|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-511 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 741.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILI 98
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEQLSVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 179 DEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRDIKQM 258
Cdd:COG1129 165 DEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRELEDL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 259 FPHRvSDTSAPIVLSVRDLSVPGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQD 338
Cdd:COG1129 245 FPKR-AAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 339 AKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKFGS-VIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKL 417
Cdd:COG1129 324 AIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRgGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 418 LLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGILEGNDRNE 497
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATE 483
|
490
....*....|....
gi 494149220 498 HEIMRHATGISGQE 511
Cdd:COG1129 484 EAIMAAATGGAAAA 497
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-510 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 518.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 14 EGKIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH 93
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 GVILIHQELNLAEQLSVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKA 173
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 174 DILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGR 253
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 254 DIKQMFPHRVSDTSAPiVLSVRDLSVPGQ-----VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDG 328
Cdd:COG3845 241 EVLLRVEKAPAEPGEV-VLEVENLSVRDDrgvpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 329 KPVRIASLQDAKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLAL--EKFGS-VIVDRKAEEAALEKAIEAFDIRAADRKAK 405
Cdd:COG3845 320 EDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYrrPPFSRgGFLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 406 VGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGR 485
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
490 500
....*....|....*....|....*
gi 494149220 486 ITGILEGNDRNEHEIMRHATGISGQ 510
Cdd:COG3845 480 IVGEVPAAEATREEIGLLMAGVKEE 504
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-506 |
4.68e-178 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 510.24 E-value: 4.68e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSG-Y-HEPTEGGLVLDGAEVSFADSEAGEGHGVILIH 99
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYpHGTYEGEIIFEGEELQASNIRDTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 100 QELNLAEQLSVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILD 179
Cdd:PRK13549 89 QELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 180 EPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRDIKQMF 259
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGRELTALY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 260 PHRVSDTSApIVLSVRDLSV-----PG--QVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRE-RSSGTIERDGKPV 331
Cdd:PRK13549 249 PREPHTIGE-VILEVRNLTAwdpvnPHikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 332 RIASLQDAKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKF--GSVIvDRKAEEAALEKAIEAFDIRAADRKAKVGDF 409
Cdd:PRK13549 328 KIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFtgGSRI-DDAAELKTILESIQRLKVKTASPELAIARL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 410 SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGI 489
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
490
....*....|....*..
gi 494149220 490 LEGNDRNEHEIMRHATG 506
Cdd:PRK13549 487 LINHNLTQEQVMEAALR 503
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-506 |
7.45e-167 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 481.43 E-value: 7.45e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVI 96
Cdd:PRK10762 5 LQLKG--IDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 LIHQELNLAEQLSVEENIFLGREIKRGW-FLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADI 175
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFVNRFgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 176 LILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRDI 255
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 256 KQMFPhRVSDTSAPIVLSVRDLSVPGqVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIAS 335
Cdd:PRK10762 243 EDQYP-RLDKAPGEVRLKVDNLSGPG-VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 336 LQDAKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKF--GSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGN 413
Cdd:PRK10762 321 PQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFsrAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 414 QQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGILEGN 493
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
490
....*....|...
gi 494149220 494 DRNEHEIMRHATG 506
Cdd:PRK10762 481 QATQEKLMAAAVG 493
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-503 |
1.45e-166 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 480.83 E-value: 1.45e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHePT---EGGLVLDGAEVSFADSEAGEGHGVILI 98
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEQLSVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:NF040905 84 HQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 179 DEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVV--DLSKDDMARLMVGRDIK 256
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRadEVTEDRIIRGMVGRDLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 257 QMFPHRVSDTsAPIVLSVRDLSV--PGQ-----VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGlreRS-----SGTI 324
Cdd:NF040905 244 DRYPERTPKI-GEVVFEVKNWTVyhPLHperkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG---RSygrniSGTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 325 ERDGKPVRIASLQDAKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKFGSV-IVDRKAEEAALEKAIEAFDIRAADRK 403
Cdd:NF040905 320 FKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRgVIDENEEIKVAEEYRKKMNIKTPSVF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 404 AKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAA 483
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNE 479
|
490 500
....*....|....*....|
gi 494149220 484 GRITGILEGNDRNEHEIMRH 503
Cdd:NF040905 480 GRITGELPREEASQERIMRL 499
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-504 |
4.00e-162 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 469.39 E-value: 4.00e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILI 98
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEQLSVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 179 DEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEP-VVDLSKDDMARLMVGRDIKQ 257
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdMAQVDRDQLVQAMVGREIGD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 258 MFPHRvSDTSAPIVLSVRDLSVPGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQ 337
Cdd:PRK11288 245 IYGYR-PRPLGEVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 338 DAKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKF--GSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQ 415
Cdd:PRK11288 324 DAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHlrAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 416 KLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGILEGNDR 495
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQA 483
|
....*....
gi 494149220 496 NEHEIMRHA 504
Cdd:PRK11288 484 TERQALSLA 492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-505 |
1.13e-153 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 447.64 E-value: 1.13e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 24 ICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQELN 103
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQLSVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTA 183
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 184 VLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRDIKQMFPHRv 263
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFPDK- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 264 SDTSAPIVLSVRDLSVPGQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKN 341
Cdd:PRK10982 243 ENKPGEVILEVRNLTSLRQpsIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 342 SGIAYLTKDRKGSGLLLNMDMRPNlTLLA-----LEKFGsvIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQK 416
Cdd:PRK10982 323 HGFALVTEERRSTGIYAYLDIGFN-SLISnirnyKNKVG--LLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 417 LLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGILEGNDRN 496
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTT 479
|
....*....
gi 494149220 497 EHEIMRHAT 505
Cdd:PRK10982 480 QNEILRLAS 488
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-505 |
1.59e-152 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 445.38 E-value: 1.59e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 23 KICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQEL 102
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 NLAEQLSVEENIFLGREIKRGWF----LDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:PRK09700 90 SVIDELTVLENLYIGRHLTKKVCgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 179 DEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRDIKQM 258
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRELQNR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 259 FP---HRVSDTSAPIVLSVRDLSV--PGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRI 333
Cdd:PRK09700 250 FNamkENVSNLAHETVFEVRNVTSrdRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 334 ASLQDAKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKFGSV-----IVDRKAEEAALEKAIEAFDIRAADRKAKVGD 408
Cdd:PRK09700 330 RSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYkgamgLFHEVDEQRTAENQRELLALKCHSVNQNITE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 409 FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITG 488
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
490
....*....|....*...
gi 494149220 489 ILEGNDR-NEHEIMRHAT 505
Cdd:PRK09700 490 ILTNRDDmSEEEIMAWAL 507
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-504 |
1.14e-139 |
|
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: 412.30 E-value: 1.14e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGY--HEPTEGGLVLDGAEVSFADSEAGEGHGVI 96
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 LIHQELNLAEQLSVEENIFLGREIK-RGWFLDKTAMRAEAKRLLDQLQCDVDPRTR-IRDLSVSDRQMVEIAKALSKKAD 174
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITlPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 175 ILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRD 254
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 255 IKQMFPHRVSDTsAPIVLSVRDLSV-------PGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRE-RSSGTIER 326
Cdd:TIGR02633 242 ITSLYPHEPHEI-GDVILEARNLTCwdvinphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 327 DGKPVRIASLQDAKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKF-GSVIVDRKAEEAALEKAIEAFDIRAADRKAK 405
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFcFKMRIDAAAELQIIGSAIQRLKVKTASPFLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 406 VGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGR 485
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
490
....*....|....*....
gi 494149220 486 ITGILEGNDRNEHEIMRHA 504
Cdd:TIGR02633 481 LKGDFVNHALTQEQVLAAA 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-514 |
4.94e-131 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 390.57 E-value: 4.94e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 12 GTEGKIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGE 91
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 92 GHGVILIHQELNLAEQLSVEENIFLGreikrgwfLDKTAMRAE-AKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALS 170
Cdd:PRK15439 85 QLGIYLVPQEPLLFPNLSVKENILFG--------LPKRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 171 KKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLM 250
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 251 VGRDIKQ----------MFP--HRVSDTSAPiVLSVRDLSVPGqVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRE 318
Cdd:PRK15439 237 TPAAREKslsasqklwlELPgnRRQQAAGAP-VLTVEDLTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 319 RSSGTIERDGKPVRIASLQDAKNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKFGSVIvDRKAEEAALEKAIEAFDIR 398
Cdd:PRK15439 315 ARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCALTHNRRGFWI-KPARENAVLERYRRALNIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 399 AADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRI 478
Cdd:PRK15439 394 FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRV 473
|
490 500 510
....*....|....*....|....*....|....*.
gi 494149220 479 AVMAAGRITGILEGNDRNEHEIMRHATGISGQEGVS 514
Cdd:PRK15439 474 LVMHQGEISGALTGAAINVDTIMRLAFGEHQAQEAS 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
268-486 |
4.57e-78 |
|
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: 242.34 E-value: 4.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 268 APIVLSVRDLSVPGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAYL 347
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 TKDRKGSGLLLNMDMRPNLTLLALekfgsvivdrkaeeaalekaieafdiraadrkakvgdFSGGNQQKLLLAKVMETDP 427
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-235 |
1.22e-73 |
|
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: 230.39 E-value: 1.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVI 96
Cdd:cd03216 1 LELRG--ITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 LIHQelnlaeqlsveeniflgreikrgwfldktamraeakrlldqlqcdvdprtrirdLSVSDRQMVEIAKALSKKADIL 176
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 177 ILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVT 235
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
29-486 |
1.36e-63 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 215.54 E-value: 1.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPT---EGGLVLDGAEVSfADSEAGEGHGVILIHQE---- 101
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL-ELSEALRGRRIGMVFQDpmtq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLaeqLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:COG1123 96 LNP---VTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 182 TAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRDIKQMFP 260
Cdd:COG1123 170 TTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 261 HRVSDTSAPIVLSVRDLSV------PGQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV 331
Cdd:COG1123 250 AAPAAAAAEPLLEVRNLSKrypvrgKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 332 RIASLQDAKN--SGIAYLTKDRKGSgllLNmdmrPNLTLL-----ALEKFGsvIVDRKAEEAALEKAIEAFDIRAADRKA 404
Cdd:COG1123 330 TKLSRRSLRElrRRVQMVFQDPYSS---LN----PRMTVGdiiaePLRLHG--LLSRAERRERVAELLERVGLPPDLADR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 405 KVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAA 483
Cdd:COG1123 401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYD 480
|
...
gi 494149220 484 GRI 486
Cdd:COG1123 481 GRI 483
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-235 |
3.89e-46 |
|
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: 161.07 E-value: 3.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILI 98
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEQLSVEENIFLGREIKRG-------WFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSK 171
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGsglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 172 KADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVT 235
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-241 |
7.57e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 7.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILihQE 101
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP--QE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:COG1131 82 PALYPDLTVRENLRFFARLYG---LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 182 TA---VLTGREVeilFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:COG1131 159 TSgldPEARREL---WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-233 |
1.54e-43 |
|
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: 154.81 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILI 98
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEQLSVEENIFLGREIKRG------------WFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIA 166
Cdd:COG0411 85 FQNPRLFPELTVLENVLVAAHARLGrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 167 KALSKKADILILDEPTAVLTGREVEILFDQIRRLR-EQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
26-259 |
1.42e-39 |
|
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: 143.84 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVilIHQELNLA 105
Cdd:COG4555 9 KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV--LPDERGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 106 EQLSVEENIflgREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:COG4555 87 DRLTVRENI---RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 186 TGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRhivtePVVDLSKDDMARLMVGRDIKQMF 259
Cdd:COG4555 164 DVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK-----VVAQGSLDELREEIGEENLEDAF 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
22-231 |
3.30e-38 |
|
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: 137.53 E-value: 3.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVilIHQE 101
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY--LPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIflgreikrgwfldktamraeakrlldqlqcdvdprtrirDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:cd03230 82 PSLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 182 TAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-231 |
6.57e-38 |
|
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: 138.72 E-value: 6.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILI 98
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEQLSVEENIFLGREIKRgwfldktamRAEAKRLLDQLqCDVDPRTRIR------DLSVSDRQMVEIAKALSKK 172
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARR---------RAKRKARLERV-YELFPRLKERrkqlagTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 173 ADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
34-183 |
2.60e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.00 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgEGHGVILIHQELNLAEQLSVEEN 113
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS-LRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 114 IFLGREIKrgwFLDKTAMRAEAKRLLDQLQCDVDPRTRIRD----LSVSDRQMVEIAKALSKKADILILDEPTA 183
Cdd:pfam00005 80 LRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-486 |
2.42e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 138.66 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKS----TLVKILSGYHEPTEGGLVLDGAEVsFADSEAG----EGHGVILIHQ 100
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-LGLSERElrriRGNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 101 E----LN-LaeqLSVEENIFLGREIKRGwfLDKTAMRAEAKRLLDQLQCDvDPRTRIRD----LSVSDRQMVEIAKALSK 171
Cdd:COG4172 100 EpmtsLNpL---HTIGKQIAEVLRLHRG--LSGAAARARALELLERVGIP-DPERRLDAyphqLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 172 KADILILDEPTAVLtgrEV----EILfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRhIV-TEPVVDL---- 241
Cdd:COG4172 174 EPDLLIADEPTTAL---DVtvqaQIL-DLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGE-IVeQGPTAELfaap 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 242 ----SKDDMARLMVGRdikqmfpHRVSDTSAPIVLSVRDLSV--PGQ-------------VRDASFDLHKGEVLGFAGIV 302
Cdd:COG4172 249 qhpyTRKLLAAEPRGD-------PRPVPPDAPPLLEARDLKVwfPIKrglfrrtvghvkaVDGVSLTLRRGETLGLVGES 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 303 GAGRTALMEAIIGLrERSSGTIERDGKPvrIASLQDAKnsgiayLTKDRK----------GSgllLNmdmrPNLT----- 367
Cdd:COG4172 322 GSGKSTLGLALLRL-IPSEGEIRFDGQD--LDGLSRRA------LRPLRRrmqvvfqdpfGS---LS----PRMTvgqii 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 368 ---LLALEkfgsVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTK 444
Cdd:COG4172 386 aegLRVHG----PGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQ 461
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 494149220 445 SQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG4172 462 AQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
29-245 |
1.42e-34 |
|
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: 129.72 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQELNLAEQL 108
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGREIKRGwfldktamRAEAKRLLDQLqCDVDPR--TRIR----DLSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:COG0410 94 TVEENLLLGAYARRD--------RAEVRADLERV-YELFPRlkERRRqragTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 183 AVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDD 245
Cdd:COG0410 165 LGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
283-486 |
5.16e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.26 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNsgIAYLTKDrkgSGLLLNMDM 362
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYVPQE---PALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLAlEKFGsviVDRKAEEAALEKAIEAFDIRAAdRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIG 442
Cdd:COG1131 91 RENLRFFA-RLYG---LPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 443 TKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG1131 166 ARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
24-231 |
3.60e-33 |
|
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: 125.32 E-value: 3.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 24 ICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGeghGVILIHQELN 103
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTA 183
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRG---VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 184 VLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
18-233 |
4.87e-33 |
|
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: 126.31 E-value: 4.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 18 RLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS------FADSEAge 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAslsrreLARRIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 92 ghgviLIHQELNLAEQLSVEENIFLGREIKRGWF--------------LDKTAMRAEAKRLLDQLqcdvdprtrirdlsv 157
Cdd:COG1120 79 -----YVPQEPPAPFGLTVRELVALGRYPHLGLFgrpsaedreaveeaLERTGLEHLADRPVDEL--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 158 SD--RQMVEIAKALSKKADILILDEPTAVL-TGREVEILfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:COG1120 139 SGgeRQRVLIARALAQEPPLLLLDEPTSHLdLAHQLEVL-ELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-231 |
1.16e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 124.39 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFG----PAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS-FADSEAGE-- 91
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISsLSERELARlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 92 GHGVILIHQELNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLqcDVDPRT--RIRDLSVSDRQMVEIAKAL 169
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERV--GLGDRLdhRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 170 SKKADILILDEPTAVL---TGREVeilFDQIRRL-REQGVAILYISHklD-EIKAIADRVTVLRDGR 231
Cdd:COG1136 160 VNRPKLILADEPTGNLdskTGEEV---LELLRELnRELGTTIVMVTH--DpELAARADRVIRLRDGR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
32-231 |
2.42e-32 |
|
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: 123.60 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQelNLAEQL--- 108
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQ--NPDDQLfap 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGREiKRGwfLDKTAMRAEAKRLLDQLQCDvDPRTR-IRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:COG1122 92 TVEEDVAFGPE-NLG--LPREEIRERVEEALELVGLE-HLADRpPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 188 REVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG1122 168 RGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
29-231 |
2.83e-32 |
|
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: 122.96 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH-GVILIHQELNLAEq 107
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLVFQNPDDQFFG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 LSVEENIFLGREiKRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:cd03225 91 PTVEEEVAFGLE-NLG--LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 188 REVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03225 168 AGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
27-249 |
3.59e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 27 SFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGglvldgaEVSFADSEAGEGHGVI--LI-HQELN 103
Cdd:COG1121 15 SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSG-------TVRLFGKPPRRARRRIgyVPqRAEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQLSVEENIFLGREIKRGWF-LDKTAMRAEAKRLLDQLQCDvDPRTR-IRDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:COG1121 88 WDFPITVRDVVLMGRYGRRGLFrRPSRADREAVDEALERVGLE-DLADRpIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 182 TAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARL 249
Cdd:COG1121 167 FAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRA 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
26-231 |
6.26e-32 |
|
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: 121.94 E-value: 6.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGaeVSFADSEAGEGH-GVILIHQELNl 104
Cdd:cd03268 8 KTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG--KSYQKNIEALRRiGALIEAPGFY- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 105 aEQLSVEENIFLGREIKRGwfldktaMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAV 184
Cdd:cd03268 85 -PNLTARENLRLLARLLGI-------RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494149220 185 LTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-231 |
8.04e-32 |
|
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: 121.62 E-value: 8.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 24 ICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADseageGHGVILIHQELN 103
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQLSVEEN-IFLGReiKRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:cd03269 81 LYPKMKVIDQlVYLAQ--LKG--LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 183 AVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-234 |
1.01e-31 |
|
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: 128.10 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 1 MTDAAVHAVNPGTEGKIRLSGRKICKSF-----GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGL 75
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 76 VLDGAEVSFADSEAGEGHG--VILIHQE----LNlaEQLSVEENIFLGREIKRGwfLDKTAMRAEAKRLLDQLQCDVDPR 149
Cdd:COG1123 323 LFDGKDLTKLSRRSLRELRrrVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGL--LSRAERRERVAELLERVGLPPDLA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 150 TR-IRDLSVSDRQMVEIAKALSKKADILILDEPTAVL--TGREvEILfDQIRRLREQ-GVAILYISHKLDEIKAIADRVT 225
Cdd:COG1123 399 DRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALdvSVQA-QIL-NLLRDLQRElGLTYLFISHDLAVVRYIADRVA 476
|
....*....
gi 494149220 226 VLRDGRhIV 234
Cdd:COG1123 477 VMYDGR-IV 484
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-231 |
2.71e-31 |
|
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: 120.29 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPA----QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGEGH- 93
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS-KLSEKELAAf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 -----GVILihQELNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKA 168
Cdd:cd03255 80 rrrhiGFVF--QSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 169 LSKKADILILDEPTAVL---TGREV-EILFDQirrLREQGVAILYISHKlDEIKAIADRVTVLRDGR 231
Cdd:cd03255 155 LANDPKIILADEPTGNLdseTGKEVmELLREL---NKEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-231 |
7.25e-31 |
|
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: 117.35 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQe 101
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR-IGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 lnlaeqlsveeniflgreikrgwfldktamraeakrlldqlqcdvdprtrirdLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 182 TAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-241 |
1.00e-30 |
|
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: 118.73 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQ----VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVsfadseAGEGHGVIL 97
Cdd:cd03293 4 RNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV------TGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 98 IHQELNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILI 177
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQG---VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 178 LDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVL--RDGRhIVTEPVVDL 241
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGR-IVAEVEVDL 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
32-249 |
6.00e-30 |
|
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: 117.28 E-value: 6.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEG--HGVILIHQELNLAEQLS 109
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrRQIGMIFQQFNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 110 VEENIFLGR----EIKRGWF-LDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAV 184
Cdd:cd03256 95 VLENVLSGRlgrrSTWRSLFgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 185 LTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARL 249
Cdd:cd03256 175 LDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
29-236 |
6.71e-30 |
|
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: 116.84 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGE--GHGVILIHQE----L 102
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirRKEIQMVFQDpmssL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 NlaEQLSVEENIflgREIKRGWFLDKTAmrAEAKRLLDQLQCDVDPRTRIRD-----LSVSDRQMVEIAKALSKKADILI 177
Cdd:cd03257 96 N--PRMTIGEQI---AEPLRIHGKLSKK--EARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 178 LDEPTA---VLTgrEVEILfDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGRhIVTE 236
Cdd:cd03257 169 ADEPTSaldVSV--QAQIL-DLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGK-IVEE 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
29-231 |
1.16e-29 |
|
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: 115.93 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVIliHQELNLAEQL 108
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFV--SDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENI-FLGREikrgWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:cd03266 94 TARENLeYFAGL----YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 188 REVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
22-231 |
2.20e-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: 113.82 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVI-LIHQ 100
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIgMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 101 ELNLAEQLSVEENIFLGreikrgwfldktamraeakrlldqlqcdvdprtrirdLSVSDRQMVEIAKALSKKADILILDE 180
Cdd:cd03229 84 DFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 181 PTAVL---TGREVEilfDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03229 127 PTSALdpiTRREVR---ALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-231 |
4.89e-29 |
|
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: 114.56 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILI 98
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCdvdprTRIRD-----LSVSDRQMVEIAKALSKKA 173
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRG---LSKKEREEKLEELLEEFHI-----THLRKskassLSGGERRRVEIARALATNP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 174 DILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-231 |
6.76e-29 |
|
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: 114.26 E-value: 6.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVsfADSEAGEgHGVI 96
Cdd:cd03300 1 IELEN--VSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHK-RPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 LIHQELNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADIL 176
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKK---LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 177 ILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
272-492 |
8.53e-29 |
|
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: 113.68 E-value: 8.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV---PGQV-RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAYL 347
Cdd:cd03224 1 LEVENLNAgygKSQIlFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 TKDRkgsGLLLNMDMRPNLTLlalekfGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDP 427
Cdd:cd03224 81 PEGR---RIFPELTVEENLLL------GAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRItgILEG 492
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV--VLEG 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-447 |
2.47e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 118.27 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKS-TLVKILSGYHEP----TEGGLVLDGAEVSFADSE---AGEGHGVILIHQE-- 101
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQtlrGVRGNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 --LN--------LAEQLSVEENifLGREIKRGWF---LDKTAMRAEAKRLLDQlqcdvdPRtrirDLSVSDRQMVEIAKA 168
Cdd:PRK15134 103 vsLNplhtlekqLYEVLSLHRG--MRREAARGEIlncLDRVGIRQAAKRLTDY------PH----QLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 169 LSKKADILILDEPTAVL-TGREVEILfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR---HIVTEPVVDLSK 243
Cdd:PRK15134 171 LLTRPELLIADEPTTALdVSVQAQIL-QLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRcveQNRAATLFSAPT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 244 DDMARLMVGRDiKQMFPHRVSDTSAPIvLSVRDLSV--PGQ-------------VRDASFDLHKGEVLGFAGIVGAGRT- 307
Cdd:PRK15134 250 HPYTQKLLNSE-PSGDPVPLPEPASPL-LDVEQLQVafPIRkgilkrtvdhnvvVKNISFTLRPGETLGLVGESGSGKSt 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 308 ---ALMEAIiglreRSSGTIERDGKPVRIASLQD--AKNSGIAYLTKDRKGSgllLNmdmrPNLTLLALEKFGSVI---- 378
Cdd:PRK15134 328 tglALLRLI-----NSQGEIWFDGQPLHNLNRRQllPVRHRIQVVFQDPNSS---LN----PRLNVLQIIEEGLRVhqpt 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 379 VDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQI 447
Cdd:PRK15134 396 LSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
27-234 |
5.34e-28 |
|
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: 111.09 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 27 SFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGeghgviLIHQELNLAE 106
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIG------YVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 Q--LSVEENIFLGREIKRGWFLD-KTAMRAEAKRLLDQLQCdVDPRTR-IRDLSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:cd03235 82 DfpISVRDVVLMGLYGHKGLFRRlSKADKAKVDEALERVGL-SELADRqIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 183 AVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLrdGRHIV 234
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL--NRTVV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
272-486 |
1.45e-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: 108.64 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV--PGQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNsgIAYL 347
Cdd:cd03230 1 IEVRNLSKryGKKtaLDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR--IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 TKDrkgSGLLLNMDMRPNLtllalekfgsvivdrkaeeaalekaieafdiraadrkakvgDFSGGNQQKLLLAKVMETDP 427
Cdd:cd03230 79 PEE---PSLYENLTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
17-231 |
1.72e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 109.50 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSgrKICKSFGPAQVLFDVSVDlyAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgegHGVI 96
Cdd:cd03298 1 VRLD--KIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 LIHQELNLAEQLSVEENIFLGREIK-RGWFLDKTAMRAEAKRL-LDQLQcdvdpRTRIRDLSVSDRQMVEIAKALSKKAD 174
Cdd:cd03298 74 MLFQENNLFAHLTVEQNVGLGLSPGlKLTAEDRQAIEVALARVgLAGLE-----KRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 175 ILILDEPTAVL-TGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03298 149 VLLLDEPFAALdPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-444 |
2.73e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.16 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGpAQVLF-DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLD-GAEVSFadseageghgvilIH 99
Cdd:COG0488 2 ENLSKSFG-GRPLLdDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGY-------------LP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 100 QELNLAEQLSVEENIFLG----REIKR------------------------------GWfldktAMRAEAKRLLDQLQCD 145
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGdaelRALEAeleeleaklaepdedlerlaelqeefealgGW-----EAEARAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 146 VDPRTR-IRDLSVSDRQMVEIAKALSKKADILILDEPT--------------------AVL------------TGREVEI 192
Cdd:COG0488 143 EEDLDRpVSELSGGWRRRVALARALLSEPDLLLLDEPTnhldlesiewleeflknypgTVLvvshdryfldrvATRILEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 193 LFDQIR----------RLREQGVAILYISH-----KLDEIKAIADRVTV-----------------LRDGRHIVTEPVVD 240
Cdd:COG0488 223 DRGKLTlypgnysaylEQRAERLEQEAAAYakqqkKIAKEEEFIRRFRAkarkakqaqsrikalekLEREEPPRRDKTVE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 241 LSKDDMARLmvGRDikqmfphrvsdtsapiVLSVRDLSV--PGQV--RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGL 316
Cdd:COG0488 303 IRFPPPERL--GKK----------------VLELEGLSKsyGDKTllDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 317 RERSSGTIERdGKPVRiaslqdaknsgIAYLTKDRKgsglllnmDMRPNLTLL-ALEKFGsvivdRKAEEAALEKAIEAF 395
Cdd:COG0488 365 LEPDSGTVKL-GETVK-----------IGYFDQHQE--------ELDPDKTVLdELRDGA-----PGGTEQEVRGYLGRF 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 494149220 396 DIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTK 444
Cdd:COG0488 420 LFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL 468
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
267-486 |
3.76e-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: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 267 SAPIVLSVRDLSV--PGQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiaslqdAKNS 342
Cdd:COG1121 2 MMMPAIELENLTVsyGGRpvLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR------RARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 343 GIAYL----TKDRK---------GSGLLLNMDMRPNLtllalekfgsvivdRKAEEAALEKAIEAFDIRA-ADRKakVGD 408
Cdd:COG1121 76 RIGYVpqraEVDWDfpitvrdvvLMGRYGRRGLFRRP--------------SRADREAVDEALERVGLEDlADRP--IGE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 409 FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-489 |
6.21e-27 |
|
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: 114.13 E-value: 6.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGY--HEPTEG----------------------------GL 75
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekcgyverpskvgepcpvcGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 76 VLDGAEVSFADSEAGEGHGV-----ILIHQELNLAEQLSVEENIFlgREIKRGWFLDKTAMRaEAKRLLDQLQCDVDPRT 150
Cdd:TIGR03269 88 TLEPEEVDFWNLSDKLRRRIrkriaIMLQRTFALYGDDTVLDNVL--EALEEIGYEGKEAVG-RAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 151 RIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRD 229
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 230 GRhIVTEPVVDlskDDMARLMVGrdIKQMFPHRVSDTSAPIvLSVRDLS---------VPGQVRDASFDLHKGEVLGFAG 300
Cdd:TIGR03269 245 GE-IKEEGTPD---EVVAVFMEG--VSEVEKECEVEVGEPI-IKVRNVSkryisvdrgVVKAVDNVSLEVKEGEIFGIVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 301 IVGAGRTALMEAIIGLRERSSGTIErdgkpVRIA-SLQDAKNSGIAYLTKDRKGSGLLLN-MDMRPNLTLlaLEKFGSVI 378
Cdd:TIGR03269 318 TSGAGKTTLSKIIAGVLEPTSGEVN-----VRVGdEWVDMTKPGPDGRGRAKRYIGILHQeYDLYPHRTV--LDNLTEAI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 379 VDRKAEEAALEKAIEAFDIRAADRKAKVG-------DFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFI 451
Cdd:TIGR03269 391 GLELPDELARMKAVITLKMVGFDEEKAEEildkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSI 470
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 494149220 452 gdLTDR---GKSVILLSSEMPEMLGLSDRIAVMAAGRITGI 489
Cdd:TIGR03269 471 --LKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
271-486 |
8.62e-27 |
|
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: 107.98 E-value: 8.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSV--PGQ------VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNS 342
Cdd:cd03257 1 LLEVKNLSVsfPTGggsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 343 G--IAYLTKDRKGSgllLNmdmrPNLTLL-----ALEKFGSVIVDRKAEEAALEKAiEAFDIRAADRKAKVGDFSGGNQQ 415
Cdd:cd03257 81 RkeIQMVFQDPMSS---LN----PRMTIGeqiaePLRIHGKLSKKEARKEAVLLLL-VGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 416 KLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTD-RGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
18-231 |
9.37e-27 |
|
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: 107.18 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 18 RLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEgHGVIL 97
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR-RLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 98 IHQeLNLAEQLSVEENI-FLGReikrgwFLDKTAMRAEAKRLLDQLqcDVDPR--TRIRDLSVSDRQMVEIAKALSKKAD 174
Cdd:COG4133 81 GHA-DGLKPELTVRENLrFWAA------LYGLRADREAIDEALEAV--GLAGLadLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 175 ILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHklDEIKAIADRVTVLRDGR 231
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
26-231 |
1.09e-26 |
|
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: 107.23 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGE-GHGVILIHQELNL 104
Cdd:cd03262 8 KSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGMVFQQFNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 105 AEQLSVEENIFLGREIKRGwfLDKTAMRAEAKRLLDQL----QCDVDPRTrirdLSVSDRQMVEIAKALSKKADILILDE 180
Cdd:cd03262 88 FPHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVgladKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 181 PTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-230 |
1.12e-26 |
|
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: 106.96 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 23 KICKSFGPAQ-VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGhgviLIHQE 101
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIG----YVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNlaEQL---SVEENIFLGREIkrgwfLDKTAMRAEA--KRL-LDQLQcDVDPRtrirDLSVSDRQMVEIAKALSKKADI 175
Cdd:cd03226 80 VD--YQLftdSVREELLLGLKE-----LDAGNEQAETvlKDLdLYALK-ERHPL----SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 176 LILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
283-486 |
1.24e-26 |
|
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: 106.98 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvriasLQDAKNSGIAYLTKDRkgsGLLLNMDM 362
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP-----LDIAARNRIGYLPEER---GLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKfgsvivDRKAEEAA--LEKAIEAFDIRAAdRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:cd03269 88 IDQLVYLAQLK------GLKKEEARrrIDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 441 IGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-231 |
1.97e-26 |
|
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: 107.43 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgegHGVILIHQE 101
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGREIK-RGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDE 180
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 181 PTAVLTGREVEILFDQIRRLR-EQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-231 |
3.46e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.12 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH-GVIL 97
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRrAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 98 IHQELNLAeqLSVEENIFLGREikrGWFLDKTAMRAEAKRLLDQLQCDvDPRTRI-RDLSVSDRQMVEIAKAL------- 169
Cdd:COG4559 82 QHSSLAFP--FTVEEVVALGRA---PHGSSAAQDRQIVREALALVGLA-HLAGRSyQTLSGGEQQRVQLARVLaqlwepv 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 170 SKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG4559 156 DGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-231 |
3.74e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.16 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEV-SFADSEAGEGHGV 95
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 96 ILihQELNLAEQLSVEENIFLGReikrgwfLDKTAMRAEAKRLLDQ--LQCDVDP-RTR-IRDLSVSDRQMVEIAKAL-- 169
Cdd:PRK13548 81 LP--QHSSLSFPFTVEEVVAMGR-------APHGLSRAEDDALVAAalAQVDLAHlAGRdYPQLSGGEQQRVQLARVLaq 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 170 ----SKKADILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK13548 152 lwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGR 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
22-231 |
4.19e-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: 109.03 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfaDSEAGEgHGVILIHQE 101
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPPEK-RNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:COG3842 86 YALFPHLTVAENVAFGLRMRG---VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 182 TAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG3842 163 LSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-234 |
5.69e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAdSEAGEGHG-- 94
Cdd:PRK11124 3 IQLNG--INCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFS-KTPSDKAIre 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 95 ----VILIHQELNLAEQLSVEENIF------LGreikrgwfLDKTAMRAEAKRLLDQLQCDvDPRTRI-RDLSVSDRQMV 163
Cdd:PRK11124 80 lrrnVGMVFQQYNLWPHLTVQQNLIeapcrvLG--------LSKDQALARAEKLLERLRLK-PYADRFpLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 164 EIAKALSKKADILILDEPTAVL----TGREVEIlfdqIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGrHIV 234
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALdpeiTAQIVSI----IRELAETGITQVIVTHEVEVARKTASRVVYMENG-HIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
29-241 |
5.92e-26 |
|
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: 105.74 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS-FADSEAGEGHGVI-LIHQELNLAE 106
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTlLSGKELRKARRRIgMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 QLSVEENIFLGREIkrgWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL- 185
Cdd:cd03258 96 SRTVFENVALPLEI---AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALd 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 186 --TGREVEILFDQIRrlREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:cd03258 173 peTTQSILALLRDIN--RELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-251 |
7.11e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 107.50 E-value: 7.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADS--------EAG 90
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigylpeERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 91 eghgvilIHQELNLAEQLsveenIFLGReiKRGwfLDKTAMRAEAKRLLDQLqcDVDPR--TRIRDLSVSDRQMVEIAKA 168
Cdd:COG4152 82 -------LYPKMKVGEQL-----VYLAR--LKG--LSKAEAKRRADEWLERL--GLGDRanKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 169 LSKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLsKDDMAR 248
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI-RRQFGR 222
|
...
