|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-503 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 627.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATL--TRRAAELGVRAVYQ 95
Cdd:COG1129 12 KSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI-----LLDGEPVRFrsPRDAQAAGIAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:COG1129 87 ELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHVDIAP 255
Cdd:COG1129 167 PTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRELEDLFP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 256 VAPQEIvDQAVLEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDML 335
Cdd:COG1129 247 KRAAAP-GEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 336 KRGIGYTPENRKEAGIIPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVI 415
Cdd:COG1129 326 RAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 416 GRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQEF-HAPVNVDE 494
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELdREEATEEA 485
|
....*....
gi 1314860479 495 LMSAILSVH 503
Cdd:COG1129 486 IMAAATGGA 494
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-495 |
9.83e-156 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 452.56 E-value: 9.83e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGDEATLT--RRAAELGVRAVYQ 95
Cdd:COG3845 13 KRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-----DGKPVRIRspRDAIALGIGMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:COG3845 88 HFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRD---HVD 252
Cdd:COG3845 168 PTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGREvllRVE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 253 IAPVAPQEIvdqaVLEVRAL-----RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT 327
Cdd:COG3845 248 KAPAEPGEV----VLEVENLsvrddRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 328 RPDYGDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTN--RQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTL 405
Cdd:COG3845 324 GLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRyrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARSL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 406 SGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
490
....*....|.
gi 1314860479 486 FHAP-VNVDEL 495
Cdd:COG3845 484 VPAAeATREEI 494
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-500 |
5.63e-146 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 427.79 E-value: 5.63e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEgdeATLTRRAAELGVRAVYQEL 97
Cdd:PRK11288 12 KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR---FASTTAALAAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PRK11288 89 HLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 178 SSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQ-VAGDVMLENTSTHHIVSLMLGRDHVDIAPV 256
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRyVATFDDMAQVDRDQLVQAMVGREIGDIYGY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 257 APQEIVDQAvLEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLK 336
Cdd:PRK11288 249 RPRPLGEVR-LRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 337 RGIGYTPENRKEAGIIPWLGVDENTVLTNRQKISANGVL---QWStiRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKV 413
Cdd:PRK11288 328 AGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLinnRWE--AENADRFIRSLNIKTPSREQLIMNLSGGNQQKA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 414 VIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQEF-HAPVNV 492
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELaREQATE 485
|
....*...
gi 1314860479 493 DELMSAIL 500
Cdd:PRK11288 486 RQALSLAL 493
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-486 |
7.86e-145 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 425.11 E-value: 7.86e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSeRPdSGDiWIGETRLEGDE--ATLTRRAAELGVRAVYQ 95
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YP-HGT-YEGEIIFEGEElqASNIRDTERAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK13549 90 ELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHVDIAP 255
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGRELTALYP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 256 VAPQEIVDQaVLEVRAL-------RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLeeYE---QGEIVINGEK 325
Cdd:PRK13549 250 REPHTIGEV-ILEVRNLtawdpvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA--YPgrwEGEIFIDGKP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 326 ITRPDYGDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTL 405
Cdd:PRK13549 327 VKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 406 SGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
.
gi 1314860479 486 F 486
Cdd:PRK13549 487 L 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-500 |
3.37e-132 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 393.00 E-value: 3.37e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETrlegDEATLTRR-AAELGVRAVYQE 96
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI----NYNKLDHKlAAQLGIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGQWPRRNGM----IDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVI 172
Cdd:PRK09700 89 LSVIDELTVLENLYIGRHLTKKVCgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 173 LDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHVD 252
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRELQN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 253 IAPvAPQEIVDQA----VLEVRAL--RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKI 326
Cdd:PRK09700 249 RFN-AMKENVSNLahetVFEVRNVtsRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 327 TRPDYGDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTNRQKIS----ANGVLQWSTIRRLTEEVMQRMTVKAASSETPI 402
Cdd:PRK09700 328 SPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGgykgAMGLFHEVDEQRTAENQRELLALKCHSVNQNI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 403 GTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTF 482
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
490 500
....*....|....*....|
gi 1314860479 483 SQEFHAPVNV--DELMSAIL 500
Cdd:PRK09700 488 TQILTNRDDMseEEIMAWAL 507
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-480 |
1.16e-126 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 377.92 E-value: 1.16e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGDEATL--TRRAAELGVRAVY 94
Cdd:PRK10982 5 SKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-----QGKEIDFksSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHVDIA 254
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 255 PV---APQEIvdqaVLEVRAL--RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRP 329
Cdd:PRK10982 240 PDkenKPGEV----ILEVRNLtsLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 330 DYGDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTN-RQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGG 408
Cdd:PRK10982 316 NANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNiRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGG 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 409 NQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-498 |
2.95e-119 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 359.32 E-value: 2.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLT--RRAAELGVRAVYQ 95
Cdd:PRK10762 12 KAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI-----LYLGKEVTFNgpKSSQEAGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQWPR-RNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK10762 87 ELNLIPQLTIAENIFLGREFVnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHVDIA 254
Cdd:PRK10762 167 EPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKLEDQY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 255 P---VAPQEIvdqaVLEVRALRhKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDY 331
Cdd:PRK10762 247 PrldKAPGEV----RLKVDNLS-GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 332 GDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTNRQKIS-ANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQ 410
Cdd:PRK10762 322 QDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSrAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 411 QKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQEF-HAP 489
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFtREQ 481
|
....*....
gi 1314860479 490 VNVDELMSA 498
Cdd:PRK10762 482 ATQEKLMAA 490
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-486 |
3.14e-118 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 356.79 E-value: 3.14e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDiwiGETRLEGDEATL--TRRAAELGVRAVYQ 95
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYE---GEILFDGEVCRFkdIRDSEALGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:NF040905 86 ELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAG--DVMLENTSTHHIVSLMLGRDHVDI 253
Cdd:NF040905 166 PTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtlDCRADEVTEDRIIRGMVGRDLEDR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 254 APVAPQEIVDqAVLEVRAL-------RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLE--EYEQGEIVINGE 324
Cdd:NF040905 246 YPERTPKIGE-VVFEVKNWtvyhplhPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 325 KITRPDYGDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGT 404
Cdd:NF040905 325 EVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSVFQKVGN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 405 LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITG 484
|
..
gi 1314860479 485 EF 486
Cdd:NF040905 485 EL 486
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-486 |
2.43e-115 |
|
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: 349.51 E-value: 2.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSgdiWIGETRLEGDE--ATLTRRAAELGVRAVYQ 95
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT---WDGEIYWSGSPlkASNIRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQWPRRNGMI-DYLQMAQDAQRCLQALGVDVSPEQL-VSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPGGRmAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHVDI 253
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREITSL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 254 APVAPQEIVDQaVLEVRAL-------RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYE-QGEIVINGEK 325
Cdd:TIGR02633 246 YPHEPHEIGDV-ILEARNLtcwdvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 326 ITRPDYGDMLKRGIGYTPENRKEAGIIPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTL 405
Cdd:TIGR02633 325 VDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 406 SGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
.
gi 1314860479 486 F 486
Cdd:TIGR02633 485 F 485
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-496 |
2.94e-107 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 328.93 E-value: 2.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 3 TATEAVPVAKVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegdeATLT 82
Cdd:PRK15439 4 SDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC----ARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 83 -RRAAELGVRAVYQELSLVEGLTVAENLCLGqWPRRNGmiDYLQMAQdaqrCLQALGVDVSPEQLVSTLSPAQKQLVEIA 161
Cdd:PRK15439 80 pAKAHQLGIYLVPQEPLLFPNLSVKENILFG-LPKRQA--SMQKMKQ----LLAALGCQLDLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 162 RVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHI 241
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 242 VSLM--LGRDH---------VDIAPVAPQEIVDQAVLEVRALRHKpKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVG 310
Cdd:PRK15439 233 IQAItpAAREKslsasqklwLELPGNRRQQAAGAPVLTVEDLTGE-GFRNISLEVRAGEILGLAGVVGAGRTELAETLYG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 311 LEEYEQGEIVINGEKITRPDYGDMLKRGIGYTPENRKEAGI-----IPW----LGVDENTVLTNRQKISAngVLqwstir 381
Cdd:PRK15439 312 LRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLyldapLAWnvcaLTHNRRGFWIKPARENA--VL------ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 382 rltEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFIS 461
Cdd:PRK15439 384 ---ERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFIS 460
|
490 500 510
....*....|....*....|....*....|....*.
gi 1314860479 462 SEVEELPLVCDRILLLQHGTFSQEF-HAPVNVDELM 496
Cdd:PRK15439 461 SDLEEIEQMADRVLVMHQGEISGALtGAAINVDTIM 496
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
265-482 |
2.51e-77 |
|
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: 240.03 E-value: 2.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIGYTPE 344
Cdd:cd03215 3 PVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 345 NRKEAGIIPWLGVDENTVLTNRqkisangvlqwstirrlteevmqrmtvkaassetpigtLSGGNQQKVVIGRWVYAASQ 424
Cdd:cd03215 83 DRKREGLVLDLSVAENIALSSL--------------------------------------LSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 425 ILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTF 482
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-230 |
7.13e-63 |
|
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: 202.27 E-value: 7.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEAtltRRAAELGVRAVYQe 96
Cdd:cd03216 7 TKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP---RDARRAGIAMVYQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 lslvegltvaenlclgqwprrngmidylqmaqdaqrclqalgvdvspeqlvstLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:cd03216 83 -----------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 177 TSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-480 |
1.74e-59 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 204.37 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSErPDSGDIwIGETRLEGDEaTLTRRAAELGVRA--VY 94
Cdd:COG1123 13 RYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRI-SGEVLLDGRD-LLELSEALRGRRIgmVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QE--LSLVeGLTVAENLCLGqwpRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVI 172
Cdd:COG1123 90 QDpmTQLN-PVTVGDQIAEA---LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 173 LDEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRDHV 251
Cdd:COG1123 166 ADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 252 DIAPVAPQEIVDQAVLEVRAL---------RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVIN 322
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNLskrypvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 323 GEKITRPDYGDMLKRgigytpenRKEAGIIPWlgvDENTVLTNRQKI--------SANGVLQWSTIRRLTEEVMQRMTVK 394
Cdd:COG1123 326 GKDLTKLSRRSLREL--------RRRVQMVFQ---DPYSSLNPRMTVgdiiaeplRLHGLLSRAERRERVAELLERVGLP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 395 AASSETPIGTLSGGNQQKVVIGRwVYAAS-QILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFIS---SEVEELpl 469
Cdd:COG1123 395 PDLADRYPHELSGGQRQRVAIAR-ALALEpKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFIShdlAVVRYI-- 471
|
490
....*....|.
