|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-509 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 686.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 11 DTPTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:COG1129 1 AEPLLEMRGISKSFgGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGDC 169
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGR 249
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 250 EIAEQAVHGTRTPGAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAA 329
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG--KPVR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 330 IRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPAQPVAELSG 409
Cdd:COG1129 318 IRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 410 GNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFE 489
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELD 477
|
490 500
....*....|....*....|
gi 490656625 490 RGGWTQDALLGAAFAGYARR 509
Cdd:COG1129 478 REEATEEAIMAAATGGAAAA 497
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-502 |
1.01e-169 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 489.04 E-value: 1.01e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 11 DTPTLVVTGIGKTYaeP---VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEA 87
Cdd:PRK11288 1 SSPYLSFDGIGKTF--PgvkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 88 LGVRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:PRK11288 79 AGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV-HVDRIDAQPTERLVALM 246
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVaTFDDMAQVDRDQLVQAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 247 AGREIAEQAVHGTRTPGAPRLRVERLSrGDAVR-DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpp 325
Cdd:PRK11288 238 VGREIGDIYGYRPRPLGEVRLRLDGLK-GPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 326 RPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGG-VVDGERENALAARQIDALRIRARGPAQPV 404
Cdd:PRK11288 315 KPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGcLINNRWEAENADRFIRSLNIKTPSREQLI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
490
....*....|....*...
gi 490656625 485 HAVFERGGWTQDALLGAA 502
Cdd:PRK11288 475 AGELAREQATERQALSLA 492
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-502 |
2.53e-157 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 457.85 E-value: 2.53e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 13 PTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGlVAPT---TGAMRLAGAEYAPHSRAHAEAL 88
Cdd:PRK13549 4 YLLEMKNITKTFgGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 GVRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGD 168
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLD-INPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 169 CRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAG 248
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 249 REIAEQAVHGTRTPGAPRLRVERLSRGDA-------VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA-DAADGGTVS 320
Cdd:PRK13549 242 RELTALYPREPHTIGEVILEVRNLTAWDPvnphikrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 321 IGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGP 400
Cdd:PRK13549 322 IDG--KPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 AQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMS 480
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMH 479
|
490 500
....*....|....*....|..
gi 490656625 481 AGRMHAVFERGGWTQDALLGAA 502
Cdd:PRK13549 480 EGKLKGDLINHNLTQEQVMEAA 501
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-505 |
2.64e-157 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 457.57 E-value: 2.64e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYAEPV-LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGV 90
Cdd:COG3845 3 PPALELRGITKRFGGVVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGRE 250
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 251 IAEQAVHGTRTPGAPRLRVERLS-----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpp 325
Cdd:COG3845 242 VLLRVEKAPAEPGEVVLEVENLSvrddrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 326 RPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQL--ARVARGGVVDGERENALAARQIDALRIRARGPAQP 403
Cdd:COG3845 320 EDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYrrPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 404 VAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
490 500
....*....|....*....|..
gi 490656625 484 MHAVFERGGWTQDAlLGAAFAG 505
Cdd:COG3845 480 IVGEVPAAEATREE-IGLLMAG 500
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-502 |
4.13e-146 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 429.04 E-value: 4.13e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYaeP---VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL 88
Cdd:PRK10762 2 QALLQLKGIDKAF--PgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 GVRMVMQELNLVPTLTVAENLFLDRLP-HRFGVIDRRRLAADARAAMARVGLdSLDPDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLGREFvNRFGRIDWKKMYAEADKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMA 247
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 248 GREIAEQAVHGTRTPGAPRLRVERLSrGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRP 327
Cdd:PRK10762 239 GRKLEDQYPRLDKAPGEVRLKVDNLS-GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG--HE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 328 AAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVAR-GGVVDGERENALAARQIDALRIRARGPAQPVAE 406
Cdd:PRK10762 316 VVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRaGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISG 475
|
490
....*....|....*.
gi 490656625 487 VFERGGWTQDALLGAA 502
Cdd:PRK10762 476 EFTREQATQEKLMAAA 491
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-499 |
1.47e-143 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 422.28 E-value: 1.47e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 19 GIGKTYAePV--LDDVSLALYPGEALALTGENGAGKSTLSKIVAGlVAPT---TGAMRLAGAEYAPHSRAHAEALGVRMV 93
Cdd:NF040905 6 GITKTFP-GVkaLDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFKDIRDSEALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:NF040905 84 HQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDE-SPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV-HVDRIDAQPTE-RLVALMAGREI 251
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIeTLDCRADEVTEdRIIRGMVGRDL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 252 AEQAVHGTRTPGAPRLRVERLSRGD-------AVRDVSFDVRAGEIFGISGLIGAGRTELLRLV----YGADAAdgGTVS 320
Cdd:NF040905 243 EDRYPERTPKIGEVVFEVKNWTVYHplhperkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsYGRNIS--GTVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 321 IGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGP 400
Cdd:NF040905 321 KDG--KEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 AQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMS 480
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
490
....*....|....*....
gi 490656625 481 AGRMHAVFERGGWTQDALL 499
Cdd:NF040905 479 EGRITGELPREEASQERIM 497
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-489 |
1.96e-135 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 401.86 E-value: 1.96e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYAePV--LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:PRK09700 3 TPYISMAGIGKSFG-PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VRMVMQELNLVPTLTVAENLFLDRLPHR--FGV--IDRRRLAADARAAMARVGLdSLDPDTLVGSLGIGHQQMVEIARSL 165
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKkvCGVniIDWREMRVRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 166 AGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVAL 245
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 246 MAGREI-----AEQAVHGtRTPGAPRLRVERLSRGDA--VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGT 318
Cdd:PRK09700 241 MVGRELqnrfnAMKENVS-NLAHETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 319 VSI-GDPPRPaaiRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVAR----GGVVDGERENALAARQIDAL 393
Cdd:PRK09700 320 IRLnGKDISP---RSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGykgaMGLFHEVDEQRTAENQRELL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 394 RIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLIC 473
Cdd:PRK09700 397 ALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVC 476
|
490
....*....|....*.
gi 490656625 474 DRIGVMSAGRMHAVFE 489
Cdd:PRK09700 477 DRIAVFCEGRLTQILT 492
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-502 |
1.49e-123 |
|
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: 371.08 E-value: 1.49e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTT--GAMRLAGAEYAPHSRAHAEALGVR 91
Cdd:TIGR02633 2 LEMKGIVKTFGGvKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 MVMQELNLVPTLTVAENLFL-DRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTL-VGSLGIGHQQMVEIARSLAGDC 169
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLgNEITLPGGRMAYNAMYLRAKNLLRELQLDA-DNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGR 249
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 250 EIAEQAVHGTRTPGAPRLRVERLSRGDA-------VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA-DAADGGTVSI 321
Cdd:TIGR02633 241 EITSLYPHEPHEIGDVILEARNLTCWDVinphrkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 322 GDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPA 401
Cdd:TIGR02633 321 NG--KPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSA 481
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
490 500
....*....|....*....|.
gi 490656625 482 GRMHAVFERGGWTQDALLGAA 502
Cdd:TIGR02633 479 GKLKGDFVNHALTQEQVLAAA 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-511 |
2.06e-117 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 355.90 E-value: 2.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGV 90
Cdd:PRK15439 9 PPLLCARSISKQYSGvEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLfLDRLPHRfgvidrRRLAADARAAMARVGLdSLDPDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENI-LFGLPKR------QASMQKMKQLLAALGC-QLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGRE 250
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 251 IAEQAV------------HGTRTPGAPRLRVERLSrGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGT 318
Cdd:PRK15439 241 REKSLSasqklwlelpgnRRQQAAGAPVLTVEDLT-GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 319 VSIGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSlgQLARVARGGVVDGERENALAARQIDALRIRAR 398
Cdd:PRK15439 320 IMLNG--KEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC--ALTHNRRGFWIKPARENAVLERYRRALNIKFN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 399 GPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGV 478
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLV 475
|
490 500 510
....*....|....*....|....*....|...
gi 490656625 479 MSAGRMHAVFERGGWTQDALLGAAFAGYARRDA 511
Cdd:PRK15439 476 MHQGEISGALTGAAINVDTIMRLAFGEHQAQEA 508
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-499 |
2.61e-117 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 354.81 E-value: 2.61e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 18 TGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVMQE 96
Cdd:PRK10982 2 SNISKSFpGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 97 LNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDsLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDID-IDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 177 PTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGREIAEQAV 256
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 257 HGTRTPGAPRLRVERLS--RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPA 334
Cdd:PRK10982 241 DKENKPGEVILEVRNLTslRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG--KKINNHNAN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 335 DAVRHGIALVSEDRKGEGlllpqsIAANLSLGQLARVA-------RGGVVDGERENALAARQIDALRIRARGPAQPVAEL 407
Cdd:PRK10982 319 EAINHGFALVTEERRSTG------IYAYLDIGFNSLISnirnyknKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 408 SGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
490
....*....|..
gi 490656625 488 FERGGWTQDALL 499
Cdd:PRK10982 473 VDTKTTTQNEIL 484
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
263-484 |
3.10e-79 |
|
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: 245.80 E-value: 3.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 263 GAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIA 342
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG--KPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKGEGLLLPQSIAANLSLGQLarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLG 422
Cdd:cd03215 79 YVPEDRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-229 |
1.31e-66 |
|
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: 212.29 E-value: 1.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMV 93
Cdd:cd03216 1 LELRGITKRFgGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQelnlvptltvaenlfldrlphrfgvidrrrlaadaraamarvgldsldpdtlvgsLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-483 |
5.95e-59 |
|
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: 203.21 E-value: 5.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTY---AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPT---TGAMRLAGAEYAPHSRAHA 85
Cdd:COG1123 2 TPLLEVRDLSVRYpggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 86 eALGVRMVMQE--LNLVPtLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVE 160
Cdd:COG1123 82 -GRRIGMVFQDpmTQLNP-VTVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRldrYPHQLSG----GQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 161 IARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV---HVDRIDA 236
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVedgPPEEILA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 237 QPteRLVALMAGREIAEQAVHGTRTPGAPRLRVERLSRG---------DAVRDVSFDVRAGEIFGISGLIGAGRTELLRL 307
Cdd:COG1123 233 AP--QALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRypvrgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 308 VYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDrkGEGLLLP-QSIAANLSLGQLARvargGVVDGERENALA 386
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQD--PYSSLNPrMTVGDIIAEPLRLH----GLLSRAERRERV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 387 ARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSD 465
Cdd:COG1123 385 AELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD 464
|
490
....*....|....*...
gi 490656625 466 LRELMLICDRIGVMSAGR 483
Cdd:COG1123 465 LAVVRYIADRVAVMYDGR 482
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
15-236 |
1.12e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.75 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmV 93
Cdd:COG1131 1 IEVRGLTKRYGDkTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENL-FLDRLphrFGvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARL---YG-LPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-229 |
3.08e-38 |
|
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: 139.88 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHaeaLGV 90
Cdd:cd03219 1 LEVRGLTKRFGGlVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIAR---LGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMA-------RVGLDSLDpDTLVGSLGIGHQQMVEIAR 163
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREAREraeelleRVGLADLA-DRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 164 SLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
15-229 |
7.61e-37 |
|
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: 136.10 E-value: 7.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:cd03257 2 LEVKNLSVSFPTgggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 --VRMVMQE----LNlvPTLTVAEnLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIAR 163
Cdd:cd03257 82 keIQMVFQDpmssLN--PRMTIGE-QIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 164 SLAGDCRVLILDEPTAML---TAREVELLFDQIARLKadGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03257 159 ALALNPKLLIADEPTSALdvsVQAQILDLLKKLQEEL--GLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-236 |
1.17e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 135.25 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 16 VVTGIGKTyaePVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHAealGVRM 92
Cdd:cd03224 6 LNAGYGKS---QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitgLPPHERARA---GIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELNLVPTLTVAENLFLDRLPHRFGVIDRRrlaadaraamarvgLD---SLDP------DTLVGSLGIGHQQMVEIAR 163
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKAR--------------LErvyELFPrlkerrKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 164 SLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-227 |
1.31e-36 |
|
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: 134.90 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAeALGVRMVMQ--ELNLVpT 102
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGLVFQnpDDQFF-G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFldrlphrFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILD 175
Cdd:cd03225 91 PTVEEEVA-------FGLenlgLPEEEIEERVEEALELVGLEGLrdrSPFTLSG----GQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 176 EPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
11-229 |
2.79e-36 |
|
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: 135.17 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 11 DTPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY---APHSRAHae 86
Cdd:COG0411 1 SDPLLEVRGLTKRFGGlVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIAR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 87 aLGVRMVMQELNLVPTLTVAENLFLDRLPHRFGVIDRRRLAADARAAMAR------------VGLDSLdPDTLVGSLGIG 154
Cdd:COG0411 79 -LGIARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEReareraeellerVGLADR-ADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
15-228 |
2.86e-36 |
|
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: 132.52 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmV 93
Cdd:cd03230 1 IEVRNLSKRYGKkTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENLFLdrlphrfgvidrrrlaadaraamarvgldsldpdtlvgSLGIghQQMVEIARSLAGDCRVLI 173
Cdd:cd03230 79 PEEPSLYENLTVRENLKL--------------------------------------SGGM--KQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-229 |
3.97e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 140.81 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 5 DPDSTPDTPTLVVTGIGKTYAE------PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA 78
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRYPVrgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 79 PHSRAHAEALG--VRMVMQ--ELNLVPTLTVAENlfLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIG 154
Cdd:COG1123 331 KLSRRSLRELRrrVQMVFQdpYSSLNPRMTVGDI--IAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-233 |
4.95e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 133.63 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRA 83
Cdd:COG1136 2 SPLLELRNLTKSYGTgegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 84 H--AEALGvrMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEI 161
Cdd:COG1136 82 RlrRRHIG--FVFQFFNLLPELTALENV---ALPLLLAGVSRKERRERARELLERVGLGDRL-DHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 162 ARSLAGDCRVLILDEPTAML---TAREVELLFDQIARlkADGVALVYISHRlEELARVAQRVAVLRDGRLVHVDR 233
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLdskTGEEVLELLRELNR--ELGTTIVMVTHD-PELAARADRVIRLRDGRIVSDER 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
15-236 |
1.26e-34 |
|
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: 130.36 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmV 93
Cdd:COG4555 2 IEVENLSKKYgKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENL-FLDRLpHRfgvIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:COG4555 80 PDERGLYDRLTVRENIrYFAEL-YG---LFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-232 |
8.76e-34 |
|
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: 127.25 E-value: 8.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRahaealGV 90
Cdd:cd03259 1 LELKGLSKTYGSvRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPERR------NI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:cd03259 75 GMVFQDYALFPHLTVAENI---AFGLKLRGVPKAEIRARVRELLELVGLEGLlnrYPHELSG----GQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
26-229 |
3.73e-33 |
|
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: 125.91 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS-RAHAEALGvrMVMQ--ELNLVpT 102
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlRELRRKVG--LVFQnpDDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENL-FLdrlPHRFGViDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:COG1122 91 PTVEEDVaFG---PENLGL-PREEIRERVEEALELVGLEHLadrPPHELSG----GQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-228 |
4.21e-33 |
|
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: 125.29 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHAE 86
Cdd:cd03255 1 IELKNLSKTYGGggekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 87 ALGVRMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLA 166
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENV---ELPLLLAGVPKKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 167 GDCRVLILDEPTAML---TAREV-ELLFDQiarLKADGVALVYISHRlEELARVAQRVAVLRDGRL 228
Cdd:cd03255 157 NDPKIILADEPTGNLdseTGKEVmELLREL---NKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-230 |
1.58e-32 |
|
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: 124.32 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 16 VVTGIGKTyaePVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHaeaLGVRM 92
Cdd:COG0410 9 LHAGYGGI---HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitgLPPHRIAR---LGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELNLVPTLTVAENLFLDRLPHRfgvidrrrlaadaraaMARVGLDSLD------P------DTLVGSLGIGHQQMVE 160
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARR----------------DRAEVRADLErvyelfPrlkerrRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 161 IARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVL 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-229 |
3.24e-32 |
|
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: 123.76 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaPHSRAHAEALG 89
Cdd:COG1124 2 LEVRNLSVSYGQggrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VRMVMQE----LNlvPTLTVAENLFLDRLPHRFGVIDRRRLAADARaamarVGLDS--LD--PDTLVGslgiGHQQMVEI 161
Cdd:COG1124 81 VQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDREERIAELLEQ-----VGLPPsfLDryPHQLSG----GQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 162 ARSLAGDCRVLILDEPTAML----TAREVELLfdqiARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG1124 150 ARALILEPELLLLDEPTSALdvsvQAEILNLL----KDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-503 |
9.08e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 128.26 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKS--TLSkiVAGLVAP----TTGAMRLAGAEYAPHSRahAEALGVR-----MVMQ 95
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtALS--ILRLLPDpaahPSGSILFDGQDLLGLSE--RELRRIRgnriaMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 96 E----LNlvPTLTV----AENLFLdrlpHRfgVIDRRRLAADARAAMARVGLDslDPDTLVGS----LGIGHQQMVEIAR 163
Cdd:COG4172 100 EpmtsLN--PLHTIgkqiAEVLRL----HR--GLSGAAARARALELLERVGIP--DPERRLDAyphqLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 164 SLAGDCRVLILDEPTamlTAREV-------ELLfdqiARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV---HVD 232
Cdd:COG4172 170 ALANEPDLLIADEPT---TALDVtvqaqilDLL----KDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVeqgPTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 233 RIDAQP----TERLVALMAGREIAEQAvhgtrTPGAPRLRVERLS------RG---------DAVRDVSFDVRAGEIFGI 293
Cdd:COG4172 243 ELFAAPqhpyTRKLLAAEPRGDPRPVP-----PDAPPLLEARDLKvwfpikRGlfrrtvghvKAVDGVSLTLRRGETLGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 294 SGLIGAGRTEL----LRLVygadaADGGTVSIGDPP----RPAAIRspadAVRHGIALVSEDRKGeglllpqSIAANLSL 365
Cdd:COG4172 318 VGESGSGKSTLglalLRLI-----PSEGEIRFDGQDldglSRRALR----PLRRRMQVVFQDPFG-------SLSPRMTV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 366 GQLA----RVARGGVVDGEREnalaARQIDALR-------IRARGPaqpvAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:COG4172 382 GQIIaeglRVHGPGLSAAERR----ARVAEALEevgldpaARHRYP----HEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 435 RGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFE--RGGWTQdALLGAAF 503
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVveqgptEQVFDapQHPYTR-ALLAAAP 530
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
267-484 |
2.31e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 121.32 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRHGIA 342
Cdd:COG1131 1 IEVRGLTKryGDktALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG----EDVARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEdrkgEGLLLPqsiaaNLSLGQ-LARVARGGVVDGERENALAARQIDALRIRARgPAQPVAELSGGNQQKVAIGRWL 421
Cdd:COG1131 77 YVPQ----EPALYP-----DLTVREnLRFFARLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-179 |
5.58e-31 |
|
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: 117.36 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAlGVRMVMQELNLVPTLTVAEN 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 109 LfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTL---VGSLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:pfam00005 80 L---RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
13-216 |
1.14e-30 |
|
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: 118.35 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 13 PTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVr 91
Cdd:COG4133 1 MMLEAENLSCRRGErLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 mVMQELNLVPTLTVAENL-FLDRLphrFGVidrRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:COG4133 80 -LGHADGLKPELTVRENLrFWAAL---YGL---RADREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARV 216
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-485 |
1.26e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.79 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyaphsrahaealGVRM--V 93
Cdd:COG0488 1 LENLSKSFgGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLRIgyL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENLF-----------------------------LDRLPHRFGVIDRRRLAADARAAMARVGLDSLDP 144
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgdaelraleaeleeleaklaepdedlerLAELQEEFEALGGWEAEARAEEILSGLGFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 145 DTLVGSLGiGHQQM-VEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAdgvALVYISHRLEELARVAQRVAVL 223
Cdd:COG0488 147 DRPVSELS-GGWRRrVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHDRYFLDRVATRILEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 224 RDGRLVH------------------------------------VDRIDA------QPTERLVALMAGREIAEQAVHGT-- 259
Cdd:COG0488 223 DRGKLTLypgnysayleqraerleqeaaayakqqkkiakeeefIRRFRAkarkakQAQSRIKALEKLEREEPPRRDKTve 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 260 -RTPGAPR-----LRVERLSRGDA----VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGdpprpaa 329
Cdd:COG0488 303 iRFPPPERlgkkvLELEGLSKSYGdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 330 irspaDAVRhgIALVSEDRkgEGLLLPQSIAANLSlgqlaRVARGGvvdGEREnalaARQI---------DALrirargp 400
Cdd:COG0488 376 -----ETVK--IGYFDQHQ--EELDPDKTVLDELR-----DGAPGG---TEQE----VRGYlgrflfsgdDAF------- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 aQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAkfdIYALLDALAR-EGrAIVVVSSDlRELM-LICDRIGV 478
Cdd:COG0488 428 -KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET---LEALEEALDDfPG-TVLLVSHD-RYFLdRVATRILE 501
|
....*..
gi 490656625 479 MSAGRMH 485
Cdd:COG0488 502 FEDGGVR 508
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
13-229 |
6.62e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 117.47 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 13 PTLVVTGIGKTYA--EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-- 88
Cdd:COG3638 1 PMLELRNLSKRYPggTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 GVRMVMQELNLVPTLTVAENLFLDRLPHR------FGVIDRRRLAAdaraamarvGLDSLD-----------PDTLVGsl 151
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTstwrslLGLFPPEDRER---------ALEALErvgladkayqrADQLSG-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 152 giGHQQMVEIARSLAGDCRVLILDEPTAML---TAREVELLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:COG3638 150 --GQQQRVAIARALVQEPKLILADEPVASLdpkTARQVMDLLRRIAR--EDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
.
gi 490656625 229 V 229
Cdd:COG3638 226 V 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-253 |
1.63e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.73 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 9 TPDTPTLVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRa 83
Cdd:COG1116 2 SAAAPALELRGVSKRFPTggggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 84 haealGVRMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGL-DSLD--PDTLVGslgiGHQQMVE 160
Cdd:COG1116 81 -----DRGVVFQEPALLPWLTVLDNV---ALGLELRGVPKAERRERARELLELVGLaGFEDayPHQLSG----GMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 161 IARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVL--RDGRLVHVDRIDAq 237
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEIDVDL- 227
|
250
....*....|....*.
gi 490656625 238 PTERLVALMAGREIAE 253
Cdd:COG1116 228 PRPRDRELRTSPEFAA 243
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
15-235 |
2.32e-29 |
|
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: 115.26 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAhaealg 89
Cdd:cd03293 1 LEVRNVSKTYGGgggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VRMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLA 166
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNV---ALGLELQGVPKAEARERAEELLELVGLSGFEnayPHQLSG----GMRQRVALARALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVL--RDGRLVHVDRID 235
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
267-487 |
3.36e-29 |
|
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: 115.34 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRHGIA 342
Cdd:COG4555 2 IEVENLSKkyGKvpALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG----EDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRkgeGLLLPQSIAANLSLgqLARVARggvVDGERENALAARQIDALRIRaRGPAQPVAELSGGNQQKVAIGRWLG 422
Cdd:COG4555 78 VLPDER---GLYDRLTVRENIRY--FAELYG---LFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-227 |
6.32e-29 |
|
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: 112.67 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG-VRM 92
Cdd:cd03229 1 LELKNVSKRYGQkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELNLVPTLTVAENLFLdrlphrfgvidrrrlaadaraamarvgldsldpdtlvgSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 173 ILDEPTAML---TAREVELLFDQIARLkaDGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:cd03229 123 LLDEPTSALdpiTRREVRALLKSLQAQ--LGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-230 |
1.80e-28 |
|
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: 112.60 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE---PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVr 91
Cdd:cd03263 1 LQIRNLTKTYKKgtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 mVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRV 171
Cdd:cd03263 80 -CPQFDALFDELTVREHL---RFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 172 LILDEPTAMLTAREVELLFDQIARLKAdGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-227 |
2.71e-28 |
|
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: 110.03 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRaHAEALGVRMVMQ 95
Cdd:cd00267 2 IENLSFRYGGrTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL-EELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 96 elnlvptltvaenlfldrlphrfgvidrrrlaadaraamarvgldsldpdtLVGslgiGHQQMVEIARSLAGDCRVLILD 175
Cdd:cd00267 81 ---------------------------------------------------LSG----GQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 176 EPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-230 |
4.77e-28 |
|
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: 112.44 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH-AEALGVrm 92
Cdd:COG1120 2 LEAENLSVGYGGrPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARRIAY-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELNLVPTLTVAENLFLDRLPHR-FGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRV 171
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLgLFGRPSAEDREAVEEALERTGLEHLA-DRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 172 LILDEPTAML-TAREVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG1120 159 LLLDEPTSHLdLAHQLEVL-ELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-228 |
5.74e-28 |
|
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: 109.61 E-value: 5.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYA---EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEALGVR 91
Cdd:cd03246 1 LEVENVSFRYPgaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG---ADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 M--VMQELNLVPTlTVAENLfldrlphrfgvidrrrlaadaraamarvgldsldpdtlvgsLGIGHQQMVEIARSLAGDC 169
Cdd:cd03246 78 VgyLPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRL 228
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
28-229 |
1.53e-27 |
|
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: 109.65 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAealgVRMVMQELNL-VPTLTVA 106
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS----IGYVMQDVDYqLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFL--DRLPHRFGVIDRRrlaadaraamarvgLDSLDPDTLVG----SLGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:cd03226 91 EELLLglKELDAGNEQAETV--------------LKDLDLYALKErhplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 181 LTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
267-484 |
2.20e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 108.25 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLS----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRspadaVRHGI 341
Cdd:cd03230 1 IEVRNLSkrygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEE-----VKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRKgegllLPQsiaaNLSLgqlarvarggvvdgeRENAlaarqidalrirargpaqpvaELSGGNQQKVAIGRWL 421
Cdd:cd03230 76 GYLPEEPS-----LYE----NLTV---------------RENL---------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
15-229 |
2.46e-27 |
|
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: 109.23 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrAHAEALGVRMV 93
Cdd:cd03268 1 LKTNDLTKTYGKkRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQEL-NLVPTLTVAENLFLDRLPHRFG------VIDrrrlaadaraamaRVGLDSlDPDTLVGSLGIGHQQMVEIARSLA 166
Cdd:cd03268 77 LIEApGFYPNLTARENLRLLARLLGIRkkrideVLD-------------VVGLKD-SAKKKVKGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-230 |
4.29e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.41 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 10 PDTPTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRahaeal 88
Cdd:COG1121 2 MMMPAIELENLTVSYgGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 gvRM--VMQELNLVPT--LTVAENLFLDRLPHR-FGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIAR 163
Cdd:COG1121 76 --RIgyVPQRAEVDWDfpITVRDVVLMGRYGRRgLFRRPSRADREAVDEALERVGLEDLA-DRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 164 SLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-244 |
7.20e-27 |
|
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: 108.48 E-value: 7.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYA-EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRahaealGV 90
Cdd:cd03300 1 IELENVSKFYGgFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnlpPHKR------PV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:cd03300 75 NTVFQNYALFPHLTVFENI---AFGLRLKKLPKAEIKERVAEALDLVQLEGYanrKPSQLSG----GQQQRVAIARALVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDR---IDAQPTERLV 243
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTpeeIYEEPANRFV 227
|
.
gi 490656625 244 A 244
Cdd:cd03300 228 A 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-229 |
1.05e-26 |
|
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: 108.42 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE--PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYapHSRAHAEALGVR- 91
Cdd:cd03256 1 IEVENLSKTYPNgkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI--NKLKGKALRQLRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 ---MVMQELNLVPTLTVAENLFLDRLPHR---------FGVIDrrrlAADARAAMARVGLDSL---DPDTLVGslgiGHQ 156
Cdd:cd03256 79 qigMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEE----KQRALAALERVGLLDKayqRADQLSG----GQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 157 QMVEIARSLAGDCRVLILDEPTAML---TAREVELLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLdpaSSRQVMDLLKRINR--EEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
11-232 |
1.42e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 110.57 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 11 DTPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRahae 86
Cdd:COG3842 2 AMPALELENVSKRYGDvTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPEKR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 87 alGVRMVMQELNLVPTLTVAENLfldrlphRFG----VIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMV 159
Cdd:COG3842 78 --NVGMVFQDYALFPHLTVAENV-------AFGlrmrGVPKAEIRARVAELLELVGLEGLAdryPHQLSG----GQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 160 EIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVG 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-229 |
2.08e-26 |
|
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: 107.13 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 8 STPDTPTLVVTGIGKTYAEP-----VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS- 81
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGageltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 82 --RAHAEALGVRMVMQELNLVPTLTVAEN----LFLDRLPHRFGvidrrrlaaDARAAMARVGL-DSLD--PDTLVGslg 152
Cdd:COG4181 82 daRARLRARHVGFVFQSFQLLPTLTALENvmlpLELAGRRDARA---------RARALLERVGLgHRLDhyPAQLSG--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 153 iGHQQMVEIARSLAGDCRVLILDEPTAMLTARE----VELLFDQIARLkadGVALVYISHRlEELARVAQRVAVLRDGRL 228
Cdd:COG4181 150 -GEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRER---GTTLVLVTHD-PALAARCDRVLRLRAGRL 224
|
.
gi 490656625 229 V 229
Cdd:COG4181 225 V 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-229 |
4.65e-26 |
|
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: 112.23 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RAHaealgVRMVMQELNLV 100
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASlRRQ-----IGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTlTVAENL-----------------------FLDRLPHRFgvidrrrlaadaraamarvgldsldpDTLVGSLGI---G 154
Cdd:COG2274 562 SG-TIRENItlgdpdatdeeiieaarlaglhdFIEALPMGY--------------------------DTVVGEGGSnlsG 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 155 HQ-QMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAdGVALVYISHRLeELARVAQRVAVLRDGRLV 229
Cdd:COG2274 615 GQrQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-228 |
1.06e-25 |
|
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: 103.67 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMV----MQELnLVPTL 103
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedrKREG-LVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRLphrfgvidrrrlaadaraamarvgldsldpdtLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLTA 183
Cdd:cd03215 94 SVAENIALSSL--------------------------------LSG----GNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490656625 184 REVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:cd03215 138 GAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
15-251 |
1.28e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 105.11 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSrahAEALGVRMVM 94
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP---PEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 95 QELNLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:cd03299 78 QNYALFPHMTVYKNI-------AYGLkkrkVDKKEIERKVLEIAEMLGIDHLlnrKPETLSG----GEQQRVAIARALVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHV---DRIDAQPTERLV 243
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVgkpEEVFKKPKNEFV 226
|
....*...