gi 494149220 249 LMV 251
Cdd:COG4152 223 NTL 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-489 |
1.45e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 110.72 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKS----TLVKIL--SGYHEPTEGGL-------VLDGAEVSFADSEAGEGHGVILIHQE- 101
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLlrrrsrqVIELSEQSAAQMRHVRGADMAMIFQEp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 -LNLAEQLSVEENIFLGREIKRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIR---DLSVSDRQMVEIAKALSKKADILI 177
Cdd:PRK10261 114 mTSLNPVFTVGEQIAESIRLHQG--ASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 178 LDEPTAVLtgrEVEILfDQIRRL-----REQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL--------SKD 244
Cdd:PRK10261 192 ADEPTTAL---DVTIQ-AQILQLikvlqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIfhapqhpyTRA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 245 DMA---RL--MVGRDIKQMFP------------HRVSDTSAP--IVLSVRDLSVPGQVR---------------DASFDL 290
Cdd:PRK10261 268 LLAavpQLgaMKGLDYPRRFPlislehpakqepPIEQDTVVDgePILQVRNLVTRFPLRsgllnrvtrevhaveKVSFDL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 291 HKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpvRIASLQDAK----NSGIAYLTKDRKGSglllnMDMRPNL 366
Cdd:PRK10261 348 WPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ--RIDTLSPGKlqalRRDIQFIFQDPYAS-----LDPRQTV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 367 TLLALEKFG-SVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKS 445
Cdd:PRK10261 421 GDSIMEPLRvHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 494149220 446 QIYHFIGDLT-DRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGI 489
Cdd:PRK10261 501 QIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
36-231 |
1.64e-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: 103.28 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILI----HQELnLAEQLSVE 111
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedrKREG-LVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 112 ENIFLGREikrgwfldktamraeakrlldqlqcdvdprtrirdLSVSDRQMVEIAKALSKKADILILDEPTA---VLTGR 188
Cdd:cd03215 97 ENIALSSL-----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRgvdVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 189 EVeilFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03215 142 EI---YRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
29-231 |
2.36e-25 |
|
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: 102.46 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQELNLAEQl 108
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPFLFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIflgreikrgwfldktamraeakrlldqlqcdvdprtrirdLSVSDRQMVEIAKALSKKADILILDEPTAVLTGR 188
Cdd:cd03228 91 TIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 189 EVEILFDQIRRLReQGVAILYISHKLDEIKaIADRVTVLRDGR 231
Cdd:cd03228 131 TEALILEALRALA-KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
283-486 |
2.37e-25 |
|
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: 103.74 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiASLQDAKNSgIAYLTKDRkgsGLLLNMDM 362
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQS-LGYCPQFD---ALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKFGSvivdRKAEEAALEKAIEAFDIRAaDRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIG 442
Cdd:cd03263 93 REHLRFYARLKGLP----KSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 443 TKSQIYHFIGDLTdRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03263 168 SRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-231 |
2.98e-25 |
|
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: 103.74 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQ--VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVilIH 99
Cdd:cd03263 4 RNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY--CP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 100 QELNLAEQLSVEENI-FLGReIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:cd03263 82 QFDALFDELTVREHLrFYAR-LKG---LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 179 DEPTA---VLTGREVeilFDQIRRLReQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03263 158 DEPTSgldPASRRAI---WDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-231 |
3.42e-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: 103.95 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQvLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfadSEAGEGHGVILIHQE 101
Cdd:cd03299 4 ENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT---NLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGREIKRgwfldktAMRAEAKRLLDQLQ--------CDVDPRTrirdLSVSDRQMVEIAKALSKKA 173
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRK-------VDKKEIERKVLEIAemlgidhlLNRKPET----LSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 174 DILILDEPTAVLTGREVEILFDQIRRLR-EQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGK 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-231 |
5.54e-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: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgeghgvilihqe 101
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 lnLAEQLSVEENIflgreikrgwfLDKTAMRAEAKRLLDQLqcdvdprtrirdlsvSD--RQMVEIAKALSKKADILILD 179
Cdd:cd03214 71 --LARKIAYVPQA-----------LELLGLAHLADRPFNEL---------------SGgeRQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494149220 180 EPTAVL-TGREVEILfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03214 123 EPTSHLdIAHQIELL-ELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
283-486 |
1.37e-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: 101.68 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAYltkdrKGSGLLLNMDM 362
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVS-----DSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLtllalEKFGSVI-VDRKAEEAALEKAIEAFDIRA-ADRKakVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:cd03266 96 RENL-----EYFAGLYgLKGDELTARLEELADRLGMEElLDRR--VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 441 IGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-236 |
1.66e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.88 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 16 KIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGV 95
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 96 ILIHQELNLAEQLSVEENIFLGreikrGWFLDKTAMRAEAKRLLDQLQCDVDPRT-RIRDLSVSDRQMVEIAKALSKKAD 174
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMG-----GFFAERDQFQERIKWVYELFPRLHERRIqRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 175 ILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGrHIVTE 236
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG-HVVLE 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-231 |
2.56e-24 |
|
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: 100.79 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 24 ICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVsfADSEAGEgHGVILIHQELN 103
Cdd:cd03301 6 VTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--TDLPPKD-RDIAMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTA 183
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRK---VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 184 VLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03301 160 NLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
35-255 |
3.55e-24 |
|
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: 103.64 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 35 FDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGaEVSFaDSEAG-----EGHGVILIHQELNLAEQLS 109
Cdd:COG4148 16 LDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQ-DSARGiflppHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 110 VEENIFLGReikrgWFLDKTAMRAEAKRLLDQLqcDVDP--RTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL-T 186
Cdd:COG4148 94 VRGNLLYGR-----KRAPRAERRISFDEVVELL--GIGHllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALdL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 187 GREVEILfDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKD-DMARLMVGRDI 255
Cdd:COG4148 167 ARKAEIL-PYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRpDLLPLAGGEEA 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
37-235 |
4.69e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.22 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 37 VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQELNLAEQLSVEENIFL 116
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 117 G--REIKRGWF--LDKTAM--RAEAKRlLDQLQCDVDprtRIRDLSVSDRQM----------VEIAKALSKKADILILDE 180
Cdd:PRK11300 104 AqhQQLKTGLFsgLLKTPAfrRAESEA-LDRAATWLE---RVGLLEHANRQAgnlaygqqrrLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 181 PTAVLTGREVEILFDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGRHIVT 235
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
283-482 |
6.86e-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: 99.53 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiaslqdAKNSGIAYLTKDRkgsglLLNMDM 362
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------KERKRIGYVPQRR-----SIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPN-----LTLLALEKFGSVIVDRKAEEAALEkAIEAFDIRA-ADRKakVGDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:cd03235 84 PISvrdvvLMGLYGHKGLFRRLSKADKAKVDE-ALERVGLSElADRQ--IGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMA 482
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
33-231 |
7.60e-24 |
|
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: 100.10 E-value: 7.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGaEVSFADSEAGEGHGVILIHQELNLAEQLSVEE 112
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 113 NIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEI 192
Cdd:cd03267 115 SFYLLAAIYD---LPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494149220 193 LFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03267 192 IRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
32-233 |
8.15e-24 |
|
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: 104.84 E-value: 8.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQELNLAeQLSVE 111
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAWVPQNPYLF-AGTIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 112 ENIFLGR------EIKRgwfldkTAMRAEAKRLLDQLQCDVDprTRI----RDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:COG4988 429 ENLRLGRpdasdeELEA------ALEAAGLDEFVAALPDGLD--TPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 182 TAVLTGREVEILFDQIRRLReQGVAILYISHKLDEIKAiADRVTVLRDGRHI 233
Cdd:COG4988 501 TAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIV 550
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-231 |
2.04e-23 |
|
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: 104.15 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 11 PGTEGKIRLsgRKICKSFGPAQ--VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSE 88
Cdd:COG2274 468 PRLKGDIEL--ENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 89 AGEGH-GVILihQELNLAEQlSVEENIFLGR------EIKrgWFLDKTAMRAEAKRLLDQLQcdvdprTRIRD----LSV 157
Cdd:COG2274 546 SLRRQiGVVL--QDVFLFSG-TIRENITLGDpdatdeEII--EAARLAGLHDFIEALPMGYD------TVVGEggsnLSG 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 158 SDRQMVEIAKALSKKADILILDEPTAVLTGREVEILFDQIRRLReQGVAILYISHKLDEIKaIADRVTVLRDGR 231
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIR-LADRIIVLDKGR 686
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
26-231 |
2.23e-23 |
|
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: 98.41 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHE-----PTEGGLVLDGAEVSFADSEAGE-GHGVILIH 99
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLElRRRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 100 QELNLAEqLSVEENIFLG---REIKRGWFLDKTAMRAEAKRLLDQlqcDVDPRTRIRDLSVSDRQMVEIAKALSKKADIL 176
Cdd:cd03260 88 QKPNPFP-GSIYDNVAYGlrlHGIKLKEELDERVEEALRKAALWD---EVKDRLHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 177 ILDEPTAVL---TGREVEILfdqIRRLREQgVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03260 164 LLDEPTSALdpiSTAKIEEL---IAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
13-231 |
3.14e-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: 98.51 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 13 TEGKIRLSGrkICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEageg 92
Cdd:COG1127 2 SEPMIEVRN--LTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 93 hgvilihqELNLAEQ--------------LSVEENI-FLGREIKRgwfLDKTAMRAEAKRLLDQLqcdvdprtrirDLSV 157
Cdd:COG1127 76 --------ELYELRRrigmlfqggalfdsLTVFENVaFPLREHTD---LSEAEIRELVLEKLELV-----------GLPG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 158 SDRQM-----------VEIAKALSKKADILILDEPTAVL---TGREVEilfDQIRRLREQ-GVAILYISHKLDEIKAIAD 222
Cdd:COG1127 134 AADKMpselsggmrkrVALARALALDPEILLYDEPTAGLdpiTSAVID---ELIRELRDElGLTSVVVTHDLDSAFAIAD 210
|
....*....
gi 494149220 223 RVTVLRDGR 231
Cdd:COG1127 211 RVAVLADGK 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-240 |
3.58e-23 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 98.87 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 20 SGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS-FADSEAGE--GHGVI 96
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAaMSRKELRElrRKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 LIHQELNLAEQLSVEENIFLGREIkRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADIL 176
Cdd:cd03294 106 MVFQSFALLPHRTVLENVAFGLEV-QG--VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 177 ILDEPTAVL---TGREVEilfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR--------HIVTEPVVD 240
Cdd:cd03294 183 LMDEAFSALdplIRREMQ---DELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRlvqvgtpeEILTNPAND 255
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
284-485 |
4.34e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 97.15 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAknsgiayltkdRKGSGLLL----N 359
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-----------RRKVGLVFqnpdD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 MDMRPNLT---LLALEKFGsviVDRKAEEAALEKAIEAFDIRAAdRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:cd03225 87 QFFGPTVEeevAFGLENLG---LPEEEIEERVEEALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGR 485
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-231 |
4.83e-23 |
|
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: 96.98 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 35 FDVSVDLYA-GEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGaeVSFADSEAG-----EGHGVILIHQELNLAEQL 108
Cdd:cd03297 13 FTLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKinlppQQRKIGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGREIKRgwfldKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGR 188
Cdd:cd03297 91 NVRENLAFGLKRKR-----NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 189 EVEILFDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-245 |
5.98e-23 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 97.57 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGEGH--- 93
Cdd:cd03261 1 IELRG--LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIS-GLSEAELYRlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 --GVILihQELNLAEQLSVEENI-FLGREIKRgwfLDKTAMRAEAKRLLDQ--LQCDVDPRTriRDLSVSDRQMVEIAKA 168
Cdd:cd03261 78 rmGMLF--QSGALFDSLTVFENVaFPLREHTR---LSEEEIREIVLEKLEAvgLRGAEDLYP--AELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 169 LSKKADILILDEPTAVLTGREVEILFDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDD 245
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-248 |
7.84e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.02 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 18 RLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfadseagegH---- 93
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT---------Hlpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 -----GVILIHQELNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCdvdprTRIRD-----LSVSDRQMV 163
Cdd:COG1137 74 krarlGIGYLPQEASIFRKLTVEDNILAVLELRK---LSKKEREERLEELLEEFGI-----THLRKskaysLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 164 EIAKALSKKADILILDE------PTAVLtgrevEIlfdQ--IRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVT 235
Cdd:COG1137 146 EIARALATNPKFILLDEpfagvdPIAVA-----DI---QkiIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
250
....*....|...
gi 494149220 236 EPVVDLSKDDMAR 248
Cdd:COG1137 218 GTPEEILNNPLVR 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
271-486 |
9.58e-23 |
|
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: 101.52 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSV--PGQ----VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGL---RERSSGTIERDGKPVRIASLQDAKN 341
Cdd:COG1123 4 LLEVRDLSVryPGGdvpaVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 342 SgIAYLTKDRKGSgllLNMdmrpnLTLLALEKFGSVIVDRKAEEAAlEKAIEAFDI--RAADRKAKVGDFSGGNQQKLLL 419
Cdd:COG1123 84 R-IGMVFQDPMTQ---LNP-----VTVGDQIAEALENLGLSRAEAR-ARVLELLEAvgLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 420 AKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLT-DRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
35-241 |
9.83e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.75 E-value: 9.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 35 FDVSVDlyAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGaeVSFADSEAGEgHGVILIHQELNLAEQLSVEENI 114
Cdd:COG3840 18 FDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG--QDLTALPPAE-RPVSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 115 FLGreIKRGWFL---DKTAMRAEAKR-----LLDQLqcdvdPRTrirdLSVSDRQMVEIAKALSKKADILILDEPTAVLt 186
Cdd:COG3840 93 GLG--LRPGLKLtaeQRAQVEQALERvglagLLDRL-----PGQ----LSGGQRQRVALARCLVRKRPILLLDEPFSAL- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 187 G----REVEILFDQIRrlREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:COG3840 161 DpalrQEMLDLVDELC--RERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
33-231 |
1.65e-22 |
|
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: 94.21 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH-GVILihQELNLAEQlSVE 111
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHvGYLP--QDDELFSG-SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 112 ENIFLGREikrgwfldktamraeakrlldqlqcdvdprtrirdlsvsdRQMVEIAKALSKKADILILDEPTAVLTGREVE 191
Cdd:cd03246 94 ENILSGGQ----------------------------------------RQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494149220 192 ILFDQIRRLREQGVAILYISHKLdEIKAIADRVTVLRDGR 231
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-231 |
2.04e-22 |
|
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: 96.31 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 27 SFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLV------LDGAEVS-------FADSEagegh 93
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWelrkrigLVSPA----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 gvilIHQELNlaEQLSVEE--------NIFLGREIKrgwfldkTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEI 165
Cdd:COG1119 87 ----LQLRFP--RDETVLDvvlsgffdSIGLYREPT-------DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 166 AKALSKKADILILDEPTAVLTGREVEILFDQIRRLREQG-VAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-241 |
2.17e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 98.23 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSF----GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEA--G 90
Cdd:COG1135 2 IELEN--LSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 91 EGHGVILIHQELNLAEQLSVEENIFLGREIKrGWflDKTAMRAEAKRLLDqlqcdvdpRTRIRD--------LSVSDRQM 162
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIA-GV--PKAEIRKRVAELLE--------LVGLSDkadaypsqLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 163 VEIAKALSKKADILILDEPTAVL---TGREVEILFDQIRRlrEQGVAILYISHKLDEIKAIADRVTVLRDGRhIVTE-PV 238
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALdpeTTRSILDLLKDINR--ELGLTIVLITHEMDVVRRICDRVAVLENGR-IVEQgPV 225
|
...
gi 494149220 239 VDL 241
Cdd:COG1135 226 LDV 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
32-233 |
3.70e-22 |
|
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: 94.98 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS-FADSEAGEGHGVILihQELNLAEQlSV 110
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdISRKSLRSMIGVVL--QDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVD--PRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGR 188
Cdd:cd03254 94 MENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDtvLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 189 EVEILFDQIRRLREQGVAILyISHKLDEIKAiADRVTVLRDGRHI 233
Cdd:cd03254 174 TEKLIQEALEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDGKII 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-237 |
3.70e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.98 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgegHGVILIHQE 101
Cdd:PRK11607 23 RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---RPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDK---LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 182 TAVLTGR-----EVEILfDQIRRLreqGVAILYISHKLDEIKAIADRVTVLRDGRHI-VTEP 237
Cdd:PRK11607 177 MGALDKKlrdrmQLEVV-DILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVqIGEP 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-227 |
4.50e-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: 99.28 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADsEAGEGHGVILIHQELNLAEQl 108
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD-ADSWRDQIAWVPQHPFLFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDprTRI----RDLSVSDRQMVEIAKALSKKADILILDEPTAV 184
Cdd:TIGR02857 411 TIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLD--TPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 185 LTGREVEILFDQIRRLReQGVAILYISHKLdEIKAIADRVTVL 227
Cdd:TIGR02857 489 LDAETEAEVLEALRALA-QGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
272-492 |
6.87e-22 |
|
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: 94.43 E-value: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVP-GQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDG------KPVRIASLqdakn 341
Cdd:cd03219 1 LEVRGLTKRfGGlvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglPPHEIARL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 342 sGIAyltkdRK--GSGLLLNMDMRPNLTLLALEKFGSVIVD---RKAEEAALEKAIEAFDI----RAADRKAkvGDFSGG 412
Cdd:cd03219 76 -GIG-----RTfqIPRLFPELTVLENVMVAAQARTGSGLLLaraRREEREARERAEELLERvglaDLADRPA--GELSYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 413 NQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRItgILEG 492
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV--IAEG 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-227 |
9.55e-22 |
|
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: 95.89 E-value: 9.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSF----GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEP---TEGGLVLDGAEVSFADSEAGE 91
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 92 ---GHGVILIHQE----LN--------LAEQLsveeniflgrEIKRGwfLDKTAMRAEAKRLLDQLQCDvDPRTRIRD-- 154
Cdd:COG0444 82 kirGREIQMIFQDpmtsLNpvmtvgdqIAEPL----------RIHGG--LSKAEARERAIELLERVGLP-DPERRLDRyp 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 155 --LSVSDRQMVEIAKALSKKADILILDEPTA---VLTgrEVEILfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVL 227
Cdd:COG0444 149 heLSGGMRQRVMIARALALEPKLLIADEPTTaldVTI--QAQIL-NLLKDLqRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-230 |
1.27e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.31 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 23 KICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfaDSEAGEGHgVILIHQEL 102
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRK-VGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 NLAEQLSVEENIFLG-REIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:PRK10851 84 ALFRHMTVFDNIAFGlTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 182 TAVLTGREVEILFDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
283-493 |
2.15e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.41 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvriasLQDAKNSGIAYLTKDRkgsGLLLNMDM 362
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP-----LDPEDRRRIGYLPEER---GLYPKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKfGsviVDRKAEEAALEKAIEAFDIrAADRKAKVGDFSGGNQQKL-LLAKVMEtDPDIVIIDEPTRGIDI 441
Cdd:COG4152 89 GEQLVYLARLK-G---LSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVqLIAALLH-DPELLILDEPFSGLDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 442 GTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRItgILEGN 493
Cdd:COG4152 163 VNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK--VLSGS 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
272-493 |
2.28e-21 |
|
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: 92.78 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV--PGQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAknsgiay 346
Cdd:COG1122 1 IELENLSFsyPGGtpaLDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 347 ltkdRKGSGLLL-NmdmrPNLTLLA----------LEKFGsviVDRKAEEAALEKAIEAFDIRA-ADRKakVGDFSGGNQ 414
Cdd:COG1122 74 ----RRKVGLVFqN----PDDQLFAptveedvafgPENLG---LPREEIRERVEEALELVGLEHlADRP--PHELSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 415 QKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRItgILEGN 493
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI--VADGT 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
272-488 |
2.49e-21 |
|
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: 90.57 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV--PGQV--RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAYl 347
Cdd:cd03216 1 LELRGITKrfGGVKalDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 tkdrkgsglllnmdmrpnltllalekfgsvivdrkaeeaalekaieafdiraadrkakVGDFSGGNQQKLLLAKVMETDP 427
Cdd:cd03216 80 ----------------------------------------------------------VYQLSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITG 488
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
272-486 |
4.35e-21 |
|
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: 92.18 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVP--GQV--RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvrIASLQDAKnsgiayL 347
Cdd:cd03261 1 IELRGLTKSfgGRTvlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGED--ISGLSEAE------L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 TKDRKGSGLLL-------NMDMRPNLTLLALEKFgsVIVDRKAEEAALEKaIEAFDIRAADRKaKVGDFSGGNQQKLLLA 420
Cdd:cd03261 73 YRLRRRMGMLFqsgalfdSLTVFENVAFPLREHT--RLSEEEIREIVLEK-LEAVGLRGAEDL-YPAELSGGMKKRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 421 KVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-231 |
4.99e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.08 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDG-------AEVSFADSEAGeghg 94
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkVDERLIRQEAG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 95 viLIHQELNLAEQLSVEENIFLGREIKRGwfldktAMRAEAKRLLDQLQCDVDPRTRIR----DLSVSDRQMVEIAKALS 170
Cdd:PRK09493 81 --MVFQQFYLFPHLTALENVMFGPLRVRG------ASKEEAEKQARELLAKVGLAERAHhypsELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 171 KKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-233 |
7.78e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.95 E-value: 7.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVIli 98
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEQLSVEENIflgREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:PRK13537 86 PQFDNLDPDFTVRENL---LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 179 DEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-233 |
8.62e-21 |
|
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: 90.89 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 24 ICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfadSEAGEGHGVI-LIHQEL 102
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV---REPREVRRRIgIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 NLAEQLSVEENIFLGREIKrGWFLDKTAMRAEakRLLDQLQCdVDPRTRI-RDLSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:cd03265 83 SVDDELTGWENLYIHARLY-GVPGAERRERID--ELLDFVGL-LEAADRLvKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 182 TAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-234 |
1.24e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVI 96
Cdd:PRK13536 42 IDLAG--VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 liHQELNLAEQLSVEENIFL-GReikrgWFLDKT-AMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKAD 174
Cdd:PRK13536 120 --PQFDNLDLEFTVRENLLVfGR-----YFGMSTrEIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 175 ILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIV 234
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIA 252
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-234 |
1.44e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.85 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVsfadseageghgvilihQELNLAE----- 106
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI-----------------RDLTLESlrrqi 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 ----------QLSVEENIFLGR------EIKRgwfldkTAMRAEAKRLLDQLqcdvdPR---TRIRD----LSVSDRQMV 163
Cdd:COG1132 417 gvvpqdtflfSGTIRENIRYGRpdatdeEVEE------AAKAAQAHEFIEAL-----PDgydTVVGErgvnLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 164 EIAKALSKKADILILDEPTAVL-TGREVEIlFDQIRRLReQGVAILYISHKLDEIKAiADRVTVLRDGRhIV 234
Cdd:COG1132 486 AIARALLKDPPILILDEATSALdTETEALI-QEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGR-IV 553
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
27-231 |
2.49e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 27 SFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGeGHGVILIHQELNLAE 106
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-SRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 QLSVEENIFLGREIKRGWFLDKT-AMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:PRK09536 91 EFDVRQVVEMGRTPHRSRFDTWTeTDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494149220 186 -TGREVEILfDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK09536 171 dINHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGR 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
283-485 |
3.89e-20 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 87.30 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNsGIAYltkdrkgsglllnmdm 362
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGY---------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 rpnltllalekfgsvivdrkaeeaalekaieafdiraadrkakVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIG 442
Cdd:cd00267 78 -------------------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 443 TKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGR 485
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
271-486 |
5.44e-20 |
|
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: 89.33 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSV--PGQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV-RIASLQDAKNsgIA 345
Cdd:COG1120 1 MLEAENLSVgyGGRpvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaSLSRRELARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 346 YLTKDRKGSGLLLNMDM-----RPNLTLLALEkfgsvivdRKAEEAALEKAIEAFDIRA-ADRKakVGDFSGGNQQKLLL 419
Cdd:COG1120 79 YVPQEPPAPFGLTVRELvalgrYPHLGLFGRP--------SAEDREAVEEALERTGLEHlADRP--VDELSGGERQRVLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 420 AKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLT-DRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
271-492 |
7.32e-20 |
|
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: 88.50 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSV---PGQV-RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV------RIASLqdak 340
Cdd:COG0410 3 MLEVENLHAgygGIHVlHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglpphRIARL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 341 nsGIAYLTKDRkgsGLLLNMDMRPNLTLLALekfgsVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLA 420
Cdd:COG0410 79 --GIGYVPEGR---RIFPSLTVEENLLLGAY-----ARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 421 KVMETDPDIVIIDEPTRG-----IDigtksQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITgiLEG 492
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV--LEG 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
283-436 |
7.64e-20 |
|
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: 86.16 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKnSGIAYLTKDrkgSGLLLNMDM 362
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR-KEIGYVFQD---PQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 363 RPNLTL-LALEKFGSVIVDRKAEEAALEKAIEAFDIRAADRkaKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:pfam00005 77 RENLRLgLLLKGLSKREKDARAEEALEKLGLGDLADRPVGE--RPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
26-231 |
9.48e-20 |
|
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: 87.63 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSVDLYAGeVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgegHGVI-LIHQELNL 104
Cdd:cd03264 8 KRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL---RRRIgYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 105 AEQLSVEEniflgreikrgwFLDKTAM---------RAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADI 175
Cdd:cd03264 84 YPNFTVRE------------FLDYIAWlkgipskevKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 176 LILDEPTAVLTGREVEILFDQIRRLREQGVAILYiSHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGEDRIVILS-THIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
283-487 |
1.17e-19 |
|
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: 87.31 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiaslqdaknsgiaylTKDRKGSGLLLNMDM 362
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---------------AKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNL---TLLALEKFGSVIVDRKAEEAalEKAIEAFDI-RAADRKAKvgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRG 438
Cdd:cd03226 81 DYQLftdSVREELLLGLKELDAGNEQA--ETVLKDLDLyALKERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 439 IDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-231 |
1.37e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLsgRKICKSFGPAQ-VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH-- 93
Cdd:COG2884 2 IRF--ENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 --GVilIHQELNLAEQLSVEENIFLGREIkRGWflDKTAMRAEAKRLLDQL----QCDVDPRTrirdLSVSDRQMVEIAK 167
Cdd:COG2884 80 riGV--VFQDFRLLPDRTVYENVALPLRV-TGK--SRKEIRRRVREVLDLVglsdKAKALPHE----LSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 168 ALSKKADILILDEPTAVL---TGREVEILFDQIRRLreqGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG2884 151 ALVNRPELLLADEPTGNLdpeTSWEIMELLEEINRR---GTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
29-215 |
1.46e-19 |
|
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: 86.71 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHG-VILIHQelNLAEQ 107
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQrVGLVFQ--DPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 L---SVEENIFLGreiKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAV 184
Cdd:TIGR01166 81 LfaaDVDQDVAFG---PLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180 190
....*....|....*....|....*....|.
gi 494149220 185 LTGREVEILFDQIRRLREQGVAILYISHKLD 215
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
33-248 |
2.10e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.44 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGaEVSFadseageghgviLIhqELNLA--EQLSV 110
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSA------------LL--ELGAGfhPELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIFLgreikRGWFLDKTamRAEAKRLLDQlqcdvdprtrIRDLSvsdrqmvEIAK---------------------AL 169
Cdd:COG1134 106 RENIYL-----NGRLLGLS--RKEIDEKFDE----------IVEFA-------ELGDfidqpvktyssgmrarlafavAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 170 SKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRhIV----TEPVVDLSKDD 245
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR-LVmdgdPEEVIAAYEAL 240
|
...