gi 1314860479 470 vCDRILLLQHG 480
Cdd:COG1123 472 -ADRVAVMYDG 481
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-227 |
3.22e-47 |
|
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: 163.76 E-value: 3.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEAtltRRAAELGVRAVYQEL 97
Cdd:cd03219 8 KRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP---HEIARLGIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLG-QWPRRNGMID------YLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRV 170
Cdd:cd03219 85 RLFPELTVLENVMVAaQARTGSGLLLararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 171 VILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
17-227 |
4.33e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.31 E-value: 4.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRaaeLGVraVYQE 96
Cdd:COG1131 7 TKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR---IGY--VPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGQWPRRngmIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:COG1131 82 PALYPDLTVRENLRFFARLYG---LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 177 TSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-227 |
2.90e-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: 153.66 E-value: 2.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEAtltRRAAELGVRAVYQEL 97
Cdd:COG0411 12 KRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP---HRIARLGIARTFQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLG-QWPRRNGMIDYL-----------QMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMK 165
Cdd:COG0411 89 RLFPELTVLENVLVAaHARLGRGLLAALlrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 166 GEPRVVILDEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-227 |
4.62e-39 |
|
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: 139.84 E-value: 4.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLeGDEATLTRRaaELGVraVYQEL 97
Cdd:cd03230 8 KRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKR--RIGY--LPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLclgqwprrngmidylqmaqdaqrclqalgvdvspeqlvsTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:cd03230 83 SLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 178 SSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-230 |
7.01e-39 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 141.32 E-value: 7.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegDEATLTRRAAELGVraVYQ-- 95
Cdd:COG1122 9 SYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI--TKKNLRELRRKVGL--VFQnp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENLCLGqwPRRNGMiDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:COG1122 85 DDQLFAP-TVEEDVAFG--PENLGL-PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-226 |
1.23e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 138.86 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 12 KVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegDEATLTRRAAELGVR 91
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--TDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 92 AVYQELSLVEGLTVAENLCLGqwprrngmidylqmaqdaqrclqalgvdvspeqlvstLSPAQKQLVEIARVMKGEPRVV 171
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 172 ILDEPTSSL---ASAEVELVISAVKKMsaLGVAVIYVSHRMEEIRRIASCATVMRDGQ 226
Cdd:cd03229 123 LLDEPTSALdpiTRREVRALLKSLQAQ--LGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
17-228 |
1.27e-38 |
|
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: 140.76 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGDEATLTRRAA--ELGVraVY 94
Cdd:COG4555 8 SKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-----DGEDVRKEPREArrQIGV--LP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENL----CLgqwprrNGMIDYlQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRV 170
Cdd:COG4555 81 DERGLYDRLTVRENIryfaEL------YGLFDE-ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 171 VILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-226 |
1.89e-38 |
|
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: 139.52 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegDEATLTRRAAELGVraVYQ- 95
Cdd:cd03225 8 SYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVGL--VFQn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 -ELSLVeGLTVAENLCLGQwprRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:cd03225 84 pDDQFF-GPTVEEEVAFGL---ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQ 226
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
17-227 |
3.47e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.81 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRA-AELGVraVY 94
Cdd:COG3638 9 SKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrRRIGM--IF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLCLGQWPRRNGMIDYLQM--AQDAQRCLQALG-VDVSPE--QLVSTLSPAQKQLVEIARVMKGEPR 169
Cdd:COG3638 87 QQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLfpPEDRERALEALErVGLADKayQRADQLSGGQQQRVAIARALVQEPK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 170 VVILDEPTSSL--ASAEVelVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG3638 167 LILADEPVASLdpKTARQ--VMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
274-481 |
2.61e-37 |
|
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: 137.30 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 274 HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYgdMLKRGIGYTPENRkeaGIIP 353
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQIGVLPDER---GLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 WLGVDENTVLTNRqkisANGvLQWSTIRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTR 433
Cdd:COG4555 88 RLTVRENIRYFAE----LYG-LFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314860479 434 GVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-178 |
3.43e-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: 131.23 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRaaelGVRAVYQELSLVEGLTV 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 106 AENLCLGqwpRRNGMIDYLQMAQDAQRCLQALGV----DVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:pfam00005 77 RENLRLG---LLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-230 |
3.94e-36 |
|
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: 134.23 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDeatltRRAAELGVRA---- 92
Cdd:cd03256 8 KTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKL-----KGKALRQLRRqigm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 93 VYQELSLVEGLTVAENL---CLGQWP------RRNGMIDYlqmaQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARV 163
Cdd:cd03256 83 IFQQFNLIERLSVLENVlsgRLGRRStwrslfGLFPKEEK----QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 164 MKGEPRVVILDEPTSSLASAEVELVISAVKKM-SALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
267-480 |
4.76e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.65 E-value: 4.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRH----KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpDYGDMLKRgIGYT 342
Cdd:COG1131 1 IEVRGLTKrygdKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 343 PEnrkEAGIIPWLGVDENTVLTNRqkisANGvLQWSTIRRLTEEVMQR--MTVKAassETPIGTLSGGNQQKVVIGRWVY 420
Cdd:COG1131 79 PQ---EPALYPDLTVRENLRFFAR----LYG-LPRKEARERIDELLELfgLTDAA---DRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 421 AASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFIS---SEVEELplvCDRILLLQHG 480
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSThylEEAERL---CDRVAIIDKG 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-231 |
6.01e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 133.24 E-value: 6.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYP----GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEATLTR-RAAELGV 90
Cdd:COG1136 11 TKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELARlRRRHIGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 raVYQELSLVEGLTVAENLCLGQWPRRngmIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRV 170
Cdd:COG1136 91 --VFQFFNLLPELTALENVALPLLLAG---VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 171 VILDEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMeeirRIASCAT---VMRDGQVAGDV 231
Cdd:COG1136 166 ILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDP----ELAARADrviRLRDGRIVSDE 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-228 |
2.47e-35 |
|
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: 131.10 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlegDEATLTRRAAEL-GVRAVYQE 96
Cdd:cd03259 8 KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-------DGRDVTGVPPERrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGqwPRRNGMiDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:cd03259 81 YALFPHLTVAENIAFG--LKLRGV-PKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 177 TSSL-ASAEVELViSAVKKM-SALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:cd03259 158 LSALdAKLREELR-EELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-227 |
3.07e-35 |
|
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: 131.07 E-value: 3.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPG----VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEATLTR-RAAELGV 90
Cdd:cd03255 7 SKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAfRRRHIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 raVYQELSLVEGLTVAENLCLGQWPRRngmIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRV 170
Cdd:cd03255 87 --VFQSFNLLPDLTALENVELPLLLAG---VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 171 VILDEPTSSLASAEVELVISAVKKMSAL-GVAVIYVSHRMeEIRRIASCATVMRDGQV 227
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-227 |
8.37e-35 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 129.93 E-value: 8.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDeatltRRAA--ELGVraV 93
Cdd:cd03263 8 KTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD-----RKAArqSLGY--C 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 94 YQELSLVEGLTVAENL-------CLGQWPRR---NGMIDYLQMAQDAQRclqalgvdvspeqLVSTLSPAQKQLVEIARV 163
Cdd:cd03263 81 PQFDALFDELTVREHLrfyarlkGLPKSEIKeevELLLRVLGLTDKANK-------------RARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 164 MKGEPRVVILDEPTSSLASA---EVELVISAVKKMSalgvAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPAsrrAIWDLILEVRKGR----SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
267-480 |
4.99e-34 |
|
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: 126.36 E-value: 4.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdYGDMLKRGIGYT 342
Cdd:cd03230 1 IEVRNLSkrygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 343 PEnrkEAGIIPWLGVDENtvltnrqkisangvLQwstirrlteevmqrmtvkaassetpigtLSGGNQQKVVIGRWVYAA 422
Cdd:cd03230 79 PE---EPSLYENLTVREN--------------LK----------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-231 |
6.69e-34 |
|
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: 127.70 E-value: 6.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 10 VAKVVAGNKRypGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEATLTRRAAEL 88
Cdd:cd03258 7 VSKVFGDTGG--KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKARRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 89 GVraVYQELSLVEGLTVAEN----LCLGQWPRRngmidylQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVM 164
Cdd:cd03258 85 GM--IFQHFNLLSSRTVFENvalpLEIAGVPKA-------EIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 165 KGEPRVVILDEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVA--GDV 231
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINReLGLTIVLITHEMEVVKRICDRVAVMEKGEVVeeGTV 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-228 |
2.14e-33 |
|
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: 126.01 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 10 VAKVVAGnkrYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEAT--LTRRAAE 87
Cdd:cd03224 3 VENLNAG---YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI-----RFDGRDITglPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 88 LGVRAVYQELSLVEGLTVAENLCLGQWPRRNGmidylqmaqDAQRCLQALgVDVSP------EQLVSTLSPAQKQLVEIA 161
Cdd:cd03224 75 AGIGYVPEGRRIFPELTVEENLLLGAYARRRA---------KRKARLERV-YELFPrlkerrKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 162 RVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
263-482 |
2.17e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.74 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 263 DQAVLEVR----ALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPdygdmlKRG 338
Cdd:COG1121 3 MMPAIELEnltvSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 339 IGYTPENRkeagiipwlGVDEN-------TVLTNRQkiSANGVLQWSTI--RRLTEEVMQRmtVKAAS-SETPIGTLSGG 408
Cdd:COG1121 77 IGYVPQRA---------EVDWDfpitvrdVVLMGRY--GRRGLFRRPSRadREAVDEALER--VGLEDlADRPIGELSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 409 NQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTF 482
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-230 |
4.50e-33 |
|
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: 125.10 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 28 NVNFTLNkGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQELSLVEGLTVAE 107
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 108 NLCLGQWPRRNGmidylQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVEL 187
Cdd:cd03297 95 NLAFGLKRKRNR-----EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314860479 188 VISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:cd03297 170 LLPELKQIKKnLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-226 |
6.50e-33 |
|
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: 122.74 E-value: 6.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 16 GNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEgdeatltrraaelgvravyq 95
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 elslvegltvaeNLCLGQWPRRNGMidylqmaqdaqrclqalgvdvspeqlVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:cd00267 65 ------------KLPLEELRRRIGY--------------------------VPQLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQ 226
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-228 |
2.04e-32 |
|
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: 124.39 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegdeATLTRR--AAELGVraVYQE 96
Cdd:COG1120 10 GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL----ASLSRRelARRIAY--VPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGQWPRRNGMIDYlqMAQDAQRCLQALG-VDVSP--EQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:COG1120 84 PPAPFGLTVRELVALGRYPHLGLFGRP--SAEDREAVEEALErTGLEHlaDRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 174 DEPTSSL-ASAEVElVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:COG1120 162 DEPTSHLdLAHQLE-VLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-227 |
2.19e-32 |
|
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: 129.64 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 3 TATEAVPVAKVVAGNKRYP-----GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEG 76
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 77 DEATLTRRAAELGVraVYQ--ELSLVEGLTVAEnlCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDvsPEQL---VSTLS 151
Cdd:COG1123 333 SRRSLRELRRRVQM--VFQdpYSSLNPRMTVGD--IIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLAdryPHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 152 PAQKQLVEIARVMKGEPRVVILDEPTSSL-AS--AEV-ELVISAVKKmsaLGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALdVSvqAQIlNLLRDLQRE---LGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
271-477 |
5.57e-32 |
|
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: 121.87 E-value: 5.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 271 ALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpdygdMLKRGIGYTPENRkeag 350
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------KERKRIGYVPQRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 351 iipwlGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRmtVKAASSET--------PIGTLSGGNQQKVVIGRWVYAA 422
Cdd:cd03235 78 -----SIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAK--VDEALERVglseladrQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLL 477
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
18-207 |
8.29e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.05 E-value: 8.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGvravyQEL 97
Cdd:COG4133 10 CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG-----HAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLgqWPRRNGMIDYLQMAQDAqrcLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:COG4133 85 GLKPELTVRENLRF--WAALYGLRADREAIDEA---LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|
gi 1314860479 178 SSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-227 |
1.96e-31 |
|
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: 121.24 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEATLTRRAAELGVraVYQE 96
Cdd:COG1127 13 KSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdGQDITGLSEKELYELRRRIGM--LFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLgqwP-RRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:COG1127 91 GALFDSLTVFENVAF---PlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 176 PTSSL---ASAEVELVISAVKKmsALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG1127 168 PTAGLdpiTSAVIDELIRELRD--ELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-227 |
2.52e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 120.05 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGdeatltRRAAELGVRAVYQE 96
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD------LPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLG----QWPRRNgmIDylqmaQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVI 172
Cdd:cd03301 81 YALYPHMTVYDNIAFGlklrKVPKDE--ID-----ERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 173 LDEPTSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03301 154 MDEPLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-481 |
2.76e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 126.72 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGEtrlegdeatltrraaelGVRAVY--Q 95
Cdd:COG0488 6 KSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------------GLRIGYlpQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQ-----------------------------DAQRCLQALGVDVSP-EQ 145
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDlDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 146 LVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVE-------------LVIS--------AVKKMSAL--GVAV 202
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwleeflknypgtvLVVShdryfldrVATRILELdrGKLT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 203 IYV---SH------------------------RMEE-IRRIASCATvmRDGQVAGDV-MLEntsthhivslmlgrdhvDI 253
Cdd:COG0488 229 LYPgnySAyleqraerleqeaaayakqqkkiaKEEEfIRRFRAKAR--KAKQAQSRIkALE-----------------KL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 254 APVAPQEIVDQA-------------VLEVRALRH----KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQ 316
Cdd:COG0488 290 EREEPPRRDKTVeirfppperlgkkVLELEGLSKsygdKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 317 GEIVInGEKITrpdygdmlkrgIGYTPENRKEagiipwlgVDEN-TVLTNRQKISANGVLQwsTIRRLteevMQRMTVKA 395
Cdd:COG0488 370 GTVKL-GETVK-----------IGYFDQHQEE--------LDPDkTVLDELRDGAPGGTEQ--EVRGY----LGRFLFSG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 396 ASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIyrivrE--LAA-EGkSVVFISSEVEELPLVCD 472
Cdd:COG0488 424 DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL-----EeaLDDfPG-TVLLVSHDRYFLDRVAT 497
|
....*....