gi 490656625 244 ALMAGREI 251
Cdd:cd03299 227 AEFLGFNN 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-233 |
1.84e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 104.36 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 19 GIGKTYAE--PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALgvR----M 92
Cdd:COG2884 6 NVSKRYPGgrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL--RrrigV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDC 169
Cdd:COG2884 84 VFQDFRLLPDRTVYENV---ALPLRVTGKSRKEIRRRVREVLDLVGLSDKAkalPHELSG----GEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 170 RVLILDEPTAML---TAREVELLFDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLVHVDR 233
Cdd:COG2884 157 ELLLADEPTGNLdpeTSWEIMELLEEINRR---GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-231 |
1.97e-25 |
|
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: 103.90 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLagaEYAPHSRAHAEALGvrMV 93
Cdd:cd03269 1 LEVENVTKRFGRvTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF---DGKPLDIAARNRIG--YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENLF----------------LDRLPHRFGVIDRRrlaadaraamarvgldsldpDTLVGSLGIGHQQ 157
Cdd:cd03269 76 PEERGLYPKMKVIDQLVylaqlkglkkeearrrIDEWLERLELSEYA--------------------NKRVEELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 158 MVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHV 231
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
267-486 |
2.90e-25 |
|
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: 104.06 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIA 342
Cdd:cd03219 1 LEVRGLTKrfGGlvALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG--EDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 ----LVSedrkgeglLLPQ-SIAANLSLGQLARVARG----GVVDGERE-NALAARQIDALRIRARGpAQPVAELSGGNQ 412
Cdd:cd03219 79 rtfqIPR--------LFPElTVLENVMVAAQARTGSGlllaRARREEREaRERAEELLERVGLADLA-DRPAGELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 413 QKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
278-486 |
4.61e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.74 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgIALVsedrkgeglllPQ 357
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--KDLASLSPKELARK-IAYV-----------PQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 siaanlslgqlarvarggvvdgerenALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGI 437
Cdd:cd03214 81 --------------------------ALELLGLAHLADR------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 438 DVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:cd03214 129 DIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
277-487 |
5.76e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 102.83 E-value: 5.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPprpAAIRSPAdAVRHGIALVSEdrkGEGLLLP 356
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPA-EARRRLGFVSD---STGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLS-LGQLARVARGGVVDgeRENALAAR-QIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:cd03266 93 LTARENLEyFAGLYGLKGDELTA--RLEELADRlGMEELLDR------RVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 435 RGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03266 165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
267-487 |
6.31e-25 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 102.60 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR----GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPAdavRHGIA 342
Cdd:cd03259 1 LELKGLSKtygsVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG--RDVTGVPPE---RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRkgeGLLLPQSIAANLSLGqlarVARGGVVDGEREnALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLG 422
Cdd:cd03259 76 MVFQDY---ALFPHLTVAENIAFG----LKLRGVPKAEIR-ARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
28-229 |
7.34e-25 |
|
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: 102.64 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV-----APTTGAMRLAGAE-YAPHSRAHAEALGVRMVMQELNLVP 101
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiYDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 tLTVAENLfldRLPHR-FGVIDRRRLAADARAAMARVGL-----DSLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILD 175
Cdd:cd03260 95 -GSIYDNV---AYGLRlHGIKLKEELDERVEEALRKAALwdevkDRLHALGLSG----GQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 176 EPTAML---TAREVELLfdqIARLKADgVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03260 167 EPTSALdpiSTAKIEEL---IAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-229 |
1.18e-24 |
|
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: 102.27 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVR 91
Cdd:cd03258 4 LKNVSKVFGDtggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 --MVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGL-DSLD--PDTLVGslgiGHQQMVEIARSLA 166
Cdd:cd03258 84 igMIFQHFNLLSSRTVFENV---ALPLEIAGVPKAEIEERVLELLELVGLeDKADayPAQLSG----GQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 167 GDCRVLILDEPTAML---TAREV-ELLFDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03258 157 NNPKVLLCDEATSALdpeTTQSIlALLRDINREL---GLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
267-483 |
1.67e-24 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 100.34 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHgIA 342
Cdd:cd03229 1 LELKNVSKRygqkTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRR-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDrkgeGLLLPQ-SIAANLSLGqlarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWL 421
Cdd:cd03229 80 MVFQD----FALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-231 |
1.86e-24 |
|
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: 102.03 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaphSRAHAEALGVRM 92
Cdd:cd03296 2 SIEVRNVSKRFGDfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELNLVPTLTVAENL-FLDRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGD 168
Cdd:cd03296 79 VFQHYALFRHMTVFDNVaFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLAdryPAQLSG----GQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 169 CRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHV 231
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
277-484 |
1.90e-24 |
|
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: 99.43 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIALVSedrkgeglllp 356
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--KEVSFASPRDARRAGIAMVY----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qsiaanlslgqlarvarggvvdgerenalaarqidalrirargpaqpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03216 82 -------------------------------------------------QLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
27-229 |
1.97e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.12 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHaealgVRMVM-QELNLVPT 102
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplAAWSPWELAR-----RRAVLpQHSSLAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLDRLPHRFGvidRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLA-------GDCRVL 172
Cdd:COG4559 90 FTVEEVVALGRAPHGSS---AAQDRQIVREALALVGLAHLagrSYQTLSG----GEQQRVQLARVLAqlwepvdGGPRWL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4559 163 FLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
267-483 |
2.31e-24 |
|
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: 100.97 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIA 342
Cdd:cd03224 1 LEVENLNAGygksQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG--RDITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKgeglLLPQ-SIAANLSLGqlARVARGGVVDGERENALAArqIDALRIRARgpaQPVAELSGGNQQKVAIGRWL 421
Cdd:cd03224 79 YVPEGRR----IFPElTVEENLLLG--AYARRRAKRKARLERVYEL--FPRLKERRK---QLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-491 |
2.32e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGL-----VAPTTGAMRLAGaeyapHSRAHAEA---LGVR-----MV 93
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHG-----ESLLHASEqtlRGVRgnkiaMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQE--LNLVPTLTVAENLFLDRLPHRfgvidrrrlaADARAAMARVGLDSLD--------------PDTLVGslgiGHQQ 157
Cdd:PRK15134 98 FQEpmVSLNPLHTLEKQLYEVLSLHR----------GMRREAARGEILNCLDrvgirqaakrltdyPHQLSG----GERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 158 MVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 237 ---QP----TERLV-ALMAGREIAEQAvhgtrtPGAPRLRVERLS------RG---------DAVRDVSFDVRAGEIFGI 293
Cdd:PRK15134 244 lfsAPthpyTQKLLnSEPSGDPVPLPE------PASPLLDVEQLQvafpirKGilkrtvdhnVVVKNISFTLRPGETLGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 294 SGLIGAGRT----ELLRLVygadaADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDrkgeglllPQSiAANLSLGQLA 369
Cdd:PRK15134 318 VGESGSGKSttglALLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQD--------PNS-SLNPRLNVLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 370 RVARGGVVDGERENALA--ARQIDALR-------IRARGPaqpvAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVG 440
Cdd:PRK15134 384 IIEEGLRVHQPTLSAAQreQQVIAVMEevgldpeTRHRYP----AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 441 AKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRmhaVFERG 491
Cdd:PRK15134 460 VQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGE---VVEQG 508
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
271-486 |
3.24e-24 |
|
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: 100.30 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairSPADAVRHGIALVsedrkg 350
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKRIGYV------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 eglllPQSIAAN----------LSLGQLARVARGGVVDGER----ENALAARQIDALRIRargpaqPVAELSGGNQQKVA 416
Cdd:cd03235 74 -----PQRRSIDrdfpisvrdvVLMGLYGHKGLFRRLSKADkakvDEALERVGLSELADR------QIGELSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIgVMSAGRMHA 486
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVA 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
277-484 |
3.51e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 100.43 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRpaairspADAVRHGIALVSEDRkgeGLLLP 356
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-------DIAARNRIGYLPEER---GLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLS-LGQLARVARggvvdgeREnalAARQID----ALRIRARGpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:cd03269 85 MKVIDQLVyLAQLKGLKK-------EE---ARRRIDewleRLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 432 EPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
266-486 |
4.21e-24 |
|
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: 101.27 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 266 RLRVERLS----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgI 341
Cdd:COG1120 1 MLEAENLSvgygGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG--RDLASLSRRELARR-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVsedrkgeglllPQSIAANLSLG-----QLARVARGGVVDGER-------ENALAARQIDALRIRargpaqPVAELSG 409
Cdd:COG1120 78 AYV-----------PQEPPAPFGLTvrelvALGRYPHLGLFGRPSaedreavEEALERTGLEHLADR------PVDELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 410 GNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
267-517 |
4.49e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 101.03 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLS--------RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRspadAV 337
Cdd:COG1124 2 LEVRNLSvsygqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRRRRK----AF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 338 RHGIALVSEDrkGEGLLLP-QSIAAnlSLGQLARVARGGVVDGERENALAARQIDAlRIRARGPAQpvaeLSGGNQQKVA 416
Cdd:COG1124 78 RRRVQMVFQD--PYASLHPrHTVDR--ILAEPLRIHGLPDREERIAELLEQVGLPP-SFLDRYPHQ----LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERggwtq 495
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV----- 223
|
250 260
....*....|....*....|....
gi 490656625 496 DALLGAAFAGYARR--DAALHPPG 517
Cdd:COG1124 224 ADLLAGPKHPYTREllAASLAFER 247
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-229 |
5.22e-24 |
|
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: 100.65 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVM- 94
Cdd:cd03261 3 LRGLTKSFGGrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 95 -QELNLVPTLTVAEN--LFLdrlpHRFGVIDRRRLAADARAAMARVGL---DSLDPDTLVGslgiGHQQMVEIARSLAGD 168
Cdd:cd03261 83 fQSGALFDSLTVFENvaFPL----REHTRLSEEEIREIVLEKLEAVGLrgaEDLYPAELSG----GMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 169 CRVLILDEPTAML---TAREVELLfdqIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03261 155 PELLLYDEPTAGLdpiASGVIDDL---IRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-229 |
7.22e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-----GV 90
Cdd:COG4161 5 LKNINCFYGShQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIrllrqKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLFldRLPHRFGVIDRRRLAADARAAMARVGL-DSLD--PDTLVGslgiGHQQMVEIARSLAG 167
Cdd:COG4161 85 GMVFQQYNLWPHLTVMENLI--EAPCKVLGLSKEQAREKAMKLLARLRLtDKADrfPLHLSG----GQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 168 DCRVLILDEPTAML----TAREVELlfdqIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4161 159 EPQVLLFDEPTAALdpeiTAQVVEI----IRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-229 |
9.07e-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: 99.36 E-value: 9.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAEP-----VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG 89
Cdd:cd03266 2 ITADALTKRFRDVkktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VrmVMQELNLVPTLTVAENL-------------FLDRLPHRFGVIDRRRLAadaraamarvgldsldpDTLVGSLGIGHQ 156
Cdd:cd03266 82 F--VSDSTGLYDRLTARENLeyfaglyglkgdeLTARLEELADRLGMEELL-----------------DRRVGGFSTGMR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 157 QMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-229 |
9.22e-24 |
|
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: 99.14 E-value: 9.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyaphsrAHAEALGVRM--VMQELNLVPT- 102
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERKRIgyVPQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 -LTVAENLFLDRLPH-RFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:cd03235 84 pISVRDVVLMGLYGHkGLFRRLSKADKAKVDEALERVGLSELA-DRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 181 LTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLrDGRLV 229
Cdd:cd03235 163 VDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
26-227 |
1.48e-23 |
|
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: 97.45 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHAEALgvrmVMQELNLVPT 102
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLRKNIAY----VPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 lTVAENLfldrlphrfgvidrrrlaadaraamarvgldsldpdtlvgsLGIGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:cd03228 91 -TIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490656625 183 AREVELLFDQIARLkADGVALVYISHRLEELARvAQRVAVLRDGR 227
Cdd:cd03228 129 PETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
277-489 |
1.81e-23 |
|
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: 98.70 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPadavRHGIALVSEDrkgeGLLLP 356
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP----VTGP----GPDRGYVFQQ----DALLP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 -QSIAANLSLGQLARvargGVVDGEREnALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03293 87 wLTVLDNVALGLELQ----GVPKAEAR-ERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 436 GIDVGAKFDIYA-LLDALAREGRAIVVVSSDLRELMLICDRIGVMSA--GRMHAVFE 489
Cdd:cd03293 161 ALDALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-227 |
2.21e-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: 98.66 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTY--------AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMR---------LAG 74
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 75 AEyaPHsrahaEALGVR-----MVMQELNLVPTLT----VAENLFLD------------RLPHRFGVIDRrrlaadaraa 133
Cdd:COG4778 82 AS--PR-----EILALRrrtigYVSQFLRVIPRVSaldvVAEPLLERgvdreearararELLARLNLPER---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 134 marvgLDSLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEEL 213
Cdd:COG4778 145 -----LWDLPPATFSG----GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
|
250
....*....|....
gi 490656625 214 ARVAQRVAVLRDGR 227
Cdd:COG4778 216 EAVADRVVDVTPFS 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
277-484 |
2.42e-23 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 98.35 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDrkgeglllP 356
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKEIQMVFQD--------P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSiAAN--LSLG-QLARVARggVVDGERENALAARQIDALRIRARGPAQ-----PvAELSGGNQQKVAIGRWLGRDMGVL 428
Cdd:cd03257 92 MS-SLNprMTIGeQIAEPLR--IHGKLSKKEARKEAVLLLLVGVGLPEEvlnryP-HELSGGQRQRVAIARALALNPKLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03257 168 IADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
27-230 |
2.69e-23 |
|
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: 96.74 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAhaealgvrmvmQELNLVPTL 103
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlASLSPKELA-----------RKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 tvaenlfLDRlphrfgvidrrrlaadaraamarVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML-T 182
Cdd:cd03214 82 -------LEL-----------------------LGLAHLA-DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLdI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 183 AREVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:cd03214 131 AHQIELL-ELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-232 |
3.09e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.99 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphSRAHAEALGVRM 92
Cdd:COG1118 2 SIEVRNISKRFGSfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELNLVPTLTVAENL--FLDRLPHRFGVIDrrrlaADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAG 167
Cdd:COG1118 80 VFQHYALFPHMTVAENIafGLRVRPPSKAEIR-----ARVEELLELVQLEGLAdryPSQLSG----GQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 168 DCRVLILDEPTAMLTA---REVELLFDQIarLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:COG1118 151 EPEVLLLDEPFGALDAkvrKELRRWLRRL--HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-235 |
4.25e-23 |
|
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: 98.13 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 10 PDTPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL 88
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDrVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 GVR--MVMQELNLVPTLTVAENLfldRLP-HRFGVIDRRRLAADARAAMARVGLDS---LDPDTLVGslgiGHQQMVEIA 162
Cdd:COG1127 81 RRRigMLFQGGALFDSLTVFENV---AFPlREHTDLSEAEIRELVLEKLELVGLPGaadKMPSELSG----GMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 163 RSLAGDCRVLILDEPTAML---TAREVELLfdqIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRID 235
Cdd:COG1127 154 RALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
277-484 |
7.45e-23 |
|
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: 96.81 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPADAVRHGIALVSEDRkgegLLLP 356
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS----IRTDRKAARQSLGYCPQFD----ALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 Q-SIAANLSLgqLARVaRGGVVDGERENALAARQIDALRIRARGPAQpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03263 89 ElTVREHLRF--YARL-KGLPKSEIKEEVELLLRVLGLTDKANKRAR---TLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 436 GIDVGAKFDIYALLDALaREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03263 163 GLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
267-484 |
7.73e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.42 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRGDAVR----DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAairSPADAVRHGIA 342
Cdd:COG4619 1 LELEGLSFRVGGKpilsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA---MPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEdrkgEGLLLPQSIAANLSLgqlARVARGGVVDGERENALAAR---QIDALrirargpAQPVAELSGGNQQKVAIGR 419
Cdd:COG4619 78 YVPQ----EPALWGGTVRDNLPF---PFQLRERKFDRERALELLERlglPPDIL-------DKPVERLSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 420 WLGRDMGVLLFDEPTRGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
268-482 |
1.41e-22 |
|
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: 95.40 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 268 RVERLSRG-----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRspadavRHGIA 342
Cdd:cd03226 1 RIENISFSykkgtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKGEglLLPQSIAANLSLGQLARVARGGVVdgerENALAARQIDALRIRargpaQPvAELSGGNQQKVAIGRWLG 422
Cdd:cd03226 75 YVMQDVDYQ--LFTDSVREELLLGLKELDAGNEQA----ETVLKDLDLYALKER-----HP-LSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
15-228 |
2.22e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 95.69 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHaeaLGV 90
Cdd:cd03218 1 LRAENLSKRYGKrKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitkLPMHKRAR---LGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLFLdrlphrfgVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGI----GHQQMVEIARSLA 166
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILA--------VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASslsgGERRRVEIARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
28-247 |
2.24e-22 |
|
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: 95.67 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHAealGVRMVMQELNLVPTLT 104
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHERARA---GIAYVPQGREIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLF--LDRLPHRFGVIDRRrlaadaraamarvgLDSLDP------DTLVGSLGIGHQQMVEIARSLAGDCRVLILDE 176
Cdd:TIGR03410 92 VEENLLtgLAALPRRSRKIPDE--------------IYELFPvlkemlGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 177 PTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMA 247
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
2.67e-22 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 100.23 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 2 DSTDPDSTPDTPTLVVTGIGKTY---AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA 78
Cdd:COG4987 321 EPAEPAPAPGGPSLELEDVSFRYpgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 79 PHSRAHAEALgVRMVMQELNLVPTlTVAENL-----------------------FLDRLPHrfgvidrrrlaadaraama 135
Cdd:COG4987 401 DLDEDDLRRR-IAVVPQRPHLFDT-TLRENLrlarpdatdeelwaalervglgdWLAALPD------------------- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 136 rvGLDsldpdTLVGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAML---TAREV-ELLFDQiarlkADGVALVYIS 207
Cdd:COG4987 460 --GLD-----TWLGEGGRrlsgGERRRLALARALLRDAPILLLDEPTEGLdaaTEQALlADLLEA-----LAGRTVLLIT 527
|
250 260
....*....|....*....|..
gi 490656625 208 HRLEELARvAQRVAVLRDGRLV 229
Cdd:COG4987 528 HRLAGLER-MDRILVLEDGRIV 548
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-229 |
2.69e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.10 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH----AEAL 88
Cdd:COG4152 1 MLELKGLTKRFGDkTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 GvrmvmqelnLVPTLTVAENL-FLDRLpH----------------RFGVIDRRrlaadaraamarvgldsldpDTLVGSL 151
Cdd:COG4152 81 G---------LYPKMKVGEQLvYLARL-KglskaeakrradewleRLGLGDRA--------------------NKKVEEL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 152 GIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-229 |
3.30e-22 |
|
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: 100.22 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 2 DSTDPDSTPDTPTLVVTGIGKTYAE--PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAP 79
Cdd:COG4988 324 AGTAPLPAAGPPSIELEDVSFSYPGgrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 80 HSRAHaealgvrmVMQELNLV---PTL---TVAENLfldrlphRFGVIDrrRLAADARAAMARVGLDSL------DPDTL 147
Cdd:COG4988 404 LDPAS--------WRRQIAWVpqnPYLfagTIRENL-------RLGRPD--ASDEELEAALEAAGLDEFvaalpdGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 148 VGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLkADGVALVYISHRLEELARvAQRVAVL 223
Cdd:COG4988 467 LGEGGRglsgGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVL 544
|
....*.
gi 490656625 224 RDGRLV 229
Cdd:COG4988 545 DDGRIV 550
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
256-483 |
3.73e-22 |
|
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: 96.17 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 256 VHGTRTPGAPRLRVERLSRGD---------AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPR 326
Cdd:cd03294 9 IFGKNPQKAFKLLAKGKSKEEilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 327 PAAIRSPADAVR-HGIALVSEDRKgeglLLPQ-SIAANLSLG-QLArvargGVVDGEREnALAARQIDALRIRARGPAQP 403
Cdd:cd03294 89 AAMSRKELRELRrKKISMVFQSFA----LLPHrTVLENVAFGlEVQ-----GVPRAERE-ERAAEALELVGLEGWEHKYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 404 vAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:cd03294 159 -DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDG 237
|
.
gi 490656625 483 R 483
Cdd:cd03294 238 R 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
27-229 |
3.87e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.61 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAhaealGVRMVM-QELNLVPT 102
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrplADWSPAELA-----RRRAVLpQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGslgiGHQQMVEIARSLA------GDCRVLILDE 176
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSG----GEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 177 PTAMLTAREVELLFdQIAR--LKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13548 167 PTSALDLAHQHHVL-RLARqlAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
277-483 |
4.98e-22 |
|
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: 92.69 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPaaiRSPADAVRHGIALVsedrkgeglllP 356
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---KLPLEELRRRIGYV-----------P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QsiaanlslgqlarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd00267 80 Q-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-232 |
5.12e-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: 94.28 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 38 PGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY---------APHSRahaealGVRMVMQELNLVPTLTVAEN 108
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinlPPQQR------KIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 109 L-----FLDRLPHRFGVidrrrlaadaRAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:cd03297 96 LafglkRKRNREDRISV----------DELLDLLGLDHLLnryPAQLSG----GEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 181 LTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
240-479 |
6.15e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.90 E-value: 6.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMAGREIAEQAVHGTRTPGAPRLRVERLS-----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAA 314
Cdd:TIGR02857 295 EALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSvaypgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 315 DGGTVSIGDPPRPAAirsPADAVRHGIALVSEdrkgEGLLLPQSIAANLslgqlaRVARGGVVDGERENALAARQID-AL 393
Cdd:TIGR02857 375 TEGSIAVNGVPLADA---DADSWRDQIAWVPQ----HPFLFAGTIAENI------RLARPDASDAEIREALERAGLDeFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 394 RIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLrEL 469
Cdd:TIGR02857 442 AALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL-AL 519
|
250
....*....|
gi 490656625 470 MLICDRIGVM 479
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-228 |
1.05e-21 |
|
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: 93.24 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 22 KTYAE--PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYApHSRAHAEALGVR---MVMQE 96
Cdd:cd03292 8 KTYPNgtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIPYLRRkigVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 97 LNLVPTLTVAEN----LFLDRLPHRfgvidrrRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:cd03292 87 FRLLPDRNVYENvafaLEVTGVPPR-------EIRKRVPAALELVGLSH-KHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 173 ILDEPTAML---TAREVELLFDQIarlKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:cd03292 159 IADEPTGNLdpdTTWEIMNLLKKI---NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
240-483 |
1.10e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 98.29 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMAGREIAEQAVHGTRT-PGAPRLRVERLS-----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADA 313
Cdd:COG4988 309 EKIFALLDAPEPAAPAGTAPLPaAGPPSIELEDVSfsypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 314 ADGGTVSIGDPPRPAAirsPADAVRHGIALVSEDrkgeGLLLPQSIAANLSLGqlarvaRGGVVDGERENALAARQIDAL 393
Cdd:COG4988 389 PYSGSILINGVDLSDL---DPASWRRQIAWVPQN----PYLFAGTIRENLRLG------RPDASDEELEAALEAAGLDEF 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 394 rIRA--RGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLr 467
Cdd:COG4988 456 -VAAlpDGLDTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL- 532
|
250
....*....|....*.
gi 490656625 468 ELMLICDRIGVMSAGR 483
Cdd:COG4988 533 ALLAQADRILVLDDGR 548
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
277-491 |
1.32e-21 |
|
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: 93.41 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP----RPAAIRspadAVRHGIALVSEdrkGEG 352
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllSGKELR----KARRRIGMIFQ---HFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLLPQSIAANLSLG-QLARVARGGVvdGERENALaarqIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:cd03258 93 LLSSRTVFENVALPlEIAGVPKAEI--EERVLEL----LELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 432 EPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRmhaVFERG 491
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGE---VVEEG 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
264-483 |
1.44e-21 |
|
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: 93.51 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLS----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRH 339
Cdd:COG0410 1 MPMLEVENLHagygGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG--EDITGLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALVSEDRKgeglLLPQ-SIAANLSLGQLARVARGGVvdgerenalaARQIDA-------LRIRARgpaQPVAELSGGN 411
Cdd:COG0410 79 GIGYVPEGRR----IFPSlTVEENLLLGAYARRDRAEV----------RADLERvyelfprLKERRR---QRAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 412 QQKVAIGRWLgrdMG---VLLFDEPTRG-----IDvgakfDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:COG0410 142 QQMLAIGRAL---MSrpkLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
261-489 |
1.44e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.00 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 261 TPGAPRLRVERLSRG--------DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairS 332
Cdd:COG1116 2 SAAAPALELRGVSKRfptggggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 333 PADAVRHGIALV-SEDRkgeglLLP-QSIAANLSLGQLARvargGVVDGEREnALAARQIDALRIRARGPAQPvAELSGG 410
Cdd:COG1116 74 PVTGPGPDRGVVfQEPA-----LLPwLTVLDNVALGLELR----GVPKAERR-ERARELLELVGLAGFEDAYP-HQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 411 NQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYA-LLDALAREGRAIVVVSSDLRELMLICDRIGVMSA--GRMHAV 487
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDeLLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
..
gi 490656625 488 FE 489
Cdd:COG1116 223 ID 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-258 |
1.46e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.49 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 33 SLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY---APHSRAhaealgVRMVMQELNLVPTLTVAENL 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHtttPPSRRP------VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 110 FLDRLPhrfGVIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTA---REV 186
Cdd:PRK10771 93 GLGLNP---GLKLNAAQREKLHAIARQMGIEDL-LARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPalrQEM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 187 ELLFDQIARLKadGVALVYISHRLEELARVAQRVAVLRDGRLVHvdriDAqPTERLVAlmagREIAEQAVHG 258
Cdd:PRK10771 169 LTLVSQVCQER--QLTLLMVSHSLEDAARIAPRSLVVADGRIAW----DG-PTDELLS----GKASASALLG 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
267-489 |
1.56e-21 |
|
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: 93.40 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG-----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGI 341
Cdd:cd03256 1 IEVENLSKTypngkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRkgeGLLLPQSIAANLSLGQLA-----RVARGGVVDGERENALAARQIDALRIRARgpaQPVAELSGGNQQKVA 416
Cdd:cd03256 81 GMIFQQF---NLIERLSVLENVLSGRLGrrstwRSLFGLFPKEEKQRALAALERVGLLDKAY---QRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMhaVFE 489
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRI--VFD 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-229 |
1.67e-21 |
|
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: 92.56 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRAhaealgVRMVMQELNLVPTLTVAE 107
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaapPADRP------VSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDRLPhrfGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAML-TA 183
Cdd:cd03298 90 NVGLGLSP---GLKLTAEDRQAIEVALARVGLAGLEkrlPGELSG----GERQRVALARVLVRDKPVLLLDEPFAALdPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490656625 184 REVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03298 163 LRAEML-DLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-248 |
1.88e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.06 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRAhaea 87
Cdd:PRK11607 17 TPLLEIRNLTKSFdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLShvpPYQRP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 88 lgVRMVMQELNLVPTLTVAEN----LFLDRLPHrfGVIDRRRLAADARAAMARVGldSLDPDTLVGslgiGHQQMVEIAR 163
Cdd:PRK11607 93 --INMMFQSYALFPHMTVEQNiafgLKQDKLPK--AEIASRVNEMLGLVHMQEFA--KRKPHQLSG----GQRQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 164 SLAGDCRVLILDEPTAMLTAR-----EVELLfDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLVHV---DRID 235
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKlrdrmQLEVV-DILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIgepEEIY 238
|
250
....*....|...
gi 490656625 236 AQPTERLVALMAG 248
Cdd:PRK11607 239 EHPTTRYSAEFIG 251
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
33-244 |
1.90e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.90 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 33 SLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRahaealGVRMVMQELNLVPTLTVAENL 109
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAER------PVSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 110 FLDRLPH-RFGVIDrrrlAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTA------ 179
Cdd:COG3840 93 GLGLRPGlKLTAEQ----RAQVEQALERVGLAGLLdrlPGQLSG----GQRQRVALARCLVRKRPILLLDEPFSaldpal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 180 ---MLTarevelLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDGRlVHVDridaQPTERLVA 244
Cdd:COG3840 165 rqeMLD------LVDELCR--ERGLTVLMVTHDPEDAARIADRVLLVADGR-IAAD----GPTAALLD 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-229 |
2.47e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.60 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL--GVRMVMQE-L 97
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrDIQMVFQDsI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 98 NLV-PTLTVAENLfldRLPHR-FGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:PRK10419 100 SAVnPRKTVREII---REPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 176 EPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-229 |
2.66e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.16 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RAHaealgVRMVMQElnlvP 101
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESlRRQ-----IGVVPQD----T 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TL---TVAENL-----------------------FLDRLPHrfgvidrrrlaadaraamarvGLdsldpDTLVGSLGI-- 153
Cdd:COG1132 424 FLfsgTIRENIrygrpdatdeeveeaakaaqaheFIEALPD---------------------GY-----DTVVGERGVnl 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 154 --GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVyISHRLeELARVAQRVAVLRDGRLV 229
Cdd:COG1132 478 sgGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV-IAHRL-STIRNADRILVLDDGRIV 553
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-227 |
2.93e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYAEP-VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaEYAPhSRAHAEALGV 90
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKlVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVP-SRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENL---LVFGRYFGLSAAAARALVPPLLEFAKLEN-KADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-227 |
2.98e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.90 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYA-EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmVMQ 95
Cdd:PRK13536 44 LAGVSKSYGdKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV--VPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 96 ELNLVPTLTVAENLFLdrlphrFGVIDRRRLAADARAAMARVGLDSLD--PDTLVGSLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:PRK13536 122 FDNLDLEFTVRENLLV------FGRYFGMSTREIEAVIPSLLEFARLEskADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
154-484 |
4.24e-21 |
|
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: 96.41 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQI-ARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVd 232
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 233 ridAQPTERLVALMAGREIAEQAVHGTRtpGAPRLRVERLS-------RG--DAVRDVSFDVRAGEIFGISGLIGAGRTE 303
Cdd:TIGR03269 251 ---GTPDEVVAVFMEGVSEVEKECEVEV--GEPIIKVRNVSkryisvdRGvvKAVDNVSLEVKEGEIFGIVGTSGAGKTT 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 304 LLRLVYGADAADGGT--VSIGDpprpaairSPADAVRHGIALVSEDRKGEGLLLPQ-------SIAANL--SLG-----Q 367
Cdd:TIGR03269 326 LSKIIAGVLEPTSGEvnVRVGD--------EWVDMTKPGPDGRGRAKRYIGILHQEydlyphrTVLDNLteAIGlelpdE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 368 LARvaRGGVVdgerenALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDI-Y 446
Cdd:TIGR03269 398 LAR--MKAVI------TLKMVGFDEEKAEEILDKYP-DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtH 468
|
330 340 350
....*....|....*....|....*....|....*...
