVRagGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDV 430
Cdd:cd03233 90 EEDVHFPTL-----------TVRETL-DFALRCKG----NEFVR--GISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 431 GAKSEIYRIMNEMAR--KGVAILMISSELPEIVGMSDRVYVMREG 473
Cdd:cd03233 152 STALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-200 |
6.93e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 27 LTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDG-------KPFhirtpkdalsagITLIYQEMQLAPNLSVA 99
Cdd:PRK13541 21 ITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPY------------CTYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 100 ENIFLGSELSHGglVQRKEMLVQAQKVIDRLgaqfnaSDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETH 179
Cdd:PRK13541 89 ENLKFWSEIYNS--AETLYAAIHYFKLHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180
....*....|....*....|.
gi 13364550 180 RLFELIMRLRDEGMAIIYISH 200
Cdd:PRK13541 161 LLNNLIVMKANSGGIVLLSSH 181
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
275-476 |
7.04e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 50.35 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAiDLGIGFltenrKEQGLFLEMAAAENI 354
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR-PVSMLF-----QENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMatlerdarwGM-----LNRKKAQTISDDAIK-----LLNiRVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:PRK10771 93 GL---------GLnpglkLNAAQREKLHAIARQmgiedLLA-RLPGQ------LSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 425 ARGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQeRQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
275-470 |
7.19e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 51.27 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfltenrkeqglflemaaaeni 354
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRE---------------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tMATLERDAR------WGMLN-RKKAQTISDDAIKLLNI-------------------------RVPHAqvraggLSGGN 402
Cdd:COG4608 90 -LRPLRRRMQmvfqdpYASLNpRMTVGDIIAEPLRIHGLaskaerrervaellelvglrpehadRYPHE------FSGGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 403 QQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVM 470
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-211 |
7.28e-07 |
|
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: 48.90 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLagaytatsgeILIDGKPFHIRTPKDALSAGITLIYQEMQLapnlsvaen 101
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAI----------GLALGGAQSATRRRSGVKAGCIVAAVSAEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGSELSHGglvqrkemlvqaqkvidrlgaqfnASDKVMTLTIaeqqqveIARALHRNSRILVMDEPTAALSSRETHRL 181
Cdd:cd03227 72 IFTRLQLSGG------------------------EKELSALALI-------LALASLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|
gi 13364550 182 FELIMRLRDEGMAIIYISHRmAEVYELSDR 211
Cdd:cd03227 121 AEAILEHLVKGAQVIVITHL-PELAELADK 149
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
282-475 |
1.04e-06 |
|
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: 51.55 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 282 EIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvIHSPREAIDLGIGFLTENRKeqgLFLEMAAAENITMATLER 361
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD--IETNLDAVRQSLGMCPQHNI---LFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 362 DARWGMLNRKKAQTISDDAikLLNIRVPHAQvragGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMN 441
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTG--LHHKRNEEAQ----DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|....
gi 13364550 442 EMaRKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:TIGR01257 1106 KY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
275-475 |
1.08e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 50.46 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfLTENRKEQG-------LFLE 347
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE--------LRAARRKIGmifqhfnLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENITMAtLErdaRWGMlnrKKAQtISDDAIKLLNiRV---PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:COG1135 97 RTVAENVALP-LE---IAGV---PKAE-IRKRVAELLE-LVglsDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 425 ARGVDVGAKSEIYRIMNEMARK-GVAILMISSElpeivgMS------DRVYVMREGSI 475
Cdd:COG1135 168 TSALDPETTRSILDLLKDINRElGLTIVLITHE------MDvvrricDRVAVLENGRI 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
282-490 |
1.17e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.77 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 282 EIVGLAGLVGAGRSELAQLI-----FGVRKATGGMIEVDGEPvvIHSPR-EAIDLgigfltenRKEQGLFLE------MA 349
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHN--IYSPRtDTVDL--------RKEIGMVFQqpnpfpMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 350 AAENITmatlerdarWGM-LNRKKAQTISDDAIK--LLNIRV-----PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLL 421
Cdd:PRK14239 102 IYENVV---------YGLrLKGIKDKQVLDEAVEksLKGASIwdevkDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 422 DEPARGVDVGAKSEIYRIMNEMaRKGVAILMISSELPEIVGMSDRVYVMregsIAGELNGKNITQENIM 490
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFF----LDGDLIEYNDTKQMFM 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
280-475 |
1.35e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 49.63 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 280 SGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIH---SPREAIDL----GIGFLTENrkeqgLFLEMAAAE 352
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqkpSEKAIRLLrqkvGMVFQQYN-----LWPHLTVME 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NITMATLerdaRWGMLNRKKAQtisDDAIKLLN-IRV-PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDV 430
Cdd:COG4161 102 NLIEAPC----KVLGLSKEQAR---EKAMKLLArLRLtDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13364550 431 GAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:COG4161 175 EITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-173 |
1.56e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 1 MNSTPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfHIRTPKDALS 80
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRSRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 81 agITLIYQEMQLAPNLSVAENIFLGSELsHGGLVQRkeMLVQAQKVIdrlGAQFNASDKVMTLTIAEQQQVEIARALHRN 160
Cdd:PRK13543 84 --MAYLGHLPGLKADLSTLENLHFLCGL-HGRRAKQ--MPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|...