gi 1314860479 473 RILLLQHGT 481
Cdd:COG0488 498 RILEFEDGG 506
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
267-480 |
6.33e-31 |
|
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: 119.46 E-value: 6.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR--PDygDMLKRGIG 340
Cdd:cd03224 1 LEVENLNagygKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlpPH--ERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 YTPENRkeaGIIPWLGVDENTVLtnrqkisANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVY 420
Cdd:cd03224 79 YVPEGR---RIFPELTVEENLLL-------GAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 421 AASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
278-482 |
9.74e-31 |
|
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: 118.13 E-value: 9.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygdmLKRGIGYTPENrkeagiipwlgV 357
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE----RRKSIGYVMQD-----------V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 D----ENTV---LTNRQKISANGVLQwstirrlTEEVMQRMTVKAASSETPIgTLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:cd03226 81 DyqlfTDSVreeLLLGLKELDAGNEQ-------AETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTF 482
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
18-231 |
1.26e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.62 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGE---TRLEGDEATLTRRaaELGVraV 93
Cdd:COG2884 9 KRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIPYLRR--RIGV--V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 94 YQELSLVEGLTVAENLCLGQ----WPRRngmidylQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPR 169
Cdd:COG2884 85 FQDFRLLPDRTVYENVALPLrvtgKSRK-------EIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 170 VVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDV 231
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
17-227 |
1.96e-30 |
|
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: 117.70 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQE 96
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLClgqwprrngMIDYlqmaQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:cd03268 87 LTARENLRLLARLL---------GIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 177 TSSLASAevelvisAVKKMSAL-------GVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03268 154 TNGLDPD-------GIKELRELilslrdqGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
17-227 |
2.17e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 118.17 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVraVYQE 96
Cdd:COG1126 8 HKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGM--VFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGqwPRRNGMIDYLQMAQDAQRCLQALG----VDVSPEQLvstlSPAQKQLVEIARVMKGEPRVVI 172
Cdd:COG1126 86 FNLFPHLTVLENVTLA--PIKVKKMSKAEAEERAMELLERVGladkADAYPAQL----SGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 173 LDEPTSSL---ASAEVELVIsavKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG1126 160 FDEPTSALdpeLVGEVLDVM---RDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-228 |
3.97e-30 |
|
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: 117.39 E-value: 3.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEatLTRRAAE----LGVRAVY 94
Cdd:COG0410 12 GYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI-----RFDGED--ITGLPPHriarLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLCLGQWPRRngmiDYLQMAQDAQRCLqalgvDVSPE------QLVSTLSPAQKQLVEIARVMKGEP 168
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYARR----DRAEVRADLERVY-----ELFPRlkerrrQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 169 RVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-227 |
4.37e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 117.91 E-value: 4.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEAtltrRAAELGVRAVYQELSLV 100
Cdd:COG4674 22 GFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGlDEH----EIARLGIGRKFQKPTVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGLTVAENLCL------------------GQWPRRNGMIDYLQMAQDAQRclqalgvdvspeqLVSTLSPAQKQLVEIAR 162
Cdd:COG4674 98 EELTVFENLELalkgdrgvfaslfarltaEERDRIEEVLETIGLTDKADR-------------LAGLLSHGQKQWLEIGM 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 163 VMKGEPRVVILDEPTSSLASAE----VELVISAVKKMSalgvaVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG4674 165 LLAQDPKLLLLDEPVAGMTDAEtertAELLKSLAGKHS-----VVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-227 |
7.09e-30 |
|
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: 116.09 E-value: 7.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVraVYQE 96
Cdd:cd03262 7 HKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM--VFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGQWPRRNgmidyLQMAQDAQRCLQAL---GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:cd03262 85 FNLFPHLTVLENITLAPIKVKG-----MSKAEAEERALELLekvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-227 |
7.33e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 117.05 E-value: 7.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGetrleGDEATlTRRAAELGVRAVYQEL 97
Cdd:cd03296 10 KRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-----GEDAT-DVPVQERNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLG-QWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:cd03296 84 ALFRHMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 177 TSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03296 164 FGALdAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-228 |
7.85e-30 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 123.41 E-value: 7.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEATLTRRaaeLGVraVYQ 95
Cdd:COG2274 482 RYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQ---IGV--VLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENLCLGqwprrNGMIDYlqmaQDAQRCLQALGVD--VS--PEQL-------VSTLSPAQKQLVEIARVM 164
Cdd:COG2274 557 DVFLFSG-TIRENITLG-----DPDATD----EEIIEAARLAGLHdfIEalPMGYdtvvgegGSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 165 KGEPRVVILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIR---RIAscatVMRDGQVA 228
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRladRII----VLDKGRIV 688
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
17-227 |
1.25e-29 |
|
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: 115.74 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTG-----SERPDSGDIWI-GETRLEGDEATLTRRAaelGV 90
Cdd:cd03260 7 NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdGKDIYDLDVDVLELRR---RV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 RAVYQELSLVEGlTVAENLCLGqwPRRNGMIDYLQMAQDAQRCLQ--ALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEP 168
Cdd:cd03260 84 GMVFQKPNPFPG-SIYDNVAYG--LRLHGIKLKEELDERVEEALRkaALWDEVKDRLHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 169 RVVILDEPTSSL---ASAEVELVISAVKKmsalGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03260 161 EVLLLDEPTSALdpiSTAKIEELIAELKK----EYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
274-481 |
1.42e-29 |
|
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: 113.49 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 274 HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmLKRGIGYTPEnrkeagiip 353
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 wlgvdentvltnrqkisangvlqwstirrlteevmqrmtvkaassetpigtLSGGNQQKVVIGRWVYAASQILLLDEPTR 433
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314860479 434 GVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
18-227 |
4.69e-29 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 114.52 E-value: 4.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEATLTRRAAELGVraVYQE 96
Cdd:cd03261 8 KSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDISGLSEAELYRLRRRMGM--LFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLgqWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:cd03261 86 GALFDSLTVFENVAF--PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 177 TSSL---ASAEVELVISAVKKmsALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03261 164 TAGLdpiASGVIDDLIRSLKK--ELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-228 |
1.19e-28 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 112.85 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRaaeLGVraVYQEL 97
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR---IGI--VFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLC----LGQWPRRngmidylQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:cd03265 83 SVDDELTGWENLYiharLYGVPGA-------ERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-480 |
1.70e-28 |
|
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: 118.63 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKS----TLIRMLTGSERPDSGDIWIGETRLEG-DEATLTR-RAAELGVraVYQE 96
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSERELRRiRGNRIAM--IFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 ------------------LSLVEGLTVAEnlclgqwpRRNGMIDYLQMAQ--DAQRCLQALgvdvsPEQLvstlSPAQKQ 156
Cdd:COG4172 101 pmtslnplhtigkqiaevLRLHRGLSGAA--------ARARALELLERVGipDPERRLDAY-----PHQL----SGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 157 LVEIARVMKGEPRVVILDEPTSSL---ASAEV-ELVISAVKKMsalGVAVIYVSHRMEEIRRIASCATVMRDGQVagdvm 232
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALdvtVQAQIlDLLKDLQREL---GMALLLITHDLGVVRRFADRVAVMRQGEI----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 233 LENTSTHHIVS---------LMLGRDHVDIAPVAPQEIVdqaVLEVRALR---------------HKPKLEDISFTLRRG 288
Cdd:COG4172 236 VEQGPTAELFAapqhpytrkLLAAEPRGDPRPVPPDAPP---LLEARDLKvwfpikrglfrrtvgHVKAVDGVSLTLRRG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 289 EVLGIAGLLGAGRSELLKAIVGLEEYEqGEIVINGEKITRPDYGDMLKRgigytpenRKEAGII---------PWLGVDE 359
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPL--------RRRMQVVfqdpfgslsPRMTVGQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 360 nTV----LTNRQKISAngvlqwSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGV 435
Cdd:COG4172 384 -IIaeglRVHGPGLSA------AERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1314860479 436 DIEAKQQIYRIVRELAAE-GKSVVFIS---SEVEELplvCDRILLLQHG 480
Cdd:COG4172 457 DVSVQAQILDLLRDLQREhGLAYLFIShdlAVVRAL---AHRVMVMKDG 502
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
268-481 |
2.51e-28 |
|
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: 111.79 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 268 EVRALRH------KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgIGY 341
Cdd:cd03225 1 ELKNLSFsypdgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 --------------------TPENrkeagiipwLGVDEntvltnrqkisangvlqwSTIRRLTEEVMQRMTVKAASsETP 401
Cdd:cd03225 80 vfqnpddqffgptveeevafGLEN---------LGLPE------------------EEIEERVEEALELVGLEGLR-DRS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 402 IGTLSGGNQQKVVIGRwVYAA-SQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03225 132 PFTLSGGQKQRVAIAG-VLAMdPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
.