gi 490656625 447 ALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:TIGR03269 469 SILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
277-483 |
4.28e-21 |
|
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: 91.37 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgIALVSEDrkgeglllP 356
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG--KDLTKLSLKELRRK-VGLVFQN--------P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QS----------IA---ANLSLGQLARVARggvvdgeRENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGR 423
Cdd:cd03225 85 DDqffgptveeeVAfglENLGLPEEEIEER-------VEEALELVGLEGLRDR------SPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
277-483 |
5.47e-21 |
|
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: 91.16 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavrHGIALVSEDRKgeglLLP 356
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG--RDVTDLPPKD---RDIAMVFQNYA----LYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 Q-SIAANLSLGQLARVARGGVVDGERENALAARQIDALRirARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03301 86 HmTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLL--DRKPKQ----LSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 436 GIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-229 |
5.78e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 93.58 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP---TTGAMRLAGAEYAPHSRAHAEALGVR---MVMQE---- 96
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRGReiqMIFQDpmts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 97 LNlvPTLTV----AENLfldrlpHRFGVIDRRRLAADARAAMARVGLDslDPDTLVGS----LGIGHQQMVEIARSLAGD 168
Cdd:COG0444 99 LN--PVMTVgdqiAEPL------RIHGGLSKAEARERAIELLERVGLP--DPERRLDRypheLSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 169 CRVLILDEPTAML---TAREV-ELLfdqiARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG0444 169 PKLLIADEPTTALdvtIQAQIlNLL----KDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-230 |
6.27e-21 |
|
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: 92.07 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGA-MRLAGAEYAPHS----RAHaeaLG-VRMVMQElNLV 100
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDvwelRKR---IGlVSPALQL-RFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTLTVAENLfldrLPHRFGVIDRRRLAADARAAM-----ARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:COG1119 93 RDETVLDVV----LSGFFDSIGLYREPTDEQRERarellELLGLAHLA-DRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 176 EPTAMLTAREVELLFDQIARLKADG-VALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-228 |
8.04e-21 |
|
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: 90.67 E-value: 8.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaPHSRAHAEAL--GVRMV 93
Cdd:cd03262 3 IKNLHKSFGDfHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELrqKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENLFLDrlPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCR 170
Cdd:cd03262 82 FQQFNLFPHLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKAdayPAQLSG----GQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 171 VLILDEPTAML---TAREVEllfDQIARLKADGVALVYISHRLeELAR-VAQRVAVLRDGRL 228
Cdd:cd03262 156 VMLFDEPTSALdpeLVGEVL---DVMKDLAEEGMTMVVVTHEM-GFAReVADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-232 |
9.60e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.60 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRahaealG 89
Cdd:COG3839 3 SLELENVSKSYgGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvTDLPPKDR------N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VRMVMQELNLVPTLTVAENL-FldrlPHRFGVIDRRRLAADARAAMARVGLDS-LD--PDTLVGslgiGHQQMVEIARSL 165
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIaF----PLKLRKVPKAEIDRRVREAAELLGLEDlLDrkPKQLSG----GQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 166 AGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-229 |
1.21e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 90.34 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAlGVRMVMQELNLVPTlTVA 106
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFLDRLPHrfgvidrrrLAADARAAMARVGLDSL---DP---DTLVG----SLGIGHQQMVEIARSLAGDCRVLILDE 176
Cdd:cd03245 96 DNITLGAPLA---------DDERILRAAELAGVTDFvnkHPnglDLQIGergrGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 177 PTAMLTAREVELLFDQIARLKADgVALVYISHRLEELArVAQRVAVLRDGRLV 229
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
31-232 |
1.59e-20 |
|
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: 91.17 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAhaEALGVR-----MVMQELNLVPTLTV 105
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRK--ELRELRrkkisMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEP-TAM 180
Cdd:cd03294 120 LENV-------AFGLevqgVPRAEREERAAEALELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAfSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 181 --LTAREVEllfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03294 192 dpLIRREMQ---DELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
267-483 |
2.45e-20 |
|
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: 89.99 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaiRSPADAVRHGIA 342
Cdd:cd03300 1 IELENVSKfyGGfvALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-----ITNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKgeglLLPQ-SIAANLSLG-QLARVARGGVvdgERENALAARQIDALRIRARGPAQpvaeLSGGNQQKVAIGRW 420
Cdd:cd03300 76 TVFQNYA----LFPHlTVFENIAFGlRLKKLPKAEI---KERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 421 LGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
15-229 |
4.65e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 89.28 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEalgVR-- 91
Cdd:COG1126 2 IEIENLHKSFgDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINK---LRrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 --MVMQELNLVPTLTVAENL---------------------FLDRlphrfgvidrrrlaadaraamarVGL-DSLD--PD 145
Cdd:COG1126 79 vgMVFQQFNLFPHLTVLENVtlapikvkkmskaeaeerameLLER-----------------------VGLaDKADayPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 146 TLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAML---TAREVEllfDQIARLKADGVALVYISHrleEL--AR-VAQR 219
Cdd:COG1126 136 QLSG----GQQQRVAIARALAMEPKVMLFDEPTSALdpeLVGEVL---DVMRDLAKEGMTMVVVTH---EMgfAReVADR 205
|
250
....*....|
gi 490656625 220 VAVLRDGRLV 229
Cdd:COG1126 206 VVFMDGGRIV 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-230 |
5.54e-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: 93.27 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRahaEALGvRMV---MQELNLVPTl 103
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELG-RHIgylPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENL--FLD--------------------RLPHRFgvidrrrlaadaraamarvgldsldpDTLVGSLGI----GHQQ 157
Cdd:COG4618 421 TIAENIarFGDadpekvvaaaklagvhemilRLPDGY--------------------------DTRIGEGGArlsgGQRQ 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 158 MVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELArVAQRVAVLRDGRLVH 230
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQA 546
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
240-483 |
5.88e-20 |
|
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: 93.29 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMAGREIAEQAVHGTRTPGAPRLRVERLS------RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADA 313
Cdd:COG4987 307 RRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSfrypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 314 ADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDrkgeGLLLPQSIAANLslgqlaRVARGGVVDGERENALAARQIDA 392
Cdd:COG4987 387 PQSGSITLGGVD----LRDlDEDDLRRRIAVVPQR----PHLFDTTLRENL------RLARPDATDEELWAALERVGLGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 393 LrIRA--RGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDL 466
Cdd:COG4987 453 W-LAAlpDGLDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRL 530
|
250
....*....|....*..
gi 490656625 467 RELMLiCDRIGVMSAGR 483
Cdd:COG4987 531 AGLER-MDRILVLEDGR 546
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-229 |
7.40e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.69 E-value: 7.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS----RAHaealgVRMVMQ----- 95
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvRRQ-----VGMVFQnpdnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 96 --------------ELNLVPTLTVAENL-----------FLDRLPHRfgvidrrrlaadaraamarvgldsldpdtlvgs 150
Cdd:PRK13635 94 fvgatvqddvafglENIGVPREEMVERVdqalrqvgmedFLNREPHR--------------------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 151 LGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
15-232 |
7.99e-20 |
|
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: 88.08 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRahaealGV 90
Cdd:cd03301 1 VELENVTKRFGNvTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvTDLPPKDR------DI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAEN----LFLDRLPHRfgVIDRRRLAADARAAMARVgLDSLdPDTLVGslgiGHQQMVEIARSLA 166
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNiafgLKLRKVPKD--EIDERVREVAELLQIEHL-LDRK-PKQLSG----GQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
277-486 |
9.91e-20 |
|
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: 88.16 E-value: 9.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRH-GI-----------ALV 344
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG--KDITKKNLRELRRKvGLvfqnpddqlfaPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 345 SEDrkgeglllpqsIA---ANLSLGQ---LARVarggvvdgerENALAARQIDALRirargpAQPVAELSGGNQQKVAIG 418
Cdd:COG1122 94 EED-----------VAfgpENLGLPReeiRERV----------EEALELVGLEHLA------DRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 419 RWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-232 |
1.39e-19 |
|
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: 87.43 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAEPV-LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmV 93
Cdd:cd03265 1 IEVENLVKKYGDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENLFLD-RLphrFGVidrRRLAADARAAMARVGLDSLD-PDTLVGSLGIGHQQMVEIARSLAGDCRV 171
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHaRL---YGV---PGAERRERIDELLDFVGLLEaADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 172 LILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
265-469 |
1.97e-19 |
|
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: 86.76 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS--RGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPADAVRHG 340
Cdd:COG4133 1 MMLEAENLScrRGERLlfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP----IRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 341 IALVSEDrkgEGLLLPQSIAANLslgQLARVARGGVVDGERENALaarqIDALRIRARGpAQPVAELSGGNQQKVAIGRW 420
Cdd:COG4133 77 LAYLGHA---DGLKPELTVRENL---RFWAALYGLRADREAIDEA----LEAVGLAGLA-DLPVRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 421 LGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLREL 469
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-229 |
2.30e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 89.39 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA----EYAPHSR-AHAEALGvrMVMQELNLVPTLTV 105
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLpPHRRRIG--YVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLfldrlphRFGVidrrrlaadaraAMARVGLDSLDPDTLVGSLGIGH-------------QQMVEIARSLAGDCRVL 172
Cdd:COG4148 95 RGNL-------LYGR------------KRAPRAERRISFDEVVELLGIGHlldrrpatlsggeRQRVAIGRALLSSPRLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 173 ILDEPTAML-TAREVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4148 156 LMDEPLAALdLARKAEIL-PYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-229 |
2.58e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.38 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-----GV 90
Cdd:PRK11124 5 LNGINCFYgAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIrelrrNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENLFldRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAG 167
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLI--EAPCRVLGLSKDQALARAEKLLERLRLKPYAdrfPLHLSG----GQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 168 DCRVLILDEPTAML----TAREVELlfdqIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK11124 159 EPQVLLFDEPTAALdpeiTAQIVSI----IRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-223 |
5.32e-19 |
|
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: 90.04 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 9 TPDTPTLVVTGIGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAE 86
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYpgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 87 AlGVRMVMQELNLVPTlTVAENLFLDRlphrfgvidRRRLAADARAAMARVGLDSLDP------DTLVGS----LGIGHQ 156
Cdd:TIGR02857 396 D-QIAWVPQHPFLFAG-TIAENIRLAR---------PDASDAEIREALERAGLDEFVAalpqglDTPIGEggagLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 157 QMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLkADGVALVYISHRLeELARVAQRVAVL 223
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
276-484 |
6.38e-19 |
|
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: 85.33 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIR--SPADaVRHGIALVSEDrkgeGL 353
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD----IRqlDPAD-LRRNIGYVPQD----VT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIAANLSLG-------QLARVARGGVVDgerenALAARQID--ALRIRARGpaqpvAELSGGNQQKVAIGRWLGRD 424
Cdd:cd03245 89 LFYGTLRDNITLGapladdeRILRAAELAGVT-----DFVNKHPNglDLQIGERG-----RGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLRELMLiCDRIGVMSAGRM 484
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDL-VDRIIVMDSGRI 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
278-483 |
8.70e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.58 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRspadAVRHGIALVSEdrkGEGLLLPQ 357
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR----LARARIGVVPQ---FDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLslgqlarvarggVVDGeRENALAARQIDAL--------RIRARGPAqPVAELSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:PRK13536 130 TVRENL------------LVFG-RYFGMSTREIEAVipsllefaRLESKADA-RVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-241 |
9.55e-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: 85.21 E-value: 9.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahaEALGVRMVM-QELNLVPTLTVAE 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-------EPGPDRMVVfQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFL--DR-LPHRfgviDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:TIGR01184 74 NIALavDRvLPDL----SKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 185 EVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTER 241
Cdd:TIGR01184 149 TRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPR 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-465 |
9.80e-19 |
|
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: 89.22 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 19 GIGKTYA--EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLagaeyaphsrahAEALGVRMVMQE 96
Cdd:TIGR03719 9 RVSKVVPpkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------------QPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 97 LNLVPTLTVAENLF------------LDRLPHRFGVIDRRRLAADARAAMARVGLDSLD-------------------PD 145
Cdd:TIGR03719 77 PQLDPTKTVRENVEegvaeikdaldrFNEISAKYAEPDADFDKLAAEQAELQEIIDAADawdldsqleiamdalrcppWD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 146 TLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAdgvALVYISHRLEELARVAQRVAVLRD 225
Cdd:TIGR03719 157 ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHDRYFLDNVAGWILELDR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 226 GRLV------------HVDRI---DAQPTERLVALMAGREIAEQAVHGTRT----------------------------P 262
Cdd:TIGR03719 234 GRGIpwegnysswleqKQKRLeqeEKEESARQKTLKRELEWVRQSPKGRQAkskarlaryeellsqefqkrnetaeiyiP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 263 GAPRL-----RVERLSR--GDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGdpprpaairsp 333
Cdd:TIGR03719 314 PGPRLgdkviEAENLTKafGDKLliDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 334 aDAVRhgIALVSEDRKGeglllpqsIAANLSLGQLarvarggVVDGERENALAARQIDAlriRA-------RGPAQ--PV 404
Cdd:TIGR03719 383 -ETVK--LAYVDQSRDA--------LDPNKTVWEE-------ISGGLDIIKLGKREIPS---RAyvgrfnfKGSDQqkKV 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAkfdIYALLDALAREGRAIVVVSSD 465
Cdd:TIGR03719 442 GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET---LRALEEALLNFAGCAVVISHD 499
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
15-230 |
1.07e-18 |
|
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: 84.55 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAEP-VLDDVSLALYPGeALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGvrMV 93
Cdd:cd03264 1 LQLENLTKRYGKKrALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG--YL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAEnlFLDRLPhRFGVIDRRRLAADARAAMARVGL-DSLdpDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:cd03264 78 PQEFGVYPNFTVRE--FLDYIA-WLKGIPSKEVKARVDEVLELVNLgDRA--KKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVYiSHRLEELARVAQRVAVLRDGRLVH 230
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRIVILS-THIVEDVESLCNQVAVLNKGKLVF 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
8-229 |
1.11e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 87.09 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 8 STPDTPTLVVTGIGKTYaePV--------------LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLA 73
Cdd:COG4608 1 AAMAEPLLEVRDLKKHF--PVrgglfgrtvgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 74 GAEYAPHSRAHAEAL--GVRMVMQE----LNlvPTLTVAENLfldRLPHR-FGVIDRRRLAADARAAMARVGLDSLD--- 143
Cdd:COG4608 79 GQDITGLSGRELRPLrrRMQMVFQDpyasLN--PRMTVGDII---AEPLRiHGLASKAERRERVAELLELVGLRPEHadr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 144 -PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAML----TAREVELLFDQIARLkadGVALVYISHRLEELARVAQ 218
Cdd:COG4608 154 yPHEFSG----GQRQRIGIARALALNPKLIVCDEPVSALdvsiQAQVLNLLEDLQDEL---GLTYLFISHDLSVVRHISD 226
|
250
....*....|.
gi 490656625 219 RVAVLRDGRLV 229
Cdd:COG4608 227 RVAVMYLGKIV 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
267-484 |
1.26e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAairspadaVRHGI 341
Cdd:COG4152 2 LELKGLTKrfGDktAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLDPE--------DRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRkgeGLLLPQSIAANLS-LGQLARVARggvvdgerenALAARQIDA----LRIRARGpAQPVAELSGGNQQKVA 416
Cdd:COG4152 74 GYLPEER---GLYPKMKVGEQLVyLARLKGLSK----------AEAKRRADEwlerLGLGDRA-NKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGID-VGAKFdIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-230 |
1.58e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahaeALGVRMVMQELNLVPT-- 102
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS--------MLSSRQLARRLALLPQhh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 -----LTVAENLFLDRLPH-----RFGVIDrrrlAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVL 172
Cdd:PRK11231 86 ltpegITVRELVAYGRSPWlslwgRLSAED----NARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 173 ILDEPTAML-TAREVELLfDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:PRK11231 161 LLDEPTTYLdINHQVELM-RLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
201-484 |
1.61e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 89.12 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 201 VALVYISHRLeeLARVAQRVAVLRDGR--LVHVDRID---AQPTERlvalmagreiAEQAVHGTRTPGAPRLRVERLS-- 273
Cdd:COG2274 415 IAFNILSGRF--LAPVAQLIGLLQRFQdaKIALERLDdilDLPPER----------EEGRSKLSLPRLKGDIELENVSfr 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 274 ----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRS-PADAVRHGIALVSEDr 348
Cdd:COG2274 483 ypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG----IDLRQiDPASLRRQIGVVLQD- 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 kgeGLLLPQSIAANLSLG-------QLARVARggvvdgereNALAARQIDAL------RIRARGpaqpvAELSGGNQQKV 415
Cdd:COG2274 558 ---VFLFSGTIRENITLGdpdatdeEIIEAAR---------LAGLHDFIEALpmgydtVVGEGG-----SNLSGGQRQRL 620
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 416 AIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLrELMLICDRIGVMSAGRM 484
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
266-484 |
1.70e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.05 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 266 RLRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavRhGI 341
Cdd:COG3839 3 SLELENVSKsyGGveALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG--RDVTDLPPKD--R-NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVsedrkgeglllPQSIA--------ANLSLG-QLARVARGgvvdgERE----NALAARQIDALRirARGPAQpvaeLS 408
Cdd:COG3839 78 AMV-----------FQSYAlyphmtvyENIAFPlKLRKVPKA-----EIDrrvrEAAELLGLEDLL--DRKPKQ----LS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 409 GGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRELMLICDRIGVMSAGRM 484
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIyVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-228 |
1.71e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 13 PTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEALGVR 91
Cdd:PRK09536 2 PMIDVSDLSVEFGDtTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG---DDVEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 M--VMQELNLVPTLTVAENLFLDRLPH--RFGVIDrRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:PRK09536 79 VasVPQDTSLSFEFDVRQVVEMGRTPHrsRFDTWT-ETDRAAVERAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
277-483 |
2.37e-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: 83.69 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIG-------DPPRPAAIRspadavRHGIALVSEDrk 349
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR------RRHIGFVFQS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 geGLLLP-QSIAANLSLGQLARvargGVVDGEREnALAARQIDALRIRARgPAQPVAELSGGNQQKVAIGRWLGRDMGVL 428
Cdd:cd03255 91 --FNLLPdLTALENVELPLLLA----GVPKKERR-ERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDlRELMLICDRIGVMSAGR 483
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
280-483 |
3.33e-18 |
|
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: 83.11 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRaGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairSPADAVRHGIALVSEDRKgEGLLLPQ-- 357
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--------TVLFDSRKKINLPPQQRK-IGLVFQQya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 -----SIAANLSLGqLARVARGgvVDGERENALAAR-QIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:cd03297 86 lfphlNVRENLAFG-LKRKRNR--EDRISVDELLDLlGLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 432 EPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-230 |
4.36e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 11 DTPTLVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHA 85
Cdd:PRK11629 2 NKILLQCDNLCKRYQEgsvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 86 EALGVR---MVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMV 159
Cdd:PRK11629 82 AELRNQklgFIYQFHHLLPDFTALENV---AMPLLIGKKKPAEINSRALEMLAAVGLEHRAnhrPSELSG----GERQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 160 EIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLeELARVAQRVAVLRDGRLVH 230
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTA 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
17-243 |
4.56e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.52 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaphSRAHAEALGVRMVMQ 95
Cdd:PRK10851 5 IANIKKSFGRtQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 96 ELNLVPTLTVAENL-F-LDRLPHRfGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCR 170
Cdd:PRK10851 82 HYALFRHMTVFDNIaFgLTVLPRR-ERPNAAAIKAKVTQLLEMVQLAHLAdryPAQLSG----GQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTA---REVELLFDQI-ARLKADGvalVYISHRLEELARVAQRVAVLRDGRLVHV---DRIDAQPTERLV 243
Cdd:PRK10851 157 ILLLDEPFGALDAqvrKELRRWLRQLhEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAgtpDQVWREPATRFV 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
271-483 |
6.80e-18 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 82.93 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDr 348
Cdd:cd03261 7 TKSFGGRTvlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQS- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 kgEGLLLPQSIAANLSL-----GQLARvarggvvdgERENALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGR 423
Cdd:cd03261 86 --GALFDSLTVFENVAFplrehTRLSE---------EEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGK 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-229 |
1.47e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.00 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeYAPHSR--AHAEALGVRMvMQELNLVPTLT 104
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRrkKFLRRIGVVF-GQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLFLDRLPHRfgvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:cd03267 112 VIDSFYLLAAIYD---LPPARFKKRLDELSELLDLEEL-LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490656625 185 EVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-235 |
1.67e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.22 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 13 PTLVVTGIGKTY-----AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAeyaPHSRAHAEA 87
Cdd:COG4525 2 SMLTVRHVSVRYpgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 88 lGVrmVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAG 167
Cdd:COG4525 79 -GV--VFQKDALLPWLNVLDNV---AFGLRLRGVPKAERRARAEELLALVGLADFA-RRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 168 DCRVLILDEPTAMLTA--REV--ELLFDqIARLKADGVALvyISHRLEELARVAQRVAVL--RDGRLVHVDRID 235
Cdd:COG4525 152 DPRFLLMDEPFGALDAltREQmqELLLD-VWQRTGKGVFL--ITHSVEEALFLATRLVVMspGPGRIVERLELD 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
277-484 |
2.61e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 80.72 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPprpaAIRSPADAVRHGIALVSedrkGEGLLLP 356
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK----SYQKNIEALRRIGALIE----APGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARGGVVDgerenalaaRQIDALRIRARGpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03268 87 LTARENLRLLARLLGIRKKRID---------EVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-204 |
2.77e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY-APHSRAHAEALGVRMVMQelnlvPTLT 104
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIdDPDVAEACHYLGHRNAMK-----PALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENL-----FLDRLPHRfgvidrrrlaadARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:PRK13539 90 VAENLefwaaFLGGEELD------------IAAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*.
gi 490656625 180 MLTAREVELLFDQI-ARLKADGVALV 204
Cdd:PRK13539 157 ALDAAAVALFAELIrAHLAQGGIVIA 182
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-227 |
3.36e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEyapHSRAHAEALGV 90
Cdd:PRK09452 12 SPLVELRGISKSFDGkEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD---ITHVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAEN----LFLDRLPH---RFGVIDrrrlaadaraAMARVGLDSL---DPDTLVGslgiGHQQMVE 160
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENvafgLRMQKTPAaeiTPRVME----------ALRMVQLEEFaqrKPHQLSG----GQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 161 IARSLAGDCRVLILDEPTAMLTAR---EVELLFDQIAR-LkadGVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKlrkQMQNELKALQRkL---GITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
266-484 |
3.90e-17 |
|
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: 80.69 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 266 RLRVERLSRGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYG-----ADAADGGTVSIGDpprpaairspaDAVR 338
Cdd:cd03260 2 ELRDLNVYYGDkhALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDG-----------KDIY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 339 HGIALVSEDRKGEGL------LLPQSIAANLSLG-QLARVARGGVVDGERENAL--------AARQIDALRirargpaqp 403
Cdd:cd03260 71 DLDVDVLELRRRVGMvfqkpnPFPGSIYDNVAYGlRLHGIKLKEELDERVEEALrkaalwdeVKDRLHALG--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 404 vaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREgRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03260 142 ---LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
.
gi 490656625 484 M 484
Cdd:cd03260 218 L 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
272-486 |
9.50e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.20 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 272 LSRGDA--VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgIALVSEDrk 349
Cdd:PRK09536 11 VEFGDTtvLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG--DDVEALSARAASRR-VASVPQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 geglllpQSIAANLSLGQLARVARG---GVVDGERENALAA--RQIDALRIrARGPAQPVAELSGGNQQKVAIGRWLGRD 424
Cdd:PRK09536 86 -------TSLSFEFDVRQVVEMGRTphrSRFDTWTETDRAAveRAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
264-487 |
9.71e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 9.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavRh 339
Cdd:COG3842 3 MPALELENVSKryGDvtALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--RDVTGLPPEK--R- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALVSEDrkgeGLLLPQ-SIAANLSLG-QLARVARGgvvdgEREnALAARQIDALRIRARGPAQPvAELSGGNQQKVAI 417
Cdd:COG3842 78 NVGMVFQD----YALFPHlTVAENVAFGlRMRGVPKA-----EIR-ARVAELLELVGLEGLADRYP-HQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 418 GRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
276-492 |
1.30e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.94 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP----RPAAIRspadAVRHGIALVSEDRKge 351
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlKRREIP----YLRRRIGVVFQDFR-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 glLLPQ-SIAANLSLGQlaRVArggvvdGERENALAARQIDALR---IRARGPAQPvAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:COG2884 90 --LLPDrTVYENVALPL--RVT------GKSRKEIRRRVREVLDlvgLSDKAKALP-HELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGG 492
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
265-484 |
1.47e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.85 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADG---GTVSI-GDPPRPaairspaDAVRHG 340
Cdd:cd03234 10 GLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFnGQPRKP-------DQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 341 IALVSE-DRKGEGLLLPQSI--AANLSLGQLARVA-RGGVVDGERENALAARQIDALRIRArgpaqpvaeLSGGNQQKVA 416
Cdd:cd03234 83 VAYVRQdDILLPGLTVRETLtyTAILRLPRKSSDAiRKKRVEDVLLRDLALTRIGGNLVKG---------ISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRaIVVVS-----SDLRELMlicDRIGVMSAGRM 484
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNR-IVILTihqprSDLFRLF---DRILLLSSGEI 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
26-229 |
1.50e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 77.35 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVrmvmqelnlvptltv 105
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 aenlfLDRLPHRFGvidrrrlaadaraamarvgldsldpDTLVGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:cd03247 80 -----LNQRPYLFD-------------------------TTLRNNLGRrfsgGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 182 ---TAREV-ELLFDQiarlkADGVALVYISHRLEELARVaQRVAVLRDGRLV 229
Cdd:cd03247 130 dpiTERQLlSLIFEV-----LKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-229 |
1.63e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSrAHAEalgVRMVMQElnlvPTL 103
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplVQYDHHY-LHRQ---VALVGQE----PVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 ---TVAENLF--LDRLPHrfgviDRRRLAADARAAMARVGLDSLDPDTLVGSLG----IGHQQMVEIARSLAGDCRVLIL 174
Cdd:TIGR00958 567 fsgSVRENIAygLTDTPD-----EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGsqlsGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 175 DEPTAMLTArEVELLFdQIARLKADGVALVyISHRLeELARVAQRVAVLRDGRLV 229
Cdd:TIGR00958 642 DEATSALDA-ECEQLL-QESRSRASRTVLL-IAHRL-STVERADQILVLKKGSVV 692
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
277-487 |
1.65e-16 |
|
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: 78.57 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRHGIALVSEDRKGEGLLlp 356
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG----HDVVREPREVRRRIGIVFQDLSVDDEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qSIAANLSLgqLARVArgGVVDGERENalaaRQIDALRIRARGPA--QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:cd03265 89 -TGWENLYI--HARLY--GVPGAERRE----RIDELLDFVGLLEAadRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 435 RGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
27-274 |
1.71e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVMQ--ELNLVPTlT 104
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQnpETQFVGR-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLfldrlphRFG----VIDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEP 177
Cdd:PRK13644 95 VEEDL-------AFGpenlCLPPIEIRKRVDRALAEIGLEKYrhrSPKTLSG----GQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 178 TAMLTAREVELLFDQIARLKADGVALVYISHRLEELaRVAQRVAVLRDGRLV---HVDRIDAQPTERLVALMAGR--EIA 252
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVlegEPENVLSDVSLQTLGLTPPSliELA 242
|
250 260
....*....|....*....|....*..
gi 490656625 253 EQ-AVHGTRTP----GAPRLRVERLSR 274
Cdd:PRK13644 243 ENlKMHGVVIPwentSSPSSFAEEICR 269
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-229 |
2.09e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.26 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHA-EALGVrmVMQEL-NLVPTLT 104
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrKKIGI--IFQNPdNQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEP 177
Cdd:PRK13632 101 VEDDI-------AFGLenkkVPPKKMKDIIDDLAKKVGMEDYldkEPQNLSG----GQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 178 TAMLTAREVELLFDQIARLKADGV-ALVYISHRLEElARVAQRVAVLRDGRLV 229
Cdd:PRK13632 170 TSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDE-AILADKVIVFSEGKLI 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
264-486 |
2.10e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 78.16 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLSR----GD----AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD-------PPRPA 328
Cdd:COG1136 2 SPLLELRNLTKsygtGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslsERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 329 AIRspadavRHGIALVSEDrkgeGLLLPQ-SIAANLSLGQLARvargGVVDGEREnALAARQIDALRIRARGPAQPvAEL 407
Cdd:COG1136 82 RLR------RRHIGFVFQF----FNLLPElTALENVALPLLLA----GVSRKERR-ERARELLERVGLGDRLDHRP-SQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 408 SGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLReLMLICDRIGVMSAGRMHA 486
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPE-LAARADRVIRLRDGRIVS 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-227 |
2.19e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVMQELNLVPTLTVAENL 109
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 110 FLDRLPH-RFGVI-----------DRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEP 177
Cdd:PRK11300 102 LVAQHQQlKTGLFsgllktpafrrAESEALDRAATWLERVGLLEH-ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 178 TAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
278-434 |
2.39e-16 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 76.15 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRspaDAVRHGIALVSEDRkgegLLLPQ 357
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER---KSLRKEIGYVFQDP----QLFPR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 358 SIAA-NLSLGQLARVARGGVVDGERENALAarQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:pfam00005 74 LTVReNLRLGLLLKGLSKREKDARAEEALE--KLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
274-508 |
2.43e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.93 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 274 RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRSpadaVRHGIALVSEDrkgeG 352
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRTVTRAS----LRRNIAVVFQD----A 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLLPQSIAANLslgqlaRVARGGVVDGE-RENALAARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGV 427
Cdd:PRK13657 419 GLFNRSIEDNI------RVGRPDATDEEmRAAAERAQAHDFIERKPDGYDTVVGErgrqLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALaREGRAIVVVS---SDLRElmliCDRIGVMSAGRmhaVFERGGWTQDALLGAAFA 504
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAhrlSTVRN----ADRILVFDNGR---VVESGSFDELVARGGRFA 564
|
....
gi 490656625 505 GYAR 508
Cdd:PRK13657 565 ALLR 568
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
28-235 |
2.74e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.58 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPhsrahaeaLGVRMVMQelnlvPTLTVAE 107
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL--------LELGAGFH-----PELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLdrlphrFGVIdrrrlaadaraamarVGLDSLDPDTLVGSL----GIG---HQQ-------MVeiAR-----SLAGD 168
Cdd:COG1134 108 NIYL------NGRL---------------LGLSRKEIDEKFDEIvefaELGdfiDQPvktyssgMR--ARlafavATAVD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 169 CRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRID 235
Cdd:COG1134 165 PDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
277-487 |
2.94e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 78.15 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavrHGIALVSEDRkgeGLLLP 356
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG--EDATDVPVQE---RNVGFVFQHY---ALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARGGV----VDGERENALAARQIDALRirARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:cd03296 89 MTVFDNVAFGLRVKPRSERPpeaeIRAKVHELLKLVQLDWLA--DRYPAQ----LSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 433 PTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-228 |
2.96e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHAEALGVRMVMQELNLVPTLT 104
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplHQMDEEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLfldRLPHRFGVIDRRRLAADARAAMARVGLDSlDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:PRK10584 105 ALENV---ELPALLRGESSRQSRNGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490656625 185 EVELLFDQIARLKAD-GVALVYISHRlEELARVAQRVAVLRDGRL 228
Cdd:PRK10584 181 TGDKIADLLFSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
13-228 |
3.50e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.15 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 13 PTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAHaeaL 88
Cdd:COG1137 2 MTLEAENLVKSYGKrTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithLPMHKRAR---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 GVRMVMQELNLVPTLTVAENL--FLDRLPhrfgvidrrrlaadaraamarvgldsLDP-------DTLVGSLGIGH--QQ 157
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNIlaVLELRK--------------------------LSKkereerlEELLEEFGITHlrKS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 158 M-----------VEIARSLAGDCRVLILDEPTA---MLTAREVELLfdqIARLKADGVAlVYIS-HRLEELARVAQRVAV 222
Cdd:COG1137 133 KayslsggerrrVEIARALATNPKFILLDEPFAgvdPIAVADIQKI---IRHLKERGIG-VLITdHNVRETLGICDRAYI 208
|
....*.