gi 13364550 161 SRILVMDEPTAAL 173
Cdd:PRK13543 156 APLWLLDEPYANL 168
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
276-503 |
1.86e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 276 LLVRSGEIVGLAGLVGAGRSELAQLIFGV---RKATGGMIEVDGEpVVIHSPREAIDLgigflTENRKEQGLFLE----- 347
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGR-TVQREGRLARDI-----RKSRANTGYIFQqfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 --MAAAENITMATLERDARWGMLNRKKAQTISDDAIKLLN-IRVPH-AQVRAGGLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:PRK09984 99 nrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTrVGMVHfAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 424 PARGVDvgakSEIYRIMNEMAR-----KGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNITQENIMTLATGVND 498
Cdd:PRK09984 179 PIASLD----PESARIVMDTLRdinqnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINR 254
|
....*
gi 13364550 499 AHSQA 503
Cdd:PRK09984 255 VEENA 259
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
276-475 |
2.05e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.29 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 276 LLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvIHSPREAIDL-----------------GIGfLTEN 338
Cdd:PRK11247 33 LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP--LAEAREDTRLmfqdarllpwkkvidnvGLG-LKGQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 339 RKEQGLflemAAAENITMAtlERDARWgmlnrkkaqtisddaikllnirvPHAqvraggLSGGNQQKLLISRWVAIGPRI 418
Cdd:PRK11247 110 WRDAAL----QALAAVGLA--DRANEW-----------------------PAA------LSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 419 LLLDEPargvdVGAKSEIYRI-MNEM-----ARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK11247 155 LLLDEP-----LGALDALTRIeMQDLieslwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-233 |
2.15e-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: 49.14 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHiRTPKDALSAGITLIYQEMQLAPNlSVAEN 101
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS-KLPLHTLRSRLSIILQDPILFSG-SIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGSELSHGGLVQRKEmLVQAQKVIDRLGAQFNA--SDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETH 179
Cdd:cd03288 115 LDPECKCTDDRLWEALE-IAQLKNMVKSLPGGLDAvvTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 180 RLFELIMRLRDEgMAIIYISHRMAEVYElSDRVSVLRDGQYVGSLTRDNLNAGE 233
Cdd:cd03288 194 ILQKVVMTAFAD-RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
231-475 |
2.21e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.10 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 231 AGELVRMMVGRPLSDLFNKERdiPLGKARLNVHHLT----DGGKV-QPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVR 305
Cdd:PRK10790 314 AGERVFELMDGPRQQYGNDDR--PLQSGRIDIDNVSfayrDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 306 KATGGMIEVDGEPVVIHSPReAIDLGIGFLtenrKEQGLFLEMAAAENITMA-TLERDARWGMLNRKK----AQTISDDA 380
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHS-VLRQGVAMV----QQDPVVLADTFLANVTLGrDISEEQVWQALETVQlaelARSLPDGL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 381 ikllnirvpHAQVRAGG--LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMnEMARKGVAILMISSELP 458
Cdd:PRK10790 467 ---------YTPLGEQGnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAHRLS 536
|
250
....*....|....*..
gi 13364550 459 EIVGmSDRVYVMREGSI 475
Cdd:PRK10790 537 TIVE-ADTILVLHRGQA 552
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
281-473 |
2.42e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 281 GEIVGLAGLVGAGRSELAQLIFGVRKA---TGGMIEVDGEPVvihsprEAIDLGIGFLTEnrkEQGLFLEMAAAENITMA 357
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnfTGTILANNRKPT------KQILKRTGFVTQ---DDILYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 358 TLERDARwgMLNRKKAQTISDDAIKLL------NIRVPHAQVRagGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:PLN03211 165 SLLRLPK--SLTKQEKILVAESVISELgltkceNTIIGNSFIR--GISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 432 AKSEIYRIMNEMARKGVAILM-ISSELPEIVGMSDRVYVMREG 473
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEG 283
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
275-475 |
2.60e-06 |
|
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: 50.12 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVV---IHSPREAID-------LGIGFLTENrkeqgl 344
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidRHTLRQFINylpqepyIFSGSILEN------ 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 345 fLEMAAAENITMATLERDARWGmlnrkkaqTISDDAIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEP 424
Cdd:TIGR01193 568 -LLLGAKENVSQDEIWAACEIA--------EIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13364550 425 ARGVDVGAKSEIyrIMNEMARKGVAILMISSELpEIVGMSDRVYVMREGSI 475
Cdd:TIGR01193 639 TSNLDTITEKKI--VNNLLNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
112-212 |
3.22e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 112 GLVQRKEMLVQaqkvidrLGAQFNASDKVM-TLTIAEQQQVEIARalHRNSRIL----VMDEPTAALSSRETHRLFELIM 186
Cdd:PRK00635 452 GLKSRLSILID-------LGLPYLTPERALaTLSGGEQERTALAK--HLGAELIgityILDEPSIGLHPQDTHKLINVIK 522
|
90 100
....*....|....*....|....*.