gi 1314860479 481 T 481
Cdd:cd03225 211 K 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-226 |
2.64e-28 |
|
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: 110.55 E-value: 2.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEATLTRRAAelgvrAVYQ 95
Cdd:cd03228 9 SYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIA-----YVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENLclgqwprrngmidylqmaqdaqrclqalgvdvspeqlvstLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:cd03228 84 DPFLFSG-TIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 176 PTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIR---RIAscatVMRDGQ 226
Cdd:cd03228 123 ATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRdadRII----VLDDGR 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-238 |
2.71e-28 |
|
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: 112.87 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSG-DIWI-GETRLEGDEATLTRRaaeLGVraVYQE 96
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfGERRGGEDVWELRKR---IGL--VSPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 L--SLVEGLTVAENLC------LGQWPRrngmIDYLQMAQdAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEP 168
Cdd:COG1119 87 LqlRFPRDETVLDVVLsgffdsIGLYRE----PTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 169 RVVILDEPTSSLASAEVELVISAVKKMSALG-VAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTST 238
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-227 |
4.91e-28 |
|
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: 109.83 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegdeATLTRRAaelgvRAvyQELS 98
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL----ASLSPKE-----LA--RKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVegltvaenlclgqwprrngmidyLQmaqdaqrCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:cd03214 77 YV-----------------------PQ-------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 179 SLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03214 127 HLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-227 |
5.48e-28 |
|
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: 111.44 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPG----VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEATLTRRAAELGVr 91
Cdd:cd03257 8 SVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLLKLSRRLRKIRRKEIQM- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 92 aVYQE--LSLVEGLTVAENLCLGQWPRRngmIDYLQMAQDAQRCLQALGVDVSPEQL---VSTLSPAQKQLVEIARVMKG 166
Cdd:cd03257 87 -VFQDpmSSLNPRMTIGEQIAEPLRIHG---KLSKKEARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 167 EPRVVILDEPTSSL-ASAEVElVISAVKKM-SALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03257 163 NPKLLIADEPTSALdVSVQAQ-ILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-482 |
5.92e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 116.83 E-value: 5.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSE--RPDSGDI-----------WIG------------ET 72
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVErpskvgepcpvcGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 73 RLEGDEA-----------TLTRRAAELGVR--AVYQELSLVEglTVAENLCLGQWPRRNGM---IDYLQMAQDAQRCLQa 136
Cdd:TIGR03269 88 TLEPEEVdfwnlsdklrrRIRKRIAIMLQRtfALYGDDTVLD--NVLEALEEIGYEGKEAVgraVDLIEMVQLSHRITH- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 137 lgvdvspeqLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKK-MSALGVAVIYVSHRMEEIRRI 215
Cdd:TIGR03269 165 ---------IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 216 ASCATVMRDGQVagdvMLENTSTHHIVSLM-------------LGRDHVDIAPVAPQEI-VDQAVleVRALrhkpklEDI 281
Cdd:TIGR03269 236 SDKAIWLENGEI----KEEGTPDEVVAVFMegvsevekeceveVGEPIIKVRNVSKRYIsVDRGV--VKAV------DNV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 282 SFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEI-VINGEkitrpDYGDMLKRGigytPENRKEAGiiPWLGV--- 357
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGD-----EWVDMTKPG----PDGRGRAK--RYIGIlhq 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 -----DENTVLTNRQK-ISANGVLQWSTIRRLTEEVMQRMTVKAASSETP--IGTLSGGNQQKVVIGRWVYAASQILLLD 429
Cdd:TIGR03269 373 eydlyPHRTVLDNLTEaIGLELPDELARMKAVITLKMVGFDEEKAEEILDkyPDELSEGERHRVALAQVLIKEPRIVILD 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 430 EPTRGVD----IEAKQQIYRIVRELaaeGKSVVFISSEVEELPLVCDRILLLQHGTF 482
Cdd:TIGR03269 453 EPTGTMDpitkVDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
278-480 |
7.26e-28 |
|
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: 110.45 E-value: 7.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmlkrgIGYTPENRkeaGIIPWLGV 357
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYLPEER---GLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTNRQKisanGvLQWSTIRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDI 437
Cdd:cd03269 88 IDQLVYLAQLK----G-LKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1314860479 438 EAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03269 162 VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
265-480 |
1.37e-27 |
|
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: 110.46 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIG 340
Cdd:COG0410 2 PMLEVENLHagygGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 YTPENRkeaGIIPWLGVDENtvLtnrqKISANGVLQWSTIRRLTEEVM-------QRMTVKAassetpiGTLSGGNQQKV 413
Cdd:COG0410 82 YVPEGR---RIFPSLTVEEN--L----LLGAYARRDRAEVRADLERVYelfprlkERRRQRA-------GTLSGGEQQML 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 414 VIGRWVYAASQILLLDEPTRG-----VdieakQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGlapliV-----EEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERG 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-228 |
1.50e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRaaELGvravY--QE 96
Cdd:COG1121 15 SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV-----RLFGKPPRRARR--RIG----YvpQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEG--LTVAENLCLGQWPRRnGMIDYLQmAQDAQRCLQALG-VDVSP--EQLVSTLSPAQKQLVEIARVMKGEPRVV 171
Cdd:COG1121 84 AEVDWDfpITVRDVVLMGRYGRR-GLFRRPS-RADREAVDEALErVGLEDlaDRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 172 ILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-227 |
1.55e-27 |
|
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: 109.68 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGETRLEGDEATLTRRAAElgvRAVYQE 96
Cdd:cd03269 8 KRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlFDGKPLDIAARNRIGYLPEE---RGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLtvaenLCLGQ---WPRRngmidylQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:cd03269 85 MKVIDQL-----VYLAQlkgLKKE-------EARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
19-228 |
2.04e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 115.63 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRL-EGDEATLTRRAAELGvravyQE 96
Cdd:COG4988 345 SYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsDLDPASWRRQIAWVP-----QN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGlTVAENLCLGqwpRRNgmidylqmAQDAQ--RCLQALGVDVSPEQLV-----------STLSPAQKQLVEIARV 163
Cdd:COG4988 420 PYLFAG-TIRENLRLG---RPD--------ASDEEleAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 164 MKGEPRVVILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQVA 228
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIV 550
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-228 |
2.51e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 112.50 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRlegdeatLTRRAAEL-GVRAVYQE 96
Cdd:COG3842 13 KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-------VTGLPPEKrNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLG----QWPRR------NGMIDYLQMAQDAQRclqalgvdvspeqLVSTLSPAQKQLVEIARVMKG 166
Cdd:COG3842 86 YALFPHLTVAENVAFGlrmrGVPKAeirarvAELLELVGLEGLADR-------------YPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 167 EPRVVILDEPTSSL-ASAEVELvISAVKKM-SALGVAVIYVSHRMEEI----RRIAscatVMRDGQVA 228
Cdd:COG3842 153 EPRVLLLDEPLSALdAKLREEM-REELRRLqRELGITFIYVTHDQEEAlalaDRIA----VMNDGRIE 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-227 |
2.91e-27 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 109.55 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEatLTRRAAeLGVRAVYQE 96
Cdd:cd03218 7 SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP--MHKRAR-LGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCL----------GQWPRRNGMIDYLQMAQDAQrclqalgvdvspeQLVSTLSPAQKQLVEIARVMKG 166
Cdd:cd03218 84 ASIFRKLTVEENILAvleirglskkEREEKLEELLEEFHITHLRK-------------SKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 167 EPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-231 |
3.18e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.09 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPG----VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGE---TRLEGDEATLTRRaaELG 89
Cdd:COG1135 8 SKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSERELRAARR--KIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 90 VraVYQELSLVEGLTVAENLCL-----GqWPRRngmidylQMAQDAQRCLQALG----VDVSPEQlvstLSPAQKQLVEI 160
Cdd:COG1135 86 M--IFQHFNLLSSRTVAENVALpleiaG-VPKA-------EIRKRVAELLELVGlsdkADAYPSQ----LSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 161 ARVMKGEPRVVILDEPTSSL---ASAEV-ELVISAVKKmsaLGVAVIYVSHRMEEIRRIASCATVMRDGQVA--GDV 231
Cdd:COG1135 152 ARALANNPKVLLCDEATSALdpeTTRSIlDLLKDINRE---LGLTIVLITHEMDVVRRICDRVAVLENGRIVeqGPV 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
267-481 |
3.63e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 107.13 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHK----PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIGYt 342
Cdd:cd03216 1 LELRGITKRfggvKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 343 penrkeagiipwlgvdentvltnrqkisangvlqwstirrlteeVMQrmtvkaassetpigtLSGGNQQKVVIGRWVYAA 422
Cdd:cd03216 80 --------------------------------------------VYQ---------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-227 |
6.27e-27 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 108.48 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrleGDEATLTRRAAELGVRAVYQEL 97
Cdd:cd03300 8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL------DGKDITNLPPHKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLGQWPRRNG----------MIDYLQMAQDAQRclqalgvdvSPEQlvstLSPAQKQLVEIARVMKGE 167
Cdd:cd03300 82 ALFPHLTVFENIAFGLRLKKLPkaeikervaeALDLVQLEGYANR---------KPSQ----LSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 168 PRVVILDEPTSSL---ASAEVELVISAVKKMsaLGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03300 149 PKVLLLDEPLGALdlkLRKDMQLELKRLQKE--LGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-480 |
7.25e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 113.65 E-value: 7.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 27 DNVNFTLNKGEVRALLGKNGAGKS----TLIRMLTGS--ERPdSGDI-WIGETRLEGDEATLTrraaelGVRA-----VY 94
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPpvVYP-SGDIrFHGESLLHASEQTLR------GVRGnkiamIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QE--LSLVEGLTV----AENLCLgqwprrngmidYLQMAQDAQR-----CLQALGVDVSPEQLVS---TLSPAQKQLVEI 160
Cdd:PRK15134 99 QEpmVSLNPLHTLekqlYEVLSL-----------HRGMRREAARgeilnCLDRVGIRQAAKRLTDyphQLSGGERQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 161 ARVMKGEPRVVILDEPTSSL---ASAEVELVISAVKKmsALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGD---VMLE 234
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALdvsVQAQILQLLRELQQ--ELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQnraATLF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 235 NTSTHHIVSLMLGRDHVDIAPVAPQEivDQAVLEVRALR---------------HKPKLEDISFTLRRGEVLGIAGLLGA 299
Cdd:PRK15134 246 SAPTHPYTQKLLNSEPSGDPVPLPEP--ASPLLDVEQLQvafpirkgilkrtvdHNVVVKNISFTLRPGETLGLVGESGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 300 GRS----ELLKAIVgleeyEQGEIVINGEKITRPDYGDMLkrgigytPENRKeagiIPWLGVDENTVLTNR---QKISAN 372
Cdd:PRK15134 324 GKSttglALLRLIN-----SQGEIWFDGQPLHNLNRRQLL-------PVRHR----IQVVFQDPNSSLNPRlnvLQIIEE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 373 GVL----QWSTIRRLTE--EVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRI 446
Cdd:PRK15134 388 GLRvhqpTLSAAQREQQviAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILAL 467
|
490 500 510
....*....|....*....|....*....|....*
gi 1314860479 447 VRELAAEGK-SVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK15134 468 LKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-228 |
7.88e-27 |
|
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: 108.74 E-value: 7.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAaelgVRAVYQ-- 95
Cdd:COG1124 13 QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR----VQMVFQdp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENL--CLgqwpRRNGMIDylqMAQDAQRCLQALGVDVS-----PEQLvstlSPAQKQLVEIARVMKGEP 168
Cdd:COG1124 89 YASLHPRHTVDRILaePL----RIHGLPD---REERIAELLEQVGLPPSfldryPHQL----SGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 169 RVVILDEPTSSL-AS--AEVELVISAVKKmsALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:COG1124 158 ELLLLDEPTSALdVSvqAEILNLLKDLRE--ERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-227 |
2.61e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 108.27 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRAA------Elgv 90
Cdd:COG4152 8 TKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV-----LWDGEPLDPEDRRRigylpeE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 RAVYQelslveGLTVAENLC-LGqwpRRNGM--------IDYLqmaqdaqrcLQALGVDVSPEQLVSTLSP--AQK-QLv 158
Cdd:COG4152 80 RGLYP------KMKVGEQLVyLA---RLKGLskaeakrrADEW---------LERLGLGDRANKKVEELSKgnQQKvQL- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 159 eIARVMkGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG4152 141 -IAALL-HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
26-207 |
3.54e-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: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEgdEATLTRRAAelgVRAVY-QELSLVEGLT 104
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA--AWSPWELAR---RRAVLpQHSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 105 VAENLCLGQWPRRNGmidYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVM-------KGEPRVVILDEPT 177
Cdd:COG4559 92 VEEVVALGRAPHGSS---AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPT 168
|
170 180 190
....*....|....*....|....*....|
gi 1314860479 178 SSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:COG4559 169 SALDLAHQHAVLRLARQLARRGGGVVAVLH 198
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
273-481 |
4.66e-26 |
|
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: 104.44 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 273 RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgIGYTPENRKEAGIi 352
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVPQALELLGL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 pwlgvdenTVLTNRqkisangvlqwstirrlteevmqrmtvkaassetPIGTLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:cd03214 88 --------AHLADR----------------------------------PFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 433 RGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
266-480 |
5.98e-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: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRAL--RHKPK--LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYgdmlkRGIGY 341
Cdd:COG4152 1 MLELKGLtkRFGDKtaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-----RRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 TPENRkeaGIIPWLGVDENTVLTNRQKisanGvLQWSTIRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIgrwvyA 421
Cdd:COG4152 76 LPEER---GLYPKMKVGEQLVYLARLK----G-LSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQL-----I 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 422 AS-----QILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFiSS----EVEELplvCDRILLLQHG 480
Cdd:COG4152 142 AAllhdpELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIF-SShqmeLVEEL---CDRIVIINKG 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-217 |
7.03e-26 |
|
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: 104.92 E-value: 7.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRaaelgvRAVY--QE 96
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-----RVFGKPLEKERK------RIGYvpQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEG--LTVAENLCLGQWPRRnGMIDYLQmAQDAQRCLQALG-VDVS--PEQLVSTLSPAQKQLVEIARVMKGEPRVV 171
Cdd:cd03235 77 RSIDRDfpISVRDVVLMGLYGHK-GLFRRLS-KADKAKVDEALErVGLSelADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314860479 172 ILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIAS 217
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFD 200
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-227 |
8.20e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.48 E-value: 8.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAEL--GVRAVY 94
Cdd:COG4161 9 NCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLLrqKVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENL------CLGQWPrrngmidylQMAQD-AQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGE 167
Cdd:COG4161 89 QQYNLWPHLTVMENLieapckVLGLSK---------EQAREkAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 168 PRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
278-480 |
1.74e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 103.99 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGdmLKRGIGYTPENRkeaGIIPWLGV 357
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE--ARRRLGFVSDST---GLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVL------TNRQKISAngvlqwstirRLtEEVMQRMTVKAaSSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:cd03266 96 RENLEYfaglygLKGDELTA----------RL-EELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-227 |