gi 494149220 246 MAR 248
Cdd:COG1134 241 LAG 243
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
283-492 |
2.98e-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: 86.27 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGT-------IERDGKPVRiaslqdaKNSGIA--YLTKDRKG 353
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPREVR-------RRIGIVfqDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 354 SGlllnmdmRPNLTLLA-LEKFGSVIVDRKAEEAalekaIEAFDI-RAADRKakVGDFSGGNQQKLLLAKVMETDPDIVI 431
Cdd:cd03265 89 TG-------WENLYIHArLYGVPGAERRERIDEL-----LDFVGLlEAADRL--VKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 432 IDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSE-MPEMLGLSDRIAVMAAGRItgILEG 492
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHyMEEAEQLCDRVAIIDHGRI--IAEG 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-231 |
3.40e-19 |
|
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: 86.37 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgeGHGVI-LIHQELNLAEQlSV 110
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY--LHSKVsLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQ--CDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGr 188
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFISELAsgYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA- 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 189 EVEILFDQIRRLREQGVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-231 |
3.66e-19 |
|
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: 86.33 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVL--DGAEVSFADSEAgegHGVILI-HQELNLAEQl 108
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASP---REILALrRRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 sveeniFLgREIKR--------------GWflDKTAMRAEAKRLLDQLQC-----DVDPRTrirdLSVSDRQMVEIAKAL 169
Cdd:COG4778 101 ------FL-RVIPRvsaldvvaepllerGV--DREEARARARELLARLNLperlwDLPPAT----FSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 170 SKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-240 |
4.01e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.90 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAD----SEAGEGH- 93
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 -----GVILIHQELNLAEQLSVEENIflG-REIKRGWfLDKTAMRAEAKRLLDQLQCDVDprtRIRDL----SVSDRQMV 163
Cdd:PRK11701 87 lrtewGFVHQHPRDGLRMQVSAGGNI--GeRLMAVGA-RHYGDIRATAGDWLERVEIDAA---RIDDLpttfSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 164 EIAKALSKKADILILDEPTAvltGREVEI---LFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRHI---VTE 236
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTG---GLDVSVqarLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVesgLTD 237
|
....
gi 494149220 237 PVVD 240
Cdd:PRK11701 238 QVLD 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
273-487 |
4.21e-19 |
|
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: 84.79 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 273 SVRDLSVP-GQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV-RIASLQDAKNsgIAYL 347
Cdd:cd03214 1 EVENLSVGyGGrtvLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaSLSPKELARK--IAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 TKdrkgsglllnmdmrpnltllALEKFGsvivdrkaeeaalekaIEAFdiraADRKakVGDFSGGNQQKLLLAKVMETDP 427
Cdd:cd03214 79 PQ--------------------ALELLG----------------LAHL----ADRP--FNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDLTD-RGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-231 |
4.55e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 31 AQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFA---DSEAGEGhgviLIHQelNLAEQ 107
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwDVRRQVG----MVFQ--NPDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 L---SVEENIFLGRE---------IKR-GWFLDKTAMRAEAKRlldqlqcdvDPRTrirdLSVSDRQMVEIAKALSKKAD 174
Cdd:PRK13635 94 FvgaTVQDDVAFGLEnigvpreemVERvDQALRQVGMEDFLNR---------EPHR----LSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 175 ILILDEPTAVL--TGREvEILfDQIRRLREQ-GVAILYISHKLDEIkAIADRVTVLRDGR 231
Cdd:PRK13635 161 IIILDEATSMLdpRGRR-EVL-ETVRQLKEQkGITVLSITHDLDEA-AQADRVIVMNKGE 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
27-231 |
4.89e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.61 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 27 SFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS-FADSEAGEghGVILIHQELNLA 105
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmLSSRQLAR--RLALLPQHHLTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 106 EQLSVEENIFLGREIKRG-WFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAV 184
Cdd:PRK11231 89 EGITVRELVAYGRSPWLSlWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 185 L-TGREVEiLFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK11231 169 LdINHQVE-LMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-233 |
5.75e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 86.97 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQ--VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAD-SEAGEGHGVILi 98
Cdd:PRK13632 11 ENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIGIIF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 hQelNLAEQ---LSVEENIFLGREIKRgwfLDKTAMR------AEAKRLLDQLqcDVDPrtriRDLSVSDRQMVEIAKAL 169
Cdd:PRK13632 90 -Q--NPDNQfigATVEDDIAFGLENKK---VPPKKMKdiiddlAKKVGMEDYL--DKEP----QNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 170 SKKADILILDEPTAVLTGREVEILFDQIRRLREQGV-AILYISHKLDEIkAIADRVTVLRDGRHI 233
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLI 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-269 |
6.90e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.93 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSF----GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAG-- 90
Cdd:PRK11153 2 IELKN--ISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT-ALSEKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 91 -EGHGVILIHQELNLAEQLSVEENIFLGREIKrGWflDKTAMRAEAKRLLDQL----QCDVDPrtriRDLSVSDRQMVEI 165
Cdd:PRK11153 79 kARRQIGMIFQHFNLLSSRTVFDNVALPLELA-GT--PKAEIKARVTELLELVglsdKADRYP----AQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 166 AKALSKKADILILDEPTAVL---TGREVEILFDQIRrlREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL- 241
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALdpaTTRSILELLKDIN--RELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVf 229
|
250 260 270
....*....|....*....|....*....|....
gi 494149220 242 --SKDDMARLMVGRDIKQMFP----HRVSDTSAP 269
Cdd:PRK11153 230 shPKHPLTREFIQSTLHLDLPedylARLQAEPTT 263
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-233 |
7.14e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.64 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGEGHGVILIHQELNLAEQl 108
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTRASLRRNIAVVFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGREikrgwflDKT--AMRAEAKR------LLDQLQC-DVDPRTRIRDLSVSDRQMVEIAKALSKKADILILD 179
Cdd:PRK13657 424 SIEDNIRVGRP-------DATdeEMRAAAERaqahdfIERKPDGyDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 180 EPTAVL---TGREVEILFDQIRRLREQGVailyISHKLDEIKAiADRVTVLRDGRHI 233
Cdd:PRK13657 497 EATSALdveTEAKVKAALDELMKGRTTFI----IAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
271-486 |
8.00e-19 |
|
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: 87.42 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSV-----PGQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGL---RERSSGTIERDGKPVRIAS---L 336
Cdd:COG0444 1 LLEVRNLKVyfptrRGVvkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSekeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 337 QDAKNSGIAYLTKDRKGSgllLNmdmrPNLTLL-----ALEKFGsvIVDRKAeeaALEKAIEAFD---IRAADRKAKV-- 406
Cdd:COG0444 81 RKIRGREIQMIFQDPMTS---LN----PVMTVGdqiaePLRIHG--GLSKAE---ARERAIELLErvgLPDPERRLDRyp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 407 GDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGR 485
Cdd:COG0444 149 HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
.
gi 494149220 486 I 486
Cdd:COG0444 229 I 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-230 |
1.08e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.83 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 23 KICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGY---HEPTEGGLVLDGAEVSFA--------DSEAGE 91
Cdd:PRK09984 9 KLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREgrlardirKSRANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 92 GHgvilIHQELNLAEQLSVEENIFLG--------REIKRgWFldKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMV 163
Cdd:PRK09984 89 GY----IFQQFNLVNRLSVLENVLIGalgstpfwRTCFS-WF--TREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 164 EIAKALSKKADILILDEPTAVLTGREVEILFDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-231 |
1.09e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.70 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 13 TEGKIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEG 92
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 93 HGVIlihQELNLAEQLSVEENIFLGREIKRGWFLDKTAMRAEAKRLLdQLQcDVDPRtRIRDLSVSDRQMVEIAKALSKK 172
Cdd:PRK09452 89 NTVF---QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMV-QLE-EFAQR-KPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 173 ADILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-231 |
1.20e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.40 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQELNLAEQlSVE 111
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 112 ENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDprTRIRD----LSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:TIGR00958 573 ENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYD--TEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 188 rEVEILFDQIRRLreQGVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:TIGR00958 651 -ECEQLLQESRSR--ASRTVLLIAHRLSTVER-ADQILVLKKGS 690
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-231 |
1.36e-18 |
|
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: 84.56 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 30 PAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAD-SEAGEGHGviLIHQELNLAEQl 108
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDpADLRRNIG--YVPQDVTLFYG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQ--CDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLT 186
Cdd:cd03245 93 TLRDNITLGAPLADDERILRAAELAGVTDFVNKHPngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 187 GREVEILFDQIRRLREQGVAILyISHKLdEIKAIADRVTVLRDGR 231
Cdd:cd03245 173 MNSEERLKERLRQLLGDKTLII-ITHRP-SLLDLVDRIIVMDSGR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
283-485 |
1.39e-18 |
|
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: 83.39 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKN-SGIAYLTKDrkgSGLLLNMD 361
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrRRIGMVFQD---FALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 MRPNLTLLalekfgsvivdrkaeeaalekaieafdiraadrkakvgdFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDI 441
Cdd:cd03229 93 VLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 442 GTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGR 485
Cdd:cd03229 134 ITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-231 |
1.41e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.41 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 18 RLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGE------ 91
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 92 ------GHGVILIHQELNLAEQLSVEENIFLGREIKRGwfLDKTAMRAEAKRLLDQLqcDVDPRTRIR---DLSVSDRQM 162
Cdd:PRK10619 85 nqlrllRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLG--LSKQEARERAVKYLAKV--GIDERAQGKypvHLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 163 VEIAKALSKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
285-486 |
1.49e-18 |
|
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: 84.63 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRE---RSSGTIERDGKPVRIASLQDAknsgIAYLTKDRKgsgLLLNMD 361
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC----VAYVRQDDI---LLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 MRPNLTLLALEKFGsvivdRKAEEAALEKAIEAFDIRA-AD---RKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:cd03234 98 VRETLTYTAILRLP-----RKSSDAIRKKRVEDVLLRDlALtriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 438 GIDIGTKSQIYHFIGDLTDRGKSVIlLSSEMP--EMLGLSDRIAVMAAGRI 486
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVI-LTIHQPrsDLFRLFDRILLLSSGEI 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-231 |
2.32e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.25 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 35 FDVSVDlyAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDgaevsfadseaGEGHG--------VILIHQELNLAE 106
Cdd:PRK10771 18 FDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-----------GQDHTttppsrrpVSMLFQENNLFS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 QLSVEENIFLGreIKRGWFLDkTAMRAEAKRLLDQLQCDvDPRTRI-RDLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:PRK10771 85 HLTVAQNIGLG--LNPGLKLN-AAQREKLHAIARQMGIE-DLLARLpGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 186 TG---REVEILFDQIrrLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK10771 161 DPalrQEMLTLVSQV--CQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-226 |
2.52e-18 |
|
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: 87.92 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 6 VHAVNPGTEGKIRLSGRKICKSFGPaqvlFDVSVD---LYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDgAEV 82
Cdd:COG1245 329 VHAPRREKEEETLVEYPDLTKSYGG----FSLEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 83 SFADseageghgvilihQELNLAEQLSVEEniFLGREIKRG----WFLDKTAMRAEAKRLLDQlqcdvdprtRIRDLSVS 158
Cdd:COG1245 404 SYKP-------------QYISPDYDGTVEE--FLRSANTDDfgssYYKTEIIKPLGLEKLLDK---------NVKDLSGG 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 159 DRQMVEIAKALSKKADILILDEPTAVLtgrEVE---ILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTV 226
Cdd:COG1245 460 ELQRVAIAACLSRDADLYLLDEPSAHL---DVEqrlAVAKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
33-231 |
2.82e-18 |
|
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: 83.82 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDG---AEVSFADSEAGEGhgviLIHQELNLAEQlS 109
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASLRRQIG----LVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 110 VEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDprTRIRD----LSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYD--TVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 186 TGREVEILFDQIRRLREQGVAILyISHKLDEIKAiADRVTVLRDGR 231
Cdd:cd03251 170 DTESERLVQAALERLMKNRTTFV-IAHRLSTIEN-ADRIVVLEDGK 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
283-486 |
3.40e-18 |
|
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: 84.62 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvrIASLQDAKNSGIayltKDRKGSGLLLNMDM 362
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQD--IAAMSRKELREL----RRKKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKFGSVI--VDRKAEEAALEKAIEAFDIrAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:cd03294 114 LPHRTVLENVAFGLEVqgVPRAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 441 --IGTKSQiYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03294 193 plIRREMQ-DELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
282-487 |
3.84e-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: 83.01 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 282 QVRDASFDLHKGeVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIAslQDAKNSGIAYLTKDrkgsglllnMD 361
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ--PQKLRRRIGYLPQE---------FG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 MRPNLTLLALEKFGSVI--VDRKAEEAALEKAIEAFDIraADR-KAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRG 438
Cdd:cd03264 83 VYPNFTVREFLDYIAWLkgIPSKEVKARVDEVLELVNL--GDRaKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 439 IDIGTKSQIYHFIGDLTDrGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:cd03264 161 LDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
272-491 |
4.50e-18 |
|
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: 83.70 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV------PGQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSg 343
Cdd:COG1124 2 LEVRNLSVsygqggRRVpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 344 IAYLTKDRKGSgllLNmdmrPNLTLLALEKFGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVM 423
Cdd:COG1124 81 VQMVFQDPYAS---LH----PRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 424 ETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLT-DRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGILE 491
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-231 |
4.66e-18 |
|
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: 82.97 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 18 RLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGeghgvil 97
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGG------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 98 ihqelnLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLD--QLQCDVDprTRIRDLSVSDRQMVEIAKALSKKADI 175
Cdd:cd03220 95 ------FNPELTGRENIYLNGRLLG---LSRKEIDEKIDEIIEfsELGDFID--LPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 176 LILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
283-493 |
6.12e-18 |
|
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: 82.98 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV------RIASLqdaknsGIAYLTKDrkgSGL 356
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhKRARL------GIGYLPQE---ASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 357 LLNMDMRPNLtLLALEKFGsviVDRKAEEAALEKAIEAFDIrAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:cd03218 87 FRKLTVEENI-LAVLEIRG---LSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRItgILEGN 493
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV--LAEGT 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
32-244 |
6.24e-18 |
|
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: 82.19 E-value: 6.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYH--EPTEGGLVLDGAEVSFADSEAGEGHGVILIHQE------LN 103
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFLAFQYppeipgVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQL-SVEENiFLGREIKRgwfldktamraeakrlldqlqcdvdprtrirdlsvsdrqmVEIAKALSKKADILILDEPT 182
Cdd:cd03217 94 NADFLrYVNEG-FSGGEKKR----------------------------------------NEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 183 AVLTGREVEILFDQIRRLREQGVAILYISHK---LDEIKaiADRVTVLRDGRhIVTEPVVDLSKD 244
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGR-IVKSGDKELALE 194
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
272-486 |
6.63e-18 |
|
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: 81.11 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV------PGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLqDAKNSGIA 345
Cdd:cd03246 1 LEVENVSFrypgaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 346 YLTKDRKgsglllnmdmrpnltLLAlekfGSVivdrkaeeaalekaieAFDIraadrkakvgdFSGGNQQKLLLAKVMET 425
Cdd:cd03246 80 YLPQDDE---------------LFS----GSI----------------AENI-----------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 426 DPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEmPEMLGLSDRIAVMAAGRI 486
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
267-485 |
1.03e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.73 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 267 SAPIvLSVRDLSVP--G--QVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvrIASLQDAKns 342
Cdd:PRK11300 2 SQPL-LSVSGLMMRfgGllAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH--IEGLPGHQ-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 343 gIAyltkdRKG-------SGLLLNMDMRPNLT--------------LLALEKFgsvivdRKAEEAALEKA---IEAFDIR 398
Cdd:PRK11300 77 -IA-----RMGvvrtfqhVRLFREMTVIENLLvaqhqqlktglfsgLLKTPAF------RRAESEALDRAatwLERVGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 399 A-ADRKAkvGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSD 476
Cdd:PRK11300 145 EhANRQA--GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISD 222
|
....*....
gi 494149220 477 RIAVMAAGR 485
Cdd:PRK11300 223 RIYVVNQGT 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-227 |
1.26e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 13 TEGKIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgeg 92
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 93 hgvilIHQELNLAEQL------SVEENIFLGREIKRgwfldktaMRAEAKRLLDQLQCDVDPRT----RIRDLSVSDRQM 162
Cdd:PRK10247 79 -----YRQQVSYCAQTptlfgdTVYDNLIFPWQIRN--------QQPDPAIFLDDLERFALPDTiltkNIAELSGGEKQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 163 VEIAKALSKKADILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAiADRVTVL 227
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
283-486 |
1.36e-17 |
|
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: 81.41 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaslqdaknsgiAYLTKDRKGSGLLL-NMD 361
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-------------TGVPPERRNIGMVFqDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 MRPNLTLL-----ALEKFGsviVDRKAEEAALEKAIEAFDIRAaDRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:cd03259 83 LFPHLTVAeniafGLKLRG---VPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 437 RGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03259 159 SALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
29-237 |
1.39e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEA-----GEGHGVILihQELN 103
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrREHFGFIF--QRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQLSVEEN-----IFLGREikrgwfldKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:PRK10535 97 LLSHLTAAQNvevpaVYAGLE--------RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 179 DEPTAVLTGREVEILFDQIRRLREQGVAILYISHKlDEIKAIADRVTVLRDGrHIVTEP 237
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDG-EIVRNP 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-256 |
1.62e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 18 RLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVIL 97
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 98 IHQELNLAEQLSVEENIFLGREIKRGWFLDKTAMRAEakRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILI 177
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRAN--ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 178 LDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIV-TEPVVDLSKDDMARLMVGRDIK 256
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAhGTPTEILQDEHVKRVYLGEDFR 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
283-486 |
2.63e-17 |
|
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: 81.19 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIAYLTKDrkgSGLLLNMDM 362
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK-IGYVIQQ---IGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLL-ALEKFGSVIVDRKAEEaaLEKAIEAFDIRAADRKAkvGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDI 441
Cdd:cd03295 93 EENIALVpKLLKWPKEKIRERADE--LLALVGLDPAEFADRYP--HELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 442 GTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03295 169 ITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
22-231 |
2.98e-17 |
|
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: 81.19 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLF-DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH-G-VIli 98
Cdd:cd03295 4 ENVTKRYGGGKKAVnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKiGyVI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 hQELNLAEQLSVEENIFLGREIKrGWflDKTAMRAEAKRLLDQLqcDVDPRTRI----RDLSVSDRQMVEIAKALSKKAD 174
Cdd:cd03295 82 -QQIGLFPHMTVEENIALVPKLL-KW--PKEKIRERADELLALV--GLDPAEFAdrypHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 175 ILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
267-486 |
5.32e-17 |
|
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: 80.41 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 267 SAPIVLSVRDLSVP--GQV--RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvrIASLQDAKns 342
Cdd:COG1127 1 MSEPMIEVRNLTKSfgDRVvlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQD--ITGLSEKE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 343 giayLTKDRK-------GSGLLLNMDMRPNLtLLALEKFGSvIVDRKAEEAALEKaIEAFDIRAADRKaKVGDFSGGNQQ 415
Cdd:COG1127 77 ----LYELRRrigmlfqGGALFDSLTVFENV-AFPLREHTD-LSEAEIRELVLEK-LELVGLPGAADK-MPSELSGGMRK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 416 KLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-234 |
6.44e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGY--HEPTEGGLVLDGAEVSFADSE--AGEGhgvilihqeLNLAEQ 107
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDerARAG---------IFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 LSVE----ENIFLGREI---KRGWFLDKTAMRAEAKRLLDQLqcDVDPRTRIRDLSVS----DRQMVEIAKALSKKADIL 176
Cdd:COG0396 85 YPVEipgvSVSNFLRTAlnaRRGEELSAREFLKLLKEKMKEL--GLDEDFLDRYVNEGfsggEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 177 ILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHK---LDEIKaiADRVTVLRDGRhIV 234
Cdd:COG0396 163 ILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGR-IV 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
283-500 |
7.27e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaslqdaknSGIAYLTKDRKGS-GLLLNMD 361
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----------PSRARHARQRVGVvPQFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 mrPNLTLLA-LEKFGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:PRK13537 93 --PDFTVREnLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 441 IGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRitGILEGNDRN--EHEI 500
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR--KIAEGAPHAliESEI 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
259-487 |
7.78e-17 |
|
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: 83.28 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 259 FPHRVSDTSAPIVLSVRDLSV--PGQ----VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVR 332
Cdd:COG4987 321 EPAEPAPAPGGPSLELEDVSFryPGAgrpvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 333 IASLQDAKNSgIAYLTKDrkgsGLLLNMDMRPNLtLLAlekfgsvivDRKAEEAALEKAIEA----FDIRAADRK--AKV 406
Cdd:COG4987 401 DLDEDDLRRR-IAVVPQR----PHLFDTTLRENL-RLA---------RPDATDEELWAALERvglgDWLAALPDGldTWL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 407 GD----FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTdRGKSVILLSSEmPEMLGLSDRIAVMA 482
Cdd:COG4987 466 GEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHR-LAGLERMDRILVLE 543
|
....*
gi 494149220 483 AGRIT 487
Cdd:COG4987 544 DGRIV 548
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-226 |
9.34e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.32 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 6 VHAVNPGTEGKIRLSGRKICKSFGPaqvlFDVSVD---LYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDgAEV 82
Cdd:PRK13409 328 ERPPRDESERETLVEYPDLTKKLGD----FSLEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 83 SFADseageghgvilihQELNLAEQLSVEEniFLgREIKRG----WFLDKTAMRAEAKRLLDQlqcdvdprtRIRDLSVS 158
Cdd:PRK13409 403 SYKP-------------QYIKPDYDGTVED--LL-RSITDDlgssYYKSEIIKPLQLERLLDK---------NVKDLSGG 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 159 DRQMVEIAKALSKKADILILDEPTAVLtgrEVE---ILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTV 226
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHL---DVEqrlAVAKAIRRIaEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-252 |
1.01e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGeGHGVILIHQELNLAEQLSVEE 112
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF-ARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 113 NIFLGReikRGWFLDKTAMRAEAKRLLDQLQCDVDPR---TRIRD-LSVSDRQMVEIAKALSKKADILILDEPTAVL-TG 187
Cdd:PRK10575 105 LVAIGR---YPWHGALGRFGAADREKVEEAISLVGLKplaHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALdIA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 188 REVEILfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVG 252
Cdd:PRK10575 182 HQVDVL-ALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-231 |
1.15e-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: 79.45 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 31 AQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH-GVILihQElNLAEQLS 109
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQvGVVL--QE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 110 VEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVS--DRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSggQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 188 REVEILFDQIRRLREqGVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGR 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-236 |
1.15e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGRKICKSFG-PAqvLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGV 95
Cdd:PRK13644 2 IRLENVSYSYPDGtPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 96 ILIHQelNLAEQL---SVEENIFLGREikrGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKK 172
Cdd:PRK13644 80 GIVFQ--NPETQFvgrTVEEDLAFGPE---NLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 173 ADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAiADRVTVLRDGRhIVTE 236
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGK-IVLE 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-243 |
1.39e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.72 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 7 HAVNPGTEgkirLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAD 86
Cdd:PRK11247 5 ARLNQGTP----LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 87 SEageghgVILIHQELNLAEQLSVEENIFLGreIKRGWfldktamRAEAKRLLDQlqcdVDPRTRIRD----LSVSDRQM 162
Cdd:PRK11247 81 ED------TRLMFQDARLLPWKKVIDNVGLG--LKGQW-------RDAALQALAA----VGLADRANEwpaaLSGGQKQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 163 VEIAKALSKKADILILDEPTA---VLTGREVEILfdqIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRhIVTEPV 238
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGaldALTRIEMQDL---IESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK-IGLDLT 217
|
....*
gi 494149220 239 VDLSK 243
Cdd:PRK11247 218 VDLPR 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-259 |
1.40e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 24 ICKSFGPAQV-----LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS--------------F 84
Cdd:COG1101 7 LSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykrakyigrvF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 85 ADSEAGEghgvilihqelnlAEQLSVEENIFL--GREIKRGWFLDKT-AMRAEAKRLLDQLQCDVDPR--TRIRDLSVSD 159
Cdd:COG1101 87 QDPMMGT-------------APSMTIEENLALayRRGKRRGLRRGLTkKRRELFRELLATLGLGLENRldTKVGLLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 160 RQMVEIAKALSKKADILILDEPTAVL---TGREVEILFDQIrrLREQGVAILYISHKLDEikAIA--DRVTVLRDGRhIv 234
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALdpkTAALVLELTEKI--VEENNLTTLMVTHNMEQ--ALDygNRLIMMHEGR-I- 227
|
250 260
....*....|....*....|....*
gi 494149220 235 tepVVDLSKDDMARLMVgRDIKQMF 259
Cdd:COG1101 228 ---ILDVSGEEKKKLTV-EDLLELF 248
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-236 |
1.49e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.65 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 13 TEGKIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS-FADSEAGE 91
Cdd:PRK10253 2 TESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 92 GHGviLIHQELNLAEQLSVEENIFLGREIKRGWFLD---------KTAMRAEAKRLLDQLQCDVdprtrirdLSVSDRQM 162
Cdd:PRK10253 82 RIG--LLAQNATTPGDITVQELVARGRYPHQPLFTRwrkedeeavTKAMQATGITHLADQSVDT--------LSGGQRQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 163 VEIAKALSKKADILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRhIVTE 236
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGK-IVAQ 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-233 |
1.51e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLvldgaevsfadsEAGEGHGVILIHQE 101
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQ--LSVEENIFLGREIKRGWFLDKTAmRAEAKRLLDQlqcdvdprtRIRDLSVSDRQMVEIAKALSKKADILILD 179
Cdd:PRK09544 76 LYLDTTlpLTVNRFLRLRPGTKKEDILPALK-RVQAGHLIDA---------PMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 180 EPTAVLTGREVEILFDQIRRLR-EQGVAILYISHKLDEIKAIADRVTVLrdGRHI 233
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEVLCL--NHHI 198
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
283-491 |
1.78e-16 |
|
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: 78.28 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiaslqdAKNSGIAYLTKDrkgsGLLLnmdm 362
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPDRGYVFQQ----DALL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 rPNLT-----LLALEKFGsviVDRKAEEAALEKAIEAFDIRAAdRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:cd03293 86 -PWLTvldnvALGLELQG---VPKAEARERAEELLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 438 GIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAA--GRITGILE 491
Cdd:cd03293 161 ALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVE 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
33-231 |
2.46e-16 |
|
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: 81.72 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH------GVilihqelnlae 106
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHigylpqDV----------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 QL---SVEENIflGReikrgwFLD-------KTAMRAEAKRLLDQLqcdvdPR---TRIRD----LSVSDRQMVEIAKAL 169
Cdd:COG4618 416 ELfdgTIAENI--AR------FGDadpekvvAAAKLAGVHEMILRL-----PDgydTRIGEggarLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 170 SKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLdEIKAIADRVTVLRDGR 231
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGR 543
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-231 |
2.64e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 16 KIRLSGRKICKSFGPAQ----VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAG- 90
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 91 --EGHGVILIHQELNLAEQLSVEENIFLGreikrgwFLDKTAMRAEAK-RLLDQLQC-DVDPRTRIR--DLSVSDRQMVE 164
Cdd:PRK11629 83 elRNQKLGFIYQFHHLLPDFTALENVAMP-------LLIGKKKPAEINsRALEMLAAvGLEHRANHRpsELSGGERQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 165 IAKALSKKADILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIaDRVTVLRDGR 231
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGR 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
283-486 |
2.74e-16 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 81.80 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIAYLTKDrkgsGLLLNMDM 362
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQD----VFLFSGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLlalekfgsvivdrKAEEAALEKAIEAFDIRAADR---------KAKVGD----FSGGNQQKLLLAKVMETDPDI 429
Cdd:COG2274 566 RENITL-------------GDPDATDEEIIEAARLAGLHDfiealpmgyDTVVGEggsnLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 430 VIIDEPTRGIDIGTKSQIYHFIGDLTdRGKSVILLSSEmPEMLGLSDRIAVMAAGRI 486
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHR-LSTIRLADRIIVLDKGRI 687
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
283-492 |
2.89e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaslqdaknSGIAYLTKDRKG-----SGLL 357
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----------PARARLARARIGvvpqfDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 358 LNMDMRPNLTLLAlEKFGsviVDRKAEEAALEKAIEaFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:PRK13536 127 LEFTVRENLLVFG-RYFG---MSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 438 GIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRitGILEG 492
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR--KIAEG 254
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
34-231 |
3.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.94 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEV---SFADSEAGEGHGVILIHQELNLAEQlSV 110
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVGLVFQYPEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIFLGrEIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREV 190
Cdd:PRK13637 102 EKDIAFG-PINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494149220 191 EILFDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-486 |
3.54e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGrkICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGL-VLDGaevSFADSEAGE--GH 93
Cdd:NF033858 2 ARLEG--VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGG---DMADARHRRavCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 GVILIHQEL--NLAEQLSVEENI-FLGReikrgWF-LDktamRAEAKRlldqlqcdvdprtRIRDLSVS-------DRQM 162
Cdd:NF033858 77 RIAYMPQGLgkNLYPTLSVFENLdFFGR-----LFgQD----AAERRR-------------RIDELLRAtglapfaDRPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 163 veiAK-------------ALSKKADILILDEPTavlTG------REVEILFDQIRRLREQG---VAILYIshklDEikai 220
Cdd:NF033858 135 ---GKlsggmkqklglccALIHDPDLLILDEPT---TGvdplsrRQFWELIDRIRAERPGMsvlVATAYM----EE---- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 221 ADR---VTVLRDGRHIVTEPVVDLskddMARLMVGrDIKQMF-----------------PHRVSDTSAPIVLSVRDLSVP 280
Cdd:NF033858 201 AERfdwLVAMDAGRVLATGTPAEL----LARTGAD-TLEAAFiallpeekrrghqpvviPPRPADDDDEPAIEARGLTMR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 281 -GQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaslqDAKNsgIAylTKDRKGSgl 356
Cdd:NF033858 276 fGDftaVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV------DAGD--IA--TRRRVGY-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 357 llnmdM------------RPNLTLLA-LekFGsviVDRKAEEAALEKAIEAFDIRA-ADRKAkvGDFSGGNQQKLLLAKV 422
Cdd:NF033858 344 -----MsqafslygeltvRQNLELHArL--FH---LPAAEIAARVAEMLERFDLADvADALP--DSLPLGIRQRLSLAVA 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 423 METDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSE-MPEMLgLSDRIAVMAAGRI 486
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHfMNEAE-RCDRISLMHAGRV 475
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-231 |
4.31e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 31 AQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADseagegHGVILIHQELNLAEQlSV 110
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK------RGLLALRQQVATVFQ-DP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIF--------------LG---REIKRGwfLDKTAMRAEAKRLLDQ-LQCdvdprtrirdLSVSDRQMVEIAKALSKK 172
Cdd:PRK13638 87 EQQIFytdidsdiafslrnLGvpeAEITRR--VDEALTLVDAQHFRHQpIQC----------LSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 173 ADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
32-241 |
4.60e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGglvldgaEVSFADSE----AGEGHG-----VILIHQEL 102
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG-------NVSWRGEPlaklNRAQRKafrrdIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 NLA--EQLSVEENIflgREIKRGWF-LDKTAMRAEAKRLLDQLQCDV-DPRTRIRDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:PRK10419 99 ISAvnPRKTVREII---REPLRHLLsLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 179 DEPTA----VLtgrEVEILfDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:PRK10419 176 DEAVSnldlVL---QAGVI-RLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-231 |
6.28e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.15 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGaEVSFaDSEAG-----EGHGVILIHQELNLAE 106
Cdd:PRK11144 12 DLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLF-DAEKGiclppEKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 QLSVEENIFLG-REIKRGWFLDKTAMRAeAKRLLDQLqcdvdPRTrirdLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:PRK11144 90 HYKVRGNLRYGmAKSMVAQFDKIVALLG-IEPLLDRY-----PGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 186 T---GREveiLFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK11144 160 DlprKRE---LLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-226 |
6.38e-16 |
|
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: 77.45 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 40 DLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADseageghgvilihQELNLAEQLSVEEniFLGRE 119
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-------------QYIKADYEGTVRD--LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 120 IKRgwFLDKTAMRAEakrLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEILFDQIRR 199
Cdd:cd03237 86 TKD--FYTHPYFKTE---IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*...