gi 13364550 187 RLRDEGMAIIYISHRmAEVYELSDRV 212
Cdd:PRK00635 523 KLRDQGNTVLLVEHD-EQMISLADRI 547
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
394-475 |
3.57e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.46 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 394 RAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDvgAKSEiYRIMN--EMARKGVAILMISSELPEIVGMsDRVYVMR 471
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSE-QLVMQalNAASRRQTTLMVTHQLEDLAQW-DQIWVMQ 557
|
....
gi 13364550 472 EGSI 475
Cdd:PRK11174 558 DGQI 561
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
276-475 |
4.15e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 276 LLVRSGEIVGLAGLVGAGRSELAQLIFG--VRKATGGMIEVDGEPVVIHSPreaidlgigfltENRKEQGLFL------E 347
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEP------------EERAHLGIFLafqypiE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENITMATLERDARwgmlnRKKAQTISDDAIKLLNIRVP------------HAQVRAGgLSGGNQQKLLISRWVAIG 415
Cdd:CHL00131 96 IPGVSNADFLRLAYNSK-----RKFQGLPELDPLEFLEIINEklklvgmdpsflSRNVNEG-FSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 416 PRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMIS--SELPEIVgMSDRVYVMREGSI 475
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyQRLLDYI-KPDYVHVMQNGKI 230
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
140-200 |
4.33e-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: 48.02 E-value: 4.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 140 VMTLTIAEQQQVEIARALHRN--SRILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH 200
Cdd:cd03270 135 APTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
291-476 |
4.38e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.81 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 291 GAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDL--GIGFLTEN-------RKEQGLFLEMAAAENITMATLER 361
Cdd:PRK11308 51 GCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQNpygslnpRKKVGQILEEPLLINTSLSAAER 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 362 darwgmlnRKKAQTIsddaIKLLNIRVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMN 441
Cdd:PRK11308 131 --------REKALAM----MAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMM 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 13364550 442 EMARK-GVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:PRK11308 199 DLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
258-484 |
4.46e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.44 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 258 ARLNVHHLTDG-GK---VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaIDLGIG 333
Cdd:PRK10253 6 ARLRGEQLTLGyGKytvAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 334 FLTENRKEQGlflEMAAAENITMATLERD---ARWgmlnRKKAQTISDDAIKLLNIRVPHAQvRAGGLSGGNQQKLLISR 410
Cdd:PRK10253 85 LLAQNATTPG---DITVQELVARGRYPHQplfTRW----RKEDEEAVTKAMQATGITHLADQ-SVDTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 411 WVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEIVGMSDRVYVMREGSIAGELNGKNI 484
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
395-425 |
4.74e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.11 E-value: 4.74e-06
10 20 30
....*....|....*....|....*....|.
gi 13364550 395 AGGLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
260-478 |
5.11e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 260 LNVHHLTDG---GKVQPS-----SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDL- 330
Cdd:PRK10584 7 VEVHHLKKSvgqGEHELSiltgvELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 331 --GIGFLTENRKeqgLFLEMAAAENITMATLERdarwGMLNRKKAQtisdDAIKLLNI-----RVPH--AQvraggLSGG 401
Cdd:PRK10584 87 akHVGFVFQSFM---LIPTLNALENVELPALLR----GESSRQSRN----GAKALLEQlglgkRLDHlpAQ-----LSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 402 NQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
275-476 |
5.63e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 47.84 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPRE----------AIDLGIGFLTEnrkeqgl 344
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrravlpqHSSLSFPFTVE------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 345 flemaaaENITMATlerdARWGmLNRKKAQTISDDAIkllnirvphAQVRAGG--------LSGGNQQKLLISR-----W 411
Cdd:PRK13548 95 -------EVVAMGR----APHG-LSRAEDDALVAAAL---------AQVDLAHlagrdypqLSGGEQQRVQLARvlaqlW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 412 -VAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIA 476
Cdd:PRK13548 154 ePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
275-429 |
7.88e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAIDLGIGFLTenrkeQGL----FLEMAA 350
Cdd:NF033858 21 SLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMP-----QGLgknlYPTLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENIT-MATL------ERDARWGMLNRkkaqtisddAIKLLnirvPHAQVRAGGLSGGNQQKL-----LISrwvaiGPRI 418
Cdd:NF033858 96 FENLDfFGRLfgqdaaERRRRIDELLR---------ATGLA----PFADRPAGKLSGGMKQKLglccaLIH-----DPDL 157
|
170
....*....|.