gi 490656625 223 LRDGRL 228
Cdd:COG1137 209 ISEGKV 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
275-486 |
3.95e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 79.77 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 275 GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaaiRSPADAvRHGIALVSEDRK----- 349
Cdd:TIGR02142 10 GDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-------RTLFDS-RKGIFLPPEKRRigyvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 GEGLLLPQ-SIAANLSLGqlarVARggvVDGERENALAARQIDALRIrarGP--AQPVAELSGGNQQKVAIGRWLGRDMG 426
Cdd:TIGR02142 82 QEARLFPHlSVRGNLRYG----MKR---ARPSERRISFERVIELLGI---GHllGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
271-490 |
4.19e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.81 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPadaVRH-GIALVSEDRk 349
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNLP---PRErRVGFVFQHY- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 gegLLLPQ-SIAANLSLGqlARVARggvVDGERENALAARQIDALRIR---ARGPAQpvaeLSGGNQQKVAIGRWLGRDM 425
Cdd:COG1118 85 ---ALFPHmTVAENIAFG--LRVRP---PSKAEIRARVEELLELVQLEglaDRYPSQ----LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 426 GVLLFDEPTRGIDVGAKFDIYALL-DALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFER 490
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLrRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIeqvgtpDEVYDR 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-280 |
4.66e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.35 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTY-----AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRahAEALGVR 91
Cdd:COG1135 4 LENLSKTFptkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE--RELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 ----MVMQELNLVPTLTVAEN----LFLDRLPHR-----------FgvidrrrlaadaraamarVGL-DSLD--PDTLVG 149
Cdd:COG1135 82 rkigMIFQHFNLLSSRTVAENvalpLEIAGVPKAeirkrvaelleL------------------VGLsDKADayPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 150 slgiGHQQMVEIARSLAGDCRVLILDEPTAML---TAREV-ELLfDQI-ARLkadGVALVYISHRLEELARVAQRVAVLR 224
Cdd:COG1135 144 ----GQKQRVGIARALANNPKVLLCDEATSALdpeTTRSIlDLL-KDInREL---GLTIVLITHEMDVVRRICDRVAVLE 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 225 DGRLV---HVDRIDAQP----TERLVALMAGREIAEQAVHGTRTPGAPRLRVeRLS-RGDAVRD 280
Cdd:COG1135 216 NGRIVeqgPVLDVFANPqselTRRFLPTVLNDELPEELLARLREAAGGGRLV-RLTfVGESADE 278
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-229 |
6.56e-16 |
|
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: 77.14 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEA-LGVrmVMQElNLVPTLTVA 106
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRqVGV--VLQE-NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFL-DRLPHRFGVIDRRRLAADARAAMARvgldSLDPDTLVGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:cd03252 94 DNIALaDPGMSMERVIEAAKLAGAHDFISEL----PEGYDTIVGEQGAglsgGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490656625 182 TArEVELLFDQIARLKADGVALVYISHRLEELaRVAQRVAVLRDGRLV 229
Cdd:cd03252 170 DY-ESEHAIMRNMHDICAGRTVIIIAHRLSTV-KNADRIIVMEKGRIV 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
27-242 |
7.27e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.06 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY-APHSRAHAEALGVRMVMQELNLVPTLTV 105
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKVDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDrlPHRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:PRK09493 95 LENVMFG--PLRVRGASKEEAEKQARELLAKVGLAERAhhyPSELSG----GQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 183 A---REVELLFDQIARlkaDGVALVYISHRLEELARVAQRVAVLRDGRLVH----VDRIDAQPTERL 242
Cdd:PRK09493 169 PelrHEVLKVMQDLAE---EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEdgdpQVLIKNPPSQRL 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-208 |
8.77e-16 |
|
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: 75.86 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHSRAHAEALGVRMVMQelnlvPTL 103
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILYLGHLPGLK-----PEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLfldrlphRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTA 183
Cdd:TIGR01189 89 SALENL-------HFWAAIHGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*
gi 490656625 184 REVELLFDQIARLKADGVALVYISH 208
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
278-483 |
1.02e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAaiRSPADAVRHGIalvsedrkgegllLPQ 357
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHARQRVGV-------------VPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 --SIAANLSLGQLARVArggvvdgERENALAARQIDAL--------RIRARGPAqPVAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:PRK13537 88 fdNLDPDFTVRENLLVF-------GRYFGLSAAAARALvppllefaKLENKADA-KVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-291 |
1.15e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.92 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL---GVRMVMQELNLVPTLTVAE 107
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDRlphRFGVIDRRRLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:PRK10070 126 NTAFGM---ELAGINAEERREKALDALRQVGLENYAhsyPDELSG----GMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 185 EVELLFDQIARLKADGV-ALVYISHRLEELARVAQRVAVLRDGRLVHV---DRIDAQPTERLV----------ALMAGRE 250
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVgtpDEILNNPANDYVrtffrgvdisQVFSAKD 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490656625 251 IAEQAVHGT--RTPG-APRLRVERLSRGDavRDVSFDVRAGEIF 291
Cdd:PRK10070 279 IARRTPNGLirKTPGfGPRSALKLLQDED--REYGYVIERGNKF 320
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
277-483 |
1.17e-15 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 74.73 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDrkgeGLLL 355
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD----LRDlDLESLRKNIAYVPQD----PFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLslgqlarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03228 89 SGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490656625 436 GIDVGAKFDIYALLDALaREGRAIVVVSSDLrELMLICDRIGVMSAGR 483
Cdd:cd03228 126 ALDPETEALILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-228 |
1.23e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.93 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG----------AEYAPHSRA 83
Cdd:PRK10619 6 LNVIDLHKRYGEhEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 84 HAEALGVR--MVMQELNLVPTLTVAENLFldRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEI 161
Cdd:PRK10619 86 QLRLLRTRltMVFQHFNLWSHMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 162 ARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-229 |
1.68e-15 |
|
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: 75.72 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHA-EALGVrmVMQELNLVPTlT 104
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrSMIGV--VLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLFLDRLPHRFGVIdrrrlaadaRAAMARVGLDSL------DPDTLVG----SLGIGHQQMVEIARSLAGDCRVLIL 174
Cdd:cd03254 93 IMENIRLGRPNATDEEV---------IEAAKEAGAHDFimklpnGYDTVLGenggNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 175 DEPTAMLTAREVELLFDQIARLKADGVALVyISHRLEELaRVAQRVAVLRDGRLV 229
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKGRTSII-IAHRLSTI-KNADKILVLDDGKII 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-270 |
1.85e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.53 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 19 GIGKTYAEP-----VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH--AEALGVR 91
Cdd:PRK11153 6 NISKVFPQGgrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 MVMQELNLVPTLTVAENLFldrLPHRFGVIDRRRLAADARAAMARVGL-DSLD--PDTLVGslgiGHQQMVEIARSLAGD 168
Cdd:PRK11153 86 MIFQHFNLLSSRTVFDNVA---LPLELAGTPKAEIKARVTELLELVGLsDKADryPAQLSG----GQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 169 CRVLILDEPTAML---TAREV-ELLFDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLV---HVDRIDAQP--- 238
Cdd:PRK11153 159 PKVLLCDEATSALdpaTTRSIlELLKDINREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLVeqgTVSEVFSHPkhp 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 490656625 239 -TERLVALMAGREIAEQ---AVHGTRTPGA-PRLRVE 270
Cdd:PRK11153 236 lTREFIQSTLHLDLPEDylaRLQAEPTTGSgPLLRLE 272
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-229 |
2.70e-15 |
|
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: 75.34 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RAHaealgVRMVMQELNLV 100
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASlRRQ-----IGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTlTVAENLfldrlphRFGVIDRRRLAADARAAMARVG--LDSLDP--DTLVGSLGI----GHQQMVEIARSLAGDCRVL 172
Cdd:cd03251 89 ND-TVAENI-------AYGRPGATREEVEEAARAANAHefIMELPEgyDTVIGERGVklsgGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKADGVALVyISHRLEELARvAQRVAVLRDGRLV 229
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-230 |
2.84e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.61 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYAE-----PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA-----PHS 81
Cdd:PRK10535 2 TALLELKDIRRSYPSgeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldadALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 82 RAHAEALGvrMVMQELNLVPTLTVAENLfldRLPHRFGVIDRRRLAADARAAMARVGLD---SLDPDTLVGslgiGHQQM 158
Cdd:PRK10535 82 QLRREHFG--FIFQRYHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGLEdrvEYQPSQLSG----GQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 159 VEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRlEELARVAQRVAVLRDGRLVH 230
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-229 |
3.36e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.47 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG-AEYAPHSRAHAEALGVR----MVMQELNLVPT 102
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkVLYFGKDIFQIDAIKLRkevgMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLDRLPHrfGVIDRRRLAADARAAMARVGLDSLDPDTL---VGSLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:PRK14246 105 LSIYDNIAYPLKSH--GIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 180 MLTAREVELLFDQIARLKADgVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
262-487 |
4.00e-15 |
|
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: 75.02 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 262 PGAPRLRVERL--SRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAV 337
Cdd:COG1127 1 MSEPMIEVRNLtkSFGDRVvlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 338 RHGI-------AL-----VSED-----RkgEGLLLPQSIAANLSLGQLARVARGGVVDgerenalaarqidalriraRGP 400
Cdd:COG1127 81 RRRIgmlfqggALfdsltVFENvafplR--EHTDLSEAEIRELVLEKLELVGLPGAAD-------------------KMP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 401 AqpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID-VGAKfDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGV 478
Cdd:COG1127 140 S----ELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSA-VIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAV 214
|
....*....
gi 490656625 479 MSAGRMHAV 487
Cdd:COG1127 215 LADGKIIAE 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
267-486 |
4.48e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRGDA----VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHgIA 342
Cdd:PRK11231 3 LRTENLTVGYGtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD--KPISMLSSRQLARR-LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDrkgegLLLPQSIAAN----------LSL-GQLARVARGGVvdgerENALAARQIDALRIRargpaqPVAELSGGN 411
Cdd:PRK11231 80 LLPQH-----HLTPEGITVRelvaygrspwLSLwGRLSAEDNARV-----NQAMEQTRINHLADR------RLTDLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 412 QQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
282-486 |
5.95e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 282 SFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------PP--RPaairspadavrhgIALVSEdrkgEGL 353
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalPPaeRP-------------VSMLFQ----ENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQ-SIAANLSLG----------QLARVARggvvdgerenalAARQIDALRIRARGPAQpvaeLSGGNQQKVAIGRWLG 422
Cdd:COG3840 82 LFPHlTVAQNIGLGlrpglkltaeQRAQVEQ------------ALERVGLAGLLDRLPGQ----LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-246 |
7.48e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.15 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMR-LAGAEY------APHSRAHAEALgVRMVMQELNLVP 101
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWvdmtkpGPDGRGRAKRY-IGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TLTVAENLF----LDrLPHRFGVIdrrrlaaDARAAMARVGLDS------LD--PDTLVGslgiGHQQMVEIARSLAGDC 169
Cdd:TIGR03269 379 HRTVLDNLTeaigLE-LPDELARM-------KAVITLKMVGFDEekaeeiLDkyPDELSE----GERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 170 RVLILDEPTAML---TAREVEllfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVhvdriDAQPTERLVAL 245
Cdd:TIGR03269 447 RIVILDEPTGTMdpiTKVDVT---HSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIV-----KIGDPEEIVEE 518
|
.
gi 490656625 246 M 246
Cdd:TIGR03269 519 L 519
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-489 |
8.40e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSR--------AHAEALGVR-----MV 93
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqvielseqSAAQMRHVRgadmaMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQE--LNLVPTLTV----AENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:PRK10261 110 FQEpmTSLNPVFTVgeqiAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG----GMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH---VDRIDAQP----T 239
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVEtgsVEQIFHAPqhpyT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVAL------MAGREI---------------AEQAVHGTRTPGAPRLRVE--------------RLSRG-DAVRDVSF 283
Cdd:PRK10261 266 RALLAAvpqlgaMKGLDYprrfplislehpakqEPPIEQDTVVDGEPILQVRnlvtrfplrsgllnRVTREvHAVEKVSF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 284 DVRAGEIFGISGLIGAGRT----ELLRLVygadAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDRKGEgllLPQSI 359
Cdd:PRK10261 346 DLWPGETLSLVGESGSGKSttgrALLRLV----ESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYAS---LDPRQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 360 AANLSLGQLARVArgGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDV 439
Cdd:PRK10261 419 TVGDSIMEPLRVH--GLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 440 GAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFE 489
Cdd:PRK10261 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIveigprRAVFE 553
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-439 |
8.54e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.30 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAM---------RL--------AGAEY---APHSRAHAE 86
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivaRLqqdpprnvEGTVYdfvAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 87 ALgvRMVMQELNLVPTLTVAENLflDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLA 166
Cdd:PRK11147 97 YL--KRYHDISHLVETDPSEKNL--NELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 167 GDCRVLILDEPTAMLTAREVELL--FdqiarLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH---------VDRID 235
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLegF-----LKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSypgnydqylLEKEE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 236 AQPTERLVALMAGREIAEQAV---HG-----TRTPGAPR----LRVERLSR----GDA---------------------- 277
Cdd:PRK11147 248 ALRVEELQNAEFDRKLAQEEVwirQGikarrTRNEGRVRalkaLRRERSERrevmGTAkmqveeasrsgkivfemenvny 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 -------VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIG--------DPPRpaAIRSPADAVrhgia 342
Cdd:PRK11147 328 qidgkqlVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklevayfDQHR--AELDPEKTV----- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 lvsEDRKGEGlllPQSIaanlslgqlarvarggVVDGERENALAARQiDAL--RIRARgpaQPVAELSGGNQQKVAIGRW 420
Cdd:PRK11147 401 ---MDNLAEG---KQEV----------------MVNGRPRHVLGYLQ-DFLfhPKRAM---TPVKALSGGERNRLLLARL 454
|
490
....*....|....*....
gi 490656625 421 LGRDMGVLLFDEPTRGIDV 439
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDV 473
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
277-483 |
1.06e-14 |
|
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: 72.95 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAiRSPADAVRHGIALVSEDRKgeglLLP 356
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD-KKNINELRQKVGMVFQQFN----LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 Q-SIAANLSLGQLarvarggVVDGERENALAARQIDALR---IRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:cd03262 90 HlTVLENITLAPI-------KVKGMSKAEAEERALELLEkvgLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 433 PTRGID---VGAKFDIyalLDALAREGRAIVVVSSDL---RElmlICDRIGVMSAGR 483
Cdd:cd03262 162 PTSALDpelVGEVLDV---MKDLAEEGMTMVVVTHEMgfaRE---VADRVIFMDDGR 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-228 |
1.13e-14 |
|
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: 77.36 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 20 IGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGvrMVMQELNL 99
Cdd:TIGR01257 937 IFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLG--MCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAEN-LFLDRLPHRfgvidrrrlaadaRAAMARVGLDSLDPDTLV--------GSLGIGHQQMVEIARSLAGDCR 170
Cdd:TIGR01257 1015 FHHLTVAEHiLFYAQLKGR-------------SWEEAQLEMEAMLEDTGLhhkrneeaQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKAdGVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
264-491 |
1.25e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.81 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLSR----GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRH 339
Cdd:PRK11701 4 QPLLSVRGLTKlygpRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM----------RDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALVSEDRK-----GEGLLLPQSIAANLSLGqlarVARGGVVdGERENALAAR----------------QIDALRIRAR 398
Cdd:PRK11701 74 DLYALSEAERrrllrTEWGFVHQHPRDGLRMQ----VSAGGNI-GERLMAVGARhygdiratagdwlervEIDAARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 399 gPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIG 477
Cdd:PRK11701 149 -PTT----FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLL 223
|
250
....*....|....
gi 490656625 478 VMSAGRmhaVFERG 491
Cdd:PRK11701 224 VMKQGR---VVESG 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
279-504 |
1.28e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 73.42 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDRkgegLLLPQ 357
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD----IREvTLDSLRRAIGVVPQDT----VLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLslgqlaRVARGGVVDGERENALAARQIDALRIRAR-GPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:cd03253 90 TIGYNI------RYGRPDATDEEVIEAAKAAQIHDKIMRFPdGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 433 PTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLRELMlICDRIGVMSAGRmhaVFERGGWTQDALLGAAFA 504
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIV-NADKIIVLKDGR---IVERGTHEELLAKGGLYA 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-251 |
1.85e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYA-EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEAlGVrmV 93
Cdd:PRK11248 2 LQISHLYADYGgKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG---KPVEGPGAER-GV--V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDC 169
Cdd:PRK11248 76 FQNEGLLPWRNVQDNV-------AFGLqlagVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAG 248
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARRFVAGESS 227
|
...
gi 490656625 249 REI 251
Cdd:PRK11248 228 RSI 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
240-499 |
2.01e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.97 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALM-AGREIAEQAVHGTRTPGAPRLRVERLS---RGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADA 313
Cdd:COG1132 312 ERIFELLdEPPEIPDPPGAVPLPPVRGEIEFENVSfsyPGDrpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 314 ADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDrkgeGLLLPQSIAANLSLGqlarvaRGGVVDGERENALAARQIDA 392
Cdd:COG1132 392 PTSGRILIDGVD----IRDlTLESLRRQIGVVPQD----TFLFSGTIRENIRYG------RPDATDEEVEEAAKAAQAHE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 393 LrIRA--RGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALaREGRAIVVVSSDL 466
Cdd:COG1132 458 F-IEAlpDGYDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRL 535
|
250 260 270
....*....|....*....|....*....|...
gi 490656625 467 RELMLiCDRIGVMSAGRmhaVFERGgwTQDALL 499
Cdd:COG1132 536 STIRN-ADRILVLDDGR---IVEQG--THEELL 562
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
271-512 |
3.75e-14 |
|
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: 73.98 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------------PPRpaairspadavR 338
Cdd:COG4148 8 RLRRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflPPH-----------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 339 HGIALVSEDrkgeGLLLP-QSIAANLSLGQlARVARGgvvdgeRENALAARQIDALRIRA---RGPAQpvaeLSGGNQQK 414
Cdd:COG4148 77 RRIGYVFQE----ARLFPhLSVRGNLLYGR-KRAPRA------ERRISFDEVVELLGIGHlldRRPAT----LSGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 415 VAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRMHAVfergGW 493
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVAS----GP 217
|
250
....*....|....*....
gi 490656625 494 TQDALLGAAFAGYARRDAA 512
Cdd:COG4148 218 LAEVLSRPDLLPLAGGEEA 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
276-471 |
4.39e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.73 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAI--RSPADAVrhgialvsedrkgegl 353
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVpqRSEVPDS---------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 lLPQSIAANLSLGQLARVARGGVVDGER----ENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:NF040873 70 -LPLTVRDLVAMGRWARRGLWRRLTRDDraavDDALERVGLADLAGR------QLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELML 471
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
276-502 |
4.64e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.77 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRSPADAVRHGIALVSEDRKgeglL 354
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMSKLSSAAKAELRNQKLGFIYQFHH----L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LP-----QSIAANLSLGQLARvarggvvdgERENALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:PRK11629 99 LPdftalENVAMPLLIGKKKP---------AEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRelmlicdrigvmSAGRMHAVFE-RGGWTQD--ALLGAA 502
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ------------LAKRMSRQLEmRDGRLTAelSLMGAE 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-229 |
5.06e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.88 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 10 PDTPTLVVTGIGKTYAEPV-LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL 88
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 GVRMVMQ----------ELNLVPTLT----VAENLFLDRLPHrFGVIDRRRLAADARAAMARVGLDSLdPDTLVGslgiG 154
Cdd:PRK11701 82 ERRRLLRtewgfvhqhpRDGLRMQVSaggnIGERLMAVGARH-YGDIRATAGDWLERVEIDAARIDDL-PTTFSG----G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPTAML----TARevelLFDQIARLKAD-GVALVYISHRLeELARV-AQRVAVLRDGRL 228
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLdvsvQAR----LLDLLRGLVRElGLAVVIVTHDL-AVARLlAHRLLVMKQGRV 230
|
.
gi 490656625 229 V 229
Cdd:PRK11701 231 V 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-228 |
5.11e-14 |
|
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: 71.35 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYApHSRAHAEalgVRMVMQElnlvPTL 103
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpiSQYE-HKYLHSK---VSLVGQE----PVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 ---TVAENLFLDRLPHRFGVIdrrRLAADARAAMARVGLDSLDPDTLVGSLGI----GHQQMVEIARSLAGDCRVLILDE 176
Cdd:cd03248 100 farSLQDNIAYGLQSCSFECV---KEAAQKAHAHSFISELASGYDTEVGEKGSqlsgGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 177 PTAMLTArEVELLFDQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRL 228
Cdd:cd03248 177 ATSALDA-ESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-229 |
5.45e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.47 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYaphsRAHAEALGVRMVMQELNLV 100
Cdd:PRK13649 15 GTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI----TSTSKNKDIKQIRKKVGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 ---PTLTVAENLFLDRL---PHRFGViDRRRLAADARAAMARVGLD----SLDPDTLVGslgiGHQQMVEIARSLAGDCR 170
Cdd:PRK13649 91 fqfPESQLFEETVLKDVafgPQNFGV-SQEEAEALAREKLALVGISeslfEKNPFELSG----GQMRRVAIAGILAMEPK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-229 |
6.08e-14 |
|
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: 71.49 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RahaEALGVrmvmqelnlVPT 102
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSlR---RAIGV---------VPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVaenLFLDRLPH--RFGVIDRRRLAADARAAMARVGlDSLDP-----DTLVGSLGI----GHQQMVEIARSLAGDCRV 171
Cdd:cd03253 83 DTV---LFNDTIGYniRYGRPDATDEEVIEAAKAAQIH-DKIMRfpdgyDTIVGERGLklsgGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 172 LILDEPTAML---TAREVellFDQIARLkADGVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:cd03253 159 LLLDEATSALdthTEREI---QAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
277-483 |
6.34e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.80 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP----RPAAIRspadAVRHGIALVSEdrkGEG 352
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltalSERELR----AARRKIGMIFQ---HFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLLPQSIAAN--LSLgQLARVARggvvdGEREnalaaRQIDAL--------RIRARgPAQpvaeLSGGNQQKVAIGRWLG 422
Cdd:COG1135 93 LLSSRTVAENvaLPL-EIAGVPK-----AEIR-----KRVAELlelvglsdKADAY-PSQ----LSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDL---RElmlICDRIGVMSAGR 483
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMdvvRR---ICDRVAVLENGR 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-236 |
7.26e-14 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 73.98 E-value: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS----RAHaealgVRMVMQELNLVPT 102
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslRRQ-----VALVSQDVVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 lTVAENLfldrlphRFGVIDRRRLAADARAAMARVGLDSLDP-----DTLVGSLGI----GHQQMVEIARSLAGDCRVLI 173
Cdd:TIGR02203 421 -TIANNI-------AYGRTEQADRAEIERALAAAYAQDFVDKlplglDTPIGENGVllsgGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKADGVALVyISHRLEELARvAQRVAVLRDGRLV----HVDRIDA 236
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQGRTTLV-IAHRLSTIEK-ADRIVVMDDGRIVergtHNELLAR 557
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
265-486 |
7.68e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 71.34 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS--RGDA--VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHg 340
Cdd:PRK13548 1 AMLEARNLSvrLGGRtlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG--RPLADWSPAELARR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 341 IAlvsedrkgeglLLPQSiaANLS----------LGQLARVARGGVVDGERENALAARQIDALRIRargpaqPVAELSGG 410
Cdd:PRK13548 78 RA-----------VLPQH--SSLSfpftveevvaMGRAPHGLSRAEDDALVAAALAQVDLAHLAGR------DYPQLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 411 NQQKVAIGRWL------GRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK13548 139 EQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGR 218
|
...
gi 490656625 484 MHA 486
Cdd:PRK13548 219 LVA 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-229 |
8.70e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.00 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG-VRMVMQ--EL 97
Cdd:PRK13637 15 GTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKkVGLVFQypEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 98 NLVPTlTVAENLFLDrlPHRFGVIDRRRLAADARAAMArVGLDSLD-----PDTLVGslgiGHQQMVEIARSLAGDCRVL 172
Cdd:PRK13637 95 QLFEE-TIEKDIAFG--PINLGLSEEEIENRVKRAMNI-VGLDYEDykdksPFELSG----GQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
240-466 |
1.52e-13 |
|
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: 72.78 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMA---GREIAEQAVHGTRTPGAPRLRVERLSRG-----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA 311
Cdd:TIGR02868 305 ERIVEVLDaagPVAEGSAPAAGAVGLGKPTLELRDLSAGypgapPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 312 DAADGGTVSIGDPPRPAAirsPADAVRHGIALVSEDRKgeglLLPQSIAANLslgqlaRVARGGVVDGERENAL-AARQI 390
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSL---DQDEVRRRVSVCAQDAH----LFDTTVRENL------RLARPDATDEELWAALeRVGLA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 391 DALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDAlAREGRAIVVVSSDL 466
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-247 |
1.65e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.48 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 9 TPDTPtLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMrLAGAeyAPHSRAHAEa 87
Cdd:PRK11247 8 NQGTP-LLLNAVSKRYGErTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--APLAEARED- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 88 lgVRMVMQELNLVPTLTVAENLFLDRLPHrfgvidrrrLAADARAAMARVGLDSLD---PDTLVGslgiGHQQMVEIARS 164
Cdd:PRK11247 83 --TRLMFQDARLLPWKKVIDNVGLGLKGQ---------WRDAALQALAAVGLADRAnewPAALSG----GQKQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 165 LAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRL---VHVD--RIDAQP 238
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDlpRPRRRG 227
|
....*....
gi 490656625 239 TERLVALMA 247
Cdd:PRK11247 228 SARLAELEA 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-208 |
1.73e-13 |
|
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: 69.44 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALgvRMVMQELNLVPTLTV 105
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL--LYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENL-FLDRLPHRFGVIDrrrlaadaraAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAR 184
Cdd:cd03231 91 LENLrFWHADHSDEQVEE----------ALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....
gi 490656625 185 EVELLFDQIARLKADGVALVYISH 208
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTH 183
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-232 |
2.10e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRlagaeyaphsrahaeaLGVRMV 93
Cdd:COG0488 316 LELEGLSKSYGDkTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK----------------LGETVK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 M----QEL-NLVPTLTVAENL--------------FLDRLphrfgvidrrrlaadaraamarvGLDSLDPDTLVGSLGIG 154
Cdd:COG0488 380 IgyfdQHQeELDPDKTVLDELrdgapggteqevrgYLGRF-----------------------LFSGDDAFKPVGVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPT-----AMLTAREvELL--FdqiarlkaDGvALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTnhldiETLEALE-EALddF--------PG-TVLLVSHDRYFLDRVATRILEFEDGG 506
|
....*
gi 490656625 228 LVHVD 232
Cdd:COG0488 507 VREYP 511
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-229 |
2.20e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 69.09 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGL--VAPTTGAMRLAG---AEYAPHSRAhaeALGVRMVMQELNLVPT 102
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGediTDLPPEERA---RLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAEnlFLdrlphRFgvidrrrlaadaraamarVGldsldpdtlVGSLGiGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:cd03217 92 VKNAD--FL-----RY------------------VN---------EGFSG-GEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490656625 183 AREVELLFDQIARLKADGVALVYISHRLEELARV-AQRVAVLRDGRLV 229
Cdd:cd03217 137 IDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIV 184
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
277-484 |
2.39e-13 |
|
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: 69.67 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPpRPAAIRspaDAVRHGIALVSedrkGEGLLLP 356
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRR---KKFLRRIGVVF----GQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARggvVDGERENALAARQIDALRIrARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03267 108 WDLPVIDSFYLLAAIYD---LPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 437 IDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
266-486 |
2.46e-13 |
|
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: 69.06 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 266 RLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAirSPADAVrhgialVS 345
Cdd:cd03298 2 RLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRP------VS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 346 EDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGpaqpvaELSGGNQQKVAIGRWLGRDM 425
Cdd:cd03298 74 MLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPG------ELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 426 GVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
267-487 |
2.51e-13 |
|
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: 69.67 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR--GD-AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI------GDPPRpaairspadav 337
Cdd:cd03299 1 LKVENLSKdwKEfKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkditNLPPE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 338 RHGIALVSEDRKgeglLLPQ-SIAANLSLGqlARVARGGVVDGEREnalaARQIDA-LRIRA---RGPAQpvaeLSGGNQ 412
Cdd:cd03299 70 KRDISYVPQNYA----LFPHmTVYKNIAYG--LKKRKVDKKEIERK----VLEIAEmLGIDHllnRKPET----LSGGEQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 413 QKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:cd03299 136 QRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-210 |
2.69e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRlagaeyaphsraHAEALGVRMVMQELNLVPTLTVAE 107
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLRIGYVPQKLYLDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLdRLphRFGVIDRRRLAADARAAMARVgldsldPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVE 187
Cdd:PRK09544 87 NRFL-RL--RPGTKKEDILPALKRVQAGHL------IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180
....*....|....*....|....