gi 494149220 200 LREQGVA-ILYISHKLDEIKAIADRVTV 226
Cdd:cd03237 161 FAENNEKtAFVVEHDIIMIDYLADRLIV 188
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
283-486 |
6.51e-16 |
|
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: 76.86 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKnSGIAYLTKDrkgsGLLLNMDM 362
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-RNIGYVPQD----VTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLlalekFGSVIVDRKAEEAALEKAIEAF--------DIRAADRkakvGDF-SGGNQQKLLLAKVMETDPDIVIID 433
Cdd:cd03245 95 RDNITL-----GAPLADDERILRAAELAGVTDFvnkhpnglDLQIGER----GRGlSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 434 EPTRGIDIGTKSQIYHFIGDLTdRGKSVILLSSEMPeMLGLSDRIAVMAAGRI 486
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
272-486 |
8.20e-16 |
|
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: 76.99 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVPG---QVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaSLQDAKNSGIAYLT 348
Cdd:cd03299 1 LKVENLSKDWkefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---TNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 349 KDRkgsGLLLNMDMRPNLTL-LALEKFGSVIVDRKAEEAALEKAIEAFdiraADRKakVGDFSGGNQQKLLLAKVMETDP 427
Cdd:cd03299 78 QNY---ALFPHMTVYKNIAYgLKKRKVDKKEIERKVLEIAEMLGIDHL----LNRK--PETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
283-486 |
8.53e-16 |
|
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: 76.37 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMeAIIGLRER-SSGTIERDGKPVRiaslqDAKNSGIAYLTKDRKG----SGLL 357
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRpTSGEVRVDGTDIS-----KLSEKELAAFRRRHIGfvfqSFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 358 LnmdmrPNLT-----LLALEKFGsvIVDRKAEEAALEkAIEAFDIRAAdRKAKVGDFSGGNQQKLLLAKVMETDPDIVII 432
Cdd:cd03255 94 L-----PDLTalenvELPLLLAG--VPKKERRERAEE-LLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 433 DEPTRGIDIGTKSQIYHFIGDLT-DRGKSVILLSSEmPEMLGLSDRIAVMAAGRI 486
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
267-487 |
1.06e-15 |
|
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: 79.80 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 267 SAPIVLSVRDLSV--PGQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKN 341
Cdd:COG4988 332 AGPPSIELEDVSFsyPGGrpaLDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 342 SgIAYLTKDrkgsGLLLNMDMRPNLTLlalekfgsviVDRKAEEAALEKAIEAfdiraadrkAKVGDF------------ 409
Cdd:COG4988 412 Q-IAWVPQN----PYLFAGTIRENLRL----------GRPDASDEELEAALEA---------AGLDEFvaalpdgldtpl 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 410 -------SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTdRGKSVILLSSEmPEMLGLSDRIAVMA 482
Cdd:COG4988 468 geggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHR-LALLAQADRILVLD 545
|
....*
gi 494149220 483 AGRIT 487
Cdd:COG4988 546 DGRIV 550
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-231 |
1.19e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGglvldgaEVSFAdseageghGVILIHQELNLAEQ-------- 107
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG-------EVRVL--------GYVPFKRRKEFARRigvvfgqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 ------LSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLqcDVDP--RTRIRDLSVSDRQMVEIAKALSKKADILILD 179
Cdd:COG4586 105 sqlwwdLPAIDSFRLLKAIYR---IPDAEYKKRLDELVELL--DLGEllDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 180 EPTA---VLTGREVEilfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG4586 180 EPTIgldVVSKEAIR---EFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-231 |
1.37e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 75.52 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQV-LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEA----GEGHGVI 96
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 LihQELNLAEQLSVEENIFLGREIKrgwfldKTAMRAEAKRLLDQLQCdVDPRTRIRD----LSVSDRQMVEIAKALSKK 172
Cdd:cd03292 84 F--QDFRLLPDRNVYENVAFALEVT------GVPPREIRKRVPAALEL-VGLSHKHRAlpaeLSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 173 ADILILDEPTAVL---TGREVEILFDQIRRlreQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03292 155 PTILIADEPTGNLdpdTTWEIMNLLKKINK---AGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-259 |
1.41e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.54 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS-FADSEAGE--GHGV 95
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkISDAELREvrRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 96 ILIHQELNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADI 175
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAG---INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 176 LILDEPTAVLTGREVEILFDQIRRLR-EQGVAILYISHKLDEIKAIADRVTVLRDGRHI---VTEPVVDLSKDDMARLMV 251
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVqvgTPDEILNNPANDYVRTFF 265
|
....*....
gi 494149220 252 -GRDIKQMF 259
Cdd:PRK10070 266 rGVDISQVF 274
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
283-486 |
1.66e-15 |
|
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: 75.37 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIAslqDAKNSGIAYLTKDrkgSGLLLNMDM 362
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL---PPKDRDIAMVFQN---YALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTL-LALEKFGSVIVDRKAEEAALEKAIEAFdiraADRKAKvgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDI 441
Cdd:cd03301 90 YDNIAFgLKLRKVPKDEIDERVREVAELLQIEHL----LDRKPK--QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 442 GTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03301 164 KLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-216 |
1.71e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.28 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 24 ICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGeghgviLIHQELN 103
Cdd:PRK11248 7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG------VVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQLSVEENIFLGREIkRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTA 183
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQL-AG--VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 494149220 184 VL---TGREVEILFDQIrrLREQGVAILYISHKLDE 216
Cdd:PRK11248 158 ALdafTREQMQTLLLKL--WQETGKQVLLITHDIEE 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
22-231 |
1.74e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.33 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGEGHGVI----- 96
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID-TARSLSQQKGLIrqlrq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 97 ---LIHQELNLAEQLSVEENIFLGREIKRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKA 173
Cdd:PRK11264 86 hvgFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 174 DILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
285-489 |
1.76e-15 |
|
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: 75.41 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLhKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvriasLQDAKNSGIayLTKDRKGSGLLL------ 358
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV-----LFDSRKKIN--LPPQQRKIGLVFqqyalf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 359 -NMDMRPNLTllalekFGSVIVDRKAEEAALEKAIEAFDIRAAdRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:cd03297 88 pHLNVRENLA------FGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 438 GIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGI 489
Cdd:cd03297 161 ALDRALRLQLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-250 |
1.78e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.84 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfadSEAGEGHGVILIHQE 101
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGREIKRgwfLDKTAMRAEAKRLLDQLQCD------VDprtrirDLSVSDRQMVEIAKALSKKADI 175
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLG---VPKEERKQRVKEALELVDLAgfedryVD------QISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 176 LILDEPTAVLTGREVEILFDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLM 250
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFM 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
272-489 |
1.94e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVP-GQVR---DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIAYL 347
Cdd:PRK09536 4 IDVSDLSVEfGDTTvldGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 TKDrkgSGLLLNMDMRPNLTLLALEKFGSVIVDRKAEEAALEKAIEAFDIRA-ADRKakVGDFSGGNQQKLLLAKVMETD 426
Cdd:PRK09536 83 PQD---TSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQfADRP--VTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 427 PDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGI 489
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAA 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-214 |
2.10e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 78.94 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 3 DAAVHAVNPGTEGKIRLSGRKICKSFGPAQ-VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAE 81
Cdd:TIGR02868 319 EGSAPAAGAVGLGKPTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 82 VSFADsEAGEGHGVILIHQELNLAEQlSVEENIFLGR----EIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIrdLSV 157
Cdd:TIGR02868 399 VSSLD-QDEVRRRVSVCAQDAHLFDT-TVRENLRLARpdatDEELWAALERVGLADWLRALPDGLDTVLGEGGAR--LSG 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 158 SDRQMVEIAKALSKKADILILDEPTAVL---TGRE-VEILFDQirrlrEQGVAILYISHKL 214
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLdaeTADElLEDLLAA-----LSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-231 |
2.37e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.61 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGEGHGVILIHQE-LNLAEqlSVE 111
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQDpVVLAD--TFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 112 ENIFLGREI--KRGWFLDKTAMRAE-AKRLLDQLQcdvdprTRI----RDLSVSDRQMVEIAKALSKKADILILDEPTA- 183
Cdd:PRK10790 433 ANVTLGRDIseEQVWQALETVQLAElARSLPDGLY------TPLgeqgNNLSVGQKQLLALARVLVQTPQILILDEATAn 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 184 VLTGREVEILfDQIRRLREQGVAILyISHKLDEIKAiADRVTVLRDGR 231
Cdd:PRK10790 507 IDSGTEQAIQ-QALAAVREHTTLVV-IAHRLSTIVE-ADTILVLHRGQ 551
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
29-231 |
2.37e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.32 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAqvLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGE----GHGVILIHQ--EL 102
Cdd:PRK13649 20 GRA--LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT-STSKNKDikqiRKKVGLVFQfpES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 NLAEQ--------------LSVEENIFLGREikrgwfldKTAMRAEAKRLLDQlqcdvDPRtrirDLSVSDRQMVEIAKA 168
Cdd:PRK13649 97 QLFEEtvlkdvafgpqnfgVSQEEAEALARE--------KLALVGISESLFEK-----NPF----ELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 169 LSKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-237 |
2.41e-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: 78.69 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 37 VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGL-VLDGAEVSFADSEAGEGHG-----VILIHQELNLAEQLSV 110
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPGPDGRGrakryIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIF--LGREikrgwFLDKTAMRA-------------EAKRLLDQLqcdvdPRTrirdLSVSDRQMVEIAKALSKKADI 175
Cdd:TIGR03269 383 LDNLTeaIGLE-----LPDELARMKavitlkmvgfdeeKAEEILDKY-----PDE----LSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 176 LILDEPTAVL---TGREVEilfDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGRHIVTEP 237
Cdd:TIGR03269 449 VILDEPTGTMdpiTKVDVT---HSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
269-486 |
2.80e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.51 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 269 PIVLSVRDLSVPGQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLR----ERSSGTIERDGKPVRIASLQDAKN 341
Cdd:PRK10418 2 PQQIELRNIALQAAqplVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRGRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 342 SGIayLTKDRKGSGLLLNMDMRPNLTLLALekfgsvivDRKAEEAALEKAIEAFDIRAADRKAKVGDF--SGGNQQKLLL 419
Cdd:PRK10418 82 ATI--MQNPRSAFNPLHTMHTHARETCLAL--------GKPADDATLTAALEAVGLENAARVLKLYPFemSGGMLQRMMI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 420 AKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLT-DRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVqKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
32-231 |
5.13e-15 |
|
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: 74.50 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQELNLAEQlSVE 111
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPVLFDG-TIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 112 ENIFLGREikrgwflDKT-AMRAEAKR----------LLDQLQCDVDPRTRIrdLSVSDRQMVEIAKALSKKADILILDE 180
Cdd:cd03249 95 ENIRYGKP-------DATdEEVEEAAKkanihdfimsLPDGYDTLVGERGSQ--LSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494149220 181 PTAVL---TGREVEILFDQIRRlreqGVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:cd03249 166 ATSALdaeSEKLVQEALDRAMK----GRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
34-231 |
8.66e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGEGHGVILIHQelNLAEQL---SV 110
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT-EENVWDIRHKIGMVFQ--NPDNQFvgaTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIFLGREIKRgwfLDKTAMRAEAKRLLDQL-QCDVDPRTRIRdLSVSDRQMVEIAKALSKKADILILDEPTAVLTGRE 189
Cdd:PRK13650 100 EDDVAFGLENKG---IPHEEMKERVNEALELVgMQDFKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 190 VEILFDQIRRLREQ-GVAILYISHKLDEIkAIADRVTVLRDGR 231
Cdd:PRK13650 176 RLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
32-233 |
9.17e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.73 E-value: 9.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEG-HGVILIHQelNLAEQL-- 108
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTVGIVFQ--NPDDQLfa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 -SVEENIFLGrEIKRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:PRK13639 94 pTVEEDVAFG-PLNLG--LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 188 REVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
37-234 |
9.32e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 9.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 37 VSVDLYAGEVHALLGENGAGKSTLVKILSGYHePTEGGLVLDGAEVSFADSEAGEGHgVILIHQELNLAEQlSVEENIFL 116
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 117 GREIKRGWFLDKTAMRAEAKRLLDQLQCDVDprTRIRD----LSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEI 192
Cdd:PRK11174 446 GNPDASDEQLQQALENAWVSEFLPLLPQGLD--TPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494149220 193 LFDQIRRLReQGVAILYISHKLDEIKAIaDRVTVLRDGRhIV 234
Cdd:PRK11174 524 VMQALNAAS-RRQTTLMVTHQLEDLAQW-DQIWVMQDGQ-IV 562
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-230 |
9.88e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.82 E-value: 9.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH-----GVILIHQELNLAE 106
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvrkriGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 QlSVEENIFLGreiKRGWFLDKTAMRAEAKRLLDQLQCDVDprtrIRDLS---VSDRQMVEIA--KALSKKADILILDEP 181
Cdd:PRK13646 101 D-TVEREIIFG---PKNFKMNLDEVKNYAHRLLMDLGFSRD----VMSQSpfqMSGGQMRKIAivSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 182 TAVL---TGREVEILFDQIRrlREQGVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:PRK13646 173 TAGLdpqSKRQVMRLLKSLQ--TDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
32-231 |
1.03e-14 |
|
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: 72.35 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAdseageghgvilihqELNLAEQLSV- 110
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL---------------EKALSSLISVl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIFLgreikrgwfLDKTAMRAEAKRlldqlqcdvdprtrirdLSVSDRQMVEIAKALSKKADILILDEPTAVL---TG 187
Cdd:cd03247 81 NQRPYL---------FDTTLRNNLGRR-----------------FSGGERQRLALARILLQDAPIVLLDEPTVGLdpiTE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 188 REV-EILFDQIRrlreqGVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:cd03247 135 RQLlSLIFEVLK-----DKTLIWITHHLTGIEH-MDKILFLENGK 173
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-231 |
1.21e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.00 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQV--LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEG--HGVILIHQ---- 100
Cdd:PRK11308 24 PERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLlrQKIQIVFQnpyg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 101 ELN--------LAEQLSVEENiflgreikrgwfLDKTAMRAEAKRLLDQlqcdVDPRTRIRD-----LSVSDRQMVEIAK 167
Cdd:PRK11308 104 SLNprkkvgqiLEEPLLINTS------------LSAAERREKALAMMAK----VGLRPEHYDryphmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 168 ALSKKADILILDEPTAVLtgrEVEILfDQIRRL-----REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK11308 168 ALMLDPDVVVADEPVSAL---DVSVQ-AQVLNLmmdlqQELGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-241 |
1.27e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 18 RLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSG----YHEP-TEGGLVLDGAEVsFADSEAGEG 92
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEArVSGEVYLDGQDI-FKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 93 HGVILIHQELNLAEQLSVEENIFLGREIKR------------GWFLDKTAMRAEAKRLLDQlqcdvdPRTRirdLSVSDR 160
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRlvkskkelqervRWALEKAQLWDEVKDRLDA------PAGK---LSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 161 QMVEIAKALSKKADILILDEPTAVL---TGREVEILFDQIRRlreqGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEP 237
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLdpeNTAKIESLFLELKK----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
....
gi 494149220 238 VVDL 241
Cdd:PRK14247 229 TREV 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
22-231 |
1.32e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.58 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILiHQE 101
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL-RQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGR--------------EIKRGW-FLDKTAMRaeaKRLLDQlqcdvdprtrirdLSVSDRQMVEIA 166
Cdd:COG4604 84 NHINSRLTVRELVAFGRfpyskgrltaedreIIDEAIaYLDLEDLA---DRYLDE-------------LSGGQRQRAFIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 167 KALSKKADILILDEPTAVLTGR-EVEILfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKhSVQMM-KLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGR 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
264-485 |
1.34e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 264 SDTSAPIVLSVRDLSVPGQ--------VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGL---RERSSGTIERDGKPV- 331
Cdd:PRK09473 5 AQQQADALLDVKDLRVTFStpdgdvtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREIl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 332 --RIASLQDAKNSGIAYLTKDRKGSgllLNMDMRPNLTL---LALEKFGSvivdrKAEeaALEKAI---EAFDIRAADRK 403
Cdd:PRK09473 85 nlPEKELNKLRAEQISMIFQDPMTS---LNPYMRVGEQLmevLMLHKGMS-----KAE--AFEESVrmlDAVKMPEARKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 404 AKV--GDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAV 480
Cdd:PRK09473 155 MKMypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLV 234
|
....*
gi 494149220 481 MAAGR 485
Cdd:PRK09473 235 MYAGR 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
284-486 |
1.56e-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: 72.56 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriasLQDAKNsgiayLTKDRKGSGLLL-NMDM 362
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL----TDDKKN-----INELRQKVGMVFqQFNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKFGSVIVDRKAEEAALEKAIEAFD-IRAADRK-AKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:cd03262 88 FPHLTVLENITLAPIKVKGMSKAEAEERALELLEkVGLADKAdAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 441 IGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03262 168 PELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-443 |
1.61e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.13 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPA-QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGglvldgaevsfaDSEAGEGHGVILIHQELNL 104
Cdd:TIGR03719 12 KVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------------EARPQPGIKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 105 AEQLSVEENIFLG-REIKR-------------------------------------GWFLDKTAMRAeakrlLDQLQCDv 146
Cdd:TIGR03719 80 DPTKTVRENVEEGvAEIKDaldrfneisakyaepdadfdklaaeqaelqeiidaadAWDLDSQLEIA-----MDALRCP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 147 DPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEILfdqIRRLREQGVAILYISHK---LDEikaIADR 223
Cdd:TIGR03719 154 PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL---ERHLQEYPGTVVAVTHDryfLDN---VAGW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 224 VTVLRDGRHIV------------TEPVVDLSKDDMARLMV-------------GRDIK-------------QMFPHRVSD 265
Cdd:TIGR03719 228 ILELDRGRGIPwegnysswleqkQKRLEQEEKEESARQKTlkrelewvrqspkGRQAKskarlaryeellsQEFQKRNET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 266 TSAPI---------VLSVRDLSVPGQVR----DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERdGKPVR 332
Cdd:TIGR03719 308 AEIYIppgprlgdkVIEAENLTKAFGDKllidDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 333 iaslqdaknsgIAYLTKDRKGsglllnmdMRPNLTL-------LALEKFGSVIVDRKAeeaalekAIEAFDIRAADRKAK 405
Cdd:TIGR03719 387 -----------LAYVDQSRDA--------LDPNKTVweeisggLDIIKLGKREIPSRA-------YVGRFNFKGSDQQKK 440
|
490 500 510
....*....|....*....|....*....|....*...
gi 494149220 406 VGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGT 443
Cdd:TIGR03719 441 VGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
36-234 |
1.75e-14 |
|
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: 75.88 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHePTEGGLVLDGAEVSFADSEAGeghgvilihQELNLAEQ-------- 107
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAL---------RPLRRRMQvvfqdpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 -----LSVEENI-----FLGREikrgwfLDKTAMRAEAKRLLDQLQcdVDPRTRIR---DLSVSDRQMVEIAKALSKKAD 174
Cdd:COG4172 374 slsprMTVGQIIaeglrVHGPG------LSAAERRARVAEALEEVG--LDPAARHRyphEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 175 ILILDEPTAVLTgREV--EILfDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRhIV 234
Cdd:COG4172 446 LLVLDEPTSALD-VSVqaQIL-DLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGK-VV 505
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
285-486 |
1.82e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIErdgkpvrIASLQDAKNSGIAYLTKDRKGSGLLLNM---D 361
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTIT-------IAGYHITPETGNKNLKKLRKKVSLVFQFpeaQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 MRPNlTLLALEKFGSV---IVDRKAEEAALeKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRG 438
Cdd:PRK13641 98 LFEN-TVLKDVEFGPKnfgFSEDEAKEKAL-KWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 439 IDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-227 |
1.84e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.56 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEP----TEGGLVLDGAEV---SFADSEAGEGHGVILIHQE 101
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlklSPRERRKIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 --------LNLAEQLsvEENIFlGREIKRGWFLDKTAMRAEAKRLLDqlqcdvdpRTRIRD-----------LSVSDRQM 162
Cdd:COG4170 98 psscldpsAKIGDQL--IEAIP-SWTFKGKWWQRFKWRKKRAIELLH--------RVGIKDhkdimnsypheLTEGECQK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 163 VEIAKALSKKADILILDEPTAVL--TGReveilfDQIRRL-----REQGVAILYISHKLDEIKAIADRVTVL 227
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMesTTQ------AQIFRLlarlnQLQGTSILLISHDLESISQWADTITVL 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-231 |
1.97e-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: 76.59 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 37 VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQElnLAEQLSVEENIFL 116
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNI--LFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 117 GREIK-RGWflDKTAMRAEAkrLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEILFD 195
Cdd:TIGR01257 1027 YAQLKgRSW--EEAQLEMEA--MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*.
gi 494149220 196 QIRRLReQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:TIGR01257 1103 LLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
272-486 |
2.88e-14 |
|
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: 72.21 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV---PGQV-RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRE-----RSSGTIERDGKPVRiaslqdAKNS 342
Cdd:cd03260 1 IELRDLNVyygDKHAlKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIY------DLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 343 GIAYLtkdRKGSGLLL------------NMDMRPNLTLLALEKFGSVIVdrkaeEAALEKAieAFDIRAADRkAKVGDFS 410
Cdd:cd03260 75 DVLEL---RRRVGMVFqkpnpfpgsiydNVAYGLRLHGIKLKEELDERV-----EEALRKA--ALWDEVKDR-LHALGLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 411 GGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRgKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
287-486 |
3.22e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 287 SFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvrIASLQDAK--NSGIAYLTKDRKgsgLLLNMDMRP 364
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD--ITDWQTAKimREAVAIVPEGRR---VFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 NLTLlalekfGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTK 444
Cdd:PRK11614 100 NLAM------GGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494149220 445 SQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
283-487 |
3.58e-14 |
|
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: 71.79 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpvRIASLQDAknsgiayltkdrkGSGLLLNMDM 362
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSLLGL-------------GGGFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKfGsviVDRKaEEAALEKAIEAFdiraadrkAKVGDF--------SGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:cd03220 102 RENIYLNGRLL-G---LSRK-EIDEKIDEIIEF--------SELGDFidlpvktySSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 435 PTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
283-506 |
3.69e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAYLTKDRKgsgLLLNMDM 362
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELS---VIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNL---TLLALEKFGSVIVDRKAEEAALEKAIEAFDIRAaDRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGI 439
Cdd:PRK09700 98 LENLyigRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 440 DIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGILEGNDRNEHEIMRHATG 506
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-231 |
3.70e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 15 GKIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLdgaevsfadseageGHG 94
Cdd:COG0488 312 GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--------------GET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 95 VIL----IHQElNLAEQLSVEENIflgREIKRGwfLDKTAMRAEAKRLL---DQLQcdvdprTRIRDLSVSDRQMVEIAK 167
Cdd:COG0488 378 VKIgyfdQHQE-ELDPDKTVLDEL---RDGAPG--GTEQEVRGYLGRFLfsgDDAF------KPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 168 ALSKKADILILDEPT---AVLTgreVEILFDQirrLRE-QGVAILyISHklDE--IKAIADRVTVLRDGR 231
Cdd:COG0488 446 LLLSPPNVLLLDEPTnhlDIET---LEALEEA---LDDfPGTVLL-VSH--DRyfLDRVATRILEFEDGG 506
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
272-486 |
4.43e-14 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 71.00 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVPGQVR----DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKnSGIAYL 347
Cdd:COG4619 1 LELEGLSFRVGGKpilsPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWR-RQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 TKDrkgSGLLLNMdMRPNLTllalekFGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDP 427
Cdd:COG4619 80 PQE---PALWGGT-VRDNLP------FPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
285-495 |
7.16e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.00 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpVRIASlQDAKnsgiayLTKDRKGSGLLLNMdmrP 364
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITD-KKVK------LSDIRKKVGLVFQY---P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 NLTLL--ALEK---FGSVIVDRKAEEAA--LEKAIEAFDIRAADRKAKVG-DFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:PRK13637 93 EYQLFeeTIEKdiaFGPINLGLSEEEIEnrVKRAMNIVGLDYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDRGK-SVILLSSEMPEMLGLSDRIAVMAAGRItgILEGNDR 495
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKC--ELQGTPR 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
283-485 |
7.29e-14 |
|
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: 69.72 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIAYLTKDrkgsGLLLNMDM 362
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQD----PFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLtllalekfgsvivdrkaeeaalekaieafdiraadrkakvgdFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIG 442
Cdd:cd03228 93 RENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 443 TKSQIYHFIGDLTdRGKSVILLSSEMpEMLGLSDRIAVMAAGR 485
Cdd:cd03228 131 TEALILEALRALA-KGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
19-231 |
8.14e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.63 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEgglvldgaevsfadseageghGVILI 98
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE---------------------GIVTW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLA--EQLSveeniflGreikrGWfldktamraeakrlldqlqcdvdpRTRIRdlsvsdrqmveIAKALSKKADIL 176
Cdd:cd03221 60 GSTVKIGyfEQLS-------G-----GE------------------------KMRLA-----------LAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 177 ILDEPTAVLTGREVEILfdqIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:cd03221 93 LLDEPTNHLDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-231 |
1.39e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfaDSEAGEgHGVILIHQE 101
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAE-RGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGREIKRgwfldktAMRAEAKRLLDQ----LQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILI 177
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAG-------AKKEEINQRVNQvaevLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 178 LDEPTAVL-TGREVEILFdQIRRLREQ-GVAILYISHklDEIKA--IADRVTVLRDGR 231
Cdd:PRK11000 157 LDEPLSNLdAALRVQMRI-EISRLHKRlGRTMIYVTH--DQVEAmtLADKIVVLDAGR 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
283-486 |
1.81e-13 |
|
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: 69.92 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpvRIASLQDAKnsgiayLTKDRKGSG------- 355
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGT--DLTLLSGKE------LRKARRRIGmifqhfn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 356 LLLNMDMRPNLTlLALEKFGsviVDRKAEEAALEKAIEAFDIrAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEP 435
Cdd:cd03258 93 LLSSRTVFENVA-LPLEIAG---VPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 436 TRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03258 168 TSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
283-486 |
1.85e-13 |
|
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: 69.96 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvriaslqdaknsgIAYLTKDRKGSGLLL-NMD 361
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-------------ITNLPPHKRPVNTVFqNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 MRPNLTL-------LALEKFGSVIVDRKAEEAALEKAIEAFdiraADRKakVGDFSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:cd03300 83 LFPHLTVfeniafgLRLKKLPKAEIKERVAEALDLVQLEGY----ANRK--PSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 435 PTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
283-487 |
2.01e-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: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAYLTKdrkgSGLLLNMDM 362
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQK----TQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLAlekfgsVIVDRKAEEAA--LEKAIEAFDIrAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:cd03267 113 IDSFYLLA------AIYDLPPARFKkrLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 441 IGTKSQIYHFIGDLT-DRGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:cd03267 186 VVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
285-489 |
2.11e-13 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 71.68 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpvriaSLQDAKnSGIAYLTKDRKGSGLLLNMDMRP 364
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-----TLFDSR-KGIFLPPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 NLTLLALEKFGSVIVDRKAEEAALEKAIEAFDIRAADRKaKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTK 444
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGR-LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 445 SQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRITGI 489
Cdd:TIGR02142 168 YEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-231 |
3.14e-13 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 69.18 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGH-GVilIHQELNLAEQlSV 110
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAiGV--VPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 EENIFLGReikrgwfLDKT--AMRAEAKrlldqlQCDVDPR-TRIRD------------LSVSDRQMVEIAKALSKKADI 175
Cdd:cd03253 92 GYNIRYGR-------PDATdeEVIEAAK------AAQIHDKiMRFPDgydtivgerglkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 176 LILDEPTAVL-TGREVEILfDQIRRLReQGVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:cd03253 159 LLLDEATSALdTHTEREIQ-AALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
283-513 |
3.63e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiaslQDAKNSGIAYLTKDRK--GSGLLLNM 360
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQSEEvdWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 361 DmrpnltLLALEKFGSVIVDRKAEE---AALEKAIEAFDIRAAdRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:PRK15056 99 D------VVMMGRYGHMGWLRRAKKrdrQIVTAALARVDMVEF-RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 438 GIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSD-----RIAVMAAG--RITGILEGNDRNEHEIMRHATGISGQ 510
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDytvmvKGTVLASGptETTFTAENLELAFSGVLRHVALNGSE 251
|
...
gi 494149220 511 EGV 513
Cdd:PRK15056 252 ESI 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
283-486 |
4.11e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 69.63 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDA-KNSGIAYLTKDRKGSGLLLNMD 361
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrKKIGIIFQNPDNQFIGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 MRPNL--TLLALEKFGSVIVDrKAEEAALEKAIeafdiraaDRKAKvgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGI 439
Cdd:PRK13632 105 IAFGLenKKVPPKKMKDIIDD-LAKKVGMEDYL--------DKEPQ--NLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 440 DIGTKSQIYHFIGDLTDRG-KSVILLSSEMPEMLgLSDRIAVMAAGRI 486
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
266-486 |
4.24e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.18 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 266 TSAPIvLSVRDLSV---PGQ-VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIE---RDGKPVRIASLQD 338
Cdd:PRK11701 2 MDQPL-LSVRGLTKlygPRKgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 339 AknsgiayltkDRKgsgLLLNMD-----------MRPNLT--------LLAL--EKFGSVivdRKAEEAALEKaIEAFDI 397
Cdd:PRK11701 81 A----------ERR---RLLRTEwgfvhqhprdgLRMQVSaggnigerLMAVgaRHYGDI---RATAGDWLER-VEIDAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 398 RAADRKAKvgdFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLT-DRGKSVILLSSEMPEMLGLSD 476
Cdd:PRK11701 144 RIDDLPTT---FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTHDLAVARLLAH 220
|
250
....*....|
gi 494149220 477 RIAVMAAGRI 486
Cdd:PRK11701 221 RLLVMKQGRV 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
266-491 |
4.59e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 69.35 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 266 TSAPIVLSVRDLSV-----PGQV---RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiaslq 337
Cdd:COG1116 2 SAAAPALELRGVSKrfptgGGGVtalDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 338 dAKNSGIAYLTKDrkgsGLLLnmdmrPNLT-----LLALEKFGsviVDRKAEEAALEKAIEAFDIRAAdRKAKVGDFSGG 412
Cdd:COG1116 77 -GPGPDRGVVFQE----PALL-----PWLTvldnvALGLELRG---VPKAERRERARELLELVGLAGF-EDAYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 413 NQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAA--GRITGI 489
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
..