1.85e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 107.19 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPG----VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GE--TRLEGDEATLTRRaaELG 89
Cdd:PRK11153 8 SKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdGQdlTALSEKELRKARR--QIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 90 VraVYQELSLVEGLTVAEN----LCLGQWPRrngmidylqmAQDAQRCLQALGV-------DVSPEQlvstLSPAQKQLV 158
Cdd:PRK11153 86 M--IFQHFNLLSSRTVFDNvalpLELAGTPK----------AEIKARVTELLELvglsdkaDRYPAQ----LSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 159 EIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINReLGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
267-481 |
2.26e-25 |
|
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: 102.65 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRAL----RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDM-LKRGIGY 341
Cdd:cd03229 1 LELKNVskryGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 TpenRKEAGIIPWLGVDENTVLTnrqkisangvlqwstirrlteevmqrmtvkaassetpigtLSGGNQQKVVIGRWVYA 421
Cdd:cd03229 81 V---FQDFALFPHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 422 ASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-227 |
3.10e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 106.70 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGdeatltRRAAELGVRAVYQEL 97
Cdd:COG3839 11 KSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD------LPPKDRNIAMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLGqwprrngmidyLQM-----AQDAQRCLQALG-VDVSP--EQLVSTLSPAQKQLVEIARVMKGEPR 169
Cdd:COG3839 85 ALYPHMTVYENIAFP-----------LKLrkvpkAEIDRRVREAAElLGLEDllDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 170 VVILDEPTSSL-----ASAEVELvisavKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG3839 154 VFLLDEPLSNLdaklrVEMRAEI-----KRLHRrLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-228 |
4.70e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 102.83 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGDEATLTRRAAELGVRAVYQELSLVEG 102
Cdd:cd03266 18 VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-----DGFDVVKEPAEARRRLGFVSDSTGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 103 LTVAENlcLGQWPRRNGmidyLQMAQDAQRC---LQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSS 179
Cdd:cd03266 93 LTAREN--LEYFAGLYG----LKGDELTARLeelADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 180 LASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:cd03266 167 LDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-228 |
4.79e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.74 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQELSLVEGl 103
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLCLGqwPRRNGMIDYlQMAQDAQRCLQALGVDV------SPEQlvstLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PRK13637 100 TIEKDIAFG--PINLGLSEE-EIENRVKRAMNIVGLDYedykdkSPFE----LSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 178 SSLASAEVELVISAVKKM-SALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
267-484 |
7.21e-25 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 102.21 E-value: 7.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRH----KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT-RPDYgdmlKRGIGY 341
Cdd:cd03259 1 LELKGLSKtygsVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTgVPPE----RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 TPENrkeAGIIPWLGVDENTV--LTNRQKISANgvlqwstIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWV 419
Cdd:cd03259 77 VFQD---YALFPHLTVAENIAfgLKLRGVPKAE-------IRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 420 YAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-227 |
9.26e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.79 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAEL--GVRAVY 94
Cdd:PRK11124 9 NCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELrrNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLClgQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK11124 89 QQYNLWPHLTVQQNLI--EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-228 |
1.01e-24 |
|
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: 101.89 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGeVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlegDEATLTRRAAELGVRAVY-- 94
Cdd:cd03264 7 TKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI-------DGQDVLKQPQKLRRRIGYlp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLCLGQWPRRngmIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKG---IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
267-482 |
1.32e-24 |
|
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: 101.43 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRH------KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygDMLKRGIG 340
Cdd:cd03263 1 LQIRNLTKtykkgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR--KAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 YTPENRkeagIIPWLgvdentvLTNRQ--KISA--NGvLQWSTIRRLTEEVMQRM--TVKAassETPIGTLSGGNQQKVV 414
Cdd:cd03263 79 YCPQFD----ALFDE-------LTVREhlRFYArlKG-LPKSEIKEEVELLLRVLglTDKA---NKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 415 IGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELaAEGKSVVFISSEVEELPLVCDRILLLQHGTF 482
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-227 |
2.52e-24 |
|
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: 99.60 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVA--LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRAaELG--VRAVY 94
Cdd:cd03246 9 RYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----RLDGADISQWDPN-ELGdhVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGlTVAENLclgqwprrngmidylqmaqdaqrclqalgvdvspeqlvstLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:cd03246 83 QDDELFSG-SIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIR---RIAscatVMRDGQV 227
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAsadRIL----VLEDGRV 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
18-211 |
3.22e-24 |
|
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: 100.62 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPG----VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGdeATLTRRAAELGVraV 93
Cdd:cd03293 8 KTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-----LVDG--EPVTGPGPDRGY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 94 YQELSLVEGLTVAENLCLGqwPRRNGMIDYLQMAQdAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:cd03293 79 FQQDALLPWLTVLDNVALG--LELQGVPKAEARER-AEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1314860479 174 DEPTSSL--ASAEV--ELVISAVKKMsalGVAVIYVSHRMEE 211
Cdd:cd03293 156 DEPFSALdaLTREQlqEELLDIWRET---GKTVLLVTHDIDE 194
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-228 |
3.72e-24 |
|
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: 105.60 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 10 VAKVVAgnkRYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLegDEATLTR-RAA 86
Cdd:COG4618 333 VENLTV---VPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV-----RL--DGADLSQwDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 87 ELGvRAV-Y--QELSLVEGlTVAENLClgqwprRNGMIDylqmAQDAQRCLQALGV-------------DVSPEQlvSTL 150
Cdd:COG4618 403 ELG-RHIgYlpQDVELFDG-TIAENIA------RFGDAD----PEKVVAAAKLAGVhemilrlpdgydtRIGEGG--ARL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 151 SPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMeeirRIASCAT---VMRDGQV 227
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP----SLLAAVDkllVLRDGRV 544
|
.
gi 1314860479 228 A 228
Cdd:COG4618 545 Q 545
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-228 |
4.37e-24 |
|
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: 100.84 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGV-VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEATLTRRaaeLGVraVYQ 95
Cdd:cd03295 8 KRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIREQDPVELRRK---IGY--VIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLC----LGQWPRrngmidylqmAQDAQRCLQALG-VDVSPEQLV----STLSPAQKQLVEIARVMKG 166
Cdd:cd03295 83 QIGLFPHMTVEENIAlvpkLLKWPK----------EKIRERADELLAlVGLDPAEFAdrypHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 167 EPRVVILDEPTSSLASAEVELVISAVKKM-SALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-227 |
5.41e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 99.99 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 21 PGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETrlegDEATLTRRAAELGVRAVYQELSLV 100
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI----DIRDISRKSLRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGlTVAENLCLGqwprRNGMIDylqmaQDAQRCLQAL-----------GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPR 169
Cdd:cd03254 90 SG-TIMENIRLG----RPNATD-----EEVIEAAKEAgahdfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 170 VVILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQV 227
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKI 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-180 |
6.41e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.55 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 1 MFTATEAVPVAKVvagNKRYP----GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrleg 76
Cdd:COG1116 1 MSAAAPALELRGV---SKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 77 DEATLTRRAAELGVraVYQELSLVEGLTVAENLCLGqwPRRNGMidylQMAQDAQRCLQALgvdvspeQLV--------- 147
Cdd:COG1116 71 DGKPVTGPGPDRGV--VFQEPALLPWLTVLDNVALG--LELRGV----PKAERRERARELL-------ELVglagfeday 135
|
170 180 190
....*....|....*....|....*....|....
gi 1314860479 148 -STLSPAQKQLVEIARVMKGEPRVVILDEPTSSL 180
Cdd:COG1116 136 pHQLSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
267-489 |
7.05e-24 |
|
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: 99.47 E-value: 7.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRH--------KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygdmlkRG 338
Cdd:cd03293 1 LEVRNVSKtygggggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG------PD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 339 IGYTPEnrkEAGIIPWLGVDENTVLTnrqkISANGVlQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRW 418
Cdd:cd03293 75 RGYVFQ---QDALLPWLTVLDNVALG----LELQGV-PKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 419 VYAASQILLLDEPTRGVDIEAKQQ----IYRIVRElaaEGKSVVFISSEVEELPLVCDRILLL--QHGTFSQEFHAP 489
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQlqeeLLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-227 |
9.94e-24 |
|
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: 98.87 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRaaelgVRAVYQELSLVE---- 101
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-----LLNGKPIKAKER-----RKSIGYVMQDVDyqlf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GLTVAENLCLgqwprrnGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLA 181
Cdd:cd03226 86 TDSVREELLL-------GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314860479 182 SAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
266-480 |
1.16e-23 |
|
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: 99.73 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRAL----RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgIGY 341
Cdd:COG1120 1 MLEAENLsvgyGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 TPENRkeagIIPW-LGVDEnTVLTNRqkISANGVLQWSTI--RRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRw 418
Cdd:COG1120 80 VPQEP----PAPFgLTVRE-LVALGR--YPHLGLFGRPSAedREAVEEALERTGL-EHLADRPVDELSGGERQRVLIAR- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 419 VYA-ASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:COG1120 151 ALAqEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDG 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
266-480 |
1.29e-23 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 99.12 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRALRHK--------PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKR 337
Cdd:cd03257 1 LLEVKNLSVSfptgggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 338 gigytpenRKEAGII---------PWLGVDE--------NTVLTNRQKISANGVLQWSTIrRLTEEVMQRMtvkaasset 400
Cdd:cd03257 81 --------RKEIQMVfqdpmsslnPRMTIGEqiaeplriHGKLSKKEARKEAVLLLLVGV-GLPEEVLNRY--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 401 PiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSeveELPLV---CDRILL 476
Cdd:cd03257 143 P-HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITH---DLGVVakiADRVAV 218
|
....
gi 1314860479 477 LQHG 480
Cdd:cd03257 219 MYAG 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-227 |
1.33e-23 |
|
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: 98.63 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGET---RLEGDEATLTRRaaELGVra 92
Cdd:cd03292 7 TKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYLRR--KIGV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 93 VYQELSLVEGLTVAENLCLG---------QWPRRNGMIdylqmaqdaqrcLQALGVDVSPEQLVSTLSPAQKQLVEIARV 163
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFAlevtgvpprEIRKRVPAA------------LELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 164 MKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
273-480 |
1.46e-23 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 97.07 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 273 RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgIGYtpenrkeagii 352
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAY----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 pwlgVDENTVLTNRqkisangvlqwsTIRrltEEVmqrmtvkaassetpigtLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:cd03228 81 ----VPQDPFLFSG------------TIR---ENI-----------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314860479 433 RGVDIEAKQQIYRIVRELaAEGKSVVFISSEVEELPLvCDRILLLQHG 480
Cdd:cd03228 125 SALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
278-432 |
1.59e-23 |
|
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: 96.56 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmLKRGIGYTPEnrkEAGIIPWLGV 357
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS-LRKEIGYVFQ---DPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 358 DENtvLTNRQKISANGvLQWSTIRRltEEVMQRMTVKAASSETP---IGTLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:pfam00005 77 REN--LRLGLLLKGLS-KREKDARA--EEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-216 |
1.79e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 98.66 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetRLEGDEATLTrRAAE---LGVRA-----VY 94
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV---RHDGGWVDLA-QASPreiLALRRrtigyVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLT----VAENLCLGQWPRrngmidylQMAQD-AQRCLQALGVdvsPEQLVStLSPA-----QKQLVEIARVM 164
Cdd:COG4778 100 QFLRVIPRVSaldvVAEPLLERGVDR--------EEARArARELLARLNL---PERLWD-LPPAtfsggEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 165 KGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIA 216
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVA 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-227 |
2.18e-23 |
|
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: 98.56 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATlTRRAAELGVRAVYQELSLVEGLTV 105
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-----LLNGKDIT-NLPPEKRDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 AENLCLGQwprRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEV 185
Cdd:cd03299 89 YKNIAYGL---KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1314860479 186 ELVISAVKKM-SALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03299 166 EKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
280-480 |
2.42e-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: 97.75 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 280 DISFTLRrGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVING-------EKITRPDYgdmlKRGIGYTPENrkeAGII 352
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQ----QRKIGLVFQQ---YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 PWLGVDENTVLTNRQKISangvlqwSTIRRLTEEVMQRMTVKAASsETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:cd03297 88 PHLNVRENLAFGLKRKRN-------REDRISVDELLDLLGLDHLL-NRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 433 RGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-229 |
3.66e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 102.94 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG-VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegDEATLTRRAAELGVraVYQEL 97
Cdd:COG1132 348 SYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLESLRRQIGV--VPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGlTVAENLCLGqwpRRNgmidylqmAQDAQ--RCLQALGVD--VS--PEQL---V----STLSPAQKQLVEIARVM 164
Cdd:COG1132 424 FLFSG-TIRENIRYG---RPD--------ATDEEveEAAKAAQAHefIEalPDGYdtvVgergVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 165 KGEPRVVILDEPTSSLaSAEVE-LVISAVKKMSAlGVAVIYVSHRMEEIR---RIAscatVMRDGQVAG 229
Cdd:COG1132 492 LKDPPILILDEATSAL-DTETEaLIQEALERLMK-GRTTIVIAHRLSTIRnadRIL----VLDDGRIVE 554
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-247 |
4.30e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.03 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 10 VAKVVAGNKRypGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGdeatLTRRAA-EL 88
Cdd:COG3845 260 VENLSVRDDR--GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG----LSPRERrRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 89 GVRAVYQE---LSLVEGLTVAENLCLGQWPR----RNGMIDYLQMAQDAQRCLQALGVDV-SPEQLVSTLS--PAQKqLV 158
Cdd:COG3845 334 GVAYIPEDrlgRGLVPDMSVAENLILGRYRRppfsRGGFLDRKAIRAFAEELIEEFDVRTpGPDTPARSLSggNQQK-VI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 159 eIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIR----RIAscatVMRDGQVAGDVMLE 234
Cdd:COG3845 413 -LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILalsdRIA----VMYEGRIVGEVPAA 487
|
250
....*....|...