gi 13364550 419 LLLDEPARGVD 429
Cdd:NF033858 158 LILDEPTTGVD 168
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-212 |
1.02e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 21 ALKGVDLTVYPGEIHALMGENGAGKSTLmkVLAGAYTatSGEILIDGKPfhirtpkdalsagitliyqemqlaPNLSVAE 100
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA--SGKARLISFL------------------------PKFSRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGselshgglvqrkemlvQAQKVIDrLGAQFNASDKVM-TLTIAEQQQVEIARALHRNSR--ILVMDEPTAALSSRE 177
Cdd:cd03238 62 LIFID----------------QLQFLID-VGLGYLTLGQKLsTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*
gi 13364550 178 THRLFELIMRLRDEGMAIIYISHRMaEVYELSDRV 212
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWI 158
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
275-475 |
1.14e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 47.90 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvIHSPREA------------IDLGIGFLTENrkeq 342
Cdd:PRK11160 360 SLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP--IADYSEAalrqaisvvsqrVHLFSATLRDN---- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 343 gLFLemaAAENITMATLErdarwGMLNRKKAQTISDDAiKLLNirvphAQVRAGG--LSGGNQQKLLISRWVAIGPRILL 420
Cdd:PRK11160 434 -LLL---AAPNASDEALI-----EVLQQVGLEKLLEDD-KGLN-----AWLGEGGrqLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 421 LDEPARGVDVGAKSEIYRIMNEMArKGVAILMISSELPEIVGMsDRVYVMREGSI 475
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
260-464 |
1.22e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.00 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 260 LNVHHLTD--GGK--VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVihSPreAIDLGIGFl 335
Cdd:PRK11248 2 LQISHLYAdyGGKpaLEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GP--GAERGVVF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 336 tenrKEQGLFLEMAAAENIT----MATLERDARwgmlnRKKAQtisdDAIKLLNIRVPHAQvRAGGLSGGNQQKLLISRW 411
Cdd:PRK11248 77 ----QNEGLLPWRNVQDNVAfglqLAGVEKMQR-----LEIAH----QMLKKVGLEGAEKR-YIWQLSGGQRQRVGIARA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13364550 412 VAIGPRILLLDEPARGVDVGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGMS 464
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMA 196
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
275-478 |
1.26e-05 |
|
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: 46.66 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPvvIHS----PREAI---DLGIGFltenRKEQgLFLE 347
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFAldedARARLrarHVGFVF----QSFQ-LLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENItMATLE----RDARwgmlnrkkaqtisDDAIKLLnirvphAQV----RA----GGLSGGNQQKLLISRWVAIG 415
Cdd:COG4181 105 LTALENV-MLPLElagrRDAR-------------ARARALL------ERVglghRLdhypAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 416 PRILLLDEPARGVDvGAKSEiyRIMNEM----ARKGVAILMISSElPEIVGMSDRVYVMREGSIAGE 478
Cdd:COG4181 165 PAILFADEPTGNLD-AATGE--QIIDLLfelnRERGTTLVLVTHD-PALAARCDRVLRLRAGRLVED 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
263-486 |
1.37e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 263 HHLTDGGKVQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPRE------AIDLGIGFLT 336
Cdd:PRK10522 331 AYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklfsAVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 337 ENRKEQGLFLEMAAAENitmaTLERdarwgmLNRKKAQTISDDaiKLLNIRvphaqvraggLSGGNQQKLLISRWVAIGP 416
Cdd:PRK10522 411 QLLGPEGKPANPALVEK----WLER------LKMAHKLELEDG--RISNLK----------LSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13364550 417 RILLLDEPARGVDVGAKSEIYR-IMNEMARKGVAILMISSElPEIVGMSDRVYVMREGSIAgELNGKNITQ 486
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLS-ELTGEERDA 537
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
398-475 |
1.39e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 1.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13364550 398 LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
368-475 |
1.42e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.55 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 368 LNRKKAQTisdDAIKLLN-IRV-PHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMAR 445
Cdd:PRK11124 113 LSKDQALA---RAEKLLErLRLkPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE 189
|
90 100 110
....*....|....*....|....*....|
gi 13364550 446 KGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK11124 190 TGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
368-478 |
1.63e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 368 LNRKKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKG 447
Cdd:NF000106 116 LSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG 194
|
90 100 110
....*....|....*....|....*....|.