gi 490656625 188 LLFDQIARLKAD-GVALVYISHRL 210
Cdd:PRK09544 158 ALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-231 |
2.82e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.56 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVapttgamrlagaEYAPHSRAHAEAL----------------GVR 91
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLI------------ELYPEARVSGEVYldgqdifkmdvielrrRVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 MVMQELNLVPTLTVAEN----LFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTlvGSLGIGHQQMVEIARSLAG 167
Cdd:PRK14247 86 MVFQIPNPIPNLSIFENvalgLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPA--GKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 168 DCRVLILDEPTAML----TAReVELLFdqiARLKADgVALVYISHRLEELARVAQRVAVLRDGRLVHV 231
Cdd:PRK14247 164 QPEVLLADEPTANLdpenTAK-IESLF---LELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-229 |
3.64e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.86 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHaealGVRMVMQELNLV---PTLTV 105
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNK----NLKKLRKKVSLVfqfPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDRL---PHRFGVIDrRRLAADARAAMARVGLD----SLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:PRK13641 99 FENTVLKDVefgPKNFGFSE-DEAKEKALKWLKKVGLSedliSKSPFELSG----GQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
29-232 |
3.67e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIV--AGLVAP---TTGAMRLAGAE-YAPHSRAHAEALGVRMVMQELNLVPt 102
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNiYSPRTDTVDLRKEIGMVFQQPNPFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLD-RLPhrfGVIDRRRLAADARAAMARVGL-----DSLDpDTLVGSLGiGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK14239 100 MSIYENVVYGlRLK---GIKDKQVLDEAVEKSLKGASIwdevkDRLH-DSALGLSG-GQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 177 PTAML---TAREVEllfDQIARLKADgVALVYISHRLEELARVAQRVAVLRDGRLVHVD 232
Cdd:PRK14239 175 PTSALdpiSAGKIE---ETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-214 |
3.83e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIG-KTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSrahAEALgv 90
Cdd:PRK10247 5 SPLLQLQNVGyLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK---PEIY-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTL---TVAENL---------------FLDRLpHRFGVidrrrlaadaraamarvgldsldPDTL----V 148
Cdd:PRK10247 80 RQQVSYCAQTPTLfgdTVYDNLifpwqirnqqpdpaiFLDDL-ERFAL-----------------------PDTIltknI 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 149 GSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELA 214
Cdd:PRK10247 136 AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEIN 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
15-227 |
4.39e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.70 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGamrlagaeyaphsrahaealgvrmv 93
Cdd:cd03221 1 IELENLSKTYGGkLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 mqELNLVPTLTVAenlFLDRLphrfgvidrrrlaadaraamarvgldsldpdtlvgSLGighQQM-VEIARSLAGDCRVL 172
Cdd:cd03221 56 --IVTWGSTVKIG---YFEQL-----------------------------------SGG---EKMrLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 173 ILDEPTAMLTAREVELLFDQIARLKAdgvALVYISHRLEELARVAQRVAVLRDGR 227
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-229 |
4.84e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.35 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS-----RAHAEalgvrMVMQELN--L 99
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdiRNKAG-----MVFQNPDnqI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLT---VA---ENLFLDRLPHRFGVIDRRRLaadaraamarVGLDSLD---PDTLVGslgiGHQQMVEIARSLAGDCR 170
Cdd:PRK13633 99 VATIVeedVAfgpENLGIPPEEIRERVDESLKK----------VGMYEYRrhaPHLLSG----GQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 171 VLILDEPTAMLTA---REVellFDQIARL-KADGVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:PRK13633 165 CIIFDEPTAMLDPsgrREV---VNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-226 |
4.94e-13 |
|
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: 72.35 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTY---AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHsrahaeal 88
Cdd:TIGR01257 1935 TDILRLNELTKVYsgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN-------- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 gVRMVMQELNLVPTLTVAENLFLDR----LPHRFGVIDRRRLAADARAAMARVGLdSLDPDTLVGSLGIGHQQMVEIARS 164
Cdd:TIGR01257 2007 -ISDVHQNMGYCPQFDAIDDLLTGRehlyLYARLRGVPAEEIEKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 165 LAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDG 226
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
281-484 |
5.13e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.01 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIrspadAVRHGIALVSEDRKGEGL------L 354
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTAR-----SLSQQKGLIRQLRQHVGFvfqnfnL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAanlslgqLARVARGGV-VDGE-RENALA-ARQIDA-LRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLF 430
Cdd:PRK11264 97 FPHRTV-------LENIIEGPViVKGEpKEEATArARELLAkVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 431 DEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
277-474 |
5.72e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRspadavRHGIALV--SEDRKGEGLL 354
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ------KNLVAYVpqSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGQLARVARGGVVDGERENALAARqIDALRIRARgpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALAR-VDMVEFRHR----QIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490656625 435 RGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICD 474
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
28-230 |
6.10e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.33 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPhsrahaeaLGVRMVMQelnlvPTLTVAE 107
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--------LGLGGGFN-----PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDrlphrfGVIdrrrlaadaraamarVGLDSLDPDTLVGSL----GIG---HQQMVE-----IAR-----SLAGDCR 170
Cdd:cd03220 104 NIYLN------GRL---------------LGLSRKEIDEKIDEIiefsELGdfiDLPVKTyssgmKARlafaiATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-229 |
6.99e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTYAEPVlddvSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAP-HSRAHAEAlgVRMVMQELNL 99
Cdd:PRK10575 23 GRTLLHPL----SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARK--VAYLPQQLPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAENLFLDRLP-H----RFGVIDrrrlAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLIL 174
Cdd:PRK10575 97 AEGMTVRELVAIGRYPwHgalgRFGAAD----REKVEEAISLVGLKPL-AHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 175 DEPTAML-TAREVELLfDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10575 172 DEPTSALdIAHQVDVL-ALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
28-208 |
7.94e-13 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 67.06 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYApHSRAHAEAL--GVRMVMQELNlvptltv 105
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLLERrqRVGLVFQDPD------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 aENLFLDRL-------PHRFGVIDRRRLAADARAAMArVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:TIGR01166 79 -DQLFAADVdqdvafgPLNLGLSEAEVERRVREALTA-VGASGLR-ERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISH 208
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
271-485 |
8.77e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 67.60 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 271 RLSRGDAVRDVSFDVRAGeIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRHGIALvsedRKG 350
Cdd:cd03264 9 RYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG----------QDVLKQPQKL----RRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 EGLLlPQ--SIAANLS-LGQLARVARGGVVDGERENALAARQIDALRIRARGpAQPVAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:cd03264 74 IGYL-PQefGVYPNFTvREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALAREgrAIVVVSSDLRE-LMLICDRIGVMSAGRMH 485
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
277-465 |
1.03e-12 |
|
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: 67.43 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDRKgegLLLP 356
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFR---LLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANlslgqlarVARGGVVDGERENALAARQIDALR---IRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDEP 433
Cdd:cd03292 93 RNVYEN--------VAFALEVTGVPPREIRKRVPAALElvgLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|..
gi 490656625 434 TRGIDVGAKFDIYALLDALAREGRAIVVVSSD 465
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
19-244 |
1.24e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.29 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 19 GIGKTYAEPVLD-DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHSRahaealGVRMVM 94
Cdd:PRK11000 8 NVTKAYGDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAER------GVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 95 QELNLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAG 167
Cdd:PRK11000 82 QSYALYPHLSVAENM-------SFGLklagAKKEEINQRVNQVAEVLQLAHLldrKPKALSG----GQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 168 DCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDR---IDAQPTERLV 243
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKpleLYHYPANRFV 230
|
.
gi 490656625 244 A 244
Cdd:PRK11000 231 A 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-229 |
1.41e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.27 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYapHSRAHAEALgvRMVMQELNLV 100
Cdd:PRK13646 15 GTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI--THKTKDKYI--RPVRKRIGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTLTVAEnLFLDRL-------PHRFGvIDRRRLAADARAAMARVGLD----SLDPDTLVGslgiGHQQMVEIARSLAGDC 169
Cdd:PRK13646 91 FQFPESQ-LFEDTVereiifgPKNFK-MNLDEVKNYAHRLLMDLGFSrdvmSQSPFQMSG----GQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 170 RVLILDEPTAML---TAREVELLFDQIArlKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13646 165 DIIVLDEPTAGLdpqSKRQVMRLLKSLQ--TDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-230 |
1.55e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.58 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeYAPHSR--AHAEALGVrmVM-QELNLVPTLTV 105
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRrkEFARRIGV--VFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDRLPHRfgvIDRRRLAADAraamarvgldsldpDTLVGSLGIGH------------QQM-VEIARSLAGDCRVL 172
Cdd:COG4586 114 IDSFRLLKAIYR---IPDAEYKKRL--------------DELVELLDLGElldtpvrqlslgQRMrCELAAALLHRPKIL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 173 ILDEPT------AMLTAREvellFdqIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:COG4586 177 FLDEPTigldvvSKEAIRE----F--LKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIY 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
280-463 |
1.59e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.43 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRhgialvsEDRKGEGL------ 353
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG----LKVNDPKVDER-------LIRQEAGMvfqqfy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIA-ANLSLGQLaRVARGGVVDGERenaLAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:PRK09493 88 LFPHLTAlENVMFGPL-RVRGASKEEAEK---QARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|.
gi 490656625 433 PTRGIDVGAKFDIYALLDALAREGRAIVVVS 463
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVT 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-465 |
1.77e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 19 GIGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLagaeyaphsrahAEALGVRMVMQE 96
Cdd:PRK11819 11 RVSKVVppKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------------APGIKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 97 LNLVPTLTVAENLF---------LDRLPH---RFGVIDRRRLAADARAAMARVGLDSLD-------------------PD 145
Cdd:PRK11819 79 PQLDPEKTVRENVEegvaevkaaLDRFNEiyaAYAEPDADFDALAAEQGELQEIIDAADawdldsqleiamdalrcppWD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 146 TLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKAdgvALVYISHRLEELARVAQRVAVLRD 225
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG---TVVAVTHDRYFLDNVAGWILELDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 226 GRLV------------HVDRI---DAQPTERLVALMA----------GR------------EIAEQAVHGTRT------P 262
Cdd:PRK11819 236 GRGIpwegnysswleqKAKRLaqeEKQEAARQKALKRelewvrqspkARqakskarlaryeELLSEEYQKRNEtneifiP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 263 GAPRL-----RVERLSR--GDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGdpprpaairsp 333
Cdd:PRK11819 316 PGPRLgdkviEAENLSKsfGDRLliDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 334 aDAVRhgIALVSEDRKgeglllpqSIAANLSLGQLarvarggVVDGERENALAARQIDAlriRA-------RGPAQ--PV 404
Cdd:PRK11819 385 -ETVK--LAYVDQSRD--------ALDPNKTVWEE-------ISGGLDIIKVGNREIPS---RAyvgrfnfKGGDQqkKV 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAkfdIYALLDALAREGRAIVVVSSD 465
Cdd:PRK11819 444 GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET---LRALEEALLEFPGCAVVISHD 501
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-238 |
1.86e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.45 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL--GVRMVMQ----ELN---- 98
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQnpygSLNprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 99 ---------LVPT-LTVAENL---------------FLDRLPHRFGvidrrrlaadaraamarvGldsldpdtlvgslgi 153
Cdd:PRK11308 111 vgqileeplLINTsLSAAERRekalammakvglrpeHYDRYPHMFS------------------G--------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAML----TAREVELLFDqiarLKAD-GVALVYISHRLEELARVAQRVAVLRDGRL 228
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALdvsvQAQVLNLMMD----LQQElGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
250
....*....|...
gi 490656625 229 VHV---DRIDAQP 238
Cdd:PRK11308 234 VEKgtkEQIFNNP 246
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
277-513 |
1.91e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIALVSEDRKgegLLLP 356
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG--KDITDWQTAKIMREAVAIVPEGRR---VFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGqlarvarGGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK11614 95 MTVEENLAMG-------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGrmHAVFERGGwtqDALLgaafAGYARRDAAL 513
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG--HVVLEDTG---DALL----ANEAVRSAYL 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-229 |
1.98e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.74 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRA-HAEAL--GVRMVMQ--ELNLVPTl 103
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkKLKPLrkKVGIVFQfpEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDrlPHRFGVIDrrrlAADARAAMARVGLDSLDPDTLVGS---LGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:PRK13634 102 TVEKDICFG--PMNFGVSE----EDAKQKAREMIELVGLPEELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 181 LTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-230 |
2.08e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.35 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVaptTG-----------------AMRLAGAeyA 78
Cdd:PRK09984 7 VEKLAKTFNQhQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGdksagshiellgrtvqrEGRLARD--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 79 PHSRAHAEAlgvrmVMQELNLVPTLTVAENLFLDRL---PHRFGVID--RRRLAADARAAMARVGLDSLdPDTLVGSLGI 153
Cdd:PRK09984 82 RKSRANTGY-----IFQQFNLVNRLSVLENVLIGALgstPFWRTCFSwfTREQKQRALQALTRVGMVHF-AHQRVSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVH 230
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
278-483 |
2.11e-12 |
|
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: 66.80 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---PPRPAAIRSpadavRHGIALvsedrkgegll 354
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqdiTKLPMHKRA-----RLGIGY----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQ--SIAANLSLGQ--LARVARGGVVDGER----ENALAARQIDALRirargpAQPVAELSGGNQQKVAIGRWLGRDMG 426
Cdd:cd03218 80 LPQeaSIFRKLTVEEniLAVLEIRGLSKKEReeklEELLEEFHITHLR------KSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
277-489 |
2.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPA-DAVRHGIALVSEdrKGEGLLL 355
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEiKPVRKKVGVVFQ--FPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLSLGqlarvARGGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:PRK13643 99 EETVLKDVAFG-----PQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 436 GIDVGAKFDIYALLDALAREGRAIVVVS------SDLRELMLICDRIGVMSAGRMHAVFE 489
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVThlmddvADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-236 |
2.14e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA--PHSRAHAEALGVrmVMQELNLVPTLTV 105
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAI--VPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENL-----------FLDRLPHRFGVIDRRRLAADARAamarvgldsldpdtlvGSLGIGHQQMVEIARSLAGDCRVLIL 174
Cdd:PRK11614 98 EENLamggffaerdqFQERIKWVYELFPRLHERRIQRA----------------GTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 175 DEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA 236
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDA 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-210 |
2.16e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 69.31 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 4 TDPDSTPDTPTLVVTGIGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeYAPHS 81
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYpgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSS 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 82 RAHAE-ALGVRMVMQELNLVPTlTVAENLfldrlphRFGVIDRRRLAADARAAMARVG--LDSLDP--DTLVGSLGI--- 153
Cdd:TIGR02868 402 LDQDEvRRRVSVCAQDAHLFDT-TVRENL-------RLARPDATDEELWAALERVGLAdwLRALPDglDTVLGEGGArls 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 154 -GHQQMVEIARSLAGDCRVLILDEPTAMLTAR-EVELLFDQIARLkaDGVALVYISHRL 210
Cdd:TIGR02868 474 gGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAAL--SGRTVVLITHHL 530
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
280-476 |
2.29e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSigdppRPAAIRspadavrhgIALVsedrkgeglllPQSI 359
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----RNGKLR---------IGYV-----------PQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 360 AAN----LSLGQLARVaRGGVVDGERENALAARQIDALRirargpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:PRK09544 77 YLDttlpLTVNRFLRL-RPGTKKEDILPALKRVQAGHLI------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490656625 436 GIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRI 476
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
277-484 |
2.46e-12 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 66.94 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDRkgeGLLL 355
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED----IREqDPVELRRKIGYVIQQI---GLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLSL-GQLARVARGGVVDGEREnALAARQIDALRIRARGPAqpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPt 434
Cdd:cd03295 89 HMTVEENIALvPKLLKWPKEKIRERADE-LLALVGLDPAEFADRYPH----ELSGGQQQRVGVARALAADPPLLLMDEP- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 435 rgidVGAkfdiyalLDALARE-------------GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:cd03295 163 ----FGA-------LDPITRDqlqeefkrlqqelGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-244 |
2.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.43 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTyaepVLDDVSLAlYPGEAL-ALTGENGAGKSTLSKIVAGLVAPTTGA-----MRLAGAEYAPHSRAHAEALGVRMVM 94
Cdd:PRK14271 33 GKT----VLDQVSMG-FPARAVtSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 95 QELNLVPtLTVAENLFLDRLPHRfgVIDRRRLAADARAAMARVGLDSLDPDTLVGS---LGIGHQQMVEIARSLAGDCRV 171
Cdd:PRK14271 108 QRPNPFP-MSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 172 LILDEPTAMLTAREVELLfDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVhvdriDAQPTERLVA 244
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLV-----EEGPTEQLFS 251
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
273-487 |
2.54e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.52 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 273 SRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------PPRpaairspadavRHGIALV 344
Cdd:PRK11000 12 AYGDVVisKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvPPA-----------ERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 345 SEDRKgeglLLPQ-SIAANLSLG-QLARVARGgVVDGERENALAARQIDALRIRargpaQPVAeLSGGNQQKVAIGRWLG 422
Cdd:PRK11000 81 FQSYA----LYPHlSVAENMSFGlKLAGAKKE-EINQRVNQVAEVLQLAHLLDR-----KPKA-LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 423 RDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
26-209 |
2.97e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGvrMVMQELNLVPTLTV 105
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLC--FVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDrlphrfgvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTARE 185
Cdd:PRK13540 92 RENCLYD--------IHFSPGAVGITELCRLFSLEHL-IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 490656625 186 VELLFDQIARLKADGVALVYISHR 209
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-229 |
4.80e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.68 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 24 YAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRaHAEALGVRMVMQELNLVPTL 103
Cdd:PRK13643 17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSK-QKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRL---PHRFGvIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:PRK13643 96 QLFEETVLKDVafgPQNFG-IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 181 LTAR---EVELLFDQIARlkaDGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13643 175 LDPKariEMMQLFESIHQ---SGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
265-483 |
5.51e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIG--DPPRPAAIRSPADAVR 338
Cdd:PRK11607 18 PLLEIRNLTKSfdgqHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvDLSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 339 HGIALVSEdrkgegLLLPQSIAANLSLGQLARvargGVVDGERENALAArqIDALRIRARGPAQpvaeLSGGNQQKVAIG 418
Cdd:PRK11607 98 QSYALFPH------MTVEQNIAFGLKQDKLPK----AEIASRVNEMLGL--VHMQEFAKRKPHQ----LSGGQRQRVALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 419 RWLGRDMGVLLFDEPTRGIDVGAKFDI-YALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
276-438 |
5.69e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.80 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD-------PPRPAAIRspadAVRHGIALVSEDR 348
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqKPSEKAIR----LLRQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 KgeglLLPQ-SIAANLS------LGQLARVARggvvdgERENALAARqidaLRIRARGPAQPVAeLSGGNQQKVAIGRWL 421
Cdd:COG4161 92 N----LWPHlTVMENLIeapckvLGLSKEQAR------EKAMKLLAR----LRLTDKADRFPLH-LSGGQQQRVAIARAL 156
|
170
....*....|....*..
gi 490656625 422 GRDMGVLLFDEPTRGID 438
Cdd:COG4161 157 MMEPQVLLFDEPTAALD 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
279-486 |
8.30e-12 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.15 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI--------GDPPRpAAIRSpadavRH-GI-------- 341
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfalDEDAR-ARLRA-----RHvGFvfqsfqll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ----ALvsedrkgEGLLLPQSIAANLSLGQLARVARGGVVDGERENALaarqidalrirargPAQpvaeLSGGNQQKVAI 417
Cdd:COG4181 103 ptltAL-------ENVMLPLELAGRRDARARARALLERVGLGHRLDHY--------------PAQ----LSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 418 GRWLGRDMGVLLFDEPTRGID--VGAKfdIYALLDALARE-GRAIVVVSSDLrELMLICDRIGVMSAGRMHA 486
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDaaTGEQ--IIDLLFELNRErGTTLVLVTHDP-ALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-229 |
8.44e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.98 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP--------TTGAMRLaGAEYAPHSRahaEALGVrmVMQEL 97
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITL-TAKTVWDIR---EKVGI--VFQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 98 -NLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVG-LDSLD--PDTLVGslgiGHQQMVEIARSLAGDC 169
Cdd:PRK13640 94 dNQFVGATVGDDV-------AFGLenraVPRPEMIKIVRDVLADVGmLDYIDsePANLSG----GQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEElARVAQRVAVLRDGRLV 229
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDE-ANMADQVLVLDDGKLL 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-229 |
9.46e-12 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 64.87 E-value: 9.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHS-RAHaealgVRMVMQELNLVPT 102
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirDLNLRWlRSQ-----IGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 lTVAENL-----------------------FLDRLPHRFgvidrrrlaadaraamarvgldsldpDTLVGSLGI----GH 155
Cdd:cd03249 92 -TIAENIrygkpdatdeeveeaakkanihdFIMSLPDGY--------------------------DTLVGERGSqlsgGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 156 QQMVEIARSLAGDCRVLILDEPTAMLTA---REVELLFDQIARlkadGVALVYISHRLEELaRVAQRVAVLRDGRLV 229
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAeseKLVQEALDRAMK----GRTTIVIAHRLSTI-RNADLIAVLQNGQVV 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
278-484 |
9.65e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSED-------RKG 350
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsisavnpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 EGLLLPQSIAANLSLGQLARVARggvvdgeRENALAARQIDAlRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLF 430
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLAR-------ASEMLRAVDLDD-SVLDKRPPQ----LSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 431 DEPTRGIDVGAKFDIYALLDAL-AREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
278-484 |
1.04e-11 |
|
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: 64.11 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLV--YGADAADGGTVSIGDPPRPAairspaDAVRHGIALVSEDRkgegLLL 355
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK------RSFRKIIGYVPQDD----ILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQsiaanlslgqlarvarggvvdgerenaLAARQidALRIRA--RGpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEP 433
Cdd:cd03213 95 PT---------------------------LTVRE--TLMFAAklRG-------LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 434 TRGIDVGAKFDIYALLDALAREGRAIVVV----SSDLRELmliCDRIGVMSAGRM 484
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSihqpSSEIFEL---FDKLLLLSQGRV 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
265-483 |
1.12e-11 |
|
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: 64.38 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS-------RGD----AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---------- 323
Cdd:COG4778 3 TLLEVENLSktftlhlQGGkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwvdlaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 324 PPRP-AAIRspadavRHGIALVSEdrkgegLL--LPQsIAAnlslgqLARVARGGVVDG-ERENAL--AARQIDALRIRA 397
Cdd:COG4778 83 SPREiLALR------RRTIGYVSQ------FLrvIPR-VSA------LDVVAEPLLERGvDREEARarARELLARLNLPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 398 RGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIG 477
Cdd:COG4778 144 RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVV 223
|
....*.
gi 490656625 478 VMSAGR 483
Cdd:COG4778 224 DVTPFS 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-229 |
1.27e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.77 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEY-APHSRAHAEAL--- 88
Cdd:PRK11264 3 AIEVKNLVKKFhGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 89 ---GVRMVMQELNLVPTLTVAENLFldRLPHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSL 165
Cdd:PRK11264 83 lrqHVGFVFQNFNLFPHRTVLENII--EGPVIVKGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 166 AGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
267-485 |
1.28e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG-----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGI 341
Cdd:PRK10908 2 IRFEHVSKAylggrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRKgegLLLPQSIAANLSLGQLARVARGgvvDGERENALAArqIDALRIRARGPAQPVaELSGGNQQKVAIGRWL 421
Cdd:PRK10908 82 GMIFQDHH---LLMDRTVYDNVAIPLIIAGASG---DDIRRRVSAA--LDKVGLLDKAKNFPI-QLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMH 485
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
276-501 |
1.39e-11 |
|
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: 64.43 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPAdAVRHGIALVSEdrkgEGLLL 355
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG--HDLALADPA-WLRRQVGVVLQ----ENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLSLGQLArvarggvVDGER--ENALAARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:cd03252 89 NRSIRDNIALADPG-------MSMERviEAAKLAGAHDFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALArEGRAIVVVSSDLRELMlICDRIGVMSAGRmhaVFERGgwTQDALLGA 501
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVK-NADRIIVMEKGR---IVEQG--SHDELLAE 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
43-234 |
1.41e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 43 ALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG-----AE----YAPHSRahaealGVRMVMQELNLVPTLTVAENLfldr 113
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEkgicLPPEKR------RIGYVFQDARLFPHYKVRGNL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 114 lphRFGVidrrrLAADARAAMARVGLDSLDP--DTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTA-REVELLf 190
Cdd:PRK11144 98 ---RYGM-----AKSMVAQFDKIVALLGIEPllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELL- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490656625 191 DQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRI 234
Cdd:PRK11144 169 PYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-229 |
1.44e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTYAEPVlddvSLALYPGEALALTGENGAGKSTLSKIVAGLvAPTTGAMRLAGAEYA----PHSRAHAEALGvrmvmQE 96
Cdd:PRK11174 362 GKTLAGPL----NFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELReldpESWRKHLSWVG-----QN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 97 lnlvPTL---TVAENL-----------------------FLDRLPHrfgvidrrrlaadaraamarvGLDSLDPDTLVGs 150
Cdd:PRK11174 432 ----PQLphgTLRDNVllgnpdasdeqlqqalenawvseFLPLLPQ---------------------GLDTPIGDQAAG- 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 151 LGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVyISHRLEELARVAQrVAVLRDGRLV 229
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQWDQ-IWVMQDGQIV 562
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
267-483 |
1.68e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.52 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVE-RLSRGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADG---GTVS-----IGDPPRPAAIRSPAD 335
Cdd:PRK09473 18 LRVTfSTPDGDvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATfngreILNLPEKELNKLRAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 336 AvrhgIALVSEDrkgeglllPQ-SIAANLSLG-QLARV--ARGGVVDGERENAlAARQIDALRI---RARGPAQPvAELS 408
Cdd:PRK09473 98 Q----ISMIFQD--------PMtSLNPYMRVGeQLMEVlmLHKGMSKAEAFEE-SVRMLDAVKMpeaRKRMKMYP-HEFS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 409 GGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-229 |
1.78e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL--GVRMVMQELNLVPTLTVA 106
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLfldRLPHRFGVIDRRRLAADARAAMARVGLdsLD-----PDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:PRK10908 98 DNV---AIPLIIAGASGDDIRRRVSAALDKVGL--LDkaknfPIQLSG----GEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 182 T---AREVELLFDQIARLkadGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10908 169 DdalSEGILRLFEEFNRV---GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
29-262 |
2.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.37 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALgVRMVMQEL-NLVPTLTVAE 107
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVFQDPdDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDrlPHRFGvIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVE 187
Cdd:PRK13647 100 DVAFG--PVNMG-LDKDEVERRVEEALKAVRMWDFR-DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 188 LLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVhvdridaqpTERLVALMAGREIAEQAvhGTRTP 262
Cdd:PRK13647 176 TLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL---------AEGDKSLLTDEDIVEQA--GLRLP 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
277-484 |
2.18e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.83 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYgadaadggtvSIGDPPRPAAIRSPADAVRHGIALVSEDRKGEGLLLP 356
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN----------RLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARG----GVVDGER-ENALAARQIDALRIRARGPAQpvaELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:PRK10070 113 QSFALMPHMTVLDNTAFGmelaGINAEERrEKALDALRQVGLENYAHSYPD---ELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 432 EPTRGIDVGAKFDIY-ALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK10070 190 EAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
240-508 |
2.19e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 66.38 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMA-GREIAEQavhgtrtPGAPRLRVERLS-RGDAV-----------RDVSFDVRAGEIFGISGLIGAGRTELLR 306
Cdd:COG5265 330 ERMFDLLDqPPEVADA-------PDAPPLVVGGGEvRFENVsfgydperpilKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 307 LVYGADAADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDRkgegLLLPQSIAANLSLGqlarvaRGGVVDGERENAL 385
Cdd:COG5265 403 LLFRFYDVTSGRILIDGQD----IRDvTQASLRAAIGIVPQDT----VLFNDTIAYNIAYG------RPDASEEEVEAAA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 386 AARQIDALrIRA--RGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAI 459
Cdd:COG5265 469 RAAQIHDF-IESlpDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTT 546
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490656625 460 VVVSSDLRELMlICDRIGVMSAGRmhaVFERGgwTQDALLgaAFAG-YAR 508
Cdd:COG5265 547 LVIAHRLSTIV-DADEILVLEAGR---IVERG--THAELL--AQGGlYAQ 588
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
279-483 |
2.39e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.86 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---PPRPAAIRspadAVRHGIALVsedrkgeglll 355
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedlTDSKKDIN----KLRRKVGMV----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQS--------IAANLSLGQlaRVARGgvVDGERENALAARQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:COG1126 83 FQQfnlfphltVLENVTLAP--IKVKK--MSKAEAEERAMELLERVGLADKADAYP-AQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 428 LLFDEPTRGID---VGakfDIYALLDALAREGRAIVVVSSDL---RElmlICDRIGVMSAGR 483
Cdd:COG1126 158 MLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMgfaRE---VADRVVFMDGGR 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
277-483 |
3.09e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRHGIALvSEDRKGEGL--- 353
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG----------VDITDKKVKL-SDIRKKVGLvfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 -----LLPQSIAANLSLGQLARvargGVVDGEREN----ALAARQIDALRIRARGPAqpvaELSGGNQQKVAIGRWLGRD 424
Cdd:PRK13637 91 ypeyqLFEETIEKDIAFGPINL----GLSEEEIENrvkrAMNIVGLDYEDYKDKSPF----ELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
17-177 |
3.85e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.18 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAphSRAHAEALGVrm 92
Cdd:COG4604 4 IKNVSKRYGGkVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvATTP--SRELAKRLAI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELNLVPTLTVAENLFLDRLPH---RFGVIDRRRLAADaraamarvgLD--SLDP------DTLVGslgiGHQQMVEI 161
Cdd:COG4604 80 LRQENHINSRLTVRELVAFGRFPYskgRLTAEDREIIDEA---------IAylDLEDladrylDELSG----GQRQRAFI 146
|
170
....*....|....*.
gi 490656625 162 ARSLAGDCRVLILDEP 177
Cdd:COG4604 147 AMVLAQDTDYVLLDEP 162
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
277-491 |
4.29e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.71 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAiRSPADAVRHGIALVSEDRKGEglLLP 356
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYS-RKGLMKLRESVGMVFQDPDNQ--LFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARVARGGVVDGERENALAARQIDALRirargpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK------DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 437 IDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRmhAVFERG 491
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR--VILQGN 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
277-482 |
4.39e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.18 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP--RPAAIRspadavrhgiALVSEDrkgEGLL 354
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPveGPGAER----------GVVFQN---EGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLG-QLARVARGgvvdgERENAlaARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEP 433
Cdd:PRK11248 83 PWRNVQDNVAFGlQLAGVEKM-----QRLEI--AHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 434 TRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-302 |
4.56e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTYAepvLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphSRAHAEALGVRMV-M-QEL- 97
Cdd:NF033858 12 GKTVA---LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIAyMpQGLg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 98 -NLVPTLTVAENL-FLDRLphrFGvIDRRRLAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:NF033858 87 kNLYPTLSVFENLdFFGRL---FG-QDAAERRRRIDELLRATGLAPF-ADRPAGKLSGGMKQKLGLCCALIHDPDLLILD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 176 EPTamlTAreVELL-----FDQIARLKADG------VALVYIshrlEELARVAQRVAvLRDGRLvhvdrIDAQPTERL-- 242
Cdd:NF033858 162 EPT---TG--VDPLsrrqfWELIDRIRAERpgmsvlVATAYM----EEAERFDWLVA-MDAGRV-----LATGTPAELla 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 243 -----------VALM-AGREIAEQAVH----GTRTPGAPRLRVERLSR--GD--AVRDVSFDVRAGEIFGISGLIGAGRT 302
Cdd:NF033858 227 rtgadtleaafIALLpEEKRRGHQPVVipprPADDDDEPAIEARGLTMrfGDftAVDHVSFRIRRGEIFGFLGSNGCGKS 306
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
277-484 |
7.32e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.67 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEdrkGEGLLLP 356
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQ---HFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLG-QLARVARGGVvdGERENALAAR-QIDALRirARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK11153 97 RTVFDNVALPlELAGTPKAEI--KARVTELLELvGLSDKA--DRYPAQ----LSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 435 RGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK11153 169 SALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-231 |
7.72e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.55 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV-----APTTGAMRLAGAE-YAPHSRAHAEALGVRMVMQELNLVP 101
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiYSPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TLTVAEN----LFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLD--PDTLVGslgiGHQQMVEIARSLAGDCRVLILD 175
Cdd:PRK14267 99 HLTIYDNvaigVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNdyPSNLSG----GQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 176 EPTAML----TAREVELLFDqiarLKADgVALVYISHRLEELARVAQRVAVLRDGRLVHV 231
Cdd:PRK14267 175 EPTANIdpvgTAKIEELLFE----LKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-229 |
8.40e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYA---PHSRAHAealG 89
Cdd:PRK10895 3 TLTAKNLAKAYkGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHARARR---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VRMVMQELNLVPTLTVAENLfldrlphrFGVIDRRRLAADARAAMARVGL-----DSLDPDTLVGSLGIGHQQMVEIARS 164
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNL--------MAVLQIRDDLSAEQREDRANELmeefhIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 165 LAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
277-484 |
8.80e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.72 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADA--VRHGIALVSEdrKGEGLL 354
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrLRKEIGLVFQ--FPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGQLARVArggvvDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK13645 104 FQETIEKDIAFGPVNLGE-----NKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 435 RGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
277-489 |
9.53e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 62.19 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPaDAVRhgiALVSEDrkgEGLLLP 356
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP----VTGP-GADR---GVVFQK---DALLPW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLG-QLARVARGgvvdgEREnALAARQIDALRIRARGpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPtr 435
Cdd:COG4525 91 LNVLDNVAFGlRLRGVPKA-----ERR-ARAEELLALVGLADFA-RRRIWQLSGGMRQRVGIARALAADPRFLLMDEP-- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 436 gidVGAkfdiyalLDALARE-------------GRAIVVVSSDLRELMLICDRIGVMSA--GRMHAVFE 489
Cdd:COG4525 162 ---FGA-------LDALTREqmqellldvwqrtGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLE 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-229 |
1.05e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 61.52 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV---APTTGAMRLAGAEYAPH----SRAHaealgvrmVMQELNLV 100
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDqfqkCVAY--------VRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTLTVAENLF---LDRLPHRFGviDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEP 177
Cdd:cd03234 94 PGLTVRETLTytaILRLPRKSS--DAIRKKRVEDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 178 TAML---TAREVELLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03234 171 TSGLdsfTALNLVSTLSQLAR--RNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
278-486 |
1.06e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIALVSEDrkgEGLLLPQ 357
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD--EDISLLPLHARARRGIGYLPQE---ASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLGQLARVARGGVVDGERENALAAR-QIDALRiRARGPAqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDRANELMEEfHIEHLR-DSMGQS-----LSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-230 |
1.07e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.41 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE------PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE---YAPHSRAha 85
Cdd:COG1101 2 LELKNLSKTFNPgtvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 86 ealgvRM---VMQE--LNLVPTLTVAENLFL-----DRLPHRFGVIDRRRLAADARAAMARVGL-DSLdpDTLVGSLGIG 154
Cdd:COG1101 80 -----KYigrVFQDpmMGTAPSMTIEENLALayrrgKRRGLRRGLTKKRRELFRELLATLGLGLeNRL--DTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 155 HQQ-----MVEIARSlagdcRVLILDEPTAML---TAREVELLFDQIARlkADGVALVYISHRLEELARVAQRVAVLRDG 226
Cdd:COG1101 153 QRQalsllMATLTKP-----KLLLLDEHTAALdpkTAALVLELTEKIVE--ENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
....