gi 494149220 490 LE 491
Cdd:COG1116 223 ID 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
285-463 |
6.06e-13 |
|
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: 67.82 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaslQDAKNSGIAYLtkdRKGSGLLLNmDMR- 363
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-----SDLRGRAIPYL---RRKIGVVFQ-DFRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 -PNLTLLALEKFGSVIVDRKAEEAAlEKAIEAFDIRAADRKAKV--GDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:cd03292 90 lPDRNVYENVAFALEVTGVPPREIR-KRVPAALELVGLSHKHRAlpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180
....*....|....*....|...
gi 494149220 441 IGTKSQIYHFIGDLTDRGKSVIL 463
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVV 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
283-487 |
6.90e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV-RIASLQDAKNsgIAYL---------TKDRK 352
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsMLSSRQLARR--LALLpqhhltpegITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 353 gsglLLNMDMRPNLTLlalekFGSVIVDrkaEEAALEKAIEAFDIRA-ADRKakVGDFSGGNQQKLLLAKVMETDPDIVI 431
Cdd:PRK11231 96 ----LVAYGRSPWLSL-----WGRLSAE---DNARVNQAMEQTRINHlADRR--LTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 432 IDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
34-230 |
8.52e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 68.62 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQelnlaeqlsvEEN 113
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQN----------PDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 114 IFLGREIKR--GWFLDKTAM-RAEAKRLLDQLQCDVDPRTRIRD----LSVSDRQMVEIAKALSKKADILILDEPTAVLT 186
Cdd:PRK13648 95 QFVGSIVKYdvAFGLENHAVpYDEMHRRVSEALKQVDMLERADYepnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 187 GREVEILFDQIRRLR-EQGVAILYISHKLDEiKAIADRVTVLRDG 230
Cdd:PRK13648 175 PDARQNLLDLVRKVKsEHNITIISITHDLSE-AMEADHVIVMNKG 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
283-493 |
1.25e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.36 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV------RIASLqdaknsGIAYLTKD----RK 352
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhKRARL------GIGYLPQEasifRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 353 gsglllnMDMRPNLtLLALEKFGsviVDRKAEEAALEKAIEAFDI-RAADRKAkvGDFSGGNQQKLLLAKVMETDPDIVI 431
Cdd:COG1137 93 -------LTVEDNI-LAVLELRK---LSKKEREERLEELLEEFGItHLRKSKA--YSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 432 IDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRItgILEGN 493
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV--LAEGT 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
272-487 |
1.61e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 65.80 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDL--SVPGQ----VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriASLQDAKNSGIA 345
Cdd:cd03247 1 LSINNVsfSYPEQeqqvLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 346 YLTKdrkgSGLLLNMDMRPNLTLlalekfgsvivdrkaeeaalekaieafdiraadrkakvgDFSGGNQQKLLLAKVMET 425
Cdd:cd03247 79 VLNQ----RPYLFDTTLRNNLGR---------------------------------------RFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 426 DPDIVIIDEPTRGIDIGTKSQIYHFIGDLTdRGKSVILLSSempEMLGLS--DRIAVMAAGRIT 487
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITH---HLTGIEhmDKILFLENGKII 175
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
283-489 |
1.65e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 69.29 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpVRIASLQDAKNSGIayltKDRKGSGLLLNMDM 362
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAELREV----RRKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKFGSVIVDRKAEEAAlEKAIEAFDIRAADRKAK--VGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGINAEERR-EKALDALRQVGLENYAHsyPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 441 IGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRITGI 489
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
236-484 |
2.05e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 236 EPVVDlSKDDMA----RLMVG---RDIKQM--FPHRVSDTSAPivlSVRDLSVpgqvrdasfDLHKGEVLGFAGIVGAGR 306
Cdd:TIGR01257 1912 EPIFD-EDDDVAeerqRIISGgnkTDILRLneLTKVYSGTSSP---AVDRLCV---------GVRPGECFGLLGVNGAGK 1978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 307 TALMEAIIGLRERSSGTIERDGKPVrIASLQDAKNSgIAYLTKDRKGSGLLLNmdmRPNLTLLALEKFgsviVDRKAEEA 386
Cdd:TIGR01257 1979 TTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQN-MGYCPQFDAIDDLLTG---REHLYLYARLRG----VPAEEIEK 2049
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 387 ALEKAIEAFDIRA-ADRKAkvGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLS 465
Cdd:TIGR01257 2050 VANWSIQSLGLSLyADRLA--GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTS 2127
|
250
....*....|....*....
gi 494149220 466 SEMPEMLGLSDRIAVMAAG 484
Cdd:TIGR01257 2128 HSMEECEALCTRLAIMVKG 2146
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
283-481 |
2.70e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.72 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpvriaslqdakNSGIAYLTKdRKGSGLLLNMDM 362
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQ-RSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKFGSVIVDRKAEEAALEKAIEAFDIrAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIG 442
Cdd:NF040873 75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 494149220 443 TKSQIYHFIGDLTDRGKSVILLSSEmPEMLGLSDRIAVM 481
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
290-486 |
2.71e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 290 LHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIAslqdaknsgiayLTKDRKGSGLLLNMD-MRPNLTL 368
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN------------LDAVRQSLGMCPQHNiLFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 369 LALEKFGSVIVDRKAEEAALEKAIEAFDIRAA-DRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQI 447
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494149220 448 YHFIgdLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:TIGR01257 1101 WDLL--LKYRsGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
48-231 |
2.75e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 48 ALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQelNLAEQL---SVEENIFLGrEIKRGw 124
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VGLVFQ--NPDDQIfspTVEQDIAFG-PINLG- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 125 fLDKTAMRAEAKRLLDQLQCDvDPRTRI-RDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEILFDQIRRLREQ 203
Cdd:PRK13652 109 -LDEETVAHRVSSALHMLGLE-ELRDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
|
170 180
....*....|....*....|....*....
gi 494149220 204 -GVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK13652 187 yGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
272-465 |
3.48e-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: 68.54 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV--PGQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASlQDAKNSGIAY 346
Cdd:TIGR02868 335 LELRDLSAgyPGAppvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD-QDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 347 LTKDRKgsglLLNMDMRPNLTLLALEkfgsviVDRKAEEAALEKAIEAFDIRAADRKA--KVGD----FSGGNQQKLLLA 420
Cdd:TIGR02868 414 CAQDAH----LFDTTVRENLRLARPD------ATDEELWAALERVGLADWLRALPDGLdtVLGEggarLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 421 KVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDlTDRGKSVILLS 465
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLIT 527
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-235 |
3.51e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 31 AQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLdGAEVSFADSEAGEGH------GVILIHQELNL 104
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKpvrkkvGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 105 AEQLSVE------ENIFLGREIKRGWFLDKTAMRAEAKRLLDQlqcdvDPRtrirDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:PRK13643 98 FEETVLKdvafgpQNFGIPKEKAEKIAAEKLEMVGLADEFWEK-----SPF----ELSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 179 DEPTAVLTGR---EVEILFDQIrrlREQGVAILYISHKLDEIKAIADRVTVLRDGrHIVT 235
Cdd:PRK13643 169 DEPTAGLDPKariEMMQLFESI---HQSGQTVVLVTHLMDDVADYADYVYLLEKG-HIIS 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
32-231 |
3.75e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.68 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGEGHGVILIHQELNlaEQL--- 108
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWVRSKVGLVFQDPD--DQVfss 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGrEIKRGWFLDKTAMRA-EAKRLLDQLQcdvdprtrIRD-----LSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:PRK13647 96 TVWDDVAFG-PVNMGLDKDEVERRVeEALKAVRMWD--------FRDkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 183 AVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
283-486 |
4.10e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAYLTKDrkgSGLLLNMDM 362
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLtLLALEKFGSVIVDRKAEEAalEKAIEAFDIrAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIG 442
Cdd:PRK10895 96 YDNL-MAVLQIRDDLSAEQREDRA--NELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 443 TKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK10895 172 SVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-441 |
4.42e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 44 GEVHALLGENGAGKSTLVKILSG--------YHEPTEGGLVLD---GAEVS--FADSEAGEghgVILIH--QELNLAEQL 108
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLKrfrGTELQnyFKKLYNGE---IKVVHkpQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 ---SVEEniFLGREIKRGwFLDKTAMRAEAKRLLDQlqcdvdprtRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:PRK13409 176 fkgKVRE--LLKKVDERG-KLDEVVERLGLENILDR---------DISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 186 TGREVEILFDQIRRLREqGVAILYISHKLDEIKAIADRVtvlrdgrHIV-TEP----VVdlSKDDMARlmVG-------- 252
Cdd:PRK13409 244 DIRQRLNVARLIRELAE-GKYVLVVEHDLAVLDYLADNV-------HIAyGEPgaygVV--SKPKGVR--VGineylkgy 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 253 --------RDIKQMF---PHRVSDTSAPIV----LSVR----DLSV-PGQVRdasfdlhKGEVLGFAGIVGAGRTALMEA 312
Cdd:PRK13409 312 lpeenmriRPEPIEFeerPPRDESERETLVeypdLTKKlgdfSLEVeGGEIY-------EGEVIGIVGPNGIGKTTFAKL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 313 IIGLRERSSGTIERD----GKPVRIASLQDAKNSGIAYLTKDRKGSGLLLNMDMRPnltlLALEKfgsvIVDRkaeeaal 388
Cdd:PRK13409 385 LAGVLKPDEGEVDPElkisYKPQYIKPDYDGTVEDLLRSITDDLGSSYYKSEIIKP----LQLER----LLDK------- 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 389 ekaieafdiraadrkaKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDI 441
Cdd:PRK13409 450 ----------------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
30-285 |
4.51e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.75 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 30 PAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGY---HEPTEGGLVLDGAEVSfADS--EAGEGHGVILIHQElNL 104
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT-AKTvwDIREKVGIVFQNPD-NQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 105 AEQLSVEENIFLGREikrgwflDKTAMRAEAKRLLDQLQCDVDPRTRIR----DLSVSDRQMVEIAKALSKKADILILDE 180
Cdd:PRK13640 97 FVGATVGDDVAFGLE-------NRAVPRPEMIKIVRDVLADVGMLDYIDsepaNLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 181 PTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEiKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRDIKqmF 259
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIP--F 246
|
250 260
....*....|....*....|....*.
gi 494149220 260 PHRVSDTsapivLSVRDLSVPGQVRD 285
Cdd:PRK13640 247 VYKLKNK-----LKEKGISVPQEINT 267
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
33-258 |
4.55e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.65 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAD------SEAGeghgviLIHQelNLAE 106
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdirNKAG------MVFQ--NPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 QLS---VEENIFLG--------REIKR--GWFLDKTAMrAEAKRLLDQLqcdvdprtrirdLSVSDRQMVEIAKALSKKA 173
Cdd:PRK13633 97 QIVatiVEEDVAFGpenlgippEEIRErvDESLKKVGM-YEYRRHAPHL------------LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 174 DILILDEPTAVL--TGREvEILfDQIRRL-REQGVAILYISHKLDEIkAIADRVTVLRDGRhIVTE-------PVVDLSK 243
Cdd:PRK13633 164 ECIIFDEPTAMLdpSGRR-EVV-NTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGK-VVMEgtpkeifKEVEMMK 239
|
250
....*....|....*
gi 494149220 244 DdmarlmVGRDIKQM 258
Cdd:PRK13633 240 K------IGLDVPQV 248
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-231 |
5.40e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.28 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 28 FGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDG--------AEVSFADSEAGeghgviLIH 99
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknREVPFLRRQIG------MIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 100 QELNLAEQLSVEENIFL--------GREIKR--GWFLDKTAMRAEAKRLLDQlqcdvdprtrirdLSVSDRQMVEIAKAL 169
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIpliiagasGDDIRRrvSAALDKVGLLDKAKNFPIQ-------------LSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 170 SKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-212 |
5.46e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 18 RLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVsfADSEAGE-----G 92
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEachylG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 93 HgvilihqeLN-LAEQLSVEENIFLGREIKRGwflDKTAMRAEAKRLldQLQcDVDPRtRIRDLSVSDRQMVEIAKALSK 171
Cdd:PRK13539 80 H--------RNaMKPALTVAENLEFWAAFLGG---EELDIAAALEAV--GLA-PLAHL-PFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494149220 172 KADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISH 212
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
264-481 |
7.50e-12 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 67.70 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 264 SDTSAPIVLSVRDLSV--PGQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASlQD 338
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVayPGRrpaLRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD-AD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 339 AKNSGIAYLTKdrkgSGLLLNMDMRPNLTLLALEkfgsvivdrkAEEAALEKAIEA--FDIRAADRKA----KVGD---- 408
Cdd:TIGR02857 393 SWRDQIAWVPQ----HPFLFAGTIAENIRLARPD----------ASDAEIREALERagLDEFVAALPQgldtPIGEggag 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 409 FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTdRGKSVILLSSEmPEMLGLSDRIAVM 481
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVVL 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
32-233 |
8.73e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.64 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSeageghGVILIHQELNLAEQ---- 107
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRK------GLMKLRESVGMVFQdpdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 ----LSVEENIFLGreiKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTA 183
Cdd:PRK13636 94 qlfsASVYQDVSFG---AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 184 VLTGREV-EILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:PRK13636 171 GLDPMGVsEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
34-230 |
9.64e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.81 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLdGAEVSFADSEAGEGH------GVILIHQELNLAEQ 107
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLKplrkkvGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 lSVEENIFLGrEIKRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRiRDLSVSDRQM--VEIAKALSKKADILILDEPTAVL 185
Cdd:PRK13634 102 -TVEKDICFG-PMNFG--VSEEDAKQKAREMIELVGLPEELLAR-SPFELSGGQMrrVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 186 TGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:PRK13634 177 DPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
283-486 |
1.01e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpvRIASLqdaknsgiayltkdrkgsgLLLNMDM 362
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSAL-------------------LELGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTllALE--KFGSVIVD-RKAEEAALEKAIEAF-DI-RAADRkaKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:COG1134 100 HPELT--GREniYLNGRLLGlSRKEIDEKFDEIVEFaELgDFIDQ--PVKTYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 438 GIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG1134 176 VGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
270-485 |
1.15e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.88 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 270 IVLSVRDLSVPGQVRD-----------------ASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVR 332
Cdd:PRK15079 7 VLLEVADLKVHFDIKDgkqwfwqppktlkavdgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 333 IASLQD--AKNSGIAYLTKDRKGSgllLNmdmrPNLTLlalekfGSVIVDR-KAEEAALEKAiEAFDiRAADRKAKVG-- 407
Cdd:PRK15079 87 GMKDDEwrAVRSDIQMIFQDPLAS---LN----PRMTI------GEIIAEPlRTYHPKLSRQ-EVKD-RVKAMMLKVGll 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 408 ---------DFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLT-DRGKSVILLSSEMPEMLGLSDR 477
Cdd:PRK15079 152 pnlinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDR 231
|
....*...
gi 494149220 478 IAVMAAGR 485
Cdd:PRK15079 232 VLVMYLGH 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-230 |
1.58e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKST----LVKILsgyhePTEGGLVLDGAEVSFADSEA--GEGHGVILIHQEL 102
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 N--LAEQLSVEENIFLGREIKRGWFldkTAMRAEAKRLLDQLQCDVDPRTRIR---DLSVSDRQMVEIAKALSKKADILI 177
Cdd:PRK15134 372 NssLNPRLNVLQIIEEGLRVHQPTL---SAAQREQQVIAVMEEVGLDPETRHRypaEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 178 LDEPTAVLTgREV--EILfDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:PRK15134 449 LDEPTSSLD-KTVqaQIL-ALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
32-208 |
2.14e-11 |
|
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: 63.03 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEP--TEGGLVLDGAEV--SFADSEAgeghgvilihqelnLAEQ 107
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLdkNFQRSTG--------------YVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 LSVEENIFLGREikrgwfldktAMRAEAKrlldqlqcdvdprtrIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:cd03232 87 QDVHSPNLTVRE----------ALRFSAL---------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|.
gi 494149220 188 REVEILFDQIRRLREQGVAIL 208
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAIL 162
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
410-496 |
2.20e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.80 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 410 SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGRItg 488
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSI-- 224
|
....*...
gi 494149220 489 ILEGNDRN 496
Cdd:PRK13646 225 VSQTSPKE 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
33-231 |
2.28e-11 |
|
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: 63.28 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQELNLaEQLSVEE 112
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR-ISIIPQDPVL-FSGTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 113 NI-FLGR----EIKRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRirDLSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:cd03244 97 NLdPFGEysdeELWQA--LERVGLKEFVESLPGGLDTVVEEGGE--NLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 188 REVEILFDQIRRlREQGVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:cd03244 173 ETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
33-241 |
2.36e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGyhEPTEGGLVlDGAEVSFADSEAGEGHGVI----------LIHQEL 102
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAP-RGARVTGDVTLNGEPLAAIdaprlarlraVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 NLAEQLSVEENIFLGR--EIKRGWFLDKtAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSK--------- 171
Cdd:PRK13547 93 QPAFAFSAREIVLLGRypHARRAGALTH-RDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 172 KADILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
283-503 |
2.49e-11 |
|
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: 63.64 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV------RIASLQDaknsgiayltkdrkgSGL 356
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdRMVVFQN---------------YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 357 LLNMDMRPNLTLlaleKFGSVIVDRKAEE--AALEKAIEAFDIRAADRKaKVGDFSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:TIGR01184 66 LPWLTVRENIAL----AVDRVLPDLSKSErrAIVEEHIALVGLTEAADK-RPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 435 PTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAG---RITGILE---GNDRNEHEIMRH 503
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEvpfPRPRDRLEVVED 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
266-486 |
2.51e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 64.75 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 266 TSAPIVLSVRDLS------------VPGQVR---DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKP 330
Cdd:COG4608 2 AMAEPLLEVRDLKkhfpvrgglfgrTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 331 VRIASLQDAKnsgiayltkdrkgsglllnmDMRPNLTLLALEKFGSVivD-RKAEEAALEKAIEAFDI-RAADRKAKVGD 408
Cdd:COG4608 82 ITGLSGRELR--------------------PLRRRMQMVFQDPYASL--NpRMTVGDIIAEPLRIHGLaSKAERRERVAE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 409 ------------------FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRgksvillssempe 470
Cdd:COG4608 140 llelvglrpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDE------------- 206
|
250 260 270
....*....|....*....|....*....|.
gi 494149220 471 mLGL---------------SDRIAVMAAGRI 486
Cdd:COG4608 207 -LGLtylfishdlsvvrhiSDRVAVMYLGKI 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-238 |
2.75e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.90 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 27 SFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEpTEGGLVLDGaEVSFADSEAGE--------GHGVILI 98
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEG-RVEFFNQNIYErrvnlnrlRRQVSMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQELNLAEqLSVEENIFLGREIKrGWF----LDKTAMRA-EAKRLLDQLQCDVDPRTriRDLSVSDRQMVEIAKALSKKA 173
Cdd:PRK14258 94 HPKPNLFP-MSVYDNVAYGVKIV-GWRpkleIDDIVESAlKDADLWDEIKHKIHKSA--LDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 174 DILILDEPTAVL---TGREVEILFdQIRRLREQgVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPV 238
Cdd:PRK14258 170 KVLLMDEPCFGLdpiASMKVESLI-QSLRLRSE-LTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLV 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
272-487 |
3.03e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 63.73 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV--PGQ------VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV------RIASLQ 337
Cdd:COG4525 4 LTVRHVSVryPGGgqpqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 338 DaknsgiayltkdrkgSGLLLNMDMRPNLTL-LALEKfgsviVDRKAEEAALEKAIEAFDIRAADRKAkVGDFSGGNQQK 416
Cdd:COG4525 84 K---------------DALLPWLNVLDNVAFgLRLRG-----VPKAERRARAEELLALVGLADFARRR-IWQLSGGMRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 417 LLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAA--GRIT 487
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
284-486 |
3.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.56 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIaslqDAKNsgiayLTKDRKGSGLLLNmdmR 363
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY----DKKS-----LLEVRKTVGIVFQ---N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 PNLTLLALE-----KFGSVIVDRKAEEAA--LEKAIEAFDIRAADRKAKvGDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:PRK13639 87 PDDQLFAPTveedvAFGPLNLGLSKEEVEkrVKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
282-486 |
4.70e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.57 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 282 QVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNS-GIAYLTKDRKGSGLLLNM 360
Cdd:PRK13642 22 QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKiGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 361 DMRPNLTLLALEKFGSVivdRKAEEAALEKAIEAFDIRAADRkakvgdFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:PRK13642 102 DVAFGMENQGIPREEMI---KRVDEALLAVNMLDFKTREPAR------LSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 441 IGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
44-231 |
5.00e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.49 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 44 GEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAG---EGHGVILIHQELNLAEQLSVEENIFLgREI 120
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklRAKHVGFVFQSFMLIPTLNALENVEL-PAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 121 KRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL---TG-REVEILFDQ 196
Cdd:PRK10584 115 LRG--ESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLdrqTGdKIADLLFSL 192
|
170 180 190
....*....|....*....|....*....|....*
gi 494149220 197 IrrlREQGVAILYISHKlDEIKAIADRVTVLRDGR 231
Cdd:PRK10584 193 N---REHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
283-496 |
6.01e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.08 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDG----KPVRIASLQdaKNSGIAYLTKDRKGSGLLL 358
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIR--KLVGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 359 NMDMR---PNLTLLALEKfgSVIVDRKAEEAALEKAieafdiraadRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEP 435
Cdd:PRK13644 96 EEDLAfgpENLCLPPIEI--RKRVDRALAEIGLEKY----------RHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 436 TRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEmLGLSDRIAVMAAGRItgILEGNDRN 496
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI--VLEGEPEN 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
272-486 |
6.71e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 61.66 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV------PGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIA 345
Cdd:cd03369 7 IEVENLSVryapdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS-LT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 346 YLTKDRkgsgLLLNMDMRPNLTllalekfgsvIVDRKAEEaalekaieafDIRAADRKAKVGD-FSGGNQQKLLLAKVME 424
Cdd:cd03369 86 IIPQDP----TLFSGTIRSNLD----------PFDEYSDE----------EIYGALRVSEGGLnLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 425 TDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDrgKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
34-231 |
7.98e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.27 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQELNLAEQlSVEEN 113
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ-VALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 114 IFLGREIKRGWF-LDKTAMRAEAKRLLDQLQCDVDprTRIRD----LSVSDRQMVEIAKALSKKADILILDEPTAVL--- 185
Cdd:PRK11176 437 IAYARTEQYSREqIEEAARMAYAMDFINKMDNGLD--TVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALdte 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 186 TGREVEILFDQIRRLReqgvAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:PRK11176 515 SERAIQAALDELQKNR----TSLVIAHRLSTIEK-ADEILVVEDGE 555
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-480 |
8.12e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 44 GEVHALLGENGAGKSTLVKILSG--------YHEPTEGGLVLDgaevSFADSEAGEgHGVILIHQELNLAEQLSVEENI- 114
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGelkpnlgdYDEEPSWDEVLK----RFRGTELQD-YFKKLANGEIKVAHKPQYVDLIp 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 115 --FLG--REIkrgwfLDKTAMRAEAKRLLDQLqcDVDP---RtRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:COG1245 174 kvFKGtvREL-----LEKVDERGKLDELAEKL--GLENildR-DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 188 RE---VEILfdqIRRLREQGVAILYISHKLDEIKAIADRVtvlrdgrHIV-TEP----VVdlSKDDMARlmVG------- 252
Cdd:COG1245 246 YQrlnVARL---IRELAEEGKYVLVVEHDLAILDYLADYV-------HILyGEPgvygVV--SKPKSVR--VGinqyldg 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 253 ---------RD--IK-QMFPHRVSDTSAPIV----LSVR----DLSV-PGQVrdasfdlHKGEVLGFAGIVGAGRTALME 311
Cdd:COG1245 312 ylpeenvriRDepIEfEVHAPRREKEEETLVeypdLTKSyggfSLEVeGGEI-------REGEVLGIVGPNGIGKTTFAK 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 312 AIIGLRERSSGTIERDG----KPVRIASLQDAknSGIAYL---TKDRKGSGLLLNMDMRPnltlLALEKfgsvIVDRkae 384
Cdd:COG1245 385 ILAGVLKPDEGEVDEDLkisyKPQYISPDYDG--TVEEFLrsaNTDDFGSSYYKTEIIKP----LGLEK----LLDK--- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 385 eaalekaieafdiraadrkaKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTD-RGKSVIL 463
Cdd:COG1245 452 --------------------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEnRGKTAMV 511
|
490
....*....|....*..
gi 494149220 464 LSSEMPEMLGLSDRIAV 480
Cdd:COG1245 512 VDHDIYLIDYISDRLMV 528
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
36-230 |
8.28e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSeAGEGHGVILIHQElnLAEQLSVEENIf 115
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY-SYRSQRIRMIFQD--PSTSLNPRQRI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 116 lgreikrGWFLD-----KTAMRAEA--KRLLDQL-QCDVDPRTRI---RDLSVSDRQMVEIAKALSKKADILILDEPTAV 184
Cdd:PRK15112 107 -------SQILDfplrlNTDLEPEQreKQIIETLrQVGLLPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494149220 185 LTGREVEILFDQIRRLRE-QGVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
260-504 |
8.82e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 260 PHRVSDTSAPIVLSVRDL--SVPGQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV-RIA 334
Cdd:PRK11607 8 PQAKTRKALTPLLEIRNLtkSFDGQhaVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLsHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 335 SLQDAKNSGIayltkdrKGSGLLLNMDMRPNLTL-LALEKFGSV-IVDRKAEEAALEKAIEAfdiraADRKAKvgDFSGG 412
Cdd:PRK11607 88 PYQRPINMMF-------QSYALFPHMTVEQNIAFgLKQDKLPKAeIASRVNEMLGLVHMQEF-----AKRKPH--QLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 413 NQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRITGILE 491
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250
....*....|...
gi 494149220 492 GNDRNEHEIMRHA 504
Cdd:PRK11607 234 PEEIYEHPTTRYS 246
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-241 |
9.53e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.42 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 28 FGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEG----GLVLDGAEVSFADSEAGE-GHGVILIHQEL 102
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysGDVLLGGRSIFNYRDVLEfRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 103 NlAEQLSVEENIFLGreIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRD----LSVSDRQMVEIAKALSKKADILIL 178
Cdd:PRK14271 111 N-PFPMSIMDNVLAG--VRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 179 DEPTAVLTGREVEILFDQIRRLREQgVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
283-486 |
1.04e-10 |
|
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: 61.97 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDaKNSGIAYltkdrKGSGLLLNMDM 362
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNVGFVF-----QHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTllalekFGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGD-----FSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:cd03296 92 FDNVA------FGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADrypaqLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 438 GIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-212 |
1.04e-10 |
|
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: 61.22 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEgHGVILI 98
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQElNLAEQLSVEENIFLGREIKRGwfldktamraeAKRLLDQLQCDVDPRTR----IRDLSVSDRQMVEIAKALSKKAD 174
Cdd:TIGR01189 80 HLP-GLKPELSALENLHFWAAIHGG-----------AQRTIEDALAAVGLTGFedlpAAQLSAGQQRRLALARLWLSRRP 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 494149220 175 ILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISH 212
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
269-486 |
1.23e-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: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 269 PIVLSVRDLSVPGQ----------VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERS--SGTIERDGKPVRIASL 336
Cdd:cd03213 1 GVTLSFRNLTVTVKsspsksgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 337 qdaknsgiayltkdRKGSGLLLNMDM-RPNLTllalekfgsvivdrkaeeaalekAIEAFDIRAADRKakvgdFSGGNQQ 415
Cdd:cd03213 81 --------------RKIIGYVPQDDIlHPTLT-----------------------VRETLMFAAKLRG-----LSGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 416 KLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVIL----LSSEMPEMLglsDRIAVMAAGRI 486
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICsihqPSSEIFELF---DKLLLLSQGRV 190
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
409-509 |
1.48e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.04 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 409 FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRgKSVILLSSEMPEMLGLSDRIAVMAAGRItg 488
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRL-- 240
|
90 100
....*....|....*....|....*..
gi 494149220 489 ILEG------NDRNEHEIMRHATGISG 509
Cdd:PRK14271 241 VEEGpteqlfSSPKHAETARYVAGLSG 267
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
32-233 |
1.55e-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: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEP--TEGGLVLDGA---EVSFADSeageghgVILIHQELNLAE 106
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldKRSFRKI-------IGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 107 QLSVEENiflgreikrgwfLDKTAmraeakrlldqlqcdvdprtRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLT 186
Cdd:cd03213 96 TLTVRET------------LMFAA--------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 187 GREVEILFDQIRRLREQGVAILYISHKL-DEIKAIADRVTVLRDGRHI 233
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
285-486 |
1.62e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTierdgkpVRIASLQDAKNSGIAYLTKDRKGSGLLLNMDMRP 364
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGK-------VTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 NL--TLLALEKFGSV---IVDRKAEEAALEKaIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGI 439
Cdd:PRK13643 97 LFeeTVLKDVAFGPQnfgIPKEKAEKIAAEK-LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494149220 440 DIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
287-506 |
1.68e-10 |
|
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: 63.31 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 287 SFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSS--GTIERDGKPVRIASLQDAKNSGIAYLTKDRKgsgLLLNMDMRP 364
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIVIIHQELT---LVPELSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 NLTLLALEKFGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTK 444
Cdd:TIGR02633 98 NIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKET 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 445 SQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGILEGNDRNEHEIMRHATG 506
Cdd:TIGR02633 178 EILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
283-493 |
2.05e-10 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 60.70 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVR---IASLQdaknSGIAYLTKDRkgsgLLLN 359
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdisRKSLR----SMIGVVLQDT----FLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 MDMRPNLTLlalekFGSVIVDRKAEEAALEKAIEAFDIRAADRKAKV-----GDFSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:cd03254 91 GTIMENIRL-----GRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 435 PTRGIDIGTKSQIYHFIGDLTDrGKSVILLSSEMPEMLGlSDRIAVMAAGRItgILEGN 493
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKI--IEEGT 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
31-182 |
2.10e-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: 60.75 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 31 AQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSG---YHEPTEGGLVLDGAEVSFADSEAGEGHGviliHQELNLAEQ 107
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQKCVAYV----RQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 LSVEE-----NIFLGREIKRGWFLDKtamRAEAKRLLDQLQCDVDpRTRIRDLSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:cd03234 96 LTVREtltytAILRLPRKSSDAIRKK---RVEDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
283-486 |
3.01e-10 |
|
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: 60.20 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIAYLTKDrkgsGLLLNMDM 362
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR-ISIIPQD----PVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTllALEKFGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVGD-FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDI 441
Cdd:cd03244 95 RSNLD--PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 442 GTKSQIYHFIGDlTDRGKSVILLSSEMPEMLGlSDRIAVMAAGRI 486
Cdd:cd03244 173 ETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
260-485 |
3.35e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 260 PHRvSDTSAPIVLSVRDLSVPGQ--------VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV 331
Cdd:PRK10261 2 PHS-DELDARDVLAVENLNIAFMqeqqkiaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 332 RIASLQDAK-NSGIAYLTKDRKGSGLLLnMDMRPNLTLLALEKFGSVIVDR------KAEEAALEKAIEAFD-IRAADRK 403
Cdd:PRK10261 81 RRRSRQVIElSEQSAAQMRHVRGADMAM-IFQEPMTSLNPVFTVGEQIAESirlhqgASREEAMVEAKRMLDqVRIPEAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 404 AKVGDF----SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRI 478
Cdd:PRK10261 160 TILSRYphqlSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRV 239
|
....*..