gi 13364550 448 VAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
398-446 |
1.81e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 46.31 E-value: 1.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 13364550 398 LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARK 446
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
275-475 |
1.88e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.26 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGE---PVVIHSPREAIdlGIGFltenrKEQGLFlEMAAA 351
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirTVTRASLRRNI--AVVF-----QDAGLF-NRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 ENITM----ATLE--RDArwgmLNRKKAQTISDDAIKLLNIRVPHaqvRAGGLSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:PRK13657 427 DNIRVgrpdATDEemRAA----AERAQAHDFIERKPDGYDTVVGE---RGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 426 RGVDVGAKSEIYRIMNEMaRKGVAILMISSELPEIVGmSDRVYVMREGSI 475
Cdd:PRK13657 500 SALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
275-475 |
1.93e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGepvvihspreaIDLGIGFLTENRK------EQGLFLEM 348
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-----------CDVAKFGLTDLRRvlsiipQSPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 349 AAAENITMATLERDAR-WGMLNRKKAQTISDDAIKLLNirvphAQVRAGG--LSGGNQQKLLISRWVAIGPRILLLDEPA 425
Cdd:PLN03232 1325 TVRFNIDPFSEHNDADlWEALERAHIKDVIDRNPFGLD-----AEVSEGGenFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13364550 426 RGVDVGAKSEIYRIMNEmARKGVAILMISSELPEIVGmSDRVYVMREGSI 475
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-102 |
2.23e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKPFHIRTPKDALSAGITL 85
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90
....*....|....*....
gi 13364550 86 IYQEM--QLAPNLSVAENI 102
Cdd:NF033858 81 MPQGLgkNLYPTLSVFENL 99
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-218 |
2.34e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYT-ATSGEILIDGKPfhirtpkdALSAGITLIYqemqlapNLSVAE 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVVIRGSV--------AYVPQVSWIF-------NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 101 NIFLGSELSHGglvqrkemlvQAQKVIDRLGAQ-----FNASDKV------MTLTIAEQQQVEIARALHRNSRILVMDEP 169
Cdd:PLN03232 698 NILFGSDFESE----------RYWRAIDVTALQhdldlLPGRDLTeigergVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13364550 170 TAALSSRETHRLFELIMRLRDEGMAIIYISHRMaEVYELSDRVSVLRDG 218
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEG 815
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
280-452 |
2.38e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 280 SGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAID-LGigfltenrKEQGLFLEMAAAENITMat 358
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG--------HRNAMKPALTVAENLEF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 359 lerdarWGMLNRKKAQTIsDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYR 438
Cdd:PRK13539 97 ------WAAFLGGEELDI-AAALEAVGLA-PLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
170
....*....|....
gi 13364550 439 IMNEMARKGVAILM 452
Cdd:PRK13539 169 LIRAHLAQGGIVIA 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
395-475 |
2.53e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.99 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 395 AGGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMaRKGVAILMISSELPEIVGMSDRVYVMREGS 474
Cdd:PRK14267 147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGK 225
|
.
gi 13364550 475 I 475
Cdd:PRK14267 226 L 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-215 |
2.83e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 32 GEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDgkpfhirtpkdalsaGITLIYqemqlapnlsvaeniflgselshg 111
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD---------------GITPVY------------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 112 glvqrkemlvQAQKVidrlgaqfnasdkvmTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELIMRLRDE 191
Cdd:cd03222 66 ----------KPQYI---------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*
gi 13364550 192 GM-AIIYISHRMAEVYELSDRVSVL 215
Cdd:cd03222 121 GKkTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
275-476 |
3.00e-05 |
|
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: 45.18 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEP---VVIHSPREAIDLgI--------GFLTENRKEQG 343
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskIGLHDLRSRISI-IpqdpvlfsGTIRSNLDPFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 344 LFLEmaaaenitmatlerDARWGMLNRKKAQTISDDAIKLLNirvphAQVRAGG--LSGGNQQKLLISRWVAIGPRILLL 421
Cdd:cd03244 103 EYSD--------------EELWQALERVGLKEFVESLPGGLD-----TVVEEGGenLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 422 DEPARGVDVGAKSEIYRIMNEmARKGVAILMISSELPEIVGmSDRVYVMREGSIA 476
Cdd:cd03244 164 DEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-169 |
3.29e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 4 TPVLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAG----AYTAT---------SGEILIDGKPf 70
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqGYSNDltlfgrrrgSGETIWDIKK- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 71 HIrtpkDALSAGITLIYQemqlaPNLSVaENIFLGSELSHGGLVQ----RKEMLvqAQKVIDRLGAQFNASDK-VMTLTI 145
Cdd:PRK10938 337 HI----GYVSSSLHLDYR-----VSTSV-RNVILSGFFDSIGIYQavsdRQQKL--AQQWLDILGIDKRTADApFHSLSW 404
|
170 180
....*....|....*....|....