gi 490656625 227 RLVH 230
Cdd:COG1101 226 RIIL 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
277-501 |
1.45e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 61.48 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLV---YGADAadgGTVSI-GDPPRPAAIRSpadaVRHGIALVSEDRkgeg 352
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfYDVDS---GRILIdGHDVRDYTLAS----LRRQIGLVSQDV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLLPQSIAANLSLGQLaRVARGGVVDGEReNALAARQIDAL------RIRARGpaqpvAELSGGNQQKVAIGRWLGRDMG 426
Cdd:cd03251 86 FLFNDTVAENIAYGRP-GATREEVEEAAR-AANAHEFIMELpegydtVIGERG-----VKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALArEGRAIVVVSSDLRELMLIcDRIGVMSAGRmhaVFERGgwTQDALLGA 501
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENA-DRIVVLEDGK---IVERG--THEELLAQ 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-229 |
1.48e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 60.64 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP--TTGAMRLAGA-EYAPHSRAHaealgV 90
Cdd:cd03213 10 TVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpLDKRSFRKI-----I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 RMVMQELNLVPTLTVAENL-FLDRLPhrfgvidrrrlaadaraamarvgldsldpdtlvgSLGIGHQQMVEIARSLAGDC 169
Cdd:cd03213 85 GYVPQDDILHPTLTVRETLmFAAKLR----------------------------------GLSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRL-EELARVAQRVAVLRDGRLV 229
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-229 |
1.86e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.39 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVaPTTGAMRLAG---AEYAPHSRAHAEAlgvrMVMQELNLVPTLTV 105
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGrplSDWSAAELARHRA----YLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLdrlpHRFGVIDRRRLAADARAAMARVGLDSLDPdTLVGSLGIGHQQMVEIAR-------SLAGDCRVLILDEPT 178
Cdd:COG4138 87 FQYLAL----HQPAGASSEAVEQLLAQLAEALGLEDKLS-RPLTQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-244 |
2.20e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 31 DVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAM-----RLAGAEYAPHSRAhaealgVRMVMQE--LNLVPTL 103
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhPLHFGDYSYRSQR------IRMIFQDpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAEnlFLDrLPHRFGV-IDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:PRK15112 105 RISQ--ILD-FPLRLNTdLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 183 AREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVH---VDRIDAQP----TERLVA 244
Cdd:PRK15112 182 MSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVErgsTADVLASPlhelTKRLIA 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
262-482 |
3.09e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.11 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 262 PGAPRLRVERLSRGdavrdvsfdVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIgdpprpaairspadAVRHGI 341
Cdd:TIGR01257 1948 SGTSSPAVDRLCVG---------VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV--------------AGKSIL 2004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 342 ALVSEDRKGEGLLlPQSIAAN-LSLGQ--LARVARGGVVDGERENALAARQIDALRIRARGPaQPVAELSGGNQQKVAIG 418
Cdd:TIGR01257 2005 TNISDVHQNMGYC-PQFDAIDdLLTGRehLYLYARLRGVPAEEIEKVANWSIQSLGLSLYAD-RLAGTYSGGNKRKLSTA 2082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 419 RWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
28-242 |
3.29e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.82 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSK-------IVAGlvAPTTGAMRLAGAE-YAPHS-----RAHaealgVRMVM 94
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPG--ARVEGEILLDGEDiYDPDVdvvelRRR-----VGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 95 QELNLVPTlTVAEN-LFLDRLphrFGVIDRRRLAADARAAMARVGL-----DSLDpdTLVGSLGIGHQQMVEIARSLAGD 168
Cdd:COG1117 99 QKPNPFPK-SIYDNvAYGLRL---HGIKSKSELDEIVEESLRKAALwdevkDRLK--KSALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 169 CRVLILDEPTAML----TAReVELLfdqIARLKADgVALVYISHRLEELARVAQRVAVLRDGRLVHVDridaqPTERL 242
Cdd:COG1117 173 PEVLLMDEPTSALdpisTAK-IEEL---ILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFG-----PTEQI 240
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
28-229 |
3.41e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.46 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP----TTGAMRLAGAE---YAPHSRAHAEALGVRMVMQELN-- 98
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDllkLSPRERRKIIGREIAMIFQEPSsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 99 LVPTLTVAENL------------FLDR----------LPHRFGVIDRRRLaadaraamarvgLDSLdPDTLvgSLGIGhq 156
Cdd:COG4170 102 LDPSAKIGDQLieaipswtfkgkWWQRfkwrkkraieLLHRVGIKDHKDI------------MNSY-PHEL--TEGEC-- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 157 QMVEIARSLAGDCRVLILDEPT-AMLTAREVellfdQIARL-----KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTnAMESTTQA-----QIFRLlarlnQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
277-438 |
3.56e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.41 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD-------PPRPAAIRspadAVRHGIALVSEDRK 349
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDKAIR----ELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 geglLLPQ-SIAANLsLGQLARVARggvVDGERENALAARQIDALRIRARGPAQPVaELSGGNQQKVAIGRWLGRDMGVL 428
Cdd:PRK11124 93 ----LWPHlTVQQNL-IEAPCRVLG---LSKDQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVL 163
|
170
....*....|
gi 490656625 429 LFDEPTRGID 438
Cdd:PRK11124 164 LFDEPTAALD 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
270-466 |
4.16e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 270 ERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADavRHGIALVSeDRK 349
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG----QTINLVRD--KDGQLKVA-DKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 GEGLLLPQ-----------SIAANLSLGQLARVARGGVVDGE-RENALaaRQIDALRIRARGPAQPVAELSGGNQQKVAI 417
Cdd:PRK10619 86 QLRLLRTRltmvfqhfnlwSHMTVLENVMEAPIQVLGLSKQEaRERAV--KYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 418 GRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDL 466
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
279-483 |
4.51e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGdpprpaaiRSPADAVRHGIALVSEDRKgeglLLP-Q 357
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG--------TAPLAEAREDTRLMFQDAR----LLPwK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLGqlarvARGGVvdgeRENALAArqIDALRIRARGPAQPVAeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGI 437
Cdd:PRK11247 97 KVIDNVGLG-----LKGQW----RDAALQA--LAAVGLADRANEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490656625 438 DVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
26-196 |
4.67e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.42 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP---TTGAMRLAGAE---YAPHSRahaealGVRMVMQELNL 99
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRltaLPAEQR------RIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAENLFLDrLPHRFGvidRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLILDE 176
Cdd:COG4136 88 FPHLSVGENLAFA-LPPTIG---RAQRRARVEQALEEAGLAGFadrDPATLSG----GQRARVALLRALLAEPRALLLDE 159
|
170 180
....*....|....*....|....
gi 490656625 177 P----TAMLTAREVELLFDQIARL 196
Cdd:COG4136 160 PfsklDAALRAQFREFVFEQIRQR 183
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
279-499 |
4.76e-10 |
|
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: 59.86 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLV---YGADAadgGTVSI-GDPPRPAAIRSpadaVRHGIALVSEdrkgEGLL 354
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfYDPTS---GEILLdGVDIRDLNLRW----LRSQIGLVSQ----EPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGqlarvaRGGVVDGERENALAARQIDAL----------RIRARGpaqpvAELSGGNQQKVAIGRWLGRD 424
Cdd:cd03249 89 FDGTIAENIRYG------KPDATDEEVEEAAKKANIHDFimslpdgydtLVGERG-----SQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDAlAREGRAIVVVS---SDLRElmliCDRIGVMSAGRmhaVFERGgwTQDALL 499
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDR-AMKGRTTIVIAhrlSTIRN----ADLIAVLQNGQ---VVEQG--THDELM 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-229 |
4.96e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.96 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHS-RAHaealgVRMVMQELNLVP 101
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrDYTLASlRNQ-----VALVSQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TlTVAENL------------------------FLDRLPHrfgvidrrrlaadaraamarvGLDsldpdTLVGSLGI---- 153
Cdd:PRK11176 431 D-TIANNIayarteqysreqieeaarmayamdFINKMDN---------------------GLD-----TVIGENGVllsg 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAML---TAREVELLFDQiarLKADGVALVyISHRLEELARvAQRVAVLRDGRLV 229
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALdteSERAIQAALDE---LQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
277-500 |
5.22e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRHGIALVSEDRKgegLLLP 356
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG--KEIDFKSSKEALENGISMVHQELN---LVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARvaRGGVVDGERENALAARQIDALRIRArGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK10982 88 RSVMDNMWLGRYPT--KGMFVDQDKMYRDTKAIFDELDIDI-DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGGWTQDALLG 500
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIA 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
277-483 |
5.56e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.12 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------PPRpaaiRSPADAVRHGIALvsedrkg 350
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvPAE----NRHVNTVFQSYAL------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 egllLPQ-SIAANLSLG-QLARVArggvvdgerENALAARQIDALRI------RARGPAQpvaeLSGGNQQKVAIGRWLG 422
Cdd:PRK09452 98 ----FPHmTVFENVAFGlRMQKTP---------AAEITPRVMEALRMvqleefAQRKPHQ----LSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 423 RDMGVLLFDEPTRGIDvgakfdiYAL-------LDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK09452 161 NKPKVLLLDESLSALD-------YKLrkqmqneLKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-228 |
5.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.13 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS----RAHaealgVRMVMQEL-NLV 100
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdiRHK-----IGMVFQNPdNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 101 PTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSL---DPDTLVGslgiGHQQMVEIARSLAGDCRVLI 173
Cdd:PRK13650 95 VGATVEDDV-------AFGLenkgIPHEEMKERVNEALELVGMQDFkerEPARLSG----GQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 174 LDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELArVAQRVAVLRDGRL 228
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-244 |
6.14e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEalgVRMV 93
Cdd:PRK11432 7 VVLKNITKRFGSnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---ICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 94 MQELNLVPTLTVAENLfldrlphRFGV----IDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDC 169
Cdd:PRK11432 84 FQSYALFPHMSLGENV-------GYGLkmlgVPKEERKQRVKEALELVDLAGFE-DRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 170 RVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDA---QPTERLVA 244
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQElyrQPASRFMA 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
267-484 |
6.20e-10 |
|
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: 60.45 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVE-RLSRGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYG---ADAADGGTVSIG-------DPPRPAAIRSp 333
Cdd:COG0444 7 LKVYfPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDgedllklSEKELRKIRG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 334 adavrHGIALVSEDrkgeglllPQSiaanlSL-------GQLARVAR-GGVVDGERENALAARQIDALRIRArgPAQpVA 405
Cdd:COG0444 86 -----REIQMIFQD--------PMT-----SLnpvmtvgDQIAEPLRiHGGLSKAEARERAIELLERVGLPD--PER-RL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 406 -----ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDL---RElmlICDRI 476
Cdd:COG0444 145 dryphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLgvvAE---IADRV 221
|
....*...
gi 490656625 477 GVMSAGRM 484
Cdd:COG0444 222 AVMYAGRI 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
277-483 |
6.57e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 58.48 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPADAVRHGIALVSEdrkgEGLLLP 356
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP----VSDLEKALSSLISVLNQ----RPYLFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLslgqlarvarggvvdGERenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03247 89 TTLRNNL---------------GRR-------------------------FSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 437 IDVGAKFDIYALLDALAREgRAIVVVSSDLR--ELMlicDRIGVMSAGR 483
Cdd:cd03247 129 LDPITERQLLSLIFEVLKD-KTLIWITHHLTgiEHM---DKILFLENGK 173
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
28-229 |
6.84e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.00 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaEYAPHSRAHAEALGVRMVMQELNLVPTLTVAE 107
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG-EHIQHYASKEVARRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NLFLDRLPH-----RFGVIDrrrlAADARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML- 181
Cdd:PRK10253 101 LVARGRYPHqplftRWRKED----EEAVTKAMQATGITHL-ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLd 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 182 TAREVEL--LFDQIARLKadGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10253 176 ISHQIDLleLLSELNREK--GYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-229 |
8.35e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 61.37 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 10 PDTPTLVVTG-------IGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEY 77
Cdd:COG5265 346 PDAPPLVVGGgevrfenVSFGYdpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 78 APHS-RAhaeALGVrmVMQElnlvpTL----TVAENL-----------------------FLDRLPHRFgvidrrrlaad 129
Cdd:COG5265 426 TQASlRA---AIGI--VPQD-----TVlfndTIAYNIaygrpdaseeeveaaaraaqihdFIESLPDGY----------- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 130 araamarvgldsldpDTLVGSLGI----GHQQMVEIARSLAGDCRVLILDEPTAML-TAREVELLfDQIARLKADGVALV 204
Cdd:COG5265 485 ---------------DTRVGERGLklsgGEKQRVAIARTLLKNPPILIFDEATSALdSRTERAIQ-AALREVARGRTTLV 548
|
250 260
....*....|....*....|....*
gi 490656625 205 yISHRLEELARvAQRVAVLRDGRLV 229
Cdd:COG5265 549 -IAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
280-487 |
8.84e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.48 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRhgiaLVSEDRK------GEGL 353
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----------TDVSR----LHARDRKvgfvfqHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIAANLSLGqLARVARGgvvdgERENALAARQ--------IDALRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDM 425
Cdd:PRK10851 86 FRHMTVFDNIAFG-LTVLPRR-----ERPNAAAIKAkvtqllemVQLAHLADRYPAQ----LSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 426 GVLLFDEPTRGIDVGAKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRMHAV 487
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQA 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-226 |
1.33e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.99 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHS----RAHaealgVRMVMQ--ELNLVPT 102
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfeklRKH-----IGIVFQnpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LT---VAENLFLDRLPHRfgvidrrRLAADARAAMARVG-LDSLD--PDTLVGslgiGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK13648 100 IVkydVAFGLENHAVPYD-------EMHRRVSEALKQVDmLERADyePNALSG----GQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 177 PTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEElARVAQRVAVLRDG 226
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSE-AMEADHVIVMNKG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
278-482 |
1.41e-09 |
|
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: 58.25 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP--RPAAIRS---------PADAVRHGIALvse 346
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitEPGPDRMvvfqnysllPWLTVRENIAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 347 drkgeglllpqsiAANLSLGQLARVARGGVVDgerenalaaRQIDALRIRARGPAQPvAELSGGNQQKVAIGRWLGRDMG 426
Cdd:TIGR01184 78 -------------AVDRVLPDLSKSERRAIVE---------EHIALVGLTEAADKRP-GQLSGGMKQRVAIARALSIRPK 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRELMLICDRIGVMSAG 482
Cdd:TIGR01184 135 VLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLmVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
277-484 |
1.58e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 57.81 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIgDPPRPAAIrsPADAVRHGIALVSEDRkgegLLLP 356
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTI--PLEDLRSSLTIIPQDP----TLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLslgqlarvarggvvdgERENALAARQI-DALRIRARGpaqpvAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:cd03369 96 GTIRSNL----------------DPFDEYSDEEIyGALRVSEGG-----LNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 436 GIDVGAKfdiyALLDALARE---GRAIVVVSSDLRELmLICDRIGVMSAGRM 484
Cdd:cd03369 155 SIDYATD----ALIQKTIREeftNSTILTIAHRLRTI-IDYDKILVMDAGEV 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
404-479 |
1.77e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 1.77e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 404 VAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVM 479
Cdd:cd03236 137 IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
278-484 |
1.78e-09 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 56.84 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPA-DAVRHGIALVSEDRKgeglLLP 356
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWDpNELGDHVGYLPQDDE----LFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLslgqlarvarggvvdgerenalaarqidalrirargpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:cd03246 90 GSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490656625 437 IDVGAKFDIYALLDALAREGRAIVVVSSDlRELMLICDRIGVMSAGRM 484
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-229 |
2.51e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTG---------------AMR-------------LAG------- 74
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGevawlgkdllgmkddEWRavrsdiqmifqdpLASlnprmti 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 75 ----AE----YAPHSRAHAEALGVRMVMQELNLVPTLtvaenlfLDRLPHRFGvidrrrlaadaraamarvgldsldpdt 146
Cdd:PRK15079 118 geiiAEplrtYHPKLSRQEVKDRVKAMMLKVGLLPNL-------INRYPHEFS--------------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 147 lvgslgiGHQ-QMVEIARSLAGDCRVLILDEPTAML----TAREVELLFDQIARLkadGVALVYISHRLEELARVAQRVA 221
Cdd:PRK15079 164 -------GGQcQRIGIARALILEPKLIICDEPVSALdvsiQAQVVNLLQQLQREM---GLSLIFIAHDLAVVKHISDRVL 233
|
....*...
gi 490656625 222 VLRDGRLV 229
Cdd:PRK15079 234 VMYLGHAV 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-244 |
2.72e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.66 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 22 KTYAEPV--LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP----TTGAMRLAGAE---YAPHSRAHAEALGVRM 92
Cdd:PRK15093 14 KTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDllrLSPRERRKLVGHNVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQELN--LVPTLTVAENL--------FLDRLPHRFGvidrrRLAADARAAMARVGLDslDPDTLVGS----LGIGHQQM 158
Cdd:PRK15093 94 IFQEPQscLDPSERVGRQLmqnipgwtYKGRWWQRFG-----WRKRRAIELLHRVGIK--DHKDAMRSfpyeLTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 159 VEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLVHvdriDAQ 237
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE----TAP 242
|
....*..
gi 490656625 238 PTERLVA 244
Cdd:PRK15093 243 SKELVTT 249
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-229 |
2.75e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV--------APTTGAMRLAGaeyAPHSRAHAEALG-VRMVM-QEL 97
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNG---EPLAAIDAPRLArLRAVLpQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 98 NLVPTLTVAENLFLDRLPHrfgvIDRRRLAADARAAMARVGLDSLDPDTLVG----SLGIGHQQMVEIARSLA------- 166
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPH----ARRAGALTHRDGEIAWQALALAGATALVGrdvtTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 167 --GDCRVLILDEPTAMLTAREVELLFDQIARLKAD-GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
277-486 |
3.09e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.40 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVsigdpprpaairspadaVRHGialvsedrkgeglllp 356
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----------------EVNG---------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qSIAANLSLGqlarvarGGvVDGE---RENA--------LAARQIDAlRIRArgpaqpVAELSGgnqqkvaIGRWlgrdm 425
Cdd:COG1134 88 -RVSALLELG-------AG-FHPEltgRENIylngrllgLSRKEIDE-KFDE------IVEFAE-------LGDF----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 426 gvllFDEPTR------------GIDVGAKFDIY------------------ALLDALAREGRAIVVVSSDLRELMLICDR 475
Cdd:COG1134 140 ----IDQPVKtyssgmrarlafAVATAVDPDILlvdevlavgdaafqkkclARIRELRESGRTVIFVSHSMGAVRRLCDR 215
|
250
....*....|.
gi 490656625 476 IGVMSAGRMHA 486
Cdd:COG1134 216 AIWLEKGRLVM 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
171-438 |
3.10e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGRE 250
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLAHSE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 251 ---------IAEQAVHGTRTPGAPR--LRVERLSRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVygadaadgg 317
Cdd:PRK10938 236 qlegvqlpePDEPSARHALPANEPRivLNNGVVSYNDRPilHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI--------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 318 tvsIGDPP------------RPAAIRSPADAVRHgIALVSEdrkgeglllpqsiaanlSLGQLARV---ARGGVVDG--- 379
Cdd:PRK10938 307 ---TGDHPqgysndltlfgrRRGSGETIWDIKKH-IGYVSS-----------------SLHLDYRVstsVRNVILSGffd 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 380 ---------ERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID 438
Cdd:PRK10938 366 sigiyqavsDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-229 |
3.27e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaEYAPHSRAHAEALGVRMVMQEL-NLVPTLTVA 106
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG-EPITKENIREVRKFVGLVFQNPdDQIFSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFLDrlPHRFGvIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREV 186
Cdd:PRK13652 98 QDIAFG--PINLG-LDEETVAHRVSSALHMLGLEELR-DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490656625 187 ELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13652 174 KELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-229 |
3.79e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.07 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 3 STDPDSTPDTPTLVVTGIGKTY---AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAP 79
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYpdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 80 HSRAhaeALGVRM--VMQELNLVPTlTVAENLFL-------DRLphrfgvidrrrlaadaRAAMARVGLDSL--DPDTLV 148
Cdd:PRK11160 407 YSEA---ALRQAIsvVSQRVHLFSA-TLRDNLLLaapnasdEAL----------------IEVLQQVGLEKLleDDKGLN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 149 GSLGIGHQQM-------VEIARSLAGDCRVLILDEPTAML---TAREV-ELLFDQiarlkADGVALVYISHRLEELARVa 217
Cdd:PRK11160 467 AWLGEGGRQLsggeqrrLGIARALLHDAPLLLLDEPTEGLdaeTERQIlELLAEH-----AQNKTVLMITHRLTGLEQF- 540
|
250
....*....|..
gi 490656625 218 QRVAVLRDGRLV 229
Cdd:PRK11160 541 DRICVMDNGQII 552
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-485 |
4.03e-09 |
|
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: 59.64 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpAAIRSPADAVRHGIALVSEdrkgEGLLLP 356
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIETNLDAVRQSLGMCPQ----HNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAAN--LSLGQLarvaRGGVVDGERENALAARQIDALRIRARGPAQpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:TIGR01257 1017 HLTVAEhiLFYAQL----KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQ---DLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 435 RGIDVGAKFDIYALLDALaREGRAIVVVSSDLRELMLICDRIGVMSAGRMH 485
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
277-483 |
4.12e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 58.32 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADavrHGIALVSEDRKgeglLLP 356
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG--RVVNELEPAD---RDIAMVFQNYA----LYP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 Q-SIAANLSLG-QLARVARGGVvdgERENALAAR--QIDALRirARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:PRK11650 90 HmSVRENMAYGlKIRGMPKAEI---EERVAEAARilELEPLL--DRKPRE----LSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 433 PTRGIDvgAKFDIYALLD--ALAREGRAI-VVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK11650 161 PLSNLD--AKLRVQMRLEiqRLHRRLKTTsLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
277-484 |
5.51e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 57.31 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaaIRSPADAVRH-----GIALVSEDRKGE 351
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG------ITISKENLKEirkkiGIIFQNPDNQFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 GLLLPQSIAANLSLGQLARVARGGVVDGerenalAARQIDALRIRARGPAqpvaELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:PRK13632 98 GATVEDDIAFGLENKKVPPKKMKDIIDD------LAKKVGMEDYLDKEPQ----NLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 432 EPTRGIDVGAKFDIYALLDALAREG-RAIVVVSSDLRELMLiCDRIGVMSAGRM 484
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKL 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
282-485 |
6.22e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.51 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 282 SFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD------PP--RPAAIrspadavrhgiaLVSEDRkgegl 353
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttPPsrRPVSM------------LFQENN----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQ-SIAANLSLGqlarVARGGVVDGERENALA--ARQIDALRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLF 430
Cdd:PRK10771 82 LFSHlTVAQNIGLG----LNPGLKLNAAQREKLHaiARQMGIEDLLARLPGQ----LSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 431 DEPTRGIDVGAKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRMH 485
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-233 |
6.92e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 55.88 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 10 PDTPTLVVTGIGKTYA---EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahae 86
Cdd:cd03369 2 PEHGEIEVENLSVRYApdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 87 ALGVRMVMQELNLV---PTL---TVAENLflDRLphrfgvidrrrlaadaraamarvglDSLDPDTLVGSLGI------- 153
Cdd:cd03369 74 TIPLEDLRSSLTIIpqdPTLfsgTIRSNL--DPF-------------------------DEYSDEEIYGALRVsegglnl 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 154 --GHQQMVEIARSLAGDCRVLILDEPTAMLTArEVELLFDQIARLKADGVALVYISHRLEELARVAqRVAVLRDGRLVHV 231
Cdd:cd03369 127 sqGQRQLLCLARALLKRPRVLVLDEATASIDY-ATDALIQKTIREEFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKEY 204
|
..
gi 490656625 232 DR 233
Cdd:cd03369 205 DH 206
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
405-462 |
7.53e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 56.73 E-value: 7.53e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID---VGakfDIYALLDALAREGRAIVVV 462
Cdd:COG4598 153 AHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelVG---EVLKVMRDLAEEGRTMLVV 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-229 |
9.03e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.05 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH-AEALGVrmVMQELNLVpTLTV 105
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlRRNIAV--VFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLDRLphrfGVIDRRRLAADARAAMARVGLDSLDP-DTLVG----SLGIGHQQMVEIARSLAGDCRVLILDEPTAM 180
Cdd:PRK13657 426 EDNIRVGRP----DATDEEMRAAAERAQAHDFIERKPDGyDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 181 L---TAREVELLFDQIARlkadGVALVYISHRLEELaRVAQRVAVLRDGRLV 229
Cdd:PRK13657 502 LdveTEAKVKAALDELMK----GRTTFIIAHRLSTV-RNADRILVFDNGRVV 548
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-255 |
9.08e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.55 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYA-EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaEYAPHSRAHAEAL--GVR 91
Cdd:PRK13638 2 LATSDLWFRYQdEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRGLLALrqQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 92 MVMQELNL--------------VPTLTVAENLFLDRLPHRFGVIDRRRLAADAraamarvgldsldpdtlVGSLGIGHQQ 157
Cdd:PRK13638 81 TVFQDPEQqifytdidsdiafsLRNLGVPEAEITRRVDEALTLVDAQHFRHQP-----------------IQCLSHGQKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 158 MVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVhvdrIDAQ 237
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL----THGA 219
|
250
....*....|....*...
gi 490656625 238 PTErlvaLMAGREIAEQA 255
Cdd:PRK13638 220 PGE----VFACTEAMEQA 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
278-484 |
9.50e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELL----RLVYGADA---ADGGTVSIG-DPPRPAAIRspadaVRHGIALV-SEDR 348
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnRLIEIYDSkikVDGKVLYFGkDIFQIDAIK-----LRKEVGMVfQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 KGEGLLLPQSIAANLSLGQLA--RVARGGVVDGERENALAARQIDALRirargpaQPVAELSGGNQQKVAIGRWLGRDMG 426
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKekREIKKIVEECLRKVGLWKEVYDRLN-------SPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALAREgRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-229 |
9.82e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 32 VSLALYPGEALALTGENGAGKSTLSKIVAGLVaPTTGAMRLAG---AEYAPHSRAHAEAlgvrMVMQELNLVPTLTVAEN 108
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGqplEAWSAAELARHRA----YLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 109 LFLDRLPHRfgviDRRRLAADARAAMARVGLDSLDPdTLVGSLGIGHQQMVEIA-------RSLAGDCRVLILDEPTAML 181
Cdd:PRK03695 90 LTLHQPDKT----RTEAVASALNEVAEALGLDDKLG-RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490656625 182 TAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
277-484 |
1.06e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.53 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-----GDPPRPAAIRSPAdavrhGIALVSEDRKGE 351
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGDFSKLQGIRKLV-----GIVFQNPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 GLLLPQSIA---ANLSLGQLARVARggvVDgereNALAarQIDALRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVL 428
Cdd:PRK13644 92 GRTVEEDLAfgpENLCLPPIEIRKR---VD----RALA--EIGLEKYRHRSPKT----LSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMlICDRIGVMSAGRM 484
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKI 213
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-204 |
1.26e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyapHSRAHAEALGVRMVMQEL-NLVPTL 103
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-----KTATRGDRSRFMAYLGHLpGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLfldrlpHRFGVIDRRRLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTA 183
Cdd:PRK13543 98 STLENL------HFLCGLHGRRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170 180
....*....|....*....|..
gi 490656625 184 REVELLFDQI-ARLKADGVALV 204
Cdd:PRK13543 171 EGITLVNRMIsAHLRGGGAALV 192
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
277-486 |
1.85e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 54.85 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSigdpprpaairspadavRHGialvsedrkgeglllp 356
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------------VRG---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qSIAANLSLGqlarvarGGvVDGE---RENA--------LAARQIDALRIRARGPA-------QPVAELSGGNQQKVAIG 418
Cdd:cd03220 84 -RVSSLLGLG-------GG-FNPEltgRENIylngrllgLSRKEIDEKIDEIIEFSelgdfidLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 419 RWLGRDMGVLLFDEptrGIDVG-AKFDI--YALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:cd03220 155 IATALEPDILLIDE---VLAVGdAAFQEkcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-227 |
1.85e-08 |
|
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: 54.78 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 21 GKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE-YAPhsrahaealgvrmvmQELNL 99
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIaYVS---------------QEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTlTVAEN-LFLDRLPHRF--GVIDRRrlaadaraamarvgldSLDPD---------TLVGSLGI----GHQQMVEIAR 163
Cdd:cd03250 78 QNG-TIRENiLFGKPFDEERyeKVIKAC----------------ALEPDleilpdgdlTEIGEKGInlsgGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 164 SLAGDCRVLILDEPTAMLTAREVELLFDQ-IARLKADGVALVYISHRLEELARvAQRVAVLRDGR 227
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
402-479 |
1.98e-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: 56.72 E-value: 1.98e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVM 479
Cdd:COG1245 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
265-482 |
3.55e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.40 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS----RGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLV-----YGADAADGGTVSIGDpprpAAIRSP-A 334
Cdd:PRK14239 4 PILQVSDLSvyynKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNG----HNIYSPrT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 335 DAVrhgialvsEDRKGEGLLL------PQSIAANLSLG-QLARVARGGVVDGERENALAARQI-----DALRIRARGpaq 402
Cdd:PRK14239 80 DTV--------DLRKEIGMVFqqpnpfPMSIYENVVYGlRLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALG--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 403 pvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALaREGRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:PRK14239 149 ----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
267-492 |
3.86e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSR----GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGadaadggtVSIGDPPRPAAIRSPADAVRHGIA 342
Cdd:PRK09984 5 IRVEKLAKtfnqHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG--------LITGDKSAGSHIELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 343 LVSEDRKGE---GLLLPQ-------SIAANLSLGQLA-----RVARGGVVDGERENALAARQIDALrirARGPAQPVAEL 407
Cdd:PRK09984 77 LARDIRKSRantGYIFQQfnlvnrlSVLENVLIGALGstpfwRTCFSWFTREQKQRALQALTRVGM---VHFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 408 SGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDV-GAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRmha 486
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPeSARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH--- 230
|
....*.