gi 1314860479 235 NTSTHHIVSLMLG 247
Cdd:COG3845 488 EATREEIGLLMAG 500
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-180 |
7.49e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.53 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRAAELGVRAVY-QEL 97
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV-----RLNGRPLADWSPAELARRRAVLpQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLGQWPRRNGmidylqMAQDAQRCLQAL-GVDVSP--EQLVSTLSPAQKQLVEIARVM------KGEP 168
Cdd:PRK13548 86 SLSFPFTVEEVVAMGRAPHGLS------RAEDDALVAAALaQVDLAHlaGRDYPQLSGGEQQRVQLARVLaqlwepDGPP 159
|
170
....*....|..
gi 1314860479 169 RVVILDEPTSSL 180
Cdd:PRK13548 160 RWLLLDEPTSAL 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
278-480 |
7.86e-23 |
|
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: 97.12 E-value: 7.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIGYTPENrkeAGIIPWLGV 357
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQI---PRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENtVLTNRQKISANGVLQWSTIRRLTE------EVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:cd03219 93 LEN-VMVAAQARTGSGLLLARARREEREareraeELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03219 171 AAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
278-480 |
9.55e-23 |
|
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: 96.06 E-value: 9.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPdygdmlKRGIgytPENRKEAGII----- 352
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD------KKNI---NELRQKVGMVfqqfn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 --PWLGVDENTVL--TNRQKISANGVLQwsTIRRLTEEVmqRMTVKAASSetpIGTLSGGNQQKVVIGRWVYAASQILLL 428
Cdd:cd03262 87 lfPHLTVLENITLapIKVKGMSKAEAEE--RALELLEKV--GLADKADAY---PAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 429 DEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-230 |
1.04e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 96.12 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRL-EGDEATLTRRaaelgVRAVYQ 95
Cdd:cd03245 11 SYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRN-----IGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENLCLGqwprrngmidyLQMAQDaQRCLQAL---GVDvspeQLVST---------------LSPAQKQL 157
Cdd:cd03245 86 DVTLFYG-TLRDNITLG-----------APLADD-ERILRAAelaGVT----DFVNKhpngldlqigergrgLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 158 VEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMeEIRRIASCATVMRDGQVAGD 230
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGRIVAD 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-230 |
1.14e-22 |
|
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: 96.02 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 32 TLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETrlegDEATLTrrAAELGVRAVYQELSLVEGLTVAENLCL 111
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV----DVTAAP--PADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 112 GQWPRrngmidyLQM-AQDAQRCLQAL---GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVEL 187
Cdd:cd03298 94 GLSPG-------LKLtAEDRQAIEVALarvGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314860479 188 VISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:cd03298 167 MLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
267-482 |
1.16e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 95.65 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR---PDYgdmlKRGI 339
Cdd:COG4619 1 LELEGLSfrvgGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmppPEW----RRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 340 GYTPEnrkEAGIIpwlgvdENTVLTNRQKISANGVLQWSTIRrlTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWV 419
Cdd:COG4619 77 AYVPQ---EPALW------GGTVRDNLPFPFQLRERKFDRER--ALELLERLGLPPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 420 YAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTF 482
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-228 |
1.42e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEatltrrAAELGVRAVYQEL 97
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP------PAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQaLG--VDVSPEqlvsTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQ-LAhlLDRKPK----ALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 176 PTSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:PRK11000 160 PLSNLdAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
265-479 |
1.70e-22 |
|
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: 95.24 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRAL---RHKPKL-EDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygDMLKRGIG 340
Cdd:COG4133 1 MMLEAENLscrRGERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR--EDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 YTPEnrkEAGIIPWLGVDENTVLTNRQKisangvlQWSTIRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVY 420
Cdd:COG4133 79 YLGH---ADGLKPELTVRENLRFWAALY-------GLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 421 AASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSevEELPLVCDRILLLQH 479
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH--QPLELAAARVLDLGD 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
25-230 |
1.88e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 96.62 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIR----MLTGSERPDSGDIWIGET-RLEGDEATLTRRA-AELGVraVYQELS 98
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTvQREGRLARDIRKSrANTGY--IFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENL---CLGQWPRRNGMIDYLQMAQDaQRCLQAL---GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVI 172
Cdd:PRK09984 97 LVNRLSVLENVligALGSTPFWRTCFSWFTREQK-QRALQALtrvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 173 LDEPTSSLASAEVELVISAVKKMSAL-GVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-230 |
1.98e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.87 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 1 MFTATEAVPVAKVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlegDEAT 80
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML-------DGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 81 LTRRAAE-LGVRAVYQELSLVEGLTVAENLCLGqwprrngmidyLQM-----AQDAQRCLQALGVdVSPEQL----VSTL 150
Cdd:PRK09452 78 ITHVPAEnRHVNTVFQSYALFPHMTVFENVAFG-----------LRMqktpaAEITPRVMEALRM-VQLEEFaqrkPHQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 151 SPAQKQLVEIARVMKGEPRVVILDEPTSSL---ASAEVELVISAVKKmsALGVAVIYVSHRMEEI----RRIAscatVMR 223
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALdykLRKQMQNELKALQR--KLGITFVFVTHDQEEAltmsDRIV----VMR 219
|
....*..
gi 1314860479 224 DGQVAGD 230
Cdd:PRK09452 220 DGRIEQD 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-230 |
2.70e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.54 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEAT--LTRRAAELgvraVYQ 95
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQEAGM----VFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGqwPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK09493 85 QFYLFPHLTALENVMFG--PLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 176 PTSSLasaEVELVISAVKKMSAL---GVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:PRK09493 163 PTSAL---DPELRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
264-480 |
3.28e-22 |
|
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: 99.59 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 264 QAVLEVRALR------HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYE---QGEIVINGEKITRPDYGDM 334
Cdd:COG1123 2 TPLLEVRDLSvrypggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 335 LKRgIGYTPENrkeagiiPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVV 414
Cdd:COG1123 82 GRR-IGMVFQD-------PMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYP-HQLSGGQRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 415 IGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-227 |
3.48e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.24 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGV--VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegDEATLTRRAAELGVraVYQ- 95
Cdd:PRK13635 14 RYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL--SEETVWDVRRQVGM--VFQn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 -ELSLVeGLTVAENLCLGQwprRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK13635 90 pDNQFV-GATVQDDVAFGL---ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRiASCATVMRDGQV 227
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-227 |
6.52e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.33 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGE---TRLegdeaTLTRRaAELGVRAVY 94
Cdd:COG1137 11 KSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGediTHL-----PMHKR-ARLGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLclgqwprrngMIdYLQM-----AQDAQRC---LQALGVDVSPEQLVSTLSPAQKQLVEIARVMKG 166
Cdd:COG1137 85 QEASIFRKLTVEDNI----------LA-VLELrklskKEREERLeelLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 167 EPRVVILDEPTSS---LASAEVELVISAVKKMsalGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG1137 154 NPKFILLDEPFAGvdpIAVADIQKIIRHLKER---GIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
280-480 |
7.23e-22 |
|
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: 96.72 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 280 DISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDML---KRGIGYTpenRKEAGIIPWLG 356
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppeKRRIGYV---FQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 357 VDENTVLTNRQKISANGVLQWSTIRRL--TEEVMQRmtvkaassetPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:TIGR02142 92 VRGNLRYGMKRARPSERRISFERVIELlgIGHLLGR----------LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314860479 435 VDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
275-484 |
7.94e-22 |
|
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: 94.29 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDyGDMLKRGIGYTPEnrkEAGIIPW 354
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD-PVELRRKIGYVIQ---QIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTNRqkisangVLQWS--TIRRLTEEVMQRMTVKAAS-SETPIGTLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:cd03295 90 MTVEENIALVPK-------LLKWPkeKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 432 TRGVD----IEAKQQIYRIVRELaaeGKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:cd03295 163 FGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
267-477 |
1.05e-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: 93.72 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR--PDYGDMLKRGIG 340
Cdd:cd03261 1 IELRGLTksfgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 YTPENrkeAGIIPWLGVDENTVLTNRQkisaNGVLQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVY 420
Cdd:cd03261 81 MLFQS---GALFDSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 421 AASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLL 477
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
267-491 |
1.17e-21 |
|
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: 93.55 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKPK---LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT--RPDygdmlKRGIGY 341
Cdd:cd03299 1 LKVENLSKDWKefkLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITnlPPE-----KRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 TPENRkeaGIIPWLGVDENTVLTNRQKISANgvlqwSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYA 421
Cdd:cd03299 76 VPQNY---ALFPHMTVYKNIAYGLKKRKVDK-----KEIERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 422 ASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRIL------LLQHGTFSQEFHAPVN 491
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAimlngkLIQVGKPEEVFKKPKN 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-227 |
1.36e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 20 YP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRlEGDEATLTRRAAELGVraVYQ--E 96
Cdd:PRK13644 11 YPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIRKLVGI--VFQnpE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVeGLTVAENLCLGQwprRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:PRK13644 88 TQFV-GRTVEEDLAFGP---ENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 177 TSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIrRIASCATVMRDGQV 227
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
278-485 |
1.43e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.62 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmlkRGIgytpenRKEAGII----- 352
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE---RLI------RQEAGMVfqqfy 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 --PWLGVDENTVLTNRQKISANGvlqwSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:PRK09493 88 lfPHLTALENVMFGPLRVRGASK----EEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-225 |
1.67e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEAtltRRAAELGVRAVYQELS 98
Cdd:PRK11300 14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG---HQIARMGVVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENLCLGQWPRRN-----GMI---DYLQMAQDA-QRC---LQALGVDVSPEQLVSTLSPAQKQLVEIARVMKG 166
Cdd:PRK11300 91 LFREMTVIENLLVAQHQQLKtglfsGLLktpAFRRAESEAlDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 167 EPRVVILDEPTSSLASAE-VEL--VISAVKKmsALGVAVIYVSHRMEEIRRIASCATVMRDG 225
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKEtKELdeLIAELRN--EHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-230 |
2.50e-21 |
|
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: 92.50 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 1 MFTATEavPVAKVVAGNKRYPG----VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG 76
Cdd:COG4181 1 MSSSSA--PIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 77 --DEATLTRRAAELGVraVYQELSLVEGLTVAENLCLgqwP-RRNGMIDYLQMAQDAqrcLQALGV----DVSPEQLvst 149
Cdd:COG4181 79 ldEDARARLRARHVGF--VFQSFQLLPTLTALENVML---PlELAGRRDARARARAL---LERVGLghrlDHYPAQL--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 150 lSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRiasCATV--MRDGQ 226
Cdd:COG4181 148 -SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAAR---CDRVlrLRAGR 223
|
....