gi 13364550 146 AEQQQVEIARALHRNSRILVMDEP 169
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEP 428
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
266-475 |
3.33e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.46 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 266 TDGGKVQPSSLLVRSGEIVGLAGLVGAGRS-----ELAQLIFGVRKaTGGMIEVDGEPV------------VIHSPREAI 328
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVapcalrgrkiatIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 329 DlGIGFLTENRKEQGLFLEMAAAENITMATLErdarwgmlnrkkAQTISDDAikllniRVPhaQVRAGGLSGGNQQKLLI 408
Cdd:PRK10418 93 N-PLHTMHTHARETCLALGKPADDATLTAALE------------AVGLENAA------RVL--KLYPFEMSGGMLQRMMI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 409 SRWVAIGPRILLLDEPARGVDVGAKSEIYR-IMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDlLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
276-475 |
4.16e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 45.13 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 276 LLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVdGEpVVIHSPR---------EAIDLGIGFLTENRKeqgLFL 346
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GD-ITIDTARslsqqkgliRQLRQHVGFVFQNFN---LFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 347 EMAAAENItmatLErdarwGMLNRKKaqTISDDAIKLlnIRVPHAQVRAGG--------LSGGNQQKLLISRWVAIGPRI 418
Cdd:PRK11264 99 HRTVLENI----IE-----GPVIVKG--EPKEEATAR--ARELLAKVGLAGketsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 419 LLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
39-201 |
4.39e-05 |
|
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: 46.28 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 39 GENGAGKSTLMKVLAGAYTATSGEILI--DGKPFHI--------RTPKDalsagiTLIYQEmqlapnlSVAENIFLGseL 108
Cdd:TIGR00954 485 GPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLFYVpqrpymtlGTLRD------QIIYPD-------SSEDMKRRG--L 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 109 SHGGLVQRKEmLVQAQKVIDRLGAQFNASDKVMTLTIAEQQQVEIARALHRNSRILVMDEPTAALSSRETHRLFELimrL 188
Cdd:TIGR00954 550 SDKDLEQILD-NVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL---C 625
|
170
....*....|...
gi 13364550 189 RDEGMAIIYISHR 201
Cdd:TIGR00954 626 REFGITLFSVSHR 638
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
275-478 |
4.45e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.14 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREaidlgigfLTENRKEQ-------GLFLE 347
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSR--------LYTVRKRMsmlfqsgALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 348 MAAAENITMATLERDArwgmLNRKKAQTISDDAIKLLNIRvPHAQVRAGGLSGGNQQKLLISRWVAIGPRILLLDEPARG 427
Cdd:PRK11831 99 MNVFDNVAYPLREHTQ----LPAPLLHSTVMMKLEAVGLR-GAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13364550 428 VDVGAKSEIYRIMNEMARK-GVAILMISSELPEIVGMSDRVYVMREGSIAGE 478
Cdd:PRK11831 174 QDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
37-66 |
1.43e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 1.43e-04
10 20 30
....*....|....*....|....*....|
gi 13364550 37 LMGENGAGKSTLMKVLAGAYTATSGEILID 66
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-481 |
1.82e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.54 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGepvviHSP---REAIDLGIGFLTENRkeQGLFLEMAAA 351
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPfkrRKEFARRIGVVFGQR--SQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 352 EnitmaTLErdarwgmLNRKKAQtISDDA--------IKLLNI----RVPhaqVRAggLSGGnqQKL-------LISRwv 412
Cdd:COG4586 115 D-----SFR-------LLKAIYR-IPDAEykkrldelVELLDLgellDTP---VRQ--LSLG--QRMrcelaaaLLHR-- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 413 aigPRILLLDEPARGVDVGAKSEIYRIMNEM-ARKGVAILMISSELPEIVGMSDRVYVMREGSIA--GELNG 481
Cdd:COG4586 173 ---PKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIydGSLEE 241
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
142-202 |
2.19e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.99 E-value: 2.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 142 TLTIAEQQQVEIARALHRNSR---ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRM 202
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
398-454 |
3.25e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 41.37 E-value: 3.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 13364550 398 LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMarkGVAILMIS 454
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVG 145
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-63 |
4.23e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 4.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 6 VLEMRNIAKAFGKFYALKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEI 63
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
278-473 |
4.44e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.46 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 278 VRSGEIVGLAGLVGAGRSELAQLIFGvRKATG---GMIEVDGEPVVIHSPREaidlgIGFLTENrkeqglflemaaaeni 354
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAG-RKTAGvitGEILINGRPLDKNFQRS-----TGYVEQQ---------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 tmatlerdarwgmlnrkkaqtisDDAIKLLNIRVP---HAQVRagGLSGGNQQKLLISRWVAIGPRILLLDEPARGVDVG 431
Cdd:cd03232 88 -----------------------DVHSPNLTVREAlrfSALLR--GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13364550 432 AKSEIYRIMNEMARKGVAIL-MISSELPEIVGMSDRVYVMREG 473
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-173 |
4.73e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.98 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAgAYTATSGEILIDGKPFHirtpkdalsaGITLiyQEMQLAPNLsVAEN 101
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWN----------SVTL--QTWRKAFGV-IPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGSelshGGLvqRKEMLVQAQ-------KVIDRLGAQ-----------FNASDKVMTLTIAEQQQVEIARALHRNSRI 163
Cdd:TIGR01271 1301 VFIFS----GTF--RKNLDPYEQwsdeeiwKVAEEVGLKsvieqfpdkldFVLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|
gi 13364550 164 LVMDEPTAAL 173
Cdd:TIGR01271 1375 LLLDEPSAHL 1384
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-183 |
6.76e-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: 41.77 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfhirtpkdalsagITLIYQEMQLAPNlSVAEN 101
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGSELSHgglvQRKEMLVQAQKVIDRLgAQFNASDKV------MTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS 175
Cdd:cd03291 118 IIFGVSYDE----YRYKSVVKACQLEEDI-TKFPEKDNTvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*...