gi 490656625 487 VFERGG 492
Cdd:PRK09984 231 VFYDGS 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
277-484 |
3.96e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.24 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---PPRPAAIRSPADAVRHGIALVSEDRKGEGL 353
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyiGDKKNNHELITNPYSKKIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 --------LLPQSIAANLSLGQlarVARGgvVDGERENALAARQIDALRIRA----RGPAqpvaELSGGNQQKVAIGRWL 421
Cdd:PRK13631 121 vfqfpeyqLFKDTIEKDIMFGP---VALG--VKKSEAKKLAKFYLNKMGLDDsyleRSPF----GLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
264-466 |
4.55e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 53.52 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 264 APRLRVERLSRgDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADavrhGIAL 343
Cdd:TIGR01189 3 ARNLACSRGER-MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE----NILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 344 VSEDRKGEGLLlpqSIAANLSLGQlarvARGGVVDGERENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGR 423
Cdd:TIGR01189 78 LGHLPGLKPEL---SALENLHFWA----AIHGGAQRTIEDALAAVGLTGFEDL------PAAQLSAGQQRRLALARLWLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDA-LAREGRAIVVVSSDL 466
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDL 188
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-224 |
5.55e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.27 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-------GVRmvmqelnlvPT 102
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpGIK---------TE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENL-FLDRLphrFGVIDrrrlAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:PRK13538 89 LTALENLrFYQRL---HGPGD----DEALWEALAQVGLAGFE-DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490656625 182 TAREVELLFDQIARLKADGVALVYISHRleELARVAQRVAVLR 224
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKVRKLR 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
406-484 |
6.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.02 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALA-REGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-229 |
6.66e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.11 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEAL--GVRMVMQElNLVPTL 103
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG---RPLSSLSHSVLrqGVAMVQQD-PVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRLPHRFGVIDrrrlaadaraAMARVGLDSLD---PD---TLVG----SLGIGHQQMVEIARSLAGDCRVLI 173
Cdd:PRK10790 430 TFLANVTLGRDISEEQVWQ----------ALETVQLAELArslPDglyTPLGeqgnNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 174 LDEPTAMLTArEVELLFDQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:PRK10790 500 LDEATANIDS-GTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
402-479 |
6.92e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 6.92e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALArEGRAIVVVSSDLRELMLICDRIGVM 479
Cdd:PRK13409 208 RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-229 |
7.10e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.08 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMrLAGAEYAPHSRAHAEAL--GVRMVMQEL-NLVPTLTV 105
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGLMKLreSVGMVFQDPdNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLfldrlphRFGVIDRR----RLAADARAAMARVGLDSLDpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:PRK13636 101 YQDV-------SFGAVNLKlpedEVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 182 TAREV-ELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13636 173 DPMGVsEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
265-483 |
7.13e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.49 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS---RG-DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGD---PPRPAAIRSpadav 337
Cdd:COG1137 2 MTLEAENLVksyGKrTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGediTHLPMHKRA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 338 RHGIAlvsedrkgeglLLPQ--SIAANLSLGQ-LARVARGGVVDGERENALAARQIDALRI--RARGPAQpvaELSGGNQ 412
Cdd:COG1137 77 RLGIG-----------YLPQeaSIFRKLTVEDnILAVLELRKLSKKEREERLEELLEEFGIthLRKSKAY---SLSGGER 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 413 QKVAIGRWLGRDMGVLLFDEPTRGID---VGakfDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:COG1137 143 RRVEIARALATNPKFILLDEPFAGVDpiaVA---DIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-229 |
7.38e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.55 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP----TTGAMRLAGAEYAPhsrAHAEALG 89
Cdd:PRK10418 4 QIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP---CALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VRMVMQE----LNLVPTLT--VAENLFldrlphrfgVIDRRRLAADARAAMARVGLDslDPDTLVGS----LGIGHQQMV 159
Cdd:PRK10418 81 IATIMQNprsaFNPLHTMHthARETCL---------ALGKPADDATLTAALEAVGLE--NAARVLKLypfeMSGGMLQRM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 160 EIARSLAGDCRVLILDEPT----AMLTAREVELLfDQIARLKADGVALVyiSHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTtdldVVAQARILDLL-ESIVQKRALGMLLV--THDMGVVARLADDVAVMSHGRIV 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-229 |
8.36e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 52.88 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG---AEYAPHS-RAHaealgVRMVMQElnlvP 101
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKIGLHDlRSR-----ISIIPQD----P 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TL---TVAENL-FLDRLP--------HRFGVIDRRRLAADaraamarvGLDSldPDTLVGS-LGIGHQQMVEIARSLAGD 168
Cdd:cd03244 88 VLfsgTIRSNLdPFGEYSdeelwqalERVGLKEFVESLPG--------GLDT--VVEEGGEnLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 169 CRVLILDEPTA---MLTAREVEllfdQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRLV 229
Cdd:cd03244 158 SKILVLDEATAsvdPETDALIQ----KTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
277-502 |
9.01e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRSpadaVRHGIALVSEDRKGEglLL 355
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVNAENEKW----VRSKVGLVFQDPDDQ--VF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:PRK13647 94 SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDK------PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 436 GIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGGWTQDALLGAA 502
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQA 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-229 |
9.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTYAEPV------LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHA 85
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 86 EalgVRMVMQELNLVPTLTVAEnLFLDRLPH--RFGVIDRRRLAADA-RAAMARVGLDSLDPDTLVGS---LGIGHQQMV 159
Cdd:PRK13645 84 E---VKRLRKEIGLVFQFPEYQ-LFQETIEKdiAFGPVNLGENKQEAyKKVPELLKLVQLPEDYVKRSpfeLSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 160 EIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-68 |
1.08e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.08e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 15 LVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTG 68
Cdd:PRK15064 320 LEVENLTKGFdNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-73 |
1.21e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.21e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 6 PDSTPDtPTLVVTGIGKTYAEP-VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLA 73
Cdd:PRK10636 305 PESLPN-PLLKMEKVSAGYGDRiILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA 372
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-474 |
1.28e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIAANLSLGQLARVARGGV-VDGERENALAARQI-DALRIRARGPAqpvAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVGWRPKLeIDDIVESALKDADLwDEIKHKIHKSA---LDLSGGQQQRLCIARALAVKPKVLLMD 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 490656625 432 EPTRGIDVGAKFDIYALLDALA-REGRAIVVVSSDLRELMLICD 474
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
275-484 |
1.42e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 275 GDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaaIRSPADAVRHGIALVsedRKGEGLL 354
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD------TLITSTSKNKDIKQI---RKKVGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 L--PQSIAANLSLgqLARVARG----GVVDGEREnALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVL 428
Cdd:PRK13649 91 FqfPESQLFEETV--LKDVAFGpqnfGVSQEEAE-ALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
272-439 |
1.92e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 272 LSRGDA--VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIG----------DPPRPAAiRSPADAVRH 339
Cdd:PRK11147 11 LSFSDAplLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqDPPRNVE-GTVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALVSEDRKGEGLLLPQsIAANLS---LGQLARVArgGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVA 416
Cdd:PRK11147 90 GIEEQAEYLKRYHDISHL-VETDPSeknLNELAKLQ--EQLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGGWLRKAA 166
|
170 180
....*....|....*....|...
gi 490656625 417 IGRWLGRDMGVLLFDEPTRGIDV 439
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDI 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
406-466 |
2.04e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID-VGAKfDIYALLDALAREGRAIVVVSSDL 466
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVK-EILEIFDNLNKQGKTIILVTHDL 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-229 |
2.10e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG---------------VRM 92
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 VMQ--ELNLVPTlTVAENLFLDrlPHRFGViDRRRLAADARAAMARVGLDS--LD--PDTLVGslgiGHQQMVEIARSLA 166
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFG--PVALGV-KKSEAKKLAKFYLNKMGLDDsyLErsPFGLSG----GQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
278-484 |
2.12e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 51.70 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAairSPADAVRHGIALVSEdrkgEGLLLPQ 357
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ---YEHKYLHSKVSLVGQ----EPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLGqLARVARGGVVdgerENALAARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEP 433
Cdd:cd03248 103 SLQDNIAYG-LQSCSFECVK----EAAQKAHAHSFISELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490656625 434 TRGIDVGAKFDIY-ALLDALARegRAIVVVSSDLrELMLICDRIGVMSAGRM 484
Cdd:cd03248 178 TSALDAESEQQVQqALYDWPER--RTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
28-242 |
2.13e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMrlagaEYA-PHSRAHAEALGVRMVMQELNLVPT---- 102
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI-----EWIfKDEKNKKKTKEKEKVLEKLVIQKTrfkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 --------------LTVAE-NLFLDRL-------PHRFGViDRRRLAADARAAMARVGLDS--LD--PDTLVGslgiGHQ 156
Cdd:PRK13651 97 ikkikeirrrvgvvFQFAEyQLFEQTIekdiifgPVSMGV-SKEEAKKRAAKYIELVGLDEsyLQrsPFELSG----GQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 157 QMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHvdriDA 236
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK----DG 247
|
....*.
gi 490656625 237 QPTERL 242
Cdd:PRK13651 248 DTYDIL 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
390-499 |
2.19e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 390 IDALRIRArgpaQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLREL 469
Cdd:PRK13638 124 VDAQHFRH----QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490656625 470 MLICDRIGVMSAGRMHA------VF------ERGGWTQDALL 499
Cdd:PRK13638 200 YEISDAVYVLRQGQILThgapgeVFacteamEQAGLTQPWLV 241
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-181 |
2.76e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.13 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLvapttgamRLAGAEYAPHSRAHAEALGVRM-------VMQELNLVP 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR--------SPKGVKGSGSVLLNGMPIDAKEmraisayVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 TLTVAENLFLD---RLPHRfgvIDRRRLAADARAAMARVGLDSLdPDTLVG------SLGIGHQQMVEIARSLAGDCRVL 172
Cdd:TIGR00955 113 TLTVREHLMFQahlRMPRR---VTKKEKRERVDEVLQALGLRKC-ANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLL 188
|
....*....
gi 490656625 173 ILDEPTAML 181
Cdd:TIGR00955 189 FCDEPTSGL 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
281-486 |
2.91e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGgTVSIGDppRPAAIRSPADAVRHGIALVSEDRKGEGLLLPQSIA 360
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAG--QPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 361 anLSLGQLARVARGGVVDGERENALaarQIDALRIRargpaqPVAELSGGNQQKV-------AIGRWLGRDMGVLLFDEP 433
Cdd:PRK03695 92 --LHQPDKTRTEAVASALNEVAEAL---GLDDKLGR------SVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 434 TRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-68 |
3.01e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 3.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTG 68
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG 79
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
290-486 |
3.43e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 290 IFGISGligAGRTELLRLVYGADAADGGTVSIGDpprpaaiRSPADAVRhGIALVSEDRK-----GEGLLLPQ-SIAANL 363
Cdd:PRK11144 29 IFGRSG---AGKTSLINAISGLTRPQKGRIVLNG-------RVLFDAEK-GICLPPEKRRigyvfQDARLFPHyKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 364 SLGqLARVARggvvdgerenALAARQIDALRIRA---RGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVG 440
Cdd:PRK11144 98 RYG-MAKSMV----------AQFDKIVALLGIEPlldRYPGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490656625 441 AKFDIYALLDALAREGR-AIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK11144 163 RKRELLPYLERLAREINiPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
262-484 |
5.67e-07 |
|
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: 51.99 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 262 PGAPRLRVERLS---RGD-----AVRDVSFDVRAGEIFGISGLIGAGRT----ELLRLVYGADAADGGTVS------IGD 323
Cdd:COG4172 2 MSMPLLSVEDLSvafGQGggtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgqdlLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 324 PPRpaAIRspadAVR-HGIALVSEDrkgeglllPQSiAAN--LSLG-QLARVARggVVDGERENALAARQIDAL-RIRAR 398
Cdd:COG4172 82 SER--ELR----RIRgNRIAMIFQE--------PMT-SLNplHTIGkQIAEVLR--LHRGLSGAAARARALELLeRVGIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 399 GPAQPVA----ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDL---RElm 470
Cdd:COG4172 145 DPERRLDayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLgvvRR-- 222
|
250
....*....|....
gi 490656625 471 lICDRIGVMSAGRM 484
Cdd:COG4172 223 -FADRVAVMRQGEI 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
273-474 |
6.76e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 273 SRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALvsedrkg 350
Cdd:PRK11831 16 TRGNRCifDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSM------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 egllLPQSIAANLSLGQLARVARGgVVDGERENALAARQIDALRIRA---RGPAQPV-AELSGGNQQKVAIGRWLGRDMG 426
Cdd:PRK11831 89 ----LFQSGALFTDMNVFDNVAYP-LREHTQLPAPLLHSTVMMKLEAvglRGAAKLMpSELSGGMARRAALARAIALEPD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICD 474
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIAD 212
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-233 |
7.09e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.80 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVApttgAMRLAGAEYAPHSRAHAEALG-VRMVMQELNLVPTLTVA 106
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ----GNNFTGTILANNRKPTKQILKrTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLF---LDRLPHRfgvIDRRRLAADARAAMARVGLDSLDpDTLVGSLGI-----GHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:PLN03211 159 ETLVfcsLLRLPKS---LTKQEKILVAESVISELGLTKCE-NTIIGNSFIrgisgGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 179 AMLTAREVELLFDQIARLKADGVALVYISHrlEELARVAQ---RVAVLRDGRLVHVDR 233
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMH--QPSSRVYQmfdSVLVLSEGRCLFFGK 290
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-84 |
9.85e-07 |
|
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: 51.34 E-value: 9.85e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 32 VSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAH 84
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA 403
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-229 |
1.02e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.46 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEAL-GVRMVMQELN---LVPtl 103
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRkTVGIVFQNPDdqlFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLTA 183
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSG----GQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490656625 184 REVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
277-491 |
1.06e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.40 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADaVRHGIALVSE--DRKGEGLL 354
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG--MVLSEETVWD-VRRQVGMVFQnpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGQlarVARGGVVdgERENAlAARQIDALRIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK13635 99 VQDDVAFGLENIG---VPREEMV--ERVDQ-ALRQVGMEDFLNREPHR----LSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 435 RGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRElMLICDRIGVMSAGRMHA------VFERG 491
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLsITHDLDE-AAQADRVIVMNKGEILEegtpeeIFKSG 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
277-486 |
1.08e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.17 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVR-------------AGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRpAAIRSPADAvRHGIAL 343
Cdd:PRK10575 13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-ESWSSKAFA-RKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 344 VSEDRKGEGLLLPQSIAanlsLGQL---ARVARGGVVDGER-ENALAARQIDALRIRArgpaqpVAELSGGNQQKVAIGR 419
Cdd:PRK10575 91 PQQLPAAEGMTVRELVA----IGRYpwhGALGRFGAADREKvEEAISLVGLKPLAHRL------VDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 420 WLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
404-476 |
1.30e-06 |
|
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: 47.83 E-value: 1.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 404 VAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAkfdIYALLDALAREGRAIVVVSSDlRELM-LICDRI 476
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKEYPGTVILVSHD-RYFLdQVATKI 137
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
32-523 |
1.37e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 51.41 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 32 VSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVMQELNLVPTLTVAEnlfL 111
Cdd:COG3321 861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALA---A 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 112 DRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFD 191
Cdd:COG3321 938 AAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAA 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 192 QIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDRIDAQPTERLVALMAGREIAEQAVHGTRTPGAPRLRVER 271
Cdd:COG3321 1018 AAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 272 LSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSEDRKGE 351
Cdd:COG3321 1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 GLLLPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALRIRARGPAQPVAELSGGNQQKVAIGRWLGRDMGVLLFD 431
Cdd:COG3321 1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 432 EPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGGWTQDALLGAAFAGYARRDA 511
Cdd:COG3321 1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
|
490
....*....|..
gi 490656625 512 ALHPPGGARSAA 523
Cdd:COG3321 1338 AAALALAAAAAA 1349
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-217 |
1.48e-06 |
|
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: 50.70 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 17 VTGIGKTYAEPVL-DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHSRAHaealgvrm 92
Cdd:TIGR03719 325 AENLTKAFGDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvklAYVDQSRDA-------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 93 vmqelnLVPTLTVAENLF--LDrlphrfgVIDRRRLAADARAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCR 170
Cdd:TIGR03719 397 ------LDPNKTVWEEISggLD-------IIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 171 VLILDEPTAML---TAREVELlfdqiARLKADGVALVyISHRLEELARVA 217
Cdd:TIGR03719 464 VLLLDEPTNDLdveTLRALEE-----ALLNFAGCAVV-ISHDRWFLDRIA 507
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-226 |
1.52e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.96 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRL-AGAEYA-------------------PHSRAHA 85
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqrpylplgtlreallyPATAEAF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 86 EALGVRMVMQELNlvptltvaenlfLDRLPHRfgvidrrrlaadaraamarvgLDSLDPDTLVgsLGIGHQQMVEIARSL 165
Cdd:COG4178 456 SDAELREALEAVG------------LGHLAER---------------------LDEEADWDQV--LSLGEQQRLAFARLL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 166 AGDCRVLILDEPTAMLTAREVELLFDQI-ARLKadGVALVYISHRlEELARVAQRVAVLRDG 226
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLrEELP--GTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
277-461 |
1.87e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 50.40 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLV---YgaDAADGGTVSIGDPPRPAAIRSpadaVRHGIALVSEDRKgegl 353
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfY--DIDEGEILLDGHDLRDYTLAS----LRNQVALVSQNVH---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 354 LLPQSIAANLSLGQLARVARGGVVdgerENALAARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLL 429
Cdd:PRK11176 428 LFNDTIANNIAYARTEQYSREQIE----EAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190
....*....|....*....|....*....|..
gi 490656625 430 FDEPTRGIDVGAKFDIYALLDALAREGRAIVV 461
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNRTSLVI 535
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-223 |
2.10e-06 |
|
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: 47.92 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGamrlagaeyaphsrahaealgvRMVMqelnlvptLTVA 106
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG----------------------RIGM--------PEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLFLDRLPHrfgvidrrrlaadaraamarvgldsLDPDTLVGS--------LGIGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:cd03223 65 DLLFLPQRPY-------------------------LPLGTLREQliypwddvLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490656625 179 AMLTArEVELLFDQIarLKADGVALVYISHRlEELARVAQRVAVL 223
Cdd:cd03223 120 SALDE-ESEDRLYQL--LKELGITVISVGHR-PSLWKFHDRVLDL 160
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-241 |
2.40e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.08 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 15 LVVTGIGKTYAE---PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVApTTGAMRLAGAEYAPHS-RAHAEALGV 90
Cdd:cd03289 3 MTVKDLTAKYTEggnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPlQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 91 rmVMQEL---------NLVP--------TLTVAENLFLDRLPHRFGvidrrrlaadaraamarvglDSLDPDTLVGS--L 151
Cdd:cd03289 82 --IPQKVfifsgtfrkNLDPygkwsdeeIWKVAEEVGLKSVIEQFP--------------------GQLDFVLVDGGcvL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 152 GIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADgVALVYISHRLEELARvAQRVAVLRDGRLVHV 231
Cdd:cd03289 140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD-CTVILSEHRIEAMLE-CQRFLVIEENKVRQY 217
|
250
....*....|
gi 490656625 232 DRIDAQPTER 241
Cdd:cd03289 218 DSIQKLLNEK 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-241 |
2.85e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 10 PDTPTLVVTGIGKTYAE---PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLvAPTTGAMRLAGAEYAPHS-RAHA 85
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYTEagrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTlQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 86 EALGVrmVMQELnLVPTLTVAENLflDrlPHrfgvidRRRLAADARAAMARVGLDSLD---PDTLV-----GS--LGIGH 155
Cdd:TIGR01271 1292 KAFGV--IPQKV-FIFSGTFRKNL--D--PY------EQWSDEEIWKVAEEVGLKSVIeqfPDKLDfvlvdGGyvLSNGH 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 156 QQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADgVALVYISHRLEELARvAQRVAVLRDGRLVHVDRID 235
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQ 1436
|
....*.
gi 490656625 236 AQPTER 241
Cdd:TIGR01271 1437 KLLNET 1442
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
276-465 |
3.00e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.11 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGT-------VSIGDPPRPAAIRspadavRHGIALVSEDR 348
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVATLDADALAQLR------REHFGFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 KgeglLLPQSIAA-NLSL----GQLARVARGgvvdgERENALAARqidaLRIRARGPAQPvAELSGGNQQKVAIGRWLGR 423
Cdd:PRK10535 96 H----LLSHLTAAqNVEVpavyAGLERKQRL-----LRAQELLQR----LGLEDRVEYQP-SQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSD 465
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-232 |
3.12e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahaeALGVRMVMQELNLVP----- 101
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--------KFGLTDLRRVLSIIPqspvl 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 102 -TLTVAENL--F-------LDRLPHRFGVIDRRRLAADaraamarvgldSLDPDTLVG--SLGIGHQQMVEIARSLAGDC 169
Cdd:PLN03232 1322 fSGTVRFNIdpFsehndadLWEALERAHIKDVIDRNPF-----------GLDAEVSEGgeNFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 170 RVLILDEPTAMLTAReVELLFDQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRLVHVD 232
Cdd:PLN03232 1391 KILVLDEATASVDVR-TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYD 1451
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-229 |
3.58e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 47.64 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPT---TGAMRLAGAEYAP-HSRAHAEALgvrMVMQELNLVPT 102
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEKYPGEII---YVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLfldrlphRFGVidrrrlaadaraamarvgldSLDPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAML- 181
Cdd:cd03233 98 LTVRETL-------DFAL--------------------RCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLd 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 182 --TAREvellFDQIARLKAD---GVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:cd03233 151 ssTALE----ILKCIRTMADvlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
276-486 |
3.91e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.65 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 276 DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRspadavrhgialvsEDRKGEGLL 354
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIR--------------EVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 LPQSIAANLSLGQLARVARGGVVDGERENALAARQIDALR------IRARGPAQpvaeLSGGNQQKVAIGRWLGRDMGVL 428
Cdd:PRK13652 84 FQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHmlgleeLRDRVPHH----LSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 429 LFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELML-ICDRIGVMSAGRMHA 486
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPeMADYIYVMDKGRIVA 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-240 |
4.63e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.55 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyaphSRAHAEAL-----GVRMVMQEL-NLVPT 102
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG------ELLTAENVwnlrrKIGMVFQNPdNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 103 LTVAENLFLDRLPHRFGVIDRRRLAADARAAMARVGLDSLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDEPTAMLT 182
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSG----GQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 183 AREVELLFDQIARLKAD-GVALVYISHRLEELARvAQRVAVLRDGRLVHvdriDAQPTE 240
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIK----EAAPSE 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-204 |
5.61e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 47.24 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAG--LVAPTTGAMRLAGAEyaphsRAHAEALGVRMVMQELNLVPTLTVA 106
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRP-----LDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 107 ENLfldrlphRFgvidrrrlaadaraamarvgldsldpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREV 186
Cdd:cd03232 98 EAL-------RF--------------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170
....*....|....*...
gi 490656625 187 ELLFDQIARLKADGVALV 204
Cdd:cd03232 145 YNIVRFLKKLADSGQAIL 162
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
277-502 |
5.74e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.42 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRHGIALVSED-------RK 349
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpygslnpRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 350 GEGLLLPQSIAANLSLGQLARvarggvvdgeRENALAARQIDALRIR--ARGPAQpvaeLSGGNQQKVAIGRWLGRDMGV 427
Cdd:PRK11308 110 KVGQILEEPLLINTSLSAAER----------REKALAMMAKVGLRPEhyDRYPHM----FSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFE--RGGWTQdAL 498
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCvekgtkEQIFNnpRHPYTQ-AL 254
|
....
gi 490656625 499 LGAA 502
Cdd:PRK11308 255 LSAT 258
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
277-484 |
6.18e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 48.67 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAirsPADAVRHGIALVSE------DRKG 350
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY---SEAALRQAISVVSQrvhlfsATLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 351 EGLLLPQSIAANLSLGQ-LARVARGGVVDGEreNALAA------RQidalrirargpaqpvaeLSGGNQQKVAIGRWLGR 423
Cdd:PRK11160 432 DNLLLAAPNASDEALIEvLQQVGLEKLLEDD--KGLNAwlgeggRQ-----------------LSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 424 DMGVLLFDEPTRGIDVGAKFDIYALLDALAReGRAIVVVSSDLREL--MlicDRIGVMSAGRM 484
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLeqF---DRICVMDNGQI 551
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
28-220 |
6.30e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGvrmvmQELNLVPTLTVAE 107
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG-----HNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 NL-----------FLDRLPHRFGVIDRRrlaadaraamarvgldsldpDTLVGSLGIGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK13541 90 NLkfwseiynsaeTLYAAIHYFKLHDLL--------------------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490656625 177 PTAMLTAREVELLFDQIArLKADGVALVYISHRLEELARVAQRV 220
Cdd:PRK13541 150 VETNLSKENRDLLNNLIV-MKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
402-478 |
7.27e-06 |
|
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: 48.63 E-value: 7.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGV 478
Cdd:COG1245 451 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
407-483 |
8.14e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.50 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVV----SSDLRELMlicDRIGVMSAG 482
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEG 243
|
.
gi 490656625 483 R 483
Cdd:TIGR00955 244 R 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
277-484 |
8.98e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPAdAVRHGIALVSEDRKGEglLLP 356
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLL-EVRKTVGIVFQNPDDQ--LFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 QSIAANLSLGQLARvarggvvdGERENALAARQIDAL-RIRARG-PAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK13639 94 PTVEEDVAFGPLNL--------GLSKEEVEKRVKEALkAVGMEGfENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 435 RGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-484 |
9.15e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.21 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLG-QLARVARGGVVDGER-ENALAARQI-DALRIRARGPAqpvAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK14247 98 SIFENVALGlKLNRLVKSKKELQERvRWALEKAQLwDEVKDRLDAPA---GKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490656625 435 RGIDVGAKFDIYALLDALAREgRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
280-495 |
1.01e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.52 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPA-DAVRHGIALVSEdrKGEGLLLPQS 358
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlKKLRKKVSLVFQ--FPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 359 IAANLSLGQLarvaRGGVVDGERENAlaarqidALR-IRARGPAQPVA-----ELSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:PRK13641 103 VLKDVEFGPK----NFGFSEDEAKEK-------ALKwLKKVGLSEDLIskspfELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 433 PTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRM--HA----VFERGGWTQ 495
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHAspkeIFSDKEWLK 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
277-483 |
1.11e-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: 46.72 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTE----LLRLVYgadaADGGTVSIGDPPrpaaIRS-PADAVRHGIALVSEDrkge 351
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSILIDGVD----ISKiGLHDLRSRISIIPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 352 GLLLPQSIAANL-SLGQLArvarggvvDGERENALAARQIDA----------LRIRARGpaqpvAELSGGNQQKVAIGRW 420
Cdd:cd03244 87 PVLFSGTIRSNLdPFGEYS--------DEELWQALERVGLKEfveslpggldTVVEEGG-----ENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 421 LGRDMGVLLFDEPTRGIDVgakfDIYALLDALARE---GRAIVVVSSDLRELMlICDRIGVMSAGR 483
Cdd:cd03244 154 LLRKSKILVLDEATASVDP----ETDALIQKTIREafkDCTVLTIAHRLDTII-DSDRILVLDKGR 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
277-498 |
1.31e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.39 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVS-IGDPPRPAAiRSPADAVRHGIALVSEDrkgeglll 355
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMK-DDEWRAVRSDIQMIFQD-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 P-QSIAANLSLGQL---------ARVARGGVVDGEREN----ALAARQIDalriraRGPAqpvaELSGGNQQKVAIGRWL 421
Cdd:PRK15079 107 PlASLNPRMTIGEIiaeplrtyhPKLSRQEVKDRVKAMmlkvGLLPNLIN------RYPH----EFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 422 GRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGrmHAVfERGgwTQDAL 498
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG--HAV-ELG--TYDEV 249
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-109 |
1.33e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 14 TLVVTGIGKTYA--EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA---EYAPHSRahaeal 88
Cdd:PRK11650 3 GLKLQAVRKSYDgkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEPADR------ 76
|
90 100
....*....|....*....|.
gi 490656625 89 GVRMVMQELNLVPTLTVAENL 109
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENM 97
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-74 |
1.38e-05 |
|
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: 46.77 E-value: 1.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 24 YAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG 74
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-321 |
1.52e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 137 VGLDSLDPDTLVGSLGIGHQQMVEIARSL-AGDCRVL-ILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRlEELA 214
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTI 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 215 RVAQRV------AVLRDGRLVH---VDRIDAQPTERLVALMAGREiaEQAVHGTRTPGAPRLRVERLSRGDAVRDVSFDV 285
Cdd:TIGR00630 554 RAADYVidigpgAGEHGGEVVAsgtPEEILANPDSLTGQYLSGRK--KIEVPAERRPGNGKFLTLKGARENNLKNITVSI 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490656625 286 RAGEIFGISGLIGAGRTELL---------RLVYGADAADGGTVSI 321
Cdd:TIGR00630 632 PLGLFTCITGVSGSGKSTLIndtlypalaNRLNGAKTVPGRYTSI 676
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-232 |
1.59e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.02 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAphsrahaeALGVRMVMQELNLVPTLTVae 107
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--------KIGLHDLRFKITIIPQDPV-- 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 108 nLF-------LD--------------RLPHRFGVIDRRRlaadaraamarvglDSLDPDTLVG--SLGIGHQQMVEIARS 164
Cdd:TIGR00957 1371 -LFsgslrmnLDpfsqysdeevwwalELAHLKTFVSALP--------------DKLDHECAEGgeNLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 165 LAGDCRVLILDEPTAMLTArEVELLFDQIARLKADGVALVYISHRLEELARVAqRVAVLRDGRLVHVD 232
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
261-468 |
1.81e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.52 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 261 TPGAPRLRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRL-------VYGADAADGGTVSigdpprpaa 329
Cdd:PRK10253 2 TESVARLRGEQLTLGygkyTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTlsrlmtpAHGHVWLDGEHIQ--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 330 iRSPADAVRHGIALVSEDRKGEGLLLPQSIAANLSLGQLARVARGGVVDGEREN-ALAARQIDALrirargPAQPVAELS 408
Cdd:PRK10253 73 -HYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTkAMQATGITHL------ADQSVDTLS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 409 GGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRE 468
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQ 206
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
154-258 |
1.97e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVAQRVAVLRDGRLVHVDR 233
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
90 100
....*....|....*....|....*
gi 490656625 234 IDAQPTErlvalMAGREIAEQAVHG 258
Cdd:NF000106 228 VDELKTK-----VGGRTLQIRPAHA 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-210 |
2.28e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 12 TPTLVVTGIGKTY--AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEALg 89
Cdd:PRK15056 4 QAGIVVNDVTVTWrnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG---QPTRQALQKNL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 90 VRMVMQ--ELNLVPTLTVAENLFLDRLPHrFGVIDRRRLAADARAAMARVGLDSLD-PDTLVGSLGIGHQQMVEIARSLA 166
Cdd:PRK15056 80 VAYVPQseEVDWSFPVLVEDVVMMGRYGH-MGWLRRAKKRDRQIVTAALARVDMVEfRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRL 210
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNL 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-240 |
2.30e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 145 DTLVGS----LGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARLKADGVAL-VYISHRLEELaRVAQR 219
Cdd:PTZ00265 570 ETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTI-RYANT 648
|
90 100
....*....|....*....|....