gi 494149220 479 AVMAAGR 485
Cdd:PRK10261 240 LVMYQGE 246
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
283-489 |
3.54e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.49 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVR---IASLQDAknsgIAYLTKDrkgsGLLLN 359
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdltLESLRRQ----IGVVPQD----TFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 MDMRPNLTllalekFGsvivdrkAEEAALEkaieafDIRAADRKAKVGDF-------------------SGGNQQKLLLA 420
Cdd:COG1132 428 GTIRENIR------YG-------RPDATDE------EVEEAAKAAQAHEFiealpdgydtvvgergvnlSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 421 KVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTdRGKSVIL----LSSempemLGLSDRIAVMAAGRITGI 489
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIViahrLST-----IRNADRILVLDDGRIVEQ 555
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
29-241 |
3.55e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYhepTEGGLVLDGAEVSFADSEAGE----------GHGVILI 98
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRFDDIDLLRlsprerrklvGHNVSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 HQE----LNLAEQLSVE--ENI----FLGREIKRGWFLDKTAMRaeakrLLDQLQCDvDPRTRIR----DLSVSDRQMVE 164
Cdd:PRK15093 95 FQEpqscLDPSERVGRQlmQNIpgwtYKGRWWQRFGWRKRRAIE-----LLHRVGIK-DHKDAMRsfpyELTEGECQKVM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 165 IAKALSKKADILILDEPTAVLTGREVEILFDQIRRLREQ-GVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
37-249 |
3.85e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 37 VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHgVILIHQELNLAEQLsveenifL 116
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSAVFTDFHLFDQL-------L 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 117 GREikrGWFLDKTAMRAEAKRLldQLQCDVDPRT-RIRDLSVSDRQMVEIAK--ALSKKADILILDEPTAvltgreveil 193
Cdd:PRK10522 414 GPE---GKPANPALVEKWLERL--KMAHKLELEDgRISNLKLSKGQKKRLALllALAEERDILLLDEWAA---------- 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 194 fDQ---IRR---------LREQGVAILYISHKlDEIKAIADRVTVLRDGR--HIVTEPVVDLSKDDMARL 249
Cdd:PRK10522 479 -DQdphFRRefyqvllplLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQlsELTGEERDAASRDAVART 546
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
284-486 |
3.98e-10 |
|
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: 59.94 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVR---IASLQDAknsgIAYLTKDRkgsgLLLNM 360
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevtLDSLRRA----IGVVPQDT----VLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 361 DMRPNLtllaleKFGSVIV-DRKAEEAALEKAIEAFDIRAADR-KAKVGD----FSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:cd03253 90 TIGYNI------RYGRPDAtDEEVIEAAKAAQIHDKIMRFPDGyDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 435 PTRGIDIGTKSQIYHFIGDLTdRGKSVILLSSEMPEMLGlSDRIAVMAAGRI 486
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-213 |
4.21e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfaDSEAGEGHGVILIHQELNLAEQLSVEE 112
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--KDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 113 NIFLGREIKRGWF-LDKTAMRAEAKRLLDqLQCDVdprtrirdLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVE 191
Cdd:PRK13540 94 NCLYDIHFSPGAVgITELCRLFSLEHLID-YPCGL--------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 494149220 192 ILFDQIRRLREQGVAILYISHK 213
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
36-231 |
4.70e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEP---TEGGLVLDGAEVsfadseageghgVILIHQELNL--AEQLSV 110
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREI------------LNLPEKELNKlrAEQISM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 111 eenIF------------LGREIKRGWFLDKTAMRAEA----KRLLDQLQCDvDPRTRIR----DLSVSDRQMVEIAKALS 170
Cdd:PRK09473 102 ---IFqdpmtslnpymrVGEQLMEVLMLHKGMSKAEAfeesVRMLDAVKMP-EARKRMKmyphEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 171 KKADILILDEPTAVLtgrEVEILfDQIRRL-----REQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK09473 178 CRPKLLIADEPTTAL---DVTVQ-AQIMTLlnelkREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
31-233 |
4.90e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 31 AQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfadSEAGEgHGVILIHQELNLAEQLS- 109
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT---PETGN-KNLKKLRKKVSLVFQFPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 110 --VEENIFLgREIKRG----WFLDKTAmRAEAKRLLDQLQCDVDPRTRIR-DLSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:PRK13641 96 aqLFENTVL-KDVEFGpknfGFSEDEA-KEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 183 AVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
289-486 |
5.91e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.76 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 289 DLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAYLtkdRKGSGLLL-NMDMRPNLT 367
Cdd:PRK11264 25 EVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQL---RQHVGFVFqNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 368 LLALEKFGSVIVDRKAEEAALEKAIEAFdiraadrkAKVG----------DFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:PRK11264 102 VLENIIEGPVIVKGEPKEEATARARELL--------AKVGlagketsyprRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 438 GIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
33-212 |
6.24e-10 |
|
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: 59.04 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFD-VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEghGVILIHQELNLAEQLSVE 111
Cdd:cd03231 14 ALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR--GLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 112 ENIFlgreikrgwFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVE 191
Cdd:cd03231 92 ENLR---------FWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 494149220 192 ILFDQIRRLREQGVAILYISH 212
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-230 |
6.81e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDG---AEVSFADSEAGeghgVILIHQE-------- 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniAKIGLHDLRFK----ITIIPQDpvlfsgsl 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 -LNLA--EQLSvEENIFlgreikrgWFLDKTAMRAEAKRLLDQL--QCDVDPRtrirDLSVSDRQMVEIAKALSKKADIL 176
Cdd:TIGR00957 1377 rMNLDpfSQYS-DEEVW--------WALELAHLKTFVSALPDKLdhECAEGGE----NLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494149220 177 ILDEPTAVLTgREVEILFDQIRRLREQGVAILYISHKLDEIKAIAdRVTVLRDG 230
Cdd:TIGR00957 1444 VLDEATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1495
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
283-486 |
8.03e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 59.17 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIAYLTKDRkgsgLLLNMDM 362
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQDV----FLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTllalekFGSVIVDRKAEEAALEKAI---------EAFDIRAADRKAKVgdfSGGNQQKLLLAKVMETDPDIVIID 433
Cdd:cd03251 93 AENIA------YGRPGATREEVEEAARAANahefimelpEGYDTVIGERGVKL---SGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 434 EPTRGIDIGTKSQIYHFIGDLT-DRGKSVIL--LSSEMPemlglSDRIAVMAAGRI 486
Cdd:cd03251 164 EATSALDTESERLVQAALERLMkNRTTFVIAhrLSTIEN-----ADRIVVLEDGKI 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
283-486 |
8.41e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKnsgiaYLTKDRKGSGLL---LN 359
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQ-----LKVADKNQLRLLrtrLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 M-----DMRPNLTLL--ALEKFGSVIVDRKAEeaALEKAIEAFDIRAADRKAKVG---DFSGGNQQKLLLAKVMETDPDI 429
Cdd:PRK10619 96 MvfqhfNLWSHMTVLenVMEAPIQVLGLSKQE--ARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 430 VIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
293-486 |
8.86e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 8.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 293 GEVLGFAGIVGAGRTALMEAIIGLRERS---SGTIERDGKPVriaslqDAKnsgiayltKDRKGSGLLLNMDM------- 362
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI------DAK--------EMRAISAYVQQDDLfiptltv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKFGSViVDRKAEEAALEKAIEAFDIRAAdRKAKVGD------FSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:TIGR00955 117 REHLMFQAHLRMPRR-VTKKEKRERVDEVLQALGLRKC-ANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDRGKSVILL----SSEMPEMLglsDRIAVMAAGRI 486
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGRV 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
37-255 |
9.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.72 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 37 VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQELNLAEQLSVEENIFL 116
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 117 GREiKRGWFLDKTAMRAEaKRLLDQLQCDVDPRTRIRdLSVSDRQMVEIAKALSKKADILILDEPTAVL--TGR-EVEIL 193
Cdd:PRK13642 106 GME-NQGIPREEMIKRVD-EALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLdpTGRqEIMRV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 194 FDQIRrlREQGVAILYISHKLDEiKAIADRVTVLRDGRHIVTEPVVDLSKDDMARLMVGRDI 255
Cdd:PRK13642 183 IHEIK--EKYQLTVLSITHDLDE-AASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDV 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
285-489 |
1.45e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSG-TIERDGK-PVRIASLQDAKNSgiayltkdRKGSGLLLNMdm 362
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAiPANLKKIKEVKRL--------RKEIGLVFQF-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 rPNLTLL--ALEK---FGSVIVDRKAEEAaLEKAIEAFDIRAADRK-AKVGDF--SGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:PRK13645 99 -PEYQLFqeTIEKdiaFGPVNLGENKQEA-YKKVPELLKLVQLPEDyVKRSPFelSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 435 PTRGID-IGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGI 489
Cdd:PRK13645 177 PTGGLDpKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-237 |
1.59e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.74 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVsfadSEAGEGHGVILIHQ--ELNLAEQLSVE 111
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQKNLVAYVPQseEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 112 ENIFLGREIKRGWFldkTAMRAEAKRLLDQLQCDVDP---RTR-IRDLSVSDRQMVEIAKALSKKADILILDEP-TAVLT 186
Cdd:PRK15056 99 DVVMMGRYGHMGWL---RRAKKRDRQIVTAALARVDMvefRHRqIGELSGGQKKRVFLARAIAQQGQVILLDEPfTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 187 GREVEILfDQIRRLREQGVAILYISHKLDEIKAIADrVTVLRDGRHIVTEP 237
Cdd:PRK15056 176 KTEARII-SLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGP 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
285-487 |
1.62e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.18 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaslqdakNSGIAYLTKDRKGSGLLLN-MDMR 363
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV---------NDPKVDERLIRQEAGMVFQqFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 PNLTllALEK--FGSVIVdRKAEEAALEKaieafdiRAADRKAKVG----------DFSGGNQQKLLLAKVMETDPDIVI 431
Cdd:PRK09493 90 PHLT--ALENvmFGPLRV-RGASKEEAEK-------QARELLAKVGlaerahhypsELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 432 IDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
280-486 |
1.76e-09 |
|
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: 58.27 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 280 PGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIAYLTKDrkgsGLLLN 359
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ-VGVVLQE----NVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 MDMRPNLtllALEKFGSVIvdRKAEEAA--------LEKAIEAFDIRAADRKAKVgdfSGGNQQKLLLAKVMETDPDIVI 431
Cdd:cd03252 90 RSIRDNI---ALADPGMSM--ERVIEAAklagahdfISELPEGYDTIVGEQGAGL---SGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 432 IDEPTRGIDIGTKSQIYHFIGDLTDrGKSVILLSSEMPEMLGlSDRIAVMAAGRI 486
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
32-234 |
1.77e-09 |
|
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: 60.22 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDG---AEVSFADseageghgvilIHQELNLAEQ- 107
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQAS-----------LRAAIGIVPQd 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 --L---SVEENIFLGR------EIKRgwfldktAMRAEA-----KRLLDQLQcdvdprTRI--RDLSVS--DRQMVEIAK 167
Cdd:COG5265 441 tvLfndTIAYNIAYGRpdaseeEVEA-------AARAAQihdfiESLPDGYD------TRVgeRGLKLSggEKQRVAIAR 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 168 ALSKKADILILDEPTAVL-TGREVEILfDQIRRLReQGVAILYISHKLDEIkAIADRVTVLRDGRhIV 234
Cdd:COG5265 508 TLLKNPPILIFDEATSALdSRTERAIQ-AALREVA-RGRTTLVIAHRLSTI-VDADEILVLEAGR-IV 571
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
28-233 |
1.81e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 28 FGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSgyhepTEGGLVldgAEVSFADSEAGEGHGV-------ILIHQ 100
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN-----RMNDLN---PEVTITGSIVYNGHNIysprtdtVDLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 101 ELNLAEQ------LSVEENIFLGREIKRgwFLDKTAMRAEAKRLLDQLQCDVDPRTRIRD----LSVSDRQMVEIAKALS 170
Cdd:PRK14239 87 EIGMVFQqpnpfpMSIYENVVYGLRLKG--IKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 171 KKADILILDEPTAVL---TGREVEilfDQIRRLREQgVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:PRK14239 165 TSPKIILLDEPTSALdpiSAGKIE---ETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
267-486 |
1.84e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.09 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 267 SAPIVLSVRDLSV------PGQVR---DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERdgKPVRIASLQ 337
Cdd:PRK13631 17 SDDIILRVKNLYCvfdekqENELValnNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 338 DAKNSGIAYLTKD-------RKGSGLLLNMdmrPNLTLL--ALEK---FGSVIVDRKAEEAAlEKA---IEAFDIRAADR 402
Cdd:PRK13631 95 NNHELITNPYSKKiknfkelRRRVSMVFQF---PEYQLFkdTIEKdimFGPVALGVKKSEAK-KLAkfyLNKMGLDDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 403 KAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMA 482
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
....
gi 494149220 483 AGRI 486
Cdd:PRK13631 251 KGKI 254
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
288-486 |
1.86e-09 |
|
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: 57.50 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 288 FDLH--KGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV-------RIASLQDAKNSGIAYLTKDrKGSGLLL 358
Cdd:cd03298 17 FDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaappadRPVSMLFQENNLFAHLTVE-QNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 359 NmdmrPNLTLLAlekfgsviVDRKAEEAALEK-AIEAFDIRAAdrkakvGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:cd03298 96 S----PGLKLTA--------EDRQAIEVALARvGLAGLEKRLP------GELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 438 GIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03298 158 ALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-231 |
2.24e-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: 57.42 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 13 TEGKIRLSGrkICKSFGP--AQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAg 90
Cdd:cd03369 3 EHGEIEVEN--LSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 91 eghgvilIHQELNLAEQlsveeniflgreikrgwflDKTAMRAEAKRLLDQL--QCDVDPRTRIR------DLSVSDRQM 162
Cdd:cd03369 80 -------LRSSLTIIPQ-------------------DPTLFSGTIRSNLDPFdeYSDEEIYGALRvsegglNLSQGQRQL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 163 VEIAKALSKKADILILDEPTAVLTgREVEILFDQIRRLREQGVAILYISHKLDEIkAIADRVTVLRDGR 231
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASID-YATDALIQKTIREEFTNSTILTIAHRLRTI-IDYDKILVMDAGE 200
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
34-231 |
2.44e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.29 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGaEVSfadseageghgVILIHQELNlaEQLSVEEN 113
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVS-----------VIAISAGLS--GQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 114 I--------FLGREIKRgwFLDKTAMRAEAKRLLDQlqcdvdprtRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:PRK13546 106 IefkmlcmgFKRKEIKA--MTPKIIEFSELGEFIYQ---------PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 186 TGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-230 |
2.50e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAD-----------SEAGeghgviLIHQE 101
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqidaiklrKEVG------MVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIflGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRD----LSVSDRQMVEIAKALSKKADILI 177
Cdd:PRK14246 99 PNPFPHLSIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 178 LDEPTA---VLTGREVEILFDQIRRlreqGVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:PRK14246 177 MDEPTSmidIVNSQAIEKLITELKN----EIAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-233 |
2.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAGEghgVILIHQELNLAEQL--- 108
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKE---VKRLRKEIGLVFQFpey 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 -----SVEENIFLGrEIKRGwfLDKTAMRAEAKRLLDQLQCdvdPRTRIR----DLSVSDRQMVEIAKALSKKADILILD 179
Cdd:PRK13645 102 qlfqeTIEKDIAFG-PVNLG--ENKQEAYKKVPELLKLVQL---PEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 180 EPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
36-227 |
2.92e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.56 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS-FADSEAGEGHGVI-LIHQE----LN------ 103
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgMKDDEWRAVRSDIqMIFQDplasLNprmtig 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 --LAEQLSVEENIFLGREIKrgwflDKT-AMRAEAKrLLDQL-----------QCdvdprtrirdlsvsdrQMVEIAKAL 169
Cdd:PRK15079 119 eiIAEPLRTYHPKLSRQEVK-----DRVkAMMLKVG-LLPNLinryphefsggQC----------------QRIGIARAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 170 SKKADILILDEPTAVLtgrEVEI------LFDQIRRlrEQGVAILYISHKLDEIKAIADRVTVL 227
Cdd:PRK15079 177 ILEPKLIICDEPVSAL---DVSIqaqvvnLLQQLQR--EMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
285-468 |
2.96e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.82 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpVRIASL-QDAKNSGIAYLTKDRkgsglllNMDMR 363
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-LRIGYVpQKLYLDTTLPLTVNR-------FLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 PNltllalekfgsviVDRKAEEAALEKAIEAFDIRAADRKakvgdFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGT 443
Cdd:PRK09544 94 PG-------------TKKEDILPALKRVQAGHLIDAPMQK-----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*.
gi 494149220 444 KSQIYHFIGDL-TDRGKSVILLSSEM 468
Cdd:PRK09544 156 QVALYDLIDQLrRELDCAVLMVSHDL 181
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
271-486 |
2.96e-09 |
|
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: 59.31 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSV----PGQ----VRDASFDLHKGEVLGFAGIVGAGR--TALmeAIIGL----RERSSGTIERDGKPVRIAS- 335
Cdd:COG4172 6 LLSVEDLSVafgqGGGtveaVKGVSFDIAAGETLALVGESGSGKsvTAL--SILRLlpdpAAHPSGSILFDGQDLLGLSe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 336 --LQDAKNSGIAY------------LTKDRK-GSGLLLNMDMRPnltllalekfgsvivdrkaeEAALEKAIEAFD---I 397
Cdd:COG4172 84 reLRRIRGNRIAMifqepmtslnplHTIGKQiAEVLRLHRGLSG--------------------AAARARALELLErvgI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 398 RAADRKAKvgDF----SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEmpemL 472
Cdd:COG4172 144 PDPERRLD--AYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHD----L 217
|
250
....*....|....*...
gi 494149220 473 GL----SDRIAVMAAGRI 486
Cdd:COG4172 218 GVvrrfADRVAVMRQGEI 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
280-484 |
3.09e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.79 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 280 PGQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQdaknSGIAYltkdrKGSGLL 357
Cdd:PRK11248 12 GGKpaLEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVF-----QNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 358 LNMDMRPNLTlLALEKFGsviVDRKAEEAALEKAIEAFDIRAADRKaKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:PRK11248 83 PWRNVQDNVA-FGLQLAG---VEKMQRLEIAHQMLKKVGLEGAEKR-YIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 438 GIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAG 484
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
284-485 |
3.13e-09 |
|
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: 56.71 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERdgkpvriaslqdakNSGIAYLTKdrkgSGLLLNMDMR 363
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--------------PGSIAYVSQ----EPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 PNLTllalekFGSVIVDRKAEEA----ALEKAIEAFDirAADRkAKVGD----FSGGNQQKLLLAKVMETDPDIVIIDEP 435
Cdd:cd03250 84 ENIL------FGKPFDEERYEKVikacALEPDLEILP--DGDL-TEIGEkginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 436 TRGIDIGTKSQIYH--FIGDLTDrGKSVILLSSEMpEMLGLSDRIAVMAAGR 485
Cdd:cd03250 155 LSAVDAHVGRHIFEncILGLLLN-NKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-230 |
3.59e-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: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 39 VDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEageghgvilIHQELNLAEQLSVEENIFLGR 118
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---------VHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 119 E---------------IKR--GWFLDKTAMRAEAKRLLDQLqcdvdprtrirdlSVSDRQMVEIAKALSKKADILILDEP 181
Cdd:TIGR01257 2031 EhlylyarlrgvpaeeIEKvaNWSIQSLGLSLYADRLAGTY-------------SGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 182 TAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDG 230
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-235 |
3.59e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.32 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGL----VLDGAEVSFADSEAGEGHGVILIHQE 101
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 L--------NLAE-QL---SVEENIFLGrEIKRGwfLDKTAMRAEAKRLLDQLQCDVDPRTRIR-DLSVSDRQMVEIAKA 168
Cdd:PRK13631 114 LrrrvsmvfQFPEyQLfkdTIEKDIMFG-PVALG--VKKSEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 169 LSKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVT 235
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
32-233 |
4.10e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.79 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVL-----------DGAEVSFADSEAGEGH------- 93
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKEKVLEKLVIQKTRfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 -------GVILIHQELNLAEQlSVEENIFLGreiKRGWFLDKTAMRAEAKRLLDQLQCDVD--PRTRIrDLSVSDRQMVE 164
Cdd:PRK13651 101 keirrrvGVVFQFAEYQLFEQ-TIEKDIIFG---PVSMGVSKEEAKKRAAKYIELVGLDESylQRSPF-ELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 165 IAKALSKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
37-231 |
4.63e-09 |
|
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: 58.66 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 37 VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgeghgviliHQELnlaeqLSVeenIF- 115
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA---------YRQL-----FSA---VFs 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 116 --------LGreikrgwfLDKTAMRAEAKRLLDQLQcdVDPRTRIRDLSVSDRqmveiakALSK--------------KA 173
Cdd:COG4615 414 dfhlfdrlLG--------LDGEADPARARELLERLE--LDHKVSVEDGRFSTT-------DLSQgqrkrlallvalleDR 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 174 DILILDE------PTAvltgREV---EILFDqirrLREQGVAILYISHKlDEIKAIADRVTVLRDGR 231
Cdd:COG4615 477 PILVFDEwaadqdPEF----RRVfytELLPE----LKARGKTVIAISHD-DRYFDLADRVLKMDYGK 534
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
284-486 |
4.82e-09 |
|
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: 56.81 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpVRIASLQDAKnsgiayLTKDRKGSGLLLNmdmR 363
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG--TDINKLKGKA------LRQLRRQIGMIFQ---Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 PNLT--LLALEkfgSVIVDRKAE------------EAALEKAIEAFDIRAADRKA--KVGDFSGGNQQKLLLAKVMETDP 427
Cdd:cd03256 87 FNLIerLSVLE---NVLSGRLGRrstwrslfglfpKEEKQRALAALERVGLLDKAyqRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
271-487 |
5.31e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.33 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSV--PGQ----VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDA-KNSG 343
Cdd:PRK13635 5 IIRVEHISFryPDAatyaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVrRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 344 IAYLTKDRKGSGLLLNMDMrpnltLLALEKFG---SVIVDRkAEEAALEKAIEAFDIRAADRkakvgdFSGGNQQKLLLA 420
Cdd:PRK13635 85 MVFQNPDNQFVGATVQDDV-----AFGLENIGvprEEMVER-VDQALRQVGMEDFLNREPHR------LSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 421 KVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGK-SVILLSSEMPEMLGlSDRIAVMAAGRIT 487
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
283-488 |
5.59e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 56.59 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEaIIGLRER-SSGTIERDGKPvrIASLQDAKnsgiayLTKDRK--------G 353
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRpTSGEVLIDGQD--ISSLSERE------LARLRRrhigfvfqF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 354 SGLLlnmdmrPNLT-----LLALEKFGsviVDRKAEEAALEKAIEAFDIraADR-KAKVGDFSGGNQQKLLLAKVMETDP 427
Cdd:COG1136 95 FNLL------PELTalenvALPLLLAG---VSRKERRERARELLERVGL--GDRlDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITG 488
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
385-491 |
6.41e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 385 EAALeKAIEAFD-IRAADRKAKVgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGK-SVI 462
Cdd:PRK14258 128 ESAL-KDADLWDeIKHKIHKSAL-DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMV 205
|
90 100 110
....*....|....*....|....*....|.
gi 494149220 463 LLSSEMPEMLGLSDRIAVMAA--GRITGILE 491
Cdd:PRK14258 206 IVSHNLHQVSRLSDFTAFFKGneNRIGQLVE 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-231 |
6.94e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.30 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfADSEAGEGHGVILIHQELNLAEQl 108
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAALRQAISVVSQRVHLFSA- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGreikrgwflDKTAMRAEAKRLLDQ--LQCDVDPRTRI--------RDLSVSDRQMVEIAKALSKKADILIL 178
Cdd:PRK11160 429 TLRDNLLLA---------APNASDEALIEVLQQvgLEKLLEDDKGLnawlgeggRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 179 DEPTAVLTGR-EVEILfdqiRRLRE--QGVAILYISHKLdeiKAIA--DRVTVLRDGR 231
Cdd:PRK11160 500 DEPTEGLDAEtERQIL----ELLAEhaQNKTVLMITHRL---TGLEqfDRICVMDNGQ 550
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
253-502 |
7.65e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 253 RDIKQMFphrvsDTSAPIVLSVRDlsvpgqvrDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIE------- 325
Cdd:PRK13651 6 KNIVKIF-----NKKLPTELKALD--------NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdek 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 326 RDGKPVRIAS------LQDAKNSGIAYLTKDRKGSGLLLNMdMRPNLTLLALEK---FGSVIVDRKAEEAaLEKAIEAFD 396
Cdd:PRK13651 73 NKKKTKEKEKvleklvIQKTRFKKIKKIKEIRRRVGVVFQF-AEYQLFEQTIEKdiiFGPVSMGVSKEEA-KKRAAKYIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 397 IRAADR---KAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID-IGTKsQIYHFIGDLTDRGKSVILLSSEMPEML 472
Cdd:PRK13651 151 LVGLDEsylQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVK-EILEIFDNLNKQGKTIILVTHDLDNVL 229
|
250 260 270
....*....|....*....|....*....|
gi 494149220 473 GLSDRIAVMAAGRITgilegNDRNEHEIMR 502
Cdd:PRK13651 230 EWTKRTIFFKDGKII-----KDGDTYDILS 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
271-484 |
1.02e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.32 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSV----PGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRE-----RSSGTIERDGKPV---RIASLQD 338
Cdd:PRK14239 5 ILQVSDLSVyynkKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 339 AKNSGIAYLTKDRkgsgllLNMDMRPNLtLLALEKFGsvIVDRKAEEAALEKAIEAFDI--RAADR--KAKVGdFSGGNQ 414
Cdd:PRK14239 85 RKEIGMVFQQPNP------FPMSIYENV-VYGLRLKG--IKDKQVLDEAVEKSLKGASIwdEVKDRlhDSALG-LSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 415 QKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRgKSVILLSSEMPEMLGLSDRIAVMAAG 484
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-466 |
1.15e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 38 SVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLD---GAEVSFADSEAgeghgviLIHQEL--NLAEQLSVEE 112
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshITRLSFEQLQK-------LVSDEWqrNNTDMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 113 NIFlGR---EIkrgwFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGRE 189
Cdd:PRK10938 96 DDT-GRttaEI----IQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 190 VEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDLSKDDM-ARLMVGRDIKQM-FP------- 260
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALvAQLAHSEQLEGVqLPepdepsa 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 261 -HRVSDTSAPIVLsvRDLSVPGQVR----DASFDLHKGEVLGFAGIVGAGRTALMEAIIG-----------L--RERSSG 322
Cdd:PRK10938 251 rHALPANEPRIVL--NNGVVSYNDRpilhNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLfgRRRGSG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 323 -TIerdgkpvriaslQDAKnSGIAYLTKDrkgsgllLNMDMRPNLTLLalekfgSVIV--------------DRKAEEAA 387
Cdd:PRK10938 329 eTI------------WDIK-KHIGYVSSS-------LHLDYRVSTSVR------NVILsgffdsigiyqavsDRQQKLAQ 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 388 LEKAIEAFDIRAADrkAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSS 466
Cdd:PRK10938 383 QWLDILGIDKRTAD--APFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVS 459
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-227 |
1.20e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.84 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 44 GEVHALLGENGAGKSTLVKILSG--------YHEPTEGGLVLD---GAEVS--FADSEAGEGHgVILIHQELNL---AEQ 107
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDefrGSELQnyFTKLLEGDVK-VIVKPQYVDLipkAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 LSVEENifLGREIKRGwFLDKTAMRAEAKRLLDQlqcdvdprtRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTG 187
Cdd:cd03236 105 GKVGEL--LKKKDERG-KLDELVDQLELRHVLDR---------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494149220 188 REVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVL 227
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
34-231 |
1.38e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.62 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHePTEGGLVLDGAEVSFADSEAGEGH-----------GVILIHQ-- 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHraylsqqqsppFAMPVFQyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 101 ELNLAEQLSVEENIFLGREIkrgwfldktamrAEAKRLLDQLQCDVDprtrirDLSVSDRQMVEIAKAL-------SKKA 173
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQL------------AEALGLEDKLSRPLT------QLSGGEWQRVRLAAVLlqvwptiNPEG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 174 DILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:COG4138 153 QLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
283-487 |
1.45e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASlqdaknSGIAYLTKDRKGSGLLLNMDM 362
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLS------SAAKAELRNQKLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTllALEKFG-SVIVDRKAEEAALEKAIE-----AFDIRAADRKAkvgDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:PRK11629 99 LPDFT--ALENVAmPLLIGKKKPAEINSRALEmlaavGLEHRANHRPS---ELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-237 |
1.48e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 28 FGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHE-----PTEGGLVLDGAEVSFADSEAGE-GHGVILIHQE 101
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIEvRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 LNLAEQLSVEENIFLGREIKR------------GWFLDKTAMRAEAK-RLLDQLQcdvdprtrirDLSVSDRQMVEIAKA 168
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGlvkskkeldervEWALKKAALWDEVKdRLNDYPS----------NLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 169 LSKKADILILDEPTA----VLTGREVEILFDqirrLREQgVAILYISHKLDEIKAIADRVTVLRDGRHIVTEP 237
Cdd:PRK14267 164 LAMKPKILLMDEPTAnidpVGTAKIEELLFE----LKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
272-486 |
2.01e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 54.76 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVPGQVRDASFDLH--KGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGK----------PVRI------ 333
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerPVSMlfqenn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 334 --ASLQDAKNSGIAyltkdrkgsglllnmdMRPNLTLLAlekfgsviVDRKAEEAALEK-AIEAFdiraADRKAkvGDFS 410
Cdd:COG3840 82 lfPHLTVAQNIGLG----------------LRPGLKLTA--------EQRAQVEQALERvGLAGL----LDRLP--GQLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 411 GGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTD-RGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG3840 132 GGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
267-485 |
2.06e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.13 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 267 SAPIVLSVRDL-----------SVPGQVR---DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVR 332
Cdd:PRK11308 1 SQQPLLQAIDLkkhypvkrglfKPERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 333 IASLQDAKnsgiayltkdrkgsglllnmDMRPNLTLLALEKFGSvIVDRKAEEAALEK--AIEAfDIRAADRKAKVGD-- 408
Cdd:PRK11308 81 KADPEAQK--------------------LLRQKIQIVFQNPYGS-LNPRKKVGQILEEplLINT-SLSAAERREKALAmm 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 409 ----------------FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEM 471
Cdd:PRK11308 139 akvglrpehydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVV 218
|
250
....*....|....