gi 13364550 176 RETHRLFE 183
Cdd:cd03291 193 FTEKEIFE 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-183 |
7.83e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.20 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 22 LKGVDLTVYPGEIHALMGENGAGKSTLMKVLAGAYTATSGEILIDGKpfhirtpkdalsagITLIYQEMQLAPNlSVAEN 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 102 IFLGseLSHGGLvqRKEMLVQAQKVIDRLgAQFNASDKV------MTLTIAEQQQVEIARALHRNSRILVMDEPTAALSS 175
Cdd:TIGR01271 507 IIFG--LSYDEY--RYTSVIKACQLEEDI-ALFPEKDKTvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*...
gi 13364550 176 RETHRLFE 183
Cdd:TIGR01271 582 VTEKEIFE 589
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-200 |
8.00e-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: 42.31 E-value: 8.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13364550 142 TLTIAEQQQveIARALHRNSR----ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH 200
Cdd:TIGR00630 488 TLSGGEAQR--IRLATQIGSGltgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
273-452 |
9.56e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.60 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 273 PSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVihspreaidlgigflTENRKEQGLFLEMAAAE 352
Cdd:PRK13543 29 PLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---------------RGDRSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 353 NITMATLERDARWGMLNRKKAQTISDDAIKLLNIrVPHAQVRAGGLSGGNQQKLLISR-WVAIGPrILLLDEPARGVDVG 431
Cdd:PRK13543 94 KADLSTLENLHFLCGLHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALARlWLSPAP-LWLLDEPYANLDLE 171
|
170 180
....*....|....*....|.
gi 13364550 432 AKSEIYRIMNEMARKGVAILM 452
Cdd:PRK13543 172 GITLVNRMISAHLRGGGAALV 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
398-496 |
1.58e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 398 LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKG-VAILMISSELPEIvGMSDRVYVMREGSIA 476
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKIVVFNNPDRT 1437
|
90 100
....*....|....*....|
gi 13364550 477 GELNGKNITQENIMTLATGV 496
Cdd:PTZ00265 1438 GSFVQAHGTHEELLSVQDGV 1457
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-202 |
2.26e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 2.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 142 TLTIAEQQQVEIARALHRNSR---ILVMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISHRM 202
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
276-476 |
2.55e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.01 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 276 LLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPREAidlGIGFLTENrkeQGLFLEMAAAENIT 355
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVFQS---YALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 356 ----MATLERDARwgmlnRKKAQTISD--DAIKLLNiRVPHAqvraggLSGGNQQKLLISRWVAIGPRILLLDEPARGVD 429
Cdd:PRK11000 98 fglkLAGAKKEEI-----NQRVNQVAEvlQLAHLLD-RKPKA------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 430 ----VGAKSEIYRIMNEMARKgvailMI--SSELPEIVGMSDRVYVMREGSIA 476
Cdd:PRK11000 166 aalrVQMRIEISRLHKRLGRT-----MIyvTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
273-475 |
2.62e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 273 PSSLLVRSGEIVGLAGLVGAGRSEL----AQLIFGVRKATGGMIEVDG---EPVVIHSPREAI-----DLGIGFLTenrk 340
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDGitpEEIKKHYRGDVVynaetDVHFPHLT---- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 341 eQGLFLEMAAAenitMATLERdaRWGMLNRKK-AQTISDDAIKLL------NIRVPHAQVRagGLSGGNQQKLLISRWVA 413
Cdd:TIGR00956 155 -VGETLDFAAR----CKTPQN--RPDGVSREEyAKHIADVYMATYglshtrNTKVGNDFVR--GVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 414 IGPRILLLDEPARGVDVGAKSEIYRIMNEMAR--KGVAILMISSELPEIVGMSDRVYVMREGSI 475
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCSQDAYELFDKVIVLYEGYQ 289
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
261-460 |
3.24e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 39.31 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 261 NVHHLTDGGKV-QPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPrEAIDLGIGFLTENr 339
Cdd:PRK10247 12 NVGYLAGDAKIlNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQT- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 340 keQGLFLEmAAAENITMAtlerdarWGMlnRKKA---QTISDDaikLLNIRVPHA--QVRAGGLSGGNQQKLLISRWVAI 414