gi 490656625 220 VAVLRD---GRLVHVDRIDAQPTE 240
Cdd:PTZ00265 649 IFVLSNrerGSTVDVDIIGEDPTK 672
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-224 |
2.47e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 13 PTLVVTGIGKTY-AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLvAPTTGAMRLAG-AEYAPHS----RAHAE 86
Cdd:PRK14258 6 PAIKVNNLSFYYdTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrVEFFNQNiyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 87 AL--GVRMVMQELNLVPtLTVAENLfldrlphRFGV----------IDRRRLAADARAAMARVGLDSLDPDTLvgSLGIG 154
Cdd:PRK14258 85 RLrrQVSMVHPKPNLFP-MSVYDNV-------AYGVkivgwrpkleIDDIVESALKDADLWDEIKHKIHKSAL--DLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656625 155 HQQMVEIARSLAGDCRVLILDEPTAML---TAREVELLFdQIARLKADgVALVYISHRLEELARVAQRVAVLR 224
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLdpiASMKVESLI-QSLRLRSE-LTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-230 |
2.48e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.01 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGaeyAPHSRAHAEALGVRMVMqeLNLVPTL--- 103
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD---IPLTKLQLDSWRSRLAV--VSQTPFLfsd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRlPhrfgviDRRRLAADARAAMARVGLDSLD-P---DTLVGSLGI----GHQQMVEIARSLAGDCRVLILD 175
Cdd:PRK10789 404 TVANNIALGR-P------DATQQEIEHVARLASVHDDILRlPqgyDTEVGERGVmlsgGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656625 176 EPTAMLTAR-EVELLfdQIARLKADGVALVYISHRLEELARvAQRVAVLRDGRLVH 230
Cdd:PRK10789 477 DALSAVDGRtEHQIL--HNLRQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-222 |
2.56e-05 |
|
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: 45.86 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 22 KTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAE--YAPhsrahaealgvrmvmQELNL 99
Cdd:cd03237 8 KTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvsYKP---------------QYIKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAENLfldrlphrFGVIDRRRLAAD-ARAAMARVGLDSLdPDTLVGSLGIGHQQMVEIARSLAGDCRVLILDEPT 178
Cdd:cd03237 73 DYEGTVRDLL--------SSITKDFYTHPYfKTEIAKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490656625 179 AMLTAREVELLFDQIAR--LKADGVALVyISHRLEELARVAQRVAV 222
Cdd:cd03237 144 AYLDVEQRLMASKVIRRfaENNEKTAFV-VEHDIIMIDYLADRLIV 188
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
27-61 |
2.68e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 2.68e-05
10 20 30
....*....|....*....|....*....|....*
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAG 61
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
267-484 |
2.88e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.85 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIgDPPRPAAIRSPADAVRHGIALVSE 346
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAENVWNLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 347 DRKGEGLLLPQSIAANLSLGQLARVARGGVVDgerENALAARQIDalrIRARGPAQpvaeLSGGNQQKVAIGRWLGRDMG 426
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVD---EALLAVNMLD---FKTREPAR----LSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 427 VLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVV-VSSDLRElMLICDRIGVMSAGRM 484
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLsITHDLDE-AASSDRILVMKAGEI 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
267-474 |
3.57e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.54 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLS--RGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLR-------LVYGADAAdgGTVSIGDPPRPAAIRSPAd 335
Cdd:PRK14243 11 LRTENLNvyYGSflAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVE--GKVTFHGKNLYAPDVDPV- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 336 AVRHGIALVSEDRKGegllLPQSIAANLSLGqlARV-ARGGVVDGERENALaaRQI-------DALRirargpaQPVAEL 407
Cdd:PRK14243 88 EVRRRIGMVFQKPNP----FPKSIYDNIAYG--ARInGYKGDMDELVERSL--RQAalwdevkDKLK-------QSGLSL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 408 SGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALaREGRAIVVVSSDLRELMLICD 474
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
258-484 |
3.75e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 258 GTRTPGAPRLRVERLS--RGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLR-------LVYGADAAdgGTVSIGDppr 326
Cdd:COG1117 3 APASTLEPKIEVRNLNvyYGDkqALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARVE--GEILLDG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 327 pAAIRSP-ADAVRHgialvsedRKGEGLL------LPQSIAANLSLG-QLARVARGGVVDGERENALaaRQI-------D 391
Cdd:COG1117 78 -EDIYDPdVDVVEL--------RRRVGMVfqkpnpFPKSIYDNVAYGlRLHGIKSKSELDEIVEESL--RKAalwdevkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 392 ALRirargpaQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREgRAIVVVSSDLRELML 471
Cdd:COG1117 147 RLK-------KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAAR 218
|
250
....*....|...
gi 490656625 472 ICDRIGVMSAGRM 484
Cdd:COG1117 219 VSDYTAFFYLGEL 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
281-513 |
3.79e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 46.38 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGAdAADGGTVSI-GDPPRpaaiRSPADAVRHGIALVSEdrkgEGLLLPQSI 359
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKInGIELR----ELDPESWRKHLSWVGQ----NPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 360 AANLSLGQLArvarggVVDGERENALAARQI-DALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK11174 440 RDNVLLGNPD------ASDEQLQQALENAWVsEFLPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 435 RGIDVGAKfdiYALLDAL--AREGRAIVVVSSDLRELMLiCDRIGVMSAGRmhaVFERGGWTQDALLGAAFAG-YARRDA 511
Cdd:PRK11174 514 ASLDAHSE---QLVMQALnaASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQ---IVQQGDYAELSQAGGLFATlLAHRQE 586
|
..
gi 490656625 512 AL 513
Cdd:PRK11174 587 EI 588
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-181 |
3.96e-05 |
|
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: 46.32 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 2 DSTDPDSTPDTPTLVV-TGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAM----RLAgae 76
Cdd:COG1245 328 EVHAPRREKEEETLVEyPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlKIS--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 77 YAPhsrahaealgvrmvmQELNLVPTLTVAENLFlDRLPHRFG-------VIDrrrlaadaraamaRVGLDSLdPDTLVG 149
Cdd:COG1245 405 YKP---------------QYISPDYDGTVEEFLR-SANTDDFGssyykteIIK-------------PLGLEKL-LDKNVK 454
|
170 180 190
....*....|....*....|....*....|..
gi 490656625 150 SLGIGHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-74 |
4.01e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 4.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 24 YAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAG 74
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG 487
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
30-178 |
4.14e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 30 DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAhaealgVRM---VM-QELNLVPTLTV 105
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA------TRRrvgYMsQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 106 AENLFLD-RLPH---------------RFGVIDRrrlaadaraamarvgLDSLdPDTLvgSLGIgHQQMveiarSLAGDC 169
Cdd:NF033858 357 RQNLELHaRLFHlpaaeiaarvaemleRFDLADV---------------ADAL-PDSL--PLGI-RQRL-----SLAVAV 412
|
170
....*....|...
gi 490656625 170 ----RVLILDEPT 178
Cdd:NF033858 413 ihkpELLILDEPT 425
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
267-463 |
4.36e-05 |
|
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: 45.95 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERLSRG----DAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADA--ADGGTV-----------------SIGD 323
Cdd:TIGR03269 1 IEVKNLTKKfdgkEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 324 P---------PRPAAIRSPADAVRHGI------------ALVSEDRkgeglLLPQSIAANLSLGQLARVARGGVVDGERE 382
Cdd:TIGR03269 81 PcpvcggtlePEEVDFWNLSDKLRRRIrkriaimlqrtfALYGDDT-----VLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 383 NALAARQIDALRirargpaqpvaELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID-VGAKFDIYALLDALAREGRAIVV 461
Cdd:TIGR03269 156 VQLSHRITHIAR-----------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKASGISMVL 224
|
..
gi 490656625 462 VS 463
Cdd:TIGR03269 225 TS 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
257-486 |
4.92e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 257 HGTRTPGAPRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAG--RTELLRLVYGADAADggtvsigDPPRPAAIRSPA 334
Cdd:NF000106 8 NGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR-------RPWRF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 335 DAVRHGIALVSEDRKGEglllPQSIAANLSLGQLARVarggvVDGERENALAarQIDALRIR---ARGPAQPVAELSGGN 411
Cdd:NF000106 81 RALRRTIG*HRPVR*GR----RESFSGRENLYMIGR*-----LDLSRKDARA--RADELLERfslTEAAGRAAAKYSGGM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656625 412 QQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHA 486
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-229 |
6.67e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 44.76 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALGVRMVM--QELNLVPTLT 104
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMlfQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 105 VAENLFL-----DRLPhrfgvidRRRLAADARAAMARVGLD---SLDPDTLVGslgiGHQQMVEIARSLAGDCRVLILDE 176
Cdd:PRK11831 101 VFDNVAYplrehTQLP-------APLLHSTVMMKLEAVGLRgaaKLMPSELSG----GMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 177 PTAMLTAREVELLFDQIARL-KADGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
406-482 |
6.82e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.01 E-value: 6.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAG 482
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-88 |
9.02e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.96 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 6 PDSTPDTPTLVVTGIGKTYAEP--VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRA 83
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNgfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393
|
....*
gi 490656625 84 HAEAL 88
Cdd:PRK10522 394 DYRKL 398
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
265-484 |
9.81e-05 |
|
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: 43.41 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLSRGDAVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADG---GTVSIGD-PPRPAAIRSPADavrhg 340
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGiPYKEFAEKYPGE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 341 IALVSEDrkgeglllpQSIAANLSLGQLARVArggvvdgerenalaarqidalrIRARGpAQPVAELSGGNQQKVAIGRW 420
Cdd:cd03233 85 IIYVSEE---------DVHFPTLTVRETLDFA----------------------LRCKG-NEFVRGISGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 421 LGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVS----SDlrELMLICDRIGVMSAGRM 484
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaSD--EIYDLFDKVLVLYEGRQ 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
284-439 |
1.05e-04 |
|
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: 43.94 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 284 DVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVsigdpprpaairspadavrhGIALVSEDRKgeglllPQSIAANL 363
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------------------EIELDTVSYK------PQYIKADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 364 SL---GQLARVARGGVVDGERENALA-ARQIDALRirargpAQPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDV 439
Cdd:cd03237 75 EGtvrDLLSSITKDFYTHPYFKTEIAkPLQIEQIL------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
279-483 |
1.25e-04 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 43.23 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspadavrhGIALVSEdrkgEGLLLPQS 358
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------------SIAYVSQ----EPWIQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 359 IAANLSLGQlarvarggVVDGER-ENALAARQIDA-LRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDE 432
Cdd:cd03250 82 IRENILFGK--------PFDEERyEKVIKACALEPdLEILPDGDLTEIGEkginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 433 PTRGID--VGAK-FDiYALLDALaREGRAIVVVSSDLrELMLICDRIGVMSAGR 483
Cdd:cd03250 154 PLSAVDahVGRHiFE-NCILGLL-LNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-72 |
1.30e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 17 VTGIGKTYAEPVL-DDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRL 72
Cdd:PRK11819 327 AENLSKSFGDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-229 |
1.38e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV----APTTGAMRLAGAEY---APHSRAHAEALGVRMVMQE--LNL 99
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLqriSEKERRNLVGAEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAENLFLDRLPHRFGviDRRRLAADARAAMARVGLDslDP----DTLVGSLGIGHQQMVEIARSLAGDCRVLILD 175
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVGIP--DPasrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 176 EPTAML----TAREVELLFDQIARlkaDGVALVYISHRLEELARVAQRVAVLRDGRLV 229
Cdd:PRK11022 179 EPTTALdvtiQAQIIELLLELQQK---ENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
402-478 |
1.46e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGV 478
Cdd:PRK13409 449 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
265-466 |
1.47e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 42.94 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 265 PRLRVERLS--RGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRSPADAVRH 339
Cdd:PRK13539 1 MMLEGEDLAcvRGGRVlfSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 340 GIALvsedrKGEglllpQSIAANLSLgqLARVARGGvvDGERENALAARQIDALRIRargpaqPVAELSGGNQQKVAIGR 419
Cdd:PRK13539 81 RNAM-----KPA-----LTVAENLEF--WAAFLGGE--ELDIAAALEAVGLAPLAHL------PFGYLSAGQKRRVALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490656625 420 WLGRDMGVLLFDEPTRGIDVGAKFDIYALLDA-LAREGRAIVVVSSDL 466
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHIPL 188
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
277-491 |
1.61e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.59 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDppRPAAIRSPADAVRH-GIALVSEDRKGEGLLL 355
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--QAITDDNFEKLRKHiGIVFQNPDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 356 PQSIAANLslgqlarvaRGGVVDGERENALAARQIDALRIRARGPAQPVAeLSGGNQQKVAIGRWLGRDMGVLLFDEPTR 435
Cdd:PRK13648 102 KYDVAFGL---------ENHAVPYDEMHRRVSEALKQVDMLERADYEPNA-LSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 436 GIDVGAKFDIYALLDALAREGR-AIVVVSSDLRELMLiCDRIGVMSAGRmhaVFERG 491
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGT---VYKEG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
150-241 |
1.62e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.62 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 150 SLGIGHQQMVEIARSLAGDCRVLILDEPTAML---TAREVELLFDQIARlkadGVALVYISHRLEELARVAQRVAVL--- 223
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALdpiSTLRIEELMHELKE----QYTIIIVTHNMQQAARVSDMTAFFnve 226
|
90 100
....*....|....*....|....*..
gi 490656625 224 ------RDGRLVHVDR---IDAQPTER 241
Cdd:PRK14243 227 ltegggRYGYLVEFDRtekIFNSPQQQ 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
281-475 |
1.87e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.84 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPRPAAIRSPADAVRhgialvsedRKGEGLLLpQSIA 360
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR---------AKHVGFVF-QSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 361 ANLSLGQLARVARGGVVDGERENALAARQIDALRIRARG------PAQpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:PRK10584 99 LIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGkrldhlPAQ----LSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490656625 435 RGIDVGAKFDIYALLDALARE-GRAIVVVSSDLReLMLICDR 475
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQ-LAARCDR 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
288-483 |
1.94e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 288 GEIFGISGLIGAGRTELLRLVYGADAADG--GTVSIGD--PPRPAAIRS----------PADAVRHGIALVSEDR----- 348
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkPTKQILKRTgfvtqddilyPHLTVRETLVFCSLLRlpksl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 349 -KGEGLLLPQSIAANLSLGQLarvarggvvdgerENALAARQIdalrIRArgpaqpvaeLSGGNQQKVAIGRWLGRDMGV 427
Cdd:PLN03211 174 tKQEKILVAESVISELGLTKC-------------ENTIIGNSF----IRG---------ISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVV----SSDLRELMlicDRIGVMSAGR 483
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmhqpSSRVYQMF---DSVLVLSEGR 284
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
406-478 |
2.04e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.17 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREG-RAIVVVSSDLRELMLICDRIGV 478
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
240-501 |
2.38e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.94 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 240 ERLVALMAGREiaEQAVHGTRTPGAPRLRVERLS---RGD--AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAA 314
Cdd:PRK10790 316 ERVFELMDGPR--QQYGNDDRPLQSGRIDIDNVSfayRDDnlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 315 DGGTVSIGDppRPAAIRSPAdAVRHGIALVSEDRkgegLLLPQSIAANLSLGQlaRVARGGVVDgerenALAARQIDAL- 393
Cdd:PRK10790 394 TEGEIRLDG--RPLSSLSHS-VLRQGVAMVQQDP----VVLADTFLANVTLGR--DISEEQVWQ-----ALETVQLAELa 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 394 RIRARGPAQPVAE----LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLdALAREGRAIVVVSSDLREL 469
Cdd:PRK10790 460 RSLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVVIAHRLSTI 538
|
250 260 270
....*....|....*....|....*....|..
gi 490656625 470 mLICDRIGVMSAGRmhaVFERGgwTQDALLGA 501
Cdd:PRK10790 539 -VEADTILVLHRGQ---AVEQG--THQQLLAA 564
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
407-484 |
2.50e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.16 E-value: 2.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490656625 407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALArEGRAIVVVSSDLRELMLICDRIGVMSAGRM 484
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-75 |
3.13e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 3.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490656625 29 LDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGA 75
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS 86
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-181 |
3.52e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 6 PDSTPDTPTLVV-TGIGKTYAEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAM----RLAgaeYAPh 80
Cdd:PRK13409 331 PRDESERETLVEyPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKIS---YKP- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 81 srahaealgvrmvmQELNLVPTLTVAEnlFLDRLPHRFG-------VIDrrrlaadaraamaRVGLDSLdPDTLVGSLGI 153
Cdd:PRK13409 407 --------------QYIKPDYDGTVED--LLRSITDDLGssyykseIIK-------------PLQLERL-LDKNVKDLSG 456
|
170 180
....*....|....*....|....*...
gi 490656625 154 GHQQMVEIARSLAGDCRVLILDEPTAML 181
Cdd:PRK13409 457 GELQRVAIAACLSRDADLYLLDEPSAHL 484
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
267-464 |
4.49e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.71 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 267 LRVERL--SRGDAV--RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPPrpaaIRSPADAVR---- 338
Cdd:PRK13538 2 LEARNLacERDERIlfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP----IRRQRDEYHqdll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 339 ---HGIALVSEDRKGEGLLLPQSIAANLSLGQ----LARVARGGvvdgeRENAlaarqidalrirargpaqPVAELSGGN 411
Cdd:PRK13538 78 ylgHQPGIKTELTALENLRFYQRLHGPGDDEAlweaLAQVGLAG-----FEDV------------------PVRQLSAGQ 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656625 412 QQKVAIGR-WLGRDMGVLLfDEPTRGIDVGAKFDIYALLDALAREGrAIVVVSS 464
Cdd:PRK13538 135 QRRVALARlWLTRAPLWIL-DEPFTAIDKQGVARLEALLAQHAEQG-GMVILTT 186
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
406-483 |
5.16e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 5.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAR-EGRAIVVVSSDLRELMLICDRIGVMSAGR 483
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
277-484 |
6.27e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.00 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaaiRSPadavrhgialvSEDRKgeglllp 356
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-------YVP-----------FKRRK------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 357 qsiaanlslgQLARvaRGGVVDGERENA---LAAR----------QIDALRIRAR----------GP--AQPVAELSggn 411
Cdd:COG4586 92 ----------EFAR--RIGVVFGQRSQLwwdLPAIdsfrllkaiyRIPDAEYKKRldelvelldlGEllDTPVRQLS--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 412 qqkvaigrwLGRDM------------GVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVVSS-DLRELMLICDRIGV 478
Cdd:COG4586 157 ---------LGQRMrcelaaallhrpKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTShDMDDIEALCDRVIV 227
|
....*.
gi 490656625 479 MSAGRM 484
Cdd:COG4586 228 IDHGRI 233
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
369-498 |
6.72e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 369 ARVARGGVVDGERENALAAR-QIDALRIRargpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYA 447
Cdd:PRK10938 103 AEIIQDEVKDPARCEQLAQQfGITALLDR------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490656625 448 LLDALAREGRAIVVVSSDLRELMLICDRIGVMSAGRMHAVFERGGWTQDAL 498
Cdd:PRK10938 177 LLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQAL 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
280-469 |
6.87e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 41.24 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDPP----RPAAIR--------SPA---DAVRHGIALV 344
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDistlKPEIYRqqvsycaqTPTlfgDTVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 345 SEDRKGEglLLPQSIAANLSLGQLArvarggvvdgerENALAarqidalrirargpaQPVAELSGGNQQKVAIGRWLGRD 424
Cdd:PRK10247 105 WQIRNQQ--PDPAIFLDDLERFALP------------DTILT---------------KNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490656625 425 MGVLLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLREL 469
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEI 201
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
406-517 |
7.52e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.65 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 406 ELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAR-EGRAIVVVSSDLRELMLICDRIGVMSA--- 481
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAgqv 232
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490656625 482 ---GRMHAVFE--RGGWTQdALLGA--AFAGYARRDAALhpPG 517
Cdd:PRK11022 233 vetGKAHDIFRapRHPYTQ-ALLRAlpEFAQDKARLASL--PG 272
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
277-321 |
9.07e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 9.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490656625 277 AVRDVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI 321
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
280-438 |
1.04e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 41.24 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 280 DVSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSI-GDPPRPAAIRspadavRHGIALVSEDRKgeglLLPQ- 357
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSIQ------QRDICMVFQSYA----LFPHm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 358 SIAANLSLG-QLARVARGGVVDGEREnALAARQIDALRIRArgpaqpVAELSGGNQQKVAIGRWLGRDMGVLLFDEPTRG 436
Cdd:PRK11432 94 SLGENVGYGlKMLGVPKEERKQRVKE-ALELVDLAGFEDRY------VDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
..
gi 490656625 437 ID 438
Cdd:PRK11432 167 LD 168
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
30-211 |
1.11e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 30 DDVSLalyPGEAL-ALTGENGAGKSTLskIVAGLVAptTGAMRLAGaeyaphsrahaealgvrmvmqelnLVPTLTVAEN 108
Cdd:cd03238 14 LDVSI---PLNVLvVVTGVSGSGKSTL--VNEGLYA--SGKARLIS------------------------FLPKFSRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 109 LFLDRLphRFgVIDrrrlaadaraamarVGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCR--VLILDEPTAMLTAREV 186
Cdd:cd03238 63 IFIDQL--QF-LID--------------VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180
....*....|....*....|....*
gi 490656625 187 ELLFDQIARLKADGVALVYISHRLE 211
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-215 |
1.17e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656625 145 DTLVG----SLGIGHQQMVEIARSLAGDCRVLILDEPTAMLTAREVELLFDQIARL--KADGvALVYISHRLEELAR 215
Cdd:PTZ00265 1349 DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADK-TIITIAHRIASIKR 1424
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-211 |
1.34e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.33 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLV--APTTGAMRLAGAEYaPHSRAHAEALGVRM----VMQELNL 99
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF-GREASLIDAIGRKGdfkdAVELLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 100 VPTLTVAenLFLDRLPHrfgvidrrrlaadaraamarvgldsldpdtlvgsLGIGHQQMVEIARSLAGDCRVLILDEPTA 179
Cdd:COG2401 122 VGLSDAV--LWLRRFKE----------------------------------LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|....*
gi 490656625 180 ML---TAREVELLFDQIARLKadGVALVYISHRLE 211
Cdd:COG2401 166 HLdrqTAKRVARNLQKLARRA--GITLVVATHHYD 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-226 |
1.61e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 26 EPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAP--TTGAMRLAGAEYAPhsrahaealgvrmvmqELNLVPTL 103
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRGSVAYVP----------------QVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFL--DRLPHRFG-VIDRRRLAADARAAMarvGLDSldpdTLVGSLGI----GHQQMVEIARSLAGDCRVLILDE 176
Cdd:PLN03232 694 TVRENILFgsDFESERYWrAIDVTALQHDLDLLP---GRDL----TEIGERGVnisgGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490656625 177 PTAMLTAREVELLFDQIARLKADGVALVYISHRLEELARVaQRVAVLRDG 226
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-220 |
3.14e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 137 VGLDSLDPDTLVGSLGIGHQQMVEIARSLAGDCR--VLILDEPTAMLTAREVELLFDQIARLKADGVALVYISHRlEELA 214
Cdd:PRK00635 463 LGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMI 541
|
....*.
gi 490656625 215 RVAQRV 220
Cdd:PRK00635 542 SLADRI 547
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-184 |
3.38e-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: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 28 VLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVapTTGAM----RLAGAeyapHSRAHAEALGVRMVMQELNLVPTL 103
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVItggdRLVNG----RPLDSSFQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENL----FLdRLPHRFG----------VIDrrrlaadaraamaRVGLDSLdPDTLVGSLGIG----HQQMVEIARSL 165
Cdd:TIGR00956 852 TVRESLrfsaYL-RQPKSVSksekmeyveeVIK-------------LLEMESY-ADAVVGVPGEGlnveQRKRLTIGVEL 916
|
170 180
....*....|....*....|
gi 490656625 166 AGDCRVLI-LDEPTAMLTAR 184
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQ 936
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
281-508 |
3.54e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 281 VSFDVRAGEIFGISGLIGAGRTELLRLVYGADAADGGTVSIGDpprpaairspADAVRHGIAlvsEDRKGEGLLlPQSia 360
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG----------CDISKFGLM---DLRKVLGII-PQA-- 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 361 anlslgqlaRVARGGVV-----------DGERENALA-ARQIDALRIRARGPAQPVAE----LSGGNQQKVAIGRWLGRD 424
Cdd:PLN03130 1322 ---------PVLFSGTVrfnldpfnehnDADLWESLErAHLKDVIRRNSLGLDAEVSEagenFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 425 MGVLLFDEPTRGIDVGAkfdiyallDALaregraivvVSSDLRE-----LMLI----------CDRIGVMSAGRmhaVFE 489
Cdd:PLN03130 1393 SKILVLDEATAAVDVRT--------DAL---------IQKTIREefkscTMLIiahrlntiidCDRILVLDAGR---VVE 1452
|
250 260
....*....|....*....|..
gi 490656625 490 RGgwTQDALL---GAAFAGYAR 508
Cdd:PLN03130 1453 FD--TPENLLsneGSAFSKMVQ 1472
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-226 |
3.74e-03 |
|
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: 38.85 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEYAPHSRAHAEALG---VRMVMQELNLVpTL 103
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 104 TVAENLFLDRlP---HRF-GVIDRRrlaadaraamarvgldSLDPD---------TLVGSLGI----GHQQMVEIARSLA 166
Cdd:cd03290 94 TVEENITFGS-PfnkQRYkAVTDAC----------------SLQPDidllpfgdqTEIGERGInlsgGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656625 167 GDCRVLILDEPTAMLTAREVELLFDQ--IARLKADGVALVYISHRLEELARvAQRVAVLRDG 226
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
407-466 |
3.85e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 40.09 E-value: 3.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKfdiYALLDALAREGRAIVVVSSDL 466
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECE---QLLQESRSRASRTVLLIAHRL 674
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
27-95 |
4.09e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 4.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656625 27 PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGL--VAPTTGAMRLAGA---EYAPHSRAhaeALGVRMVMQ 95
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllELSPEDRA---GEGIFMAFQ 85
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-464 |
4.19e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 39.05 E-value: 4.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 405 AELSGGNQQKVAIGRWLGRDMGVLLFDEPTRGID-VGAKfDIYALLDALAREGRAIVVVSS 464
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpVGTA-KIEELLFELKKEYTIVLVTHS 207
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
400-476 |
4.94e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 400 PAQPVAELSGGNQQKVAIGRWLGRD-MGVL-LFDEPTRGIDvgaKFDIYALLDALAR---EGRAIVVVSSDlrELML-IC 473
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAElIGITyILDEPSIGLH---PQDTHKLINVIKKlrdQGNTVLLVEHD--EQMIsLA 544
|
...
gi 490656625 474 DRI 476
Cdd:PRK00635 545 DRI 547
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
407-501 |
5.21e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 407 LSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGA-KFDIYALLDALAREGRAIVVVSSDLRELMLiCDRIGVMSAGRMH 485
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDRT 1437
|
90
....*....|....*.
gi 490656625 486 AVFERGGWTQDALLGA 501
Cdd:PTZ00265 1438 GSFVQAHGTHEELLSV 1453
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-61 |
5.29e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.23 E-value: 5.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490656625 10 PDTPTLVVTGIGKTYAE-PVLDDVSLALYPGEALALTGENGAGKSTLSKIVAG 61
Cdd:PRK10938 256 ANEPRIVLNNGVVSYNDrPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
402-467 |
5.65e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.07 E-value: 5.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490656625 402 QPVAELSGGNQQKVAIGRWLGRDMG--VLLFDEPTRGIDvgaKFDIYALLDALAR---EGRAIVVVSSDLR 467
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDINQLLEVIKGlidLGNTVILIEHNLD 150
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-68 |
5.73e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 5.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 490656625 25 AEPVLDDVSLALYPGEALALTGENGAGKSTLSKIVAGLVAPTTG 68
Cdd:PRK15064 13 AKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAG 56
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
278-490 |
8.17e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.14 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 278 VRDVSFDVRAGEIFGISGLIGAGRT----ELLRLVYGADAADGGTVSI-GDPPRPAAIRSpadavRHGIALVSEDRKGEG 352
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLdGKPVAPCALRG-----RKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 353 LLlpQSIAAN-----LSLGQLARVARggVVDGERENALAarqiDALRIRARGPaqpvAELSGGNQQKVAIGRWLGRDMGV 427
Cdd:PRK10418 94 PL--HTMHTHaretcLALGKPADDAT--LTAALEAVGLE----NAARVLKLYP----FEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 428 LLFDEPTRGIDVGAKFDIYALLDALARE-GRAIVVVSSDLRELMLICDRIGVMSAGRM------HAVFER 490
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIveqgdvETLFNA 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-235 |
8.40e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 36.97 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 38 PGEALALTGENGAGKSTLSKIVAGLVAPTTGAMRLAGAEyaphsrahaealgvrmvmqelnlvptltvaenlfldrlphr 117
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 118 fgvidrrrlaadarAAMARVGLDSLDPDTLVGSLGIGHQQMVEIARSLA--GDCRVLILDEPTAMLTAREVELLFDQIA- 194
Cdd:smart00382 40 --------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLLLEEl 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490656625 195 -----RLKADGVALVYISHRLEELARvaqRVAVLRDGRLVHVDRID 235
Cdd:smart00382 106 rllllLKSEKNLTVILTTNDEKDLGP---ALLRRRFDRRIVLLLIL 148
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
390-477 |
8.46e-03 |
|
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: 37.61 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 390 IDALRIRA--RGpaqpvaeLSGGNQQKVAIGRWLGRDMGVLLFDEPTRGIDVGAKFDIYALLDALAREGRAIVVV----S 463
Cdd:cd03232 97 REALRFSAllRG-------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTihqpS 169
|
90
....*....|....*..
gi 490656625 464 SDLREL---MLICDRIG 477
Cdd:cd03232 170 ASIFEKfdrLLLLKRGG 186
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
279-463 |
1.00e-02 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 37.63 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 279 RDVSFDVRAGEIFGISGLIGAGRTELLRLVYGA--DAADGGTVSIGD--PPRPAAIrspADAVrhgialvseDRKGEgll 354
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDnqFGREASL---IDAI---------GRKGD--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656625 355 lpqsiaANLSLGQLARVARGgvvdgerenalaarqiDALRIRArgpaqPVAELSGGNQQKVAIGRWLGRDMGVLLFDEPT 434
Cdd:COG2401 112 ------FKDAVELLNAVGLS----------------DAVLWLR-----RFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|
gi 490656625 435 RGID-VGAKFDIYALLDALAREGRAIVVVS 463
Cdd:COG2401 165 SHLDrQTAKRVARNLQKLARRAGITLVVAT 194
|
|
|