gi 1314860479 227 VAGD 230
Cdd:COG4181 224 LVED 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-214 |
2.52e-21 |
|
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: 96.97 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 4 ATEAVPVAKVVAG-NKRYPGV-VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEAT 80
Cdd:TIGR02857 314 VTAAPASSLEFSGvSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 81 LTRRAAELGvravyQELSLVEGlTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQAL--GVDVSPEQLVSTLSPAQKQLV 158
Cdd:TIGR02857 394 WRDQIAWVP-----QHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRL 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 159 EIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMsALGVAVIYVSHRMEEIRR 214
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL 522
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
278-480 |
2.82e-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: 92.05 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPdyGDMLKRGIGYTPENrkeagiipwLGV 357
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE--PREVRRRIGIVFQD---------LSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENtvLTNRQKISANGVLQ---WSTIRRLTEEVMQRMTVKAASSEtPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:cd03265 85 DDE--LTGWENLYIHARLYgvpGAERRERIDELLDFVGLLEAADR-LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314860479 435 VDIEAKQQIYRIVRELAAEGKSVVFISSE-VEELPLVCDRILLLQHG 480
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHyMEEAEQLCDRVAIIDHG 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-230 |
3.42e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.21 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 15 AGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGDEATLTrraaELGVravy 94
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-----RGRVSSLL----GLGG---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 qelSLVEGLTVAENLclgqwpRRNGMI---DYLQMAQDAQRCLQ--ALGVDVspEQLVSTLSPAQKQLVEIARVMKGEPR 169
Cdd:cd03220 94 ---GFNPELTGRENI------YLNGRLlglSRKEIDEKIDEIIEfsELGDFI--DLPVKTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 170 VVILDEptsSLASAEVELVISAVKKMSAL---GVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:cd03220 163 ILLIDE---VLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-227 |
6.82e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 95.64 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 9 PVAKVVAGNKRY----PGVV-ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetRLEGDEATLTR 83
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 84 RAAELGVRA------VYQELSLVEGLTVAENLCLG-------QWPRRNGMIDYLQMAQDAQRCLQALgvdvspEQLVSTL 150
Cdd:TIGR03269 355 PGPDGRGRAkryigiLHQEYDLYPHRTVLDNLTEAiglelpdELARMKAVITLKMVGFDEEKAEEIL------DKYPDEL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 151 SPAQKQLVEIARVMKGEPRVVILDEPTSSLAS-AEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-226 |
7.07e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLT---RRAaelgVRAVY 94
Cdd:PRK11607 27 KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-----MLDGVDLSHVppyQRP----INMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLCLG----QWP------RRNGMIDYLQMAQDAQRclqalgvdvSPEQlvstLSPAQKQLVEIARVM 164
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGlkqdKLPkaeiasRVNEMLGLVHMQEFAKR---------KPHQ----LSGGQRQRVALARSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 165 KGEPRVVILDEPTSSLASAEVE-LVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQ 226
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDrMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-230 |
1.28e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.58 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 30 NFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlegDEATLTRRA-AELGVRAVYQELSLVEGLTVAEN 108
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-------NGQDLTALPpAERPVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 109 LCLGQWPRRNgmidyLQmAQDAQRCLQALG-VDVS------PEQlvstLSPAQKQLVEIARVMKGEPRVVILDEPTSSLA 181
Cdd:COG3840 92 IGLGLRPGLK-----LT-AEQRAQVEQALErVGLAglldrlPGQ----LSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 182 SAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:COG3840 162 PALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAAD 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
267-480 |
1.40e-20 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 90.24 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRH--------KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMlkrg 338
Cdd:cd03255 1 IELKNLSKtyggggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 339 igyTPENRKEAGII-------PWLGVDENTVLTNRqkisANGVLQWSTIRRLtEEVMQRMTVKAASSETPiGTLSGGNQQ 411
Cdd:cd03255 77 ---AAFRRRHIGFVfqsfnllPDLTALENVELPLL----LAGVPKKERRERA-EELLERVGLGDRLNHYP-SELSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 412 KVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFIS--SEVEELplvCDRILLLQHG 480
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVThdPELAEY---ADRIIELRDG 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-227 |
1.42e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEATLTRRAAELGvravyQEL 97
Cdd:PRK10575 20 RVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLP-----QQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLGQWPRRNGMIDYlqMAQDAQRCLQALG-VDVSP--EQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPWHGALGRF--GAADREKVEEAISlVGLKPlaHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSAL-GVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
270-480 |
2.38e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 270 RALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKItrPDYGDMLKRGIGYTPENRKea 349
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV--PARARLARARIGVVPQFDN-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 350 gIIPWLGVDENTVLTNRqkisangVLQWSTirRLTEEVM------QRMTVKAassETPIGTLSGGNQQKVVIGRWVYAAS 423
Cdd:PRK13536 125 -LDLEFTVRENLLVFGR-------YFGMST--REIEAVIpsllefARLESKA---DARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 424 QILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-227 |
3.43e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 9 PVAKVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETrlegdeatltrraael 88
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET---------------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 89 gVRAVY--QEL-SLVEGLTVAENLclgqWPRRNGMIDylqmaQDAQRCLQAL---GVDVspEQLVSTLSPAQKQLVEIAR 162
Cdd:COG0488 378 -VKIGYfdQHQeELDPDKTVLDEL----RDGAPGGTE-----QEVRGYLGRFlfsGDDA--FKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 163 VMKGEPRVVILDEPTSSLASAEVELVISAVKKMSalGvAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP--G-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
267-480 |
3.53e-20 |
|
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: 89.52 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKPK----LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR-PdygdMLKR---G 338
Cdd:cd03218 1 LRAENLSKRYGkrkvVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlP----MHKRarlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 339 IGYTPEnrkEAGIIPWLGVDEN--TVLTNRQKISAngvlqwsTIRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIG 416
Cdd:cd03218 77 IGYLPQ---EASIFRKLTVEENilAVLEIRGLSKK-------EREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 417 RWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEG 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
26-246 |
4.82e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGE--TRLEGDEATLTRRAaelgVRAVYQE-LSLVE 101
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVsWRGEplAKLNRAQRKAFRRD----IQMVFQDsISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 -----GLTVAENLclgqwpRRNGMIDYLQMAQDAQRCLQALGVDVS-PEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK10419 104 prktvREIIREPL------RHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 176 PTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVAGD-VMLENTSTHHIVSLML 246
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqPVGDKLTFSSPAGRVL 250
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-207 |
5.50e-20 |
|
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: 87.80 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAvyqelSLVE 101
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP-----GLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GLTVAENLclgQWPRRNGmidylqmaQDAQR-CLQAL---GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:TIGR01189 87 ELSALENL---HFWAAIH--------GGAQRtIEDALaavGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 1314860479 178 SSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-233 |
1.16e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.95 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLE--GDEATLTRRAAELGVraVYQELSLVEGL 103
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklSSAAKAELRNQKLGF--IYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLCLgqwPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASA 183
Cdd:PRK11629 103 TALENVAM---PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 184 EVELVISAVKKMSAL-GVAVIYVSHRMEEIRRIaSCATVMRDGQVAGDVML 233
Cdd:PRK11629 180 NADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-227 |
1.32e-19 |
|
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: 87.67 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRaaELGVraVYQE 96
Cdd:cd03251 9 RYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR--QIGL--VSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGlTVAENLCLGqwpRRNG----MIDYLQMAQdAQRCLQAL--GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRV 170
Cdd:cd03251 85 VFLFND-TVAENIAYG---RPGAtreeVEEAARAAN-AHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 171 VILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQV 227
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-234 |
1.35e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.15 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 16 GNKRypgvvALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEA-TLTRRAAELGvravy 94
Cdd:PRK11231 13 GTKR-----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLCLGQWPrrngmidYL----QMAQD----AQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKG 166
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSP-------WLslwgRLSAEdnarVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 167 EPRVVILDEPTSSL-ASAEVELvISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA-----GDVMLE 234
Cdd:PRK11231 156 DTPVVLLDEPTTYLdINHQVEL-MRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMaqgtpEEVMTP 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
254-477 |
1.89e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 91.19 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 254 APVAPQEIVDQAVLEVRALRH-----KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR 328
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVaypgrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 329 PDyGDMLKRGIGYTPENrkeagiiPWLGvdENTVLTNRQkISANGVlqwstirrlTEEVMQRMTVKAASSE--------- 399
Cdd:TIGR02857 389 AD-ADSWRDQIAWVPQH-------PFLF--AGTIAENIR-LARPDA---------SDAEIREALERAGLDEfvaalpqgl 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 400 -TPIGT----LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELaAEGKSVVFISSEVEELPLvCDRI 474
Cdd:TIGR02857 449 dTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRI 526
|
...
gi 1314860479 475 LLL 477
Cdd:TIGR02857 527 VVL 529
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-227 |
2.62e-19 |
|
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: 87.70 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGDEATLTRRAAELGVRA-----VYQEL 97
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-----DGQDIAAMSRKELRELRRkkismVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLGQWPRRngmIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQG---VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 178 SSL---ASAEV-ELVISAVKKMsalGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03294 189 SALdplIRREMqDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
263-482 |
2.79e-19 |
|
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: 86.96 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 263 DQAVLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDM--LK 336
Cdd:COG1127 2 SEPMIEVRNLTksfgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 337 RGIGY-----------TpenrkeagiipwlgVDENTVLTNRQkisaNGVLQWSTIRRLTEEVMQRMTVKAAS----SEtp 401
Cdd:COG1127 82 RRIGMlfqggalfdslT--------------VFENVAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAAdkmpSE-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 402 igtLSGGNQQKVVIGRwvyaA----SQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILL 476
Cdd:COG1127 142 ---LSGGMRKRVALAR----AlaldPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAV 214
|
....*.
gi 1314860479 477 LQHGTF 482
Cdd:COG1127 215 LADGKI 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-217 |
3.12e-19 |
|
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: 86.62 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEATLTRRAAELGVRA-VY 94
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaGLVPWKRRKKFLRRIGVVFGQKTqLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAenlclgqwpRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:cd03267 108 WDLPVIDSFYLL---------AAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSAL-GVAVIYVSHRMEEIRRIAS 217
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALAR 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-227 |
3.27e-19 |
|
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: 86.82 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 21 PGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLtgsER---PDSGDIWIGETRLEgdEATLTRRAAELGVraVYQEL 97
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIR--DLNLRWLRSQIGL--VSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGlTVAENLCLGQWPRrngmidylQMAQDAQRCLQALGVDVS---PEQ---LV----STLSPAQKQLVEIARVMKGE 167
Cdd:cd03249 87 VLFDG-TIAENIRYGKPDA--------TDEEVEEAAKKANIHDFImslPDGydtLVgergSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 168 PRVVILDEPTSSLaSAEVELVISAVKKMSALGVAVIYVSHRMEEIRRiASCATVMRDGQV 227
Cdd:cd03249 158 PKILLLDEATSAL-DAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-228 |
3.80e-19 |
|
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: 90.60 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEATLTRRAAelgvrAVYQ 95
Cdd:COG4987 342 RYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIA-----VVPQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENLCLGqwpRRNgmidylqmAQDAQrCLQALG-------VDVSPEQLVS-------TLSPAQKQLVEIA 161
Cdd:COG4987 417 RPHLFDT-TLRENLRLA---RPD--------ATDEE-LWAALErvglgdwLAALPDGLDTwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 162 RVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQVA 228
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIV 548
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
254-482 |
4.27e-19 |
|
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: 90.21 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 254 APVAPQEIVDQAVLEVRALR------HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT 327
Cdd:COG4987 321 EPAEPAPAPGGPSLELEDVSfrypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 328 RPDyGDMLKRGIGYtpenrkeagiipwlgVDENTVLTNrqkisangvlqwSTIR---RL-----TEEVMQRMTVKAASSE 399
Cdd:COG4987 401 DLD-EDDLRRRIAV---------------VPQRPHLFD------------TTLRenlRLarpdaTDEELWAALERVGLGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 400 ----------TPIG----TLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRElAAEGKSVVFISSEVE 465
Cdd:COG4987 453 wlaalpdgldTWLGeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLA 531
|
250
....*....|....*..