gi 494149220 472 LGLSDRIAVMAAGR 485
Cdd:PRK11308 219 EHIADEVMVMYLGR 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
283-504 |
2.10e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.62 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV---RIASLQDAKNSGIAYLTKDRKGSGLLLN 359
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDPDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 MDMRPNLTLLALEKFGsviVDRKAEEAALEKAIEAFdiraadRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGI 439
Cdd:PRK13636 102 QDVSFGAVNLKLPEDE---VRKRVDNALKRTGIEHL------KDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 440 DIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGL-SDRIAVMAAGRItgILEGNDRN---EHEIMRHA 504
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRV--ILQGNPKEvfaEKEMLRKV 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-217 |
2.27e-08 |
|
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: 56.48 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 15 GKIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVL-DGAEVSFADseagegh 93
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVD------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 94 gviliHQELNLAEQLSVEENIFLGREIKRgwfLDKTAM--RAEAKRL----LDQlqcdvdpRTRIRDLSVSDRQMVEIAK 167
Cdd:TIGR03719 392 -----QSRDALDPNKTVWEEISGGLDIIK---LGKREIpsRAYVGRFnfkgSDQ-------QKKVGQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 168 ALSKKADILILDEPTAVLtgrEVEILfdqiRRLREQ-----GVAILyISHK---LDEI 217
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDL---DVETL----RALEEAllnfaGCAVV-ISHDrwfLDRI 506
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
379-486 |
2.39e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 379 VDRKAEEAALEKAIEAFDIRAADRKAkVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRG 458
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRA-AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG 194
|
90 100
....*....|....*....|....*...
gi 494149220 459 KSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
268-486 |
2.58e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 55.87 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 268 APIVLSVRDLSVP-GQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvrIASL------- 336
Cdd:COG3842 2 AMPALELENVSKRyGDvtaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD--VTGLppekrnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 337 ----QD---------AKNsgIAYltkdrkgsGLllnmDMRpnltllaleKFGSVIVDRKAEEAaLEK-AIEAFdiraADR 402
Cdd:COG3842 80 gmvfQDyalfphltvAEN--VAF--------GL----RMR---------GVPKAEIRARVAEL-LELvGLEGL----ADR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 403 KakVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVM 481
Cdd:COG3842 132 Y--PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVM 209
|
....*
gi 494149220 482 AAGRI 486
Cdd:COG3842 210 NDGRI 214
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-227 |
3.00e-08 |
|
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: 53.34 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSvDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFadseageghgvilihqelnla 105
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY--------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 106 eqlsveeniflgreikrgwfldktamraeakrlldqlqcdvdpRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:cd03222 66 -------------------------------------------KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYL 102
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 186 TGREVEILFDQIRRLREQGV-AILYISHKLDEIKAIADRVTVL 227
Cdd:cd03222 103 DIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
287-463 |
3.43e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 53.65 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 287 SFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriASLQDAKNSGIAYLTKdrkGSGLLLNMDMRPNL 366
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL--DFQRDSIARGLLYLGH---APGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 367 TLLAleKFGSvivDRKAEEAALEKAIEAFDIRAadrkakVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQ 446
Cdd:cd03231 95 RFWH--ADHS---DEQVEEALARVGLNGFEDRP------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170
....*....|....*..
gi 494149220 447 IYHFIGDLTDRGKSVIL 463
Cdd:cd03231 164 FAEAMAGHCARGGMVVL 180
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
285-486 |
3.65e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.48 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaSLQDAKNSGIAYLTKDRkgsGLLLNMDMRP 364
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQHY---ALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 NLTllalekFG-SVIVDRKAEEAAL--EKAIEAFDI----RAADRKAkvGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:PRK10851 94 NIA------FGlTVLPRRERPNAAAikAKVTQLLEMvqlaHLADRYP--AQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 438 GIDIGTKSQIYHFIGDLTDRGK-SVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
271-444 |
3.91e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 271 VLSVRDLSVpgqVR-------DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAknsg 343
Cdd:PRK13539 2 MLEGEDLAC---VRggrvlfsGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 344 IAYL-TKDRkgsglllnmdMRPNLTLLALEKFGSVIvdRKAEEAALEKAIEAFDI-RAADRKAkvGDFSGGNQQKLLLAK 421
Cdd:PRK13539 75 CHYLgHRNA----------MKPALTVAENLEFWAAF--LGGEELDIAAALEAVGLaPLAHLPF--GYLSAGQKRRVALAR 140
|
170 180
....*....|....*....|...
gi 494149220 422 VMETDPDIVIIDEPTRGIDIGTK 444
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAV 163
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-231 |
5.32e-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: 53.24 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAeVSFADSEAgeghgviLIHQElnla 105
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAYVSQEP-------WIQNG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 106 eqlSVEENIFLGREIKRGWFldKTAMRAEA-KRLLDQLqCDVDpRTRIRD----LSVSDRQMVEIAKALSKKADILILDE 180
Cdd:cd03250 81 ---TIRENILFGKPFDEERY--EKVIKACAlEPDLEIL-PDGD-LTEIGEkginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 181 P-TAV--LTGREveiLFDQ-IRRLREQGVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:cd03250 154 PlSAVdaHVGRH---IFENcILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-182 |
5.46e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 26 KSFGPA-QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGglvldgaEVSFAdseagEGHGVILIHQELNL 104
Cdd:PRK11819 14 KVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPA-----PGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 105 AEQLSVEENIFLG-REIKR-------------------------------------GWFLDKTAMRAeakrlLDQLQCDv 146
Cdd:PRK11819 82 DPEKTVRENVEEGvAEVKAaldrfneiyaayaepdadfdalaaeqgelqeiidaadAWDLDSQLEIA-----MDALRCP- 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 494149220 147 DPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:PRK11819 156 PWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
267-487 |
5.70e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.59 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 267 SAPIVLSVRDL--SVP---GQV---RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPvrIASL-Q 337
Cdd:COG4181 4 SSAPIIELRGLtkTVGtgaGELtilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFALdE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 338 DAKnsgiAYLTKDRKG----SGLLLnmdmrPNLTllALEkfgSVIVdrKAEEAAlekAIEAFDiRAADRKAKVG------ 407
Cdd:COG4181 82 DAR----ARLRARHVGfvfqSFQLL-----PTLT--ALE---NVML--PLELAG---RRDARA-RARALLERVGlghrld 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 408 ----DFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAA 483
Cdd:COG4181 142 hypaQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRA 221
|
....
gi 494149220 484 GRIT 487
Cdd:COG4181 222 GRLV 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-233 |
6.91e-08 |
|
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: 53.04 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPT---EGGLVLDGAEVS-FADSEAGEghgVIL 97
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKeFAEKYPGE---IIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 98 IHQELNLAEQLSVEENIflgreikrgwfldKTAMRAEAKRLldqlqcdvdprtrIRDLSVSDRQMVEIAKALSKKADILI 177
Cdd:cd03233 88 VSEEDVHFPTLTVRETL-------------DFALRCKGNEF-------------VRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 178 LDEPTavlTGREVEILFDQIRRLREQ-----GVAILYISHKLDEIKAIADRVTVLRDGRHI 233
Cdd:cd03233 142 WDNST---RGLDSSTALEILKCIRTMadvlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
283-496 |
7.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.94 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpvriASLQDAKNsgiayLTKDRKGSGLLLNmdm 362
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-----LDTSDEEN-----LWDIRNKAGMVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLAlekfgsVIVDRKAEEAALEKAIEAFDIRAADRKA--KVGDF----------SGGNQQKLLLAKVMETDPDIV 430
Cdd:PRK13633 93 NPDNQIVA------TIVEEDVAFGPENLGIPPEEIRERVDESlkKVGMYeyrrhaphllSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 431 IIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGlSDRIAVMAAGRItgILEGNDRN 496
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKV--VMEGTPKE 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
303-488 |
7.55e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 303 GAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDA-KNSGIAYLTKDRKGSGLLLNMDMRPNLTLLALEKfgsVIVDR 381
Cdd:PRK13652 40 GAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVrKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDE---ETVAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 382 KAEEAALEKAIEAFDIRAADRkakvgdFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKS 460
Cdd:PRK13652 117 RVSSALHMLGLEELRDRVPHH------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMT 190
|
170 180
....*....|....*....|....*...
gi 494149220 461 VILLSSEMPEMLGLSDRIAVMAAGRITG 488
Cdd:PRK13652 191 VIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
284-486 |
7.69e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.27 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpvRIASLQDAKNS-GIAYltkdrKGSGLLLNMDM 362
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGvGMVF-----QSYALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTL-LALEKFGSVIVDRKAEEAA--LEKAieafdiRAADRKAKvgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGI 439
Cdd:PRK11000 93 AENMSFgLKLAGAKKEEINQRVNQVAevLQLA------HLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 440 DIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-237 |
9.17e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 22 RKICKSFGPAQ------VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEgglvlDGAEVSFADSEageghgv 95
Cdd:COG2401 28 AIVLEAFGVELrvveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP-----VAGCVDVPDNQ------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 96 ilIHQELNLAEQLSVEENIflgreikrgwfldktamrAEAKRLLDQ--LqcdVDP---RTRIRDLSVSDRQMVEIAKALS 170
Cdd:COG2401 96 --FGREASLIDAIGRKGDF------------------KDAVELLNAvgL---SDAvlwLRRFKELSTGQKFRFRLALLLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 171 KKADILILDEPTAVLTGREVEILFDQIRRL-REQGVAILYISHKLDEIKAIA-DRVTVLRDGRHIVTEP 237
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEEKR 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
285-487 |
9.64e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.59 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiaslQDAKNSGIAYLtkdRKGSGLLLNMDMRP 364
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT----STSKNKDIKQI---RKKVGLVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 --NLTLLALEKFGSV---IVDRKAEEAALEK-AIEAFDIRAADRKAKvgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRG 438
Cdd:PRK13649 98 lfEETVLKDVAFGPQnfgVSQEEAEALAREKlALVGISESLFEKNPF--ELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 439 IDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRIT 487
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
269-485 |
1.01e-07 |
|
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: 52.82 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 269 PIVLSVRDLS------------VPGqVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTI--ERDGKPVRIA 334
Cdd:COG4778 2 TTLLEVENLSktftlhlqggkrLPV-LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvRHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 335 SLQDaknSGIAYLTKDRKG--SGLLlnmDMRPNLTllALEkfgsvIVdrkaEEAALEKAIEAfdiRAADRKAKV------ 406
Cdd:COG4778 81 QASP---REILALRRRTIGyvSQFL---RVIPRVS--ALD-----VV----AEPLLERGVDR---EEARARAREllarln 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 407 ----------GDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSD 476
Cdd:COG4778 141 lperlwdlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVAD 220
|
....*....
gi 494149220 477 RIAVMAAGR 485
Cdd:COG4778 221 RVVDVTPFS 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
283-484 |
1.07e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 53.32 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpvRIA-SLQDA-------KNSGIAYLTKDRKgs 354
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG---RISfSSQFSwimpgtiKENIIFGVSYDEY-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 355 glllnmdmrpnltllaleKFGSVIvdrkaEEAALEKAIEAFDIRAADRKAKVG-DFSGGNQQKLLLAKVMETDPDIVIID 433
Cdd:cd03291 128 ------------------RYKSVV-----KACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 434 EPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMpEMLGLSDRIAVMAAG 484
Cdd:cd03291 185 SPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKM-EHLKKADKILILHEG 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
373-486 |
1.09e-07 |
|
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: 53.16 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 373 KFGSVIVDRKAEEAALEKA---IEAFDIRA-ADRKakVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIY 448
Cdd:COG1119 105 FFDSIGLYREPTDEQRERArelLELLGLAHlADRP--FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLL 182
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 494149220 449 HFIGDLTDRGKSVILLSS----EMPEMLglsDRIAVMAAGRI 486
Cdd:COG1119 183 ALLDKLAAEGAPTLVLVThhveEIPPGI---THVLLLKDGRV 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
283-462 |
1.26e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 52.36 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRiaslqDAKNSGIAYLtkdRKGSGL------ 356
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS-----RLKRREIPYL---RRRIGVvfqdfr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 357 LLnmdmrPNLTL-----LALEKFGsviVDRKAEEAALEKAIEAFDIraADR-KAKVGDFSGGNQQKLLLAKVMETDPDIV 430
Cdd:COG2884 90 LL-----PDRTVyenvaLPLRVTG---KSRKEIRRRVREVLDLVGL--SDKaKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190
....*....|....*....|....*....|..
gi 494149220 431 IIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVI 462
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVL 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
283-484 |
1.62e-07 |
|
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: 54.15 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpvriaslqdaknsgIAYLTKdrkgSGLLLNMDM 362
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQ----TSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLtLLALE----KFGSVIvdrKAeeAALEKAIEAFdirAADRKAKVGD----FSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:TIGR01271 504 KDNI-IFGLSydeyRYTSVI---KA--CQLEEDIALF---PEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 435 PTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMpEMLGLSDRIAVMAAG 484
Cdd:TIGR01271 575 PFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-224 |
1.81e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 17 IRLSGRKIckSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDG--------------AEV 82
Cdd:PRK11147 4 ISIHGAWL--SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdpprnVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 83 SFAD--SEAGEGHGVIL--IHQELNLAEQLSVEENIF-LGR-----EIKRGWFLDktamrAEAKRLLDQLqcDVDPRTRI 152
Cdd:PRK11147 82 TVYDfvAEGIEEQAEYLkrYHDISHLVETDPSEKNLNeLAKlqeqlDHHNLWQLE-----NRINEVLAQL--GLDPDAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 153 RDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEIL--FdqirrLREQGVAILYISHKLDEIKAIADRV 224
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLegF-----LKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
32-244 |
2.08e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGY--HEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQelNLAEQLS 109
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERAHLGIFLAFQ--YPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 110 VEENIFLgreikrgwfldKTAMRAEAKRL----LDQLQ-----------CDVDPRTRIRDL----SVSDRQMVEIAKALS 170
Cdd:CHL00131 99 VSNADFL-----------RLAYNSKRKFQglpeLDPLEfleiineklklVGMDPSFLSRNVnegfSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 171 KKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHK---LDEIKaiADRVTVLRDGRhIVTEPVVDLSKD 244
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK--PDYVHVMQNGK-IIKTGDAELAKE 241
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
106-241 |
3.17e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 106 EQLSVEENIFLgreIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:NF000106 99 ESFSGRENLYM---IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 186 TGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
272-487 |
3.26e-07 |
|
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: 52.83 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV--PGQ----VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIA 345
Cdd:COG4618 331 LSVENLTVvpPGSkrpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 346 YLTKDrkgsglllnmdmrpnLTLLAlekfGSVivdrkAE------EAALEKAIEAfdIRAAD------RKAK-----VGD 408
Cdd:COG4618 410 YLPQD---------------VELFD----GTI-----AEniarfgDADPEKVVAA--AKLAGvhemilRLPDgydtrIGE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 409 ----FSGGNQQKLLLAKVMETDPDIVIIDEPTRGID-IGTKSqIYHFIGDLTDRGKSVILLSSEmPEMLGLSDRIAVMAA 483
Cdd:COG4618 464 ggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdEGEAA-LAAAIRALKARGATVVVITHR-PSLLAAVDKLLVLRD 541
|
....
gi 494149220 484 GRIT 487
Cdd:COG4618 542 GRVQ 545
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
272-478 |
3.39e-07 |
|
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: 50.40 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVpGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAII--GLRERSSGTIER--DGKPVRIASLQDAKNSGIAYL 347
Cdd:cd03238 1 LTVSGANV-HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLyaSGKARLISFLPKfsRNKLIFIDQLQFLIDVGLGYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 348 TKDRKGSGLllnmdmrpnltllalekfgsvivdrkaeeaalekaieafdiraadrkakvgdfSGGNQQKLLLAKVM--ET 425
Cdd:cd03238 80 TLGQKLSTL-----------------------------------------------------SGGELQRVKLASELfsEP 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 426 DPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEmPEMLGLSDRI 478
Cdd:cd03238 107 PGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWI 158
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
285-486 |
3.65e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDA-KNSGIAYLTKDRKGSGLLLNMDMR 363
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLrKHIGIVFQNPDNQFVGSIVKYDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 pnltlLALEKFgSVIVDRKAEEAAleKAIEAFDIRA-ADRKAKvgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIG 442
Cdd:PRK13648 107 -----FGLENH-AVPYDEMHRRVS--EALKQVDMLErADYEPN--ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 443 TKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGlSDRIAVMAAGRI 486
Cdd:PRK13648 177 ARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
272-485 |
3.77e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVP----GQVR----DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLR-----ERSSGTIERDGKPVRIAS--- 335
Cdd:PRK15134 6 LAIENLSVAfrqqQTVRtvvnDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLLHASeqt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 336 LQDAKNSGIAYLTKDRKGSgllLNmdmrpnlTLLALEK-FGSVI-----VDRKAEEAALEKAIEAFDIRAAdrKAKVGDF 409
Cdd:PRK15134 86 LRGVRGNKIAMIFQEPMVS---LN-------PLHTLEKqLYEVLslhrgMRREAARGEILNCLDRVGIRQA--AKRLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 410 ----SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAG 484
Cdd:PRK15134 154 phqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
.
gi 494149220 485 R 485
Cdd:PRK15134 234 R 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-231 |
4.54e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.09 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGyheptegglVLDGA-EVSFADSEAGEGHGVILIHQELNLAEQLS--- 109
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG---------LLPGSgSIQFAGQPLEAWSAAELARHRAYLSQQQTppf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 110 ---VEENIFLGREIKRGWFLDKTAMR--AEAKRLLDQLqcdvdPRTrIRDLSVSDRQMVEIA-------KALSKKADILI 177
Cdd:PRK03695 83 ampVFQYLTLHQPDKTRTEAVASALNevAEALGLDDKL-----GRS-VNQLSGGEWQRVRLAavvlqvwPDINPAGQLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494149220 178 LDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGR 231
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
410-493 |
4.78e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.52 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 410 SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTdRGKSVILLS---SEMPEMlglsDRIAVMAAGRI 486
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMIThrlTGLEQF----DRICVMDNGQI 551
|
....*..
gi 494149220 487 tgILEGN 493
Cdd:PRK11160 552 --IEQGT 556
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
32-233 |
4.86e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGY--HEPTEGGLVLDGAEVSFADSEAGEGHGVILIHQ---EL-NLA 105
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQypvEIpGVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 106 EQLSVEENIFLGREIKRGWFLDKTAMR--AEAKRLLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADILILDEPTA 183
Cdd:PRK09580 95 NQFFLQTALNAVRSYRGQEPLDRFDFQdlMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 184 VLTGREVEILFDQIRRLREQGVAILYISHK---LDEIKaiADRVTVLRDGRHI 233
Cdd:PRK09580 175 GLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK--PDYVHVLYQGRIV 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
278-487 |
7.12e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 278 SVPGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpvriaslqdaknsgIAYLTKdrkgSGLL 357
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQ----QAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 358 LNMDMRPNLTllalekFGSVIvdrkaEEAALEKAIEA------FDIRAADRKAKVGD----FSGGNQQKLLLAKVMETDP 427
Cdd:TIGR00957 711 QNDSLRENIL------FGKAL-----NEKYYQQVLEAcallpdLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIY-HFIGDL-TDRGKSVILLSSEMpEMLGLSDRIAVMAAGRIT 487
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFeHVIGPEgVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKIS 840
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
272-485 |
7.65e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSVPGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRErSSGTIERDGKPVRIASLQD-AKNSgiAYLTKD 350
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElARHR--AYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 351 RKGsglLLNMDMRPNLTLlalekFGSVIVDRKAEEAALEKAIEAFDIraADRKAK-VGDFSGGNQQKLLLAKV-METDPD 428
Cdd:PRK03695 78 QTP---PFAMPVFQYLTL-----HQPDKTRTEAVASALNEVAEALGL--DDKLGRsVNQLSGGEWQRVRLAAVvLQVWPD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 429 I------VIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGR 485
Cdd:PRK03695 148 InpagqlLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
270-486 |
7.67e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.54 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 270 IVLSVRDLSVP-GQ---VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQD-AKNSGI 344
Cdd:PRK13548 1 AMLEARNLSVRlGGrtlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 345 ayltkdrkgsglllnMDMRPNLT--LLALEkfgsvIV---------DRKAEEAALEKAIEAFDIRA-ADRkakvgDF--- 409
Cdd:PRK13548 81 ---------------LPQHSSLSfpFTVEE-----VVamgraphglSRAEDDALVAAALAQVDLAHlAGR-----DYpql 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 410 SGGNQQKLLLAKVM------ETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLT-DRGKSVILLssempeM--LGL----SD 476
Cdd:PRK13548 136 SGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVV------LhdLNLaaryAD 209
|
250
....*....|
gi 494149220 477 RIAVMAAGRI 486
Cdd:PRK13548 210 RIVLLHQGRL 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
282-486 |
7.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.89 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 282 QVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNS-GIAYLTKDRKGSGLLLNM 360
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKiGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 361 DMRpnltlLALEKFGSVIVDRK--AEEAALEKAIEAFDIRAADRkakvgdFSGGNQQKLLLAKVMETDPDIVIIDEPTRG 438
Cdd:PRK13650 102 DVA-----FGLENKGIPHEEMKerVNEALELVGMQDFKEREPAR------LSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 439 IDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEmLGLSDRIAVMAAGRI 486
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
283-486 |
9.54e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpvriaslqdaknsgIAYLTKD---------RKG 353
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGK--------------VLYFGKDifqidaiklRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 354 SGLLLNM-DMRPNLTL---LALEKFGSVIVDRKAEEAALEKAIEAFDI--RAADR-KAKVGDFSGGNQQKLLLAKVMETD 426
Cdd:PRK14246 92 VGMVFQQpNPFPHLSIydnIAYPLKSHGIKEKREIKKIVEECLRKVGLwkEVYDRlNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 427 PDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRgKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
283-462 |
9.69e-07 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 49.70 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTI--ERDGKPVRIASLQDAKnsgIAYLTKDRKG--SGLLl 358
Cdd:TIGR02324 24 LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRIlvRHEGAWVDLAQASPRE---VLEVRRKTIGyvSQFL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 359 nmDMRPNLTllALEKFGSVIVDRKAE-EAALEKAIEAFD-IRAADRKAKV--GDFSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:TIGR02324 100 --RVIPRVS--ALEVVAEPLLERGVPrEAARARARELLArLNIPERLWHLppATFSGGEQQRVNIARGFIADYPILLLDE 175
|
170 180
....*....|....*....|....*...
gi 494149220 435 PTRGIDIGTKSQIYHFIGDLTDRGKSVI 462
Cdd:TIGR02324 176 PTASLDAANRQVVVELIAEAKARGAALI 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-231 |
9.96e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 9.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfadseageGHGVILIHQELNLAEQL---- 108
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--------KFGLTDLRRVLSIIPQSpvlf 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 --SVEENI--FLGREIKRGWfldKTAMRAEAKRLLDQLQCDVDPRTRI--RDLSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:PLN03232 1323 sgTVRFNIdpFSEHNDADLW---EALERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 183 AvltgrEVEILFDQI--RRLREQ--GVAILYISHKLDEIKAiADRVTVLRDGR 231
Cdd:PLN03232 1400 A-----SVDVRTDSLiqRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
36-241 |
1.04e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKS----TLVKILSGYHEPTEGGLVLDGAEVSFADSEageGHGVILIHQE--------LN 103
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALR---GRKIATIMQNprsafnplHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 104 LAEQlsveeniflGREIKRGwfLDKTAMRAEAKRLLDQLQCDvDPRTRIR----DLSVSDRQMVEIAKALSKKADILILD 179
Cdd:PRK10418 98 MHTH---------ARETCLA--LGKPADDATLTAALEAVGLE-NAARVLKlypfEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 180 EPT----AVLTGREVEILfdqIRRLREQGVAILYISHKLDEIKAIADRVTVLRDGRHIVTEPVVDL 241
Cdd:PRK10418 166 EPTtdldVVAQARILDLL---ESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
283-486 |
1.55e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.73 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALmeaiIGLRER----SSGTIERDGKPVRIASLQDAKNSgIAYLTKDrkgsGLLL 358
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLQRvfdpQSGRILIDGTDIRTVTRASLRRN-IAVVFQD----AGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 359 NMDMRPNLTLlalEKFGSVIVD-RKAEEAA-----LEKAIEAFDIRAADRKAKVgdfSGGNQQKLLLAKVMETDPDIVII 432
Cdd:PRK13657 422 NRSIEDNIRV---GRPDATDEEmRAAAERAqahdfIERKPDGYDTVVGERGRQL---SGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 433 DEPTRGIDIGTKSQIYHFIGDL-TDRGKSVIL--LSSempemLGLSDRIAVMAAGRI 486
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELmKGRTTFIIAhrLST-----VRNADRILVFDNGRV 547
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-486 |
1.73e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 PNLTL---LALEKFGSVIVDRKAE-----EAALEKAiEAFDiRAADR-KAKVGDFSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:PRK14247 95 PNLSIfenVALGLKLNRLVKSKKElqervRWALEKA-QLWD-EVKDRlDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 435 PTRGIDIGTKSQIYHFIGDLTdRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
409-503 |
1.77e-06 |
|
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: 48.68 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 409 FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLsSEMPEMLGL--SDRIAVMAAGRI 486
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLII-THYQRLLDYikPDRVHVLYDGRI 183
|
90
....*....|....*..
gi 494149220 487 tgILEGNDRNEHEIMRH 503
Cdd:cd03217 184 --VKSGDKELALEIEKK 198
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
283-486 |
2.85e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.91 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAK--NSGIAYLTKD-------RKG 353
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafRRDIQMVFQDsisavnpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 354 SGLLLNMDMRPNLTLlalekfgsvivDRKAEEAALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMETDPDIVIID 433
Cdd:PRK10419 108 VREIIREPLRHLLSL-----------DKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494149220 434 EPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
272-471 |
3.04e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.81 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV--P-GQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIER-DGKPV-----R----IASL 336
Cdd:COG4178 363 LALEDLTLrtPdGRplLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflpqRpylpLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 337 QDAknsgIAYltkdrkgsglllnmdmrPNLtllalekfgsvivDRKAEEAALEKAIEAFDI-RAADRKAKVGD----FSG 411
Cdd:COG4178 443 REA----LLY-----------------PAT-------------AEAFSDAELREALEAVGLgHLAERLDEEADwdqvLSL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 412 GNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHfigdltdrgksviLLSSEMPEM 471
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ-------------LLREELPGT 535
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-231 |
3.19e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS---FADSEAGEG---------HGVILI-- 98
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfgLMDLRKVLGiipqapvlfSGTVRFnl 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 99 -----HQELNLAEQLsveENIFLGREIKRGWF-LDktAMRAEAKRlldqlqcdvdprtrirDLSVSDRQMVEIAKALSKK 172
Cdd:PLN03130 1334 dpfneHNDADLWESL---ERAHLKDVIRRNSLgLD--AEVSEAGE----------------NFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 173 ADILILDEPTAVltgreVEILFDQI--RRLREQ--GVAILYISHKLDEIkaI-ADRVTVLRDGR 231
Cdd:PLN03130 1393 SKILVLDEATAA-----VDVRTDALiqKTIREEfkSCTMLIIAHRLNTI--IdCDRILVLDAGR 1449
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
283-486 |
3.35e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.54 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV-RIASLQDAKNsgIAYLTKDrkgsgllLNMD 361
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKR--LAILRQE-------NHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 362 MRpnLTLLALEKFGsvivdR---------KAEEAALEKAIEAFDIRA-ADRkakvgdF----SGGNQQKLLLAKVMETDP 427
Cdd:COG4604 88 SR--LTVRELVAFG-----RfpyskgrltAEDREIIDEAIAYLDLEDlADR------YldelSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 428 DIVIIDEPTRGIDIGTKSQIYHFIGDLTD-RGKSVILL-------SSempemlgLSDRIAVMAAGRI 486
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVlhdinfaSC-------YADHIVAMKDGRV 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
244-449 |
3.41e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.72 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 244 DDMARLMVGR-DIKQM-FPHRvsdtSAPIVLSVRDLSVPgqvrDASFdlhkgevLGFAGIVGAGRTALMEAIIGLRERSS 321
Cdd:PRK10790 331 NDDRPLQSGRiDIDNVsFAYR----DDNLVLQNINLSVP----SRGF-------VALVGHTGSGKSTLASLLMGYYPLTE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 322 GTIERDGKPVRIASLQDAKNsGIAYLTKDrkgsglllnmdmrPnlTLLALEKFGSVIVDRKAEEAALEKAIEAFDIRAAD 401
Cdd:PRK10790 396 GEIRLDGRPLSSLSHSVLRQ-GVAMVQQD-------------P--VVLADTFLANVTLGRDISEEQVWQALETVQLAELA 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 402 RKAKVG----------DFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYH 449
Cdd:PRK10790 460 RSLPDGlytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ 517
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
319-513 |
3.81e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 319 RSSGTIERDGKPVRIASLQDAKNsgiayLTKDRKGSGLLLNMDMRPNLtllaleKFGSV-----IVDRKAEEAALEKAIE 393
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKDLRN-----LFSIVSQEPMLFNMSIYENI------KFGKEdatreDVKRACKFAAIDEFIE 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 394 AFDIRAADRKAKVG-DFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEML 472
Cdd:PTZ00265 1343 SLPNKYDTNVGPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 473 GLSDRIAVmaagritgiLEGNDRNEHEIMRHATG---ISGQEGV 513
Cdd:PTZ00265 1423 KRSDKIVV---------FNNPDRTGSFVQAHGTHeelLSVQDGV 1457
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
262-482 |
3.97e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 262 RVSDTsapivlsvRDLSVPgqvrdaSFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGtiERDGKPVRIASLQDAKN 341
Cdd:PRK10938 12 RLSDT--------KTLQLP------SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--ERQSQFSHITRLSFEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 342 SGIAYLTKDRKgsglllNMDMrpnltLLALEK-FG----SVIVDRKAEEAALEKAIEAFDIRAA-DRKAKVgdFSGGNQQ 415
Cdd:PRK10938 76 QKLVSDEWQRN------NTDM-----LSPGEDdTGrttaEIIQDEVKDPARCEQLAQQFGITALlDRRFKY--LSTGETR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494149220 416 KLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMA 482
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLA 209
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
385-509 |
4.11e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.30 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 385 EAALEKAieAFDIRAADR-KAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRgKSVIL 463
Cdd:PRK14267 127 EWALKKA--ALWDEVKDRlNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVL 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 464 LSSEMPEMLGLSDRIAVMAAGRITGIleGNDRN-----EHEIM-RHATGISG 509
Cdd:PRK14267 204 VTHSPAQAARVSDYVAFLYLGKLIEV--GPTRKvfenpEHELTeKYVTGALG 253
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
36-245 |
4.64e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 36 DVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAE----------------VS-----FADSEAGEGHG 94
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrskigvVSqdpllFSNSIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 95 VILIHQELN-LAEQLSVEENIFLGREIKRGWFLDKTA-----------------MRAEAKRLLDQLQCDVDPRTRIRD-- 154
Cdd:PTZ00265 483 SLYSLKDLEaLSNYYNEDGNDSQENKNKRNSCRAKCAgdlndmsnttdsnelieMRKNYQTIKDSEVVDVSKKVLIHDfv 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 155 -----------------LSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEILFDQIRRLR--EQGVAILyISHKLD 215
Cdd:PTZ00265 563 salpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITII-IAHRLS 641
|
250 260 270
....*....|....*....|....*....|....