Cdd:PRK10247 90 --PTLFGD-TVYDNLIFP-------WQI--RNQQpdpAIFLDD---LERFALPDTilTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13364550 415 GPRILLLDEPARGVDVGAKSEIYRIMNEMAR-KGVAILMISSELPEI 460
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEI 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
271-424 |
3.29e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.83 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 271 VQPSSLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIHSPReaiDLGIGFLTENrkeQGLFLEMAA 350
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA---DRDIAMVFQN---YALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 351 AENitMAtlerdarWGMLNRK--KAQtIS---DDAIKLLNI-----RVPHAqvraggLSGGNQQKllisrwVAIG----- 415
Cdd:PRK11650 94 REN--MA-------YGLKIRGmpKAE-IEervAEAARILELeplldRKPRE------LSGGQRQR------VAMGraivr 151
|
170
....*....|
gi 13364550 416 -PRILLLDEP 424
Cdd:PRK11650 152 ePAVFLFDEP 161
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-76 |
3.53e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 3.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 13364550 25 VDLTVYPGeIHALMGENGAGKSTLMKVLAGAYTATSGEI-LIDGKPFHIRTPK 76
Cdd:COG3950 19 IDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLdDVKFRKLLIRNGE 70
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
275-476 |
3.55e-03 |
|
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: 39.80 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEP---VVIHSPREAIdlgigfltenrkeqG-------L 344
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdVTQASLRAAI--------------GivpqdtvL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 345 FLEmAAAENI-------TMATLERDARwgmlnrkKAQTisDDAIKLLnirvP---HAQVRAGG--LSGGNQQKLLISRWV 412
Cdd:COG5265 444 FND-TIAYNIaygrpdaSEEEVEAAAR-------AAQI--HDFIESL----PdgyDTRVGERGlkLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13364550 413 AIGPRILLLDEPARGVDVGAKSEIYRIMNEMARkGVAILMISSELPEIVGmSDRVYVMREGSIA 476
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
275-423 |
4.18e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 275 SLLVRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIhspreAIDlgigfltenrkeQGLFLEMAAAENI 354
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI-----AIS------------AGLSGQLTGIENI 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 355 TMATLERDarwgmLNRKKAQTISDDAIKLLNI-RVPHAQVRAggLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:PRK13546 107 EFKMLCMG-----FKRKEIKAMTPKIIEFSELgEFIYQPVKK--YSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
278-341 |
4.61e-03 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 38.08 E-value: 4.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13364550 278 VRSGEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEV-DGEPVvihspREAIDLGIGFLTENRKE 341
Cdd:PRK00889 1 KQRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVlDGDAV-----RTNLSKGLGFSKEDRDT 60
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
142-200 |
6.53e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 6.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13364550 142 TLTIAEQQQVEIARALHRNS--RIL-VMDEPTAALSSRETHRLFELIMRLRDEGMAIIYISH 200
Cdd:PRK00349 830 TLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEH 891
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
398-462 |
6.72e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 6.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13364550 398 LSGGNQQKLLISRWVAIGPRILLLDEPARGVDVGAKSEIYRIMNEMARKGVAILMIS---SELPEIVG 462
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLnrfDEIPDFVQ 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
281-430 |
8.14e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.78 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 281 GEIVGLAGLVGAGRSELAQLIFGVRKATGGMIEVDGEPVVIH----SPREAIDLGIGFLTENRKEQGLFLEMAAAENITM 356
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdPPRNVEGTVYDFVAEGIEEQAEYLKRYHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13364550 357 ATLERDArwgMLNR-KKAQTISD------------DAIKLLNIRvPHAQVRAggLSGGNQQKLLISRWVAIGPRILLLDE 423
Cdd:PRK11147 109 ETDPSEK---NLNElAKLQEQLDhhnlwqlenrinEVLAQLGLD-PDAALSS--LSGGWLRKAALGRALVSNPDVLLLDE 182
|
....*..
gi 13364550 424 PARGVDV 430
Cdd:PRK11147 183 PTNHLDI 189
|
|
| |