gi 494149220 216 EIKaIADRVTVL----RDGRHIVTEPVVDLSKDD 245
Cdd:PTZ00265 642 TIR-YANTIFVLsnreRGSTVDVDIIGEDPTKDN 674
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
155-224 |
4.67e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 4.67e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 155 LSVSDRQMVEIAKAL--SKKADILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAiADRV 224
Cdd:cd03238 88 LSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
379-486 |
4.83e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.19 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 379 VDRKAEEAAleKAIEAFDIRaadRKAKVgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRG 458
Cdd:PRK13647 115 VERRVEEAL--KAVRMWDFR---DKPPY-HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQG 188
|
90 100
....*....|....*....|....*...
gi 494149220 459 KSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK13647 189 KTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
155-222 |
6.66e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 6.66e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 155 LSVSDRQMVEIAKALSKKAD---ILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAiAD 222
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-AD 899
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-219 |
7.21e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGglvldgaEVSFADSEAGEGHGVIL--IHQELNLAEQLS 109
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSG-------NIYYKNCNINNIAKPYCtyIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 110 VEENIFLGREIKRGWFLDKTAMRA-EAKRLLDQlqcdvdprtRIRDLSVSDRQMVEIAKALSKKADILILDEPTAVLTGR 188
Cdd:PRK13541 87 VFENLKFWSEIYNSAETLYAAIHYfKLHDLLDE---------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180 190
....*....|....*....|....*....|.
gi 494149220 189 EVEILFDQIRRLREQGVAILYISHKLDEIKA 219
Cdd:PRK13541 158 NRDLLNNLIVMKANSGGIVLLSSHLESSIKS 188
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
274-486 |
7.45e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 274 VRDLSVPGQ-------VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIAslqdaknsgiay 346
Cdd:PRK13546 24 MKDALIPKHknktffaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 347 ltkdrkgsgllLNMDMRPNLTLLALEKFGSVIVDRKAEE-AALEKAIEAFDIRAADRKAKVGDFSGGNQQKLLLAKVMET 425
Cdd:PRK13546 92 -----------ISAGLSGQLTGIENIEFKMLCMGFKRKEiKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 426 DPDIVIIDEptrGIDIGTKS-------QIYHFigdlTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK13546 161 NPDILVIDE---ALSVGDQTfaqkcldKIYEF----KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
293-485 |
8.03e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 293 GEVLGFAGIVGAGRTALMEAIIGLRERSS--GTI-ERDGKPVRiaslQDAKNSGiaYLTKDrkgSGLLLNMDMRPNLTLL 369
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTIlANNRKPTK----QILKRTG--FVTQD---DILYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 370 ALEKFGSVIvDRKAEEAALEKAIEAFDIRAADRKAKVGDF----SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKS 445
Cdd:PLN03211 165 SLLRLPKSL-TKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494149220 446 QIYHFIGDLTDRGKSVILL----SSEMPEMLglsDRIAVMAAGR 485
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSmhqpSSRVYQMF---DSVLVLSEGR 284
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
283-486 |
8.04e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 47.77 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGK-PVriaslqdaknsgiayltKDRKG-------- 353
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPF-----------------KRRKEfarrigvv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 354 ----SGLLLNMDMRPNLTLLAlekfgsVI--VDRKAEEAALEKAIEAFDIraadrkakvGDF--------SGGNQQKLLL 419
Cdd:COG4586 101 fgqrSQLWWDLPAIDSFRLLK------AIyrIPDAEYKKRLDELVELLDL---------GELldtpvrqlSLGQRMRCEL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 420 AKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG4586 166 AAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
287-492 |
9.11e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 287 SFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKpvRIASLqdaKNSGIAYLTKD----RKGSGLLLNMDM 362
Cdd:PRK10908 22 TFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DITRL---KNREVPFLRRQigmiFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLTLLALEKFGSVIVDRKAEEAALEKaIEAFDiraadrKAKVG--DFSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDK-VGLLD------KAKNFpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 441 IGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRITGILEG 492
Cdd:PRK10908 170 DALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGG 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
287-481 |
1.16e-05 |
|
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: 46.98 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 287 SFDLHK------GEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDG------KPVRIASLQDaknsgiaYLTKdrkgs 354
Cdd:cd03236 14 SFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeilDEFRGSELQN-------YFTK----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 355 glLLNMDMRP-----NLTLLALEKFGSV--IVDRKAEEAALEKAIEAFDIRAA-DRKakVGDFSGGNQQKLLLAKVMETD 426
Cdd:cd03236 82 --LLEGDVKVivkpqYVDLIPKAVKGKVgeLLKKKDERGKLDELVDQLELRHVlDRN--IDQLSGGELQRVAIAAALARD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 427 PDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVM 481
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
283-486 |
1.23e-05 |
|
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: 46.70 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaSLQDAK--NSGIAYLTKDRkgsgLLLNM 360
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKylHSKVSLVGQEP----VLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 361 DMRPNLTL-LALEKFGSVIvdrkaeEAALEKAIEAFDIRAA-----DRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:cd03248 103 SLQDNIAYgLQSCSFECVK------EAAQKAHAHSFISELAsgydtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494149220 435 PTRGIDIGTKSQIYHFI-GDLTDRGKSVIllsSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03248 177 ATSALDAESEQQVQQALyDWPERRTVLVI---AHRLSTVERADQILVLDGGRI 226
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
155-222 |
1.27e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 1.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 155 LSVSDRQMVEIAKALSKKAD---ILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAiAD 222
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKC-AD 239
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
44-197 |
1.33e-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: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 44 GEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAeVSFADSEAgeghgvilihqelnLAEQLSVEENIFLGREIKRG 123
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQA--------------WIQNDSLRENILFGKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 124 WFldKTAMRAEAkrLLDQLQcdVDP---RTRIRD----LSVSDRQMVEIAKALSKKADILILDEPTAVLTGREVEILFDQ 196
Cdd:TIGR00957 729 YY--QQVLEACA--LLPDLE--ILPsgdRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
.
gi 494149220 197 I 197
Cdd:TIGR00957 803 V 803
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
5-185 |
1.43e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 47.73 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 5 AVHAVNPGTEGKIRLSGrKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEP---TEGGLVLDGAE 81
Cdd:TIGR00955 13 RVAQDGSWKQLVSRLRG-CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 82 VsfadsEAGEGHGV--ILIHQELNLAeQLSVEENIFLGREIKRGWFLDKTAMRAEAKRLLDQLQCDVDPRTRI------R 153
Cdd:TIGR00955 92 I-----DAKEMRAIsaYVQQDDLFIP-TLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvK 165
|
170 180 190
....*....|....*....|....*....|..
gi 494149220 154 DLSVSDRQMVEIAKALSKKADILILDEPTAVL 185
Cdd:TIGR00955 166 GLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
415-484 |
1.44e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.21 E-value: 1.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 415 QKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTD-RGKSVILLSSEMPEMLGLSDRIAVMAAG 484
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCG 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
29-231 |
1.63e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.15 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 29 GPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSfaDSEAGEgHGVILIHQELNLAEQL 108
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN--ELEPAD-RDIAMVFQNYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 109 SVEENIFLGREIkRGwfLDKTAMR---AEAKRLL--DQLqCDVDPrtriRDLSVSDRQMVEIAKALSKKADILILDEPTA 183
Cdd:PRK11650 92 SVRENMAYGLKI-RG--MPKAEIEervAEAARILelEPL-LDRKP----RELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 184 VLTGR-----EVEilfdqIRRL-REQGVAILYISHklDEIKA--IADRVTVLRDGR 231
Cdd:PRK11650 164 NLDAKlrvqmRLE-----IQRLhRRLKTTSLYVTH--DQVEAmtLADRVVVMNGGV 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
285-486 |
1.70e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGlrerssgtierDGKPVRIASLqDAKNSgIAYLTKdrkgSGLLLNMDMRP 364
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------ELSHAETSSV-VIRGS-VAYVPQ----VSWIFNATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 NLtlLALEKFGSVIVDRKAEEAALEKAIEAFDIRAADRKAKVG-DFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGT 443
Cdd:PLN03232 698 NI--LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494149220 444 KSQIYHFIGDLTDRGKSVILLSSEMpEMLGLSDRIAVMAAGRI 486
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
284-486 |
1.76e-05 |
|
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: 45.99 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTAlmeaIIGLRER----SSGTIERDGKPVRIASLQDAKNSgIAYLTKDRkgsgLLLN 359
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfydpTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEP----VLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 MDMRPNLtLLALEKFGSVIVDRKAEEAALEKAI----EAFDIRAADRKAKVgdfSGGNQQKLLLAKVMETDPDIVIIDEP 435
Cdd:cd03249 91 GTIAENI-RYGKPDATDEEVEEAAKKANIHDFImslpDGYDTLVGERGSQL---SGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 436 TRGIDIGTKSQIYHFIGDLTdRGKSVIL----LSSempemLGLSDRIAVMAAGRI 486
Cdd:cd03249 167 TSALDAESEKLVQEALDRAM-KGRTTIViahrLST-----IRNADLIAVLQNGQV 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
284-451 |
1.76e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 44.75 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDgkpvriaslqdaKNSGIAYLTKdrkgsglllnmdmr 363
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKIGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 pnltllalekfgsvivdrkaeeaalekaieafdiraadrkakvgdFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGT 443
Cdd:cd03221 71 ---------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
....*...
gi 494149220 444 KSQIYHFI 451
Cdd:cd03221 106 IEALEEAL 113
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
292-484 |
1.81e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.78 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 292 KGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGK--PVRIASLQDAKNSG-IAYLTKdrkgSGLLLNMDMRPNLTl 368
Cdd:cd03290 26 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRYsVAYAAQ----KPWLLNATVEENIT- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 369 lalekFGSVIVDRK----AEEAALEKAIeafDIRAADRKAKVGD----FSGGNQQKLLLAKVMETDPDIVIIDEPTRGID 440
Cdd:cd03290 101 -----FGSPFNKQRykavTDACSLQPDI---DLLPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494149220 441 IGTKSQIYH--FIGDLTDRGKSVILLSSEMpEMLGLSDRIAVMAAG 484
Cdd:cd03290 173 IHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
285-486 |
1.82e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.16 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIErdgkpvrIASLQ-DAKNSgiaylTKDRKGSGLLLNMDMR 363
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLN-------IAGNHfDFSKT-----PSDKAIRELRRNVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 -------PNLTLLALEKFGSVIVDRKAEEAALEKAIEAFD-IRAADrkaKVGDF----SGGNQQKLLLAKVMETDPDIVI 431
Cdd:PRK11124 88 fqqynlwPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLErLRLKP---YADRFplhlSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 432 IDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-73 |
1.92e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 1.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 494149220 23 KICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEG 73
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
412-485 |
2.04e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 2.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 412 GNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLG-LSDRIAVMAAGR 485
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSqWADKINVLYCGQ 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
283-493 |
2.28e-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: 47.10 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLR--ERSSGTI----------------ERDGKPVRI--ASLQ----D 338
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpSKVGEPCPVcgGTLEpeevD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 339 AKNSGIAYLTKDRKGSGLLLN--MDMRPNLTLL-----ALEKFGSvivdrKAEEAaLEKAIEAFD-IRAADRKAKVG-DF 409
Cdd:TIGR03269 96 FWNLSDKLRRRIRKRIAIMLQrtFALYGDDTVLdnvleALEEIGY-----EGKEA-VGRAVDLIEmVQLSHRITHIArDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 410 SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLG-LSDRIAVMAAGRItg 488
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLSDKAIWLENGEI-- 247
|
....*
gi 494149220 489 ILEGN 493
Cdd:TIGR03269 248 KEEGT 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
279-506 |
2.33e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 279 VPGQVRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSgIAYLTKdrkgSGLLL 358
Cdd:PLN03232 1248 LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQ----SPVLF 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 359 NMDMRPNLTLLAlekfgsvivdrKAEEAALEKAIEAFDIRAADRKAKVG----------DFSGGNQQKLLLAKVMETDPD 428
Cdd:PLN03232 1323 SGTVRFNIDPFS-----------EHNDADLWEALERAHIKDVIDRNPFGldaevseggeNFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 429 IVIIDEPTRGIDIGTKSQIYHFIGDlTDRGKSVILLSSEMPEMLGlSDRIAVMAAGRITGI-----LEGNDRNEHEIMRH 503
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYdspqeLLSRDTSAFFRMVH 1469
|
...
gi 494149220 504 ATG 506
Cdd:PLN03232 1470 STG 1472
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
409-487 |
2.69e-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: 45.33 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 409 FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTD--RGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
.
gi 494149220 487 T 487
Cdd:cd03233 199 I 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-78 |
2.89e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 2.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494149220 19 LSGRKICKSFGpAQVLFD-VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLD 78
Cdd:PRK15064 2 LSTANITMQFG-AKPLFEnISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-182 |
3.30e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 15 GKIRLSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEG----GLVLdgaEVSFADSeag 90
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcGTKL---EVAYFDQ--- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 91 eghgviliHQElNLAEQLSVEENIFLGReikrgwfldKTAMRAEAKR-LLDQLQcdvD-------PRTRIRDLSVSDRQM 162
Cdd:PRK11147 390 --------HRA-ELDPEKTVMDNLAEGK---------QEVMVNGRPRhVLGYLQ---DflfhpkrAMTPVKALSGGERNR 448
|
170 180
....*....|....*....|
gi 494149220 163 VEIAKALSKKADILILDEPT 182
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPT 468
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-230 |
3.43e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 34 LFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFAdseageghgvilihQELNLAEQLSVEEN 113
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYV--------------PQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 114 IFLGR--EIKRGW-FLDKTAmraeakrlldqLQCDVD-----PRTRI--RDLSVS--DRQMVEIAKALSKKADILILDEP 181
Cdd:PLN03232 699 ILFGSdfESERYWrAIDVTA-----------LQHDLDllpgrDLTEIgeRGVNISggQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494149220 182 TAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAIaDRVTVLRDG 230
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
284-488 |
3.87e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKNSGIAY----LtkdrkGSGLLLN 359
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYmpqgL-----GKNLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 MDMRPNLTLLA-LekFGSVIVDRKAEEAALEKA--IEAFdiraADRKAkvGDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:NF033858 93 LSVFENLDFFGrL--FGQDAAERRRRIDELLRAtgLAPF----ADRPA--GKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDR--GKSVILLSSEMPEMLGLsDRIAVMAAGRI--TG 488
Cdd:NF033858 165 TGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVlaTG 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
285-486 |
4.57e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 45.00 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 285 DASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIErdgkpvrIA----SLQDAKNSGIAYLTkdRKGSGLLL-N 359
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLN-------IAghqfDFSQKPSEKAIRLL--RQKVGMVFqQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 360 MDMRPNLTLLALEKFGSVIVDRKAEEAALEKAIEAFD-IRAADrkaKVGDF----SGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:COG4161 91 YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLArLRLTD---KADRFplhlSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 435 PTRGIDIGTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:COG4161 168 PTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
384-486 |
5.56e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.01 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 384 EEAALEKAIEAFDIraadrkakVG-----------DFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIG 452
Cdd:PRK13634 118 EEDAKQKAREMIEL--------VGlpeellarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFY 189
|
90 100 110
....*....|....*....|....*....|....*
gi 494149220 453 DL-TDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK13634 190 KLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
33-234 |
5.65e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.86 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGglvldgaEVSFadseagegHGVILIHQELN-------LA 105
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-------DIRF--------HDIPLTKLQLDswrsrlaVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 106 EQL------SVEENIFLGR------EIKRGWFLdkTAMRAEAKRLLDQLQCDVDPRTRIrdLSVSDRQMVEIAKALSKKA 173
Cdd:PRK10789 395 SQTpflfsdTVANNIALGRpdatqqEIEHVARL--ASVHDDILRLPQGYDTEVGERGVM--LSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 174 DILILDEPTAVLTGR-EVEILfDQIRRLREQGVAIlyIS-HKLDEIKAiADRVTVLRDGrHIV 234
Cdd:PRK10789 471 EILILDDALSAVDGRtEHQIL-HNLRQWGEGRTVI--ISaHRLSALTE-ASEILVMQHG-HIA 528
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
283-486 |
6.16e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.32 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPV-RIASLQDAKNSGI-AYltkdrkgsGLLLNM 360
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDItHVPAENRHVNTVFqSY--------ALFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 361 DMRPNLTL-LALEKFGSVIVDRKAEEAALEKAIEAFdiraADRKAKvgDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGI 439
Cdd:PRK09452 102 TVFENVAFgLRMQKTPAAEITPRVMEALRMVQLEEF----AQRKPH--QLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494149220 440 DIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-212 |
7.37e-05 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 43.30 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 33 VLFDVSVDLYAGEVHALLGENGAGKSTLVKILsgyhepteGGLvldgaevsfadSEAGEGHgvILIHQELNLaeqlsvee 112
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL--------AGL-----------WPWGSGR--IGMPEGEDL-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 113 nIFLGReikRGWFLDKTamraeakrLLDQLqcdVDPRTRIrdLSVSDRQMVEIAKALSKKADILILDEPTAVLTGrEVEI 192
Cdd:cd03223 67 -LFLPQ---RPYLPLGT--------LREQL---IYPWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE-ESED 128
|
170 180
....*....|....*....|
gi 494149220 193 LFDQIrrLREQGVAILYISH 212
Cdd:cd03223 129 RLYQL--LKELGITVISVGH 146
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
287-486 |
8.19e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 44.61 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 287 SFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIAS---LQDAKNSGIAYLTKDRKgsglLLNMDMR 363
Cdd:PRK13638 21 NLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVATVFQDPEQQ----IFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 364 PNLTLlALEKFGSvivdrkAEEAALEKAIEAFDIRAAD--RKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDI 441
Cdd:PRK13638 97 SDIAF-SLRNLGV------PEAEITRRVDEALTLVDAQhfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 442 GTKSQIYHFIGDLTDRGKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-208 |
8.62e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.68 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 28 FGPaqvlFDVSVDlyAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVSFADSEAgegHGVILIHQElNLAEQ 107
Cdd:PRK13543 27 FGP----LDFHVD--AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSR---FMAYLGHLP-GLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 LSVEENI-FL----GREIKRgwfldktaMRAEAKRLLDQLQCDvdpRTRIRDLSVSDRQMVEIAKALSKKADILILDEPT 182
Cdd:PRK13543 97 LSTLENLhFLcglhGRRAKQ--------MPGSALAIVGLAGYE---DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180
....*....|....*....|....*..
gi 494149220 183 AVLTGREVEILFDQIR-RLREQGVAIL 208
Cdd:PRK13543 166 ANLDLEGITLVNRMISaHLRGGGAALV 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
409-462 |
1.09e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 42.91 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 494149220 409 FSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFigdLTDRGKSVI 462
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL---LKELGITVI 142
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
161-222 |
1.46e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 1.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 161 QMVEIAKALSKKAD---ILILDEPTavlTG---REVEILFDQIRRLREQGVAILYISHKLDEIKAiAD 222
Cdd:COG0178 833 QRVKLASELSKRSTgktLYILDEPT---TGlhfHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT-AD 896
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-77 |
1.57e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 1.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 494149220 19 LSGRKICKSFGPAQVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVL 77
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-224 |
1.61e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 148 PRTRIRDLSVSDRQMVEIAKALSkkADIL----ILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKlDEIKAIADR 223
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADR 546
|
.
gi 494149220 224 V 224
Cdd:PRK00635 547 I 547
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
410-486 |
2.11e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.58 E-value: 2.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494149220 410 SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
381-454 |
2.16e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.05 E-value: 2.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494149220 381 RKAEEAALEKAIEAFDIRAADRKAkVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL 454
Cdd:PRK10253 117 RKEDEEAVTKAMQATGITHLADQS-VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL 189
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
108-229 |
2.21e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 108 LSVEENIFLGREikrgwfldkTAMRAEAKR-------------LLDQLQCDVDPRTRirDLSVSDRQMVEIAKALSKKAD 174
Cdd:PTZ00265 1310 MSIYENIKFGKE---------DATREDVKRackfaaidefiesLPNKYDTNVGPYGK--SLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 494149220 175 ILILDEPTAVLTGREVEILFDQIRRLREQG-VAILYISHKLDEIKAiADRVTVLRD 229
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-83 |
2.32e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 2.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 494149220 33 VLFD-VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVLDGAEVS 83
Cdd:PRK13538 15 ILFSgLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR 66
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-238 |
2.68e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 32 QVLFDVSVDLYAGEVHALLGENGAGKSTLVKILSGYHEP--TEGGLVLDG---AEVSFAD----SEAGEGHGVILIHQE- 101
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpkKQETFARisgyCEQNDIHSPQVTVREs 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 ------LNLAEQLSVEENIFlgreikrgwFLDKTAMRAEakrlLDQLQCDVDPRTRIRDLSVSDRQMVEIAKALSKKADI 175
Cdd:PLN03140 974 liysafLRLPKEVSKEEKMM---------FVDEVMELVE----LDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSI 1040
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494149220 176 LILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHK--LDEIKAIADRVTVLRDGRHIVTEPV 238
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSGPL 1105
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
392-492 |
3.25e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.44 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 392 IEAFDIRAAdRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPE 470
Cdd:PRK11831 128 LEAVGLRGA-AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPE 206
|
90 100
....*....|....*....|..
gi 494149220 471 MLGLSDRIAVMAAGRItgILEG 492
Cdd:PRK11831 207 VLSIADHAYIVADKKI--VAHG 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-182 |
3.30e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 24 ICKSFGpAQVLFD-VSVDLYAGEVHALLGENGAGKSTLVKILSGYHEPTEGGLVL-DGAEVSFADSEAGeghgvilihqe 101
Cdd:PRK11819 330 LSKSFG-DRLLIDdLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVDQSRD----------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 102 lNLAEQLSVEENIFLGREIKRgwfLDKTAM--RAEAKRL----LDQLQcdvdprtRIRDLSVSDRQMVEIAKALSKKADI 175
Cdd:PRK11819 398 -ALDPNKTVWEEISGGLDIIK---VGNREIpsRAYVGRFnfkgGDQQK-------KVGVLSGGERNRLHLAKTLKQGGNV 466
|
....*..
gi 494149220 176 LILDEPT 182
Cdd:PRK11819 467 LLLDEPT 473
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
161-222 |
3.74e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 3.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494149220 161 QMVEIAKALSKKAD---ILILDEPTavlTGreveiL-FDQIR-------RLREQGVAILYISHKLDEIKAiAD 222
Cdd:PRK00349 837 QRVKLAKELSKRSTgktLYILDEPT---TG-----LhFEDIRkllevlhRLVDKGNTVVVIEHNLDVIKT-AD 900
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
283-440 |
4.15e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.36 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRErSSGTIERDGKPVRIASLQdaknsgiayltKDRKGSGL------ 356
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQ-----------TWRKAFGVipqkvf 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 357 LLNMDMRPNLTllALEKFGSVIVDRKAEEAALEKAIEAF----DIRAADrkakvGDF--SGGNQQKLLLAKVMETDPDIV 430
Cdd:TIGR01271 1303 IFSGTFRKNLD--PYEQWSDEEIWKVAEEVGLKSVIEQFpdklDFVLVD-----GGYvlSNGHKQLMCLARSILSKAKIL 1375
|
170
....*....|
gi 494149220 431 IIDEPTRGID 440
Cdd:TIGR01271 1376 LLDEPSAHLD 1385
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
283-486 |
4.24e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.48 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGL---RERSSGTIERDGKPVRIASLQDAKNS-GIAYLTKDRKGSGLLL 358
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIREKvGIVFQNPDNQFVGATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 359 NMDMRpnltlLALEKFGsviVDRKAEEAALEKAIEafDIRAAD-RKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTR 437
Cdd:PRK13640 103 GDDVA-----FGLENRA---VPRPEMIKIVRDVLA--DVGMLDyIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 438 GIDIGTKSQIYHFIGDL-TDRGKSVILLSSEMPEMlGLSDRIAVMAAGRI 486
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
283-486 |
4.50e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.48 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGkpVRIASLQDAKnsgiayLTKDRKGSGLLLNmdm 362
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG--QDLTALSEKE------LRKARRQIGMIFQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 rpNLTLLAlekfgSVIVdrkAEEAALekAIEAFDIRAADRKAKVGDF-----------------SGGNQQKLLLAKVMET 425
Cdd:PRK11153 90 --HFNLLS-----SRTV---FDNVAL--PLELAGTPKAEIKARVTELlelvglsdkadrypaqlSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 426 DPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDR-GKSVILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
375-462 |
6.46e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 375 GSV--IVDRKAEEAALEKAIEAFDIRAA-DRKakVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFI 451
Cdd:PRK13409 178 GKVreLLKKVDERGKLDEVVERLGLENIlDRD--ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLI 255
|
90
....*....|.
gi 494149220 452 GDLTdRGKSVI 462
Cdd:PRK13409 256 RELA-EGKYVL 265
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
283-447 |
8.69e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 42.24 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 283 VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASLQDAKnSGIAYLTKDRkgsgLLLNMDM 362
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR-FKITIIPQDP----VLFSGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 363 RPNLtllalEKFGSVI---VDRKAEEAALEKAIEAFDIRAADRKAKVGD-FSGGNQQKLLLAKVMETDPDIVIIDEPTRG 438
Cdd:TIGR00957 1377 RMNL-----DPFSQYSdeeVWWALELAHLKTFVSALPDKLDHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
....*....
gi 494149220 439 IDIGTKSQI 447
Cdd:TIGR00957 1452 VDLETDNLI 1460
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
287-434 |
1.19e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 287 SFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIA--SLQDAKNSGIAyltkdrkgsglllNMDMRP 364
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAisSGLNGQLTGIE-------------NIELKG 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 365 NLTLLALEKFGSVIvdrkaeeaalEKAIEAFDIRAADRKAkVGDFSGGNQQKLLLAKVMETDPDIVIIDE 434
Cdd:PRK13545 111 LMMGLTKEKIKEII----------PEIIEFADIGKFIYQP-VKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
130-223 |
1.72e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.27 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 130 AMRAEAKRLLDQLQC-----DVDPRTRIRDLSVSDRQMVEIAKALS----KKADILILDEPTAVLTGREVEILFDQIRRL 200
Cdd:cd03227 48 AQSATRRRSGVKAGCivaavSAELIFTRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEH 127
|
90 100
....*....|....*....|...
gi 494149220 201 REQGVAILYISHKLdEIKAIADR 223
Cdd:cd03227 128 LVKGAQVIVITHLP-ELAELADK 149
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
284-486 |
2.09e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 40.86 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 284 RDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVriaslQDAKNSGIAYLTKDRKG-----SGLLL 358
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV-----ATLDADALAQLRREHFGfifqrYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 359 NMDMRPNLTLLAlekfgsvIVDRKAEEAALEKAIEAFD-IRAADR-KAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPT 436
Cdd:PRK10535 100 HLTAAQNVEVPA-------VYAGLERKQRLLRAQELLQrLGLEDRvEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494149220 437 RGIDIGTKSQIYHFIGDLTDRGKSVILLSSEmPEMLGLSDRIAVMAAGRI 486
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
267-441 |
2.32e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.45 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 267 SAPIVLSVRDLSVPgqvRDAS-------FDLHKGEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRIASlqda 339
Cdd:PRK13543 7 TAPPLLAAHALAFS---RNEEpvfgpldFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 340 KNSGIAYLTKDrkgSGLLLNMDMRPNLTLL-ALEKFGSvivdRKAEEAALekAIEAFdirAADRKAKVGDFSGGNQQKLL 418
Cdd:PRK13543 80 RSRFMAYLGHL---PGLKADLSTLENLHFLcGLHGRRA----KQMPGSAL--AIVGL---AGYEDTLVRQLSAGQKKRLA 147
|
170 180
....*....|....*....|...
gi 494149220 419 LAKVMETDPDIVIIDEPTRGIDI 441
Cdd:PRK13543 148 LARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
410-479 |
2.71e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.77 E-value: 2.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 410 SGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRgKSVILLSSEMPEMLGLSDRIA 479
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
293-477 |
2.93e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 39.38 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 293 GEVLGFAGIVGAGRTALMEAIIGLRERSSGTIERDGKPVRI------ASLQdAKNSGIAYltkdrKGSGLLLNMDMRPNL 366
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearAKLR-AKHVGFVF-----QSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 367 TLLALEKFGSVIVDRKAEEAALEKAieAFDIRAADRKAKVgdfSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQ 446
Cdd:PRK10584 110 ELPALLRGESSRQSRNGAKALLEQL--GLGKRLDHLPAQL---SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190
....*....|....*....|....*....|.
gi 494149220 447 IYHFIGDLTDRGKSVILLSSEMPEMLGLSDR 477
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLAARCDR 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
401-443 |
3.28e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 3.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 494149220 401 DRKAKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGT 443
Cdd:PRK11147 149 DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
385-486 |
3.87e-03 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 39.28 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 385 EAALEkAIEAFDI--RAADRKAKVgdfSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDL-TDRGKSV 461
Cdd:PRK11247 112 DAALQ-ALAAVGLadRANEWPAAL---SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTV 187
|
90 100
....*....|....*....|....*
gi 494149220 462 ILLSSEMPEMLGLSDRIAVMAAGRI 486
Cdd:PRK11247 188 LLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
49-134 |
5.60e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.59 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 49 LLGENGAGKSTLVKIL-SGYHEPTEGGlvldGAEVSFADSEAgeghgvilihqELNLAEQLSVEENIflgREIKRGWFLd 127
Cdd:COG3910 42 FVGENGSGKSTLLEAIaVAAGFNPEGG----SKNFRFSTRES-----------ESALGEYLRLSRGL---PKPRDGFFL- 102
|
....*..
gi 494149220 128 ktamRAE 134
Cdd:COG3910 103 ----RAE 105
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
300-469 |
6.60e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 300 GIVGAGRTALMEAIIGLRERSSGTIERdgKPVRIASLQDaknsgiAYLTKDRKGSGLLLNMDMRPNLtllaleKFGSVIV 379
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAK------PYCTYIGHNLGLKLEMTVFENL------KFWSEIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 380 DrkaEEAALEKAIEAFDIRAADRKaKVGDFSGGNQQKLLLAKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGDLTDRGk 459
Cdd:PRK13541 99 N---SAETLYAAIHYFKLHDLLDE-KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSG- 173
|
170
....*....|
gi 494149220 460 SVILLSSEMP 469
Cdd:PRK13541 174 GIVLLSSHLE 183
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
155-224 |
8.09e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.01 E-value: 8.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494149220 155 LSVSDRQMVEIAKALSKKAD--ILILDEPTAVLTGREVEILFDQIRRLREQGVAILYISHKLDEIKAiADRV 224
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
272-463 |
8.36e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 37.85 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 272 LSVRDLSV--PGQ--VRDASFDLHKGEVLGFAGIVGAGRTALMEAIIGLRE---RSSGTIERDGKpvRIASLQdAKNSGI 344
Cdd:COG4136 2 LSLENLTItlGGRplLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGR--RLTALP-AEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494149220 345 AYLTKDRkgsglLL--NMDMRPNLtLLAL-EKFGSVivDRKAE-EAALEKA-IEAFdiraADRKakVGDFSGGNQQKLLL 419
Cdd:COG4136 79 GILFQDD-----LLfpHLSVGENL-AFALpPTIGRA--QRRARvEQALEEAgLAGF----ADRD--PATLSGGQRARVAL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494149220 420 AKVMETDPDIVIIDEPTRGIDIGTKSQIYHFIGD-LTDRGKSVIL 463
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALL 189
|
|
| |