gi 1314860479 466 ELPLVcDRILLLQHGTF 482
Cdd:COG4987 532 GLERM-DRILVLEDGRI 547
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
276-484 |
4.35e-19 |
|
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: 86.24 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmlkRGIGYTPENRkeaGIIPWL 355
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFVFQHY---ALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 GVDENTVLTNRQKISANGVLQwSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGV 435
Cdd:cd03296 90 TVFDNVAFGLRVKPRSERPPE-AEIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 436 DIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:cd03296 168 DAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-227 |
4.97e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.06 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVraVYQEL 97
Cdd:PRK13639 10 SYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGI--VFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 -SLVEGLTVAENLCLGqwPRRNGMiDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:PRK13639 88 dDQLFAPTVEEDVAFG--PLNLGL-SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 177 TSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
267-480 |
7.03e-19 |
|
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: 89.43 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmLKRGIGYTPENr 346
Cdd:COG4988 342 VSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS-WRRQIAWVPQN- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 347 keagiiPWL--G-VDENTVLTNRQkisANGVLQWSTIRR--LTEEVMQRmtvkAASSETPIG----TLSGGNQQKVVIGR 417
Cdd:COG4988 420 ------PYLfaGtIRENLRLGRPD---ASDEELEAALEAagLDEFVAAL----PDGLDTPLGeggrGLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 418 WVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAeGKSVVFIS---SEVEElplvCDRILLLQHG 480
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILIThrlALLAQ----ADRILVLDDG 547
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
276-480 |
7.42e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDyGDMLKRGIGYTPENRKEAGIIPWL 355
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 GVDENTVLTNRQKISANGvlqwSTIRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGV 435
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWT----ETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1314860479 436 DIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-229 |
9.15e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 9.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGE---TRLEGDEATLTRRaaELGVraVYQELS 98
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRR--QIGM--IFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENLCLgqwprrnGMIDYLQMAQDAQR----CLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK10908 90 LLMDRTVYDNVAI-------PLIIAGASGDDIRRrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAG 229
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-230 |
9.32e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.40 E-value: 9.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 30 NFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWigetrLEGDEATLT---RRAaelgVRAVYQELSLVEGLTVA 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-----LNGQDHTTTppsRRP----VSMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 107 ENLCLGQWP--RRNGMiDYLQMAQDAQRclqaLGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASA- 183
Cdd:PRK10771 90 QNIGLGLNPglKLNAA-QREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAl 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 184 ---EVELV--ISAVKKMSALgvaviYVSHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:PRK10771 165 rqeMLTLVsqVCQERQLTLL-----MVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
270-480 |
9.92e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.33 E-value: 9.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 270 RALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIGYTPEnrkEA 349
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQ---EA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 350 GIIPWLGVDEN--TVLTNRQKIS-------ANGVLQWSTIRRLTEEVMQrmtvkaassetpigTLSGGNQQKVVIGRWVY 420
Cdd:PRK10895 88 SIFRRLSVYDNlmAVLQIRDDLSaeqredrANELMEEFHIEHLRDSMGQ--------------SLSGGERRRVEIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 421 AASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-225 |
1.03e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 9 PVAKVVAG-NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigeTRLeGDEATLTRRAAE 87
Cdd:PRK13536 39 TVAIDLAGvSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI----TVL-GVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 88 LGVRAVYQELSLVEGLTVAENLCLgqWPRRNGMidylqMAQDAQRCLQAL----GVDVSPEQLVSTLSPAQKQLVEIARV 163
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLV--FGRYFGM-----STREIEAVIPSLlefaRLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 164 MKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDG 225
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
267-480 |
1.17e-18 |
|
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: 85.31 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT--RPDYGDMLKRGIGYTpe 344
Cdd:cd03256 6 LSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLRRQIGMI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 345 nRKEAGIIPWLGVDENtVLTNRqkisangVLQWSTIR----RLTEEVMQR---------MTVKAassETPIGTLSGGNQQ 411
Cdd:cd03256 84 -FQQFNLIERLSVLEN-VLSGR-------LGRRSTWRslfgLFPKEEKQRalaalervgLLDKA---YQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 412 KVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-227 |
1.19e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.57 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTR----RAAELGVRAV 93
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQkgliRQLRQHVGFV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 94 YQELSLVEGLTVAENLCLGqwPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:PRK11264 91 FQNFNLFPHRTVLENIIEG--PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
273-488 |
1.27e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.68 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 273 RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygdmLKRGIGYtpenRKEAgII 352
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----ADRGVVF----QKDA-LL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 PWLGVDENTVLTNR-QKISAngvlqwSTIRRLTEEVMQRMTVKAASSEtPIGTLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:COG4525 89 PWLNVLDNVAFGLRlRGVPK------AERRARAEELLALVGLADFARR-RIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG----------TFSQEFHA 488
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVMSPGpgriverlelDFSRRFLA 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
263-477 |
1.32e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.53 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 263 DQAVLEVRALRH--------KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygdm 334
Cdd:COG1116 4 AAPALELRGVSKrfptggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 335 lkRGIGYTPEnrkEAGIIPWLGVDENTVL-TNRQKISAngvlqwSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKV 413
Cdd:COG1116 80 --PDRGVVFQ---EPALLPWLTVLDNVALgLELRGVPK------AERRERARELLELVGLAGFEDAYP-HQLSGGMRQRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 414 VIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVREL-AAEGKSVVFISSEVEELPLVCDRILLL 477
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-226 |
1.36e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRAAELGVRAVYQEL 97
Cdd:PRK13537 15 KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-----SLCGEPVPSRARHARQRVGVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCLgqWPRRNGMiDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PRK13537 90 NLDPDFTVRENLLV--FGRYFGL-SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 178 SSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQ 226
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
278-484 |
1.77e-18 |
|
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: 84.44 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgigytpenrKEAGIIPWLGV 357
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF---------QNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTNRqkiSANGVLQWSTIRRLTEEVMQRMTVKAASsETPIGTLSGGNQQKVVIGRWVYAASQILLLDEP------ 431
Cdd:TIGR01184 72 RENIALAVD---RVLPDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPfgalda 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 432 -TRGvdiEAKQQIYRIVRElaaEGKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:TIGR01184 148 lTRG---NLQEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNGPAAN 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
275-480 |
1.84e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygdmLKRGIGYTPEnrkeaGIIPW 354
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVFQNE-----GLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTnrqkisangvLQWSTI-RRLTEEVMQRMTVK---AASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:PRK11248 85 RNVQDNVAFG----------LQLAGVeKMQRLEIAHQMLKKvglEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
278-480 |
2.29e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgigytpeNRKEAGII---PW 354
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKK-------LRKKVSLVfqfPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTN----------RQKISANGVLQWSTIRRLTEEVMqrmtvkaasSETPIgTLSGGNQQKVVIGRWVYAASQ 424
Cdd:PRK13641 96 AQLFENTVLKDvefgpknfgfSEDEAKEKALKWLKKVGLSEDLI---------SKSPF-ELSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 425 ILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
278-480 |
2.51e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIGYTPENRKeagIIPWLGV 357
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVL----TNRQKISANGVLQWSTIRRLTEEVMQRMtvkaassetpiGTLSGGNQQKVVIGRWVYAASQILLLDEPTR 433
Cdd:PRK11614 98 EENLAMggffAERDQFQERIKWVYELFPRLHERRIQRA-----------GTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314860479 434 GVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-180 |
2.77e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.53 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG----VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDeatltrrAAELGVraVY 94
Cdd:COG4525 12 RYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-------GADRGV--VF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLCLGqwprrngmidyLQMA--------QDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKG 166
Cdd:COG4525 83 QKDALLPWLNVLDNVAFG-----------LRLRgvpkaerrARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170
....*....|....
gi 1314860479 167 EPRVVILDEPTSSL 180
Cdd:COG4525 152 DPRFLLMDEPFGAL 165
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-238 |
2.92e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.78 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGDEATltrraaELGVRAVYQELSLV----- 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII-----DGDLLT------EENVWDIRHKIGMVfqnpd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 ---EGLTVAENLCLGqwpRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PRK13650 92 nqfVGATVEDDVAFG---LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 178 SSL-ASAEVELvISAVKKM-SALGVAVIYVSHRMEEIrRIASCATVMRDGQVagdvmlENTST 238
Cdd:PRK13650 169 SMLdPEGRLEL-IKTIKGIrDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV------ESTST 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-228 |
3.42e-18 |
|
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: 83.69 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRaaELGVraVYQELSLVE 101
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR--QVGV--VLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GlTVAENLCLGQ-WPRRNGMIDYLQMAqDAQRCLQAL--GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:cd03252 90 R-SIRDNIALADpGMSMERVIEAAKLA-GAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 179 SLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQVA 228
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-227 |
3.48e-18 |
|
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: 82.09 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATL--TRRAAELGVRAV---YQELSL 99
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI-----TLDGKPVTRrsPRDAIRAGIAYVpedRKREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 VEGLTVAENLCLGQWprrngmidylqmaqdaqrclqalgvdvspeqlvstLSPAQKQLVEIARVMKGEPRVVILDEPTSS 179
Cdd:cd03215 90 VLDLSVAENIALSSL-----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314860479 180 LASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
278-480 |
4.35e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 87.58 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmLKRGIGYTPENrkeagIIPWLG- 356
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS-LRRQIGVVLQD-----VFLFSGt 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 357 VDENTVLTNRQkISANGVLQWSTIRRLTEEVMQRmtvkAASSETPIG----TLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:COG2274 565 IRENITLGDPD-ATDEEIIEAARLAGLHDFIEAL----PMGYDTVVGeggsNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 433 RGVDIEAKQQIYRIVRELAAeGKSVVFISSeveELPLV--CDRILLLQHG 480
Cdd:COG2274 640 SALDAETEAIILENLRRLLK-GRTVIIIAH---RLSTIrlADRIIVLDKG 685
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
275-480 |
6.35e-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: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPD---YGDMlkrgIGYtpenrkeagi 351
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDpneLGDH----VGY---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 ipwlgvdentvltnrqkisangvlqwstirrlteeVMQRMTVKAASSETPIgtLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:cd03246 81 -----------------------------------LPQDDELFSGSIAENI--LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLvCDRILLLQHG 480
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-227 |
6.83e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.06 E-value: 6.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlegDEATLTRRAAELGVRAVYQELSLVEGL 103
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-------DDITITHKTKDKYIRPVRKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 --------TVAENLCLGqwPRRNGMiDYLQMAQDAQRCLQALG-----VDVSPEQlvstLSPAQKQLVEIARVMKGEPRV 170
Cdd:PRK13646 94 pesqlfedTVEREIIFG--PKNFKM-NLDEVKNYAHRLLMDLGfsrdvMSQSPFQ----MSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 171 VILDEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-207 |
7.06e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.23 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTR---RAAELGVR-AVYQEl 97
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI-----KLDGGDIDDPDvaeACHYLGHRnAMKPA- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 slvegLTVAENLCLgqWPRRNGMIDYlqmaqDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PRK13539 88 -----LTVAENLEF--WAAFLGGEEL-----DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 1314860479 178 SSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-180 |
8.04e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 8.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDeatltrrAAELGVraVYQELS 98
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-------GAERGV--VFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENLCLGQwprRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:PRK11248 81 LLPWRNVQDNVAFGL---QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
..
gi 1314860479 179 SL 180
Cdd:PRK11248 158 AL 159
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
275-480 |
1.01e-17 |
|
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: 81.87 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmLKRGIGYTPENrkeagiiPW 354
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQD-------VT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 L---GVDENTVLtNRQKISANGVLQWSTIRRLTEEVMQRmtvkAASSETPIG----TLSGGNQQKVVIGRWVYAASQILL 427
Cdd:cd03245 89 LfygTLRDNITL-GAPLADDERILRAAELAGVTDFVNKH----PNGLDLQIGergrGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 428 LDEPTRGVDIEAKQQIYRIVRELAAeGKSVVFISSEVEELPLVcDRILLLQHG 480
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDLV-DRIIVMDSG 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-254 |
1.21e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 28 NVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEatlTRRAAELGVraVY-QELSLVEGL--- 103
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---TAQRLARGL--VYlPEDRQSSGLyld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 -TVAENLC------LGQWprrngmidyLQMAQDA---QRCLQALGVDVS-PEQLVSTLSPAQKQLVEIARVMKGEPRVVI 172
Cdd:PRK15439 356 aPLAWNVCalthnrRGFW---------IKPARENavlERYRRALNIKFNhAEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 173 LDEPTSSL---ASAEVELVIsavKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRD 249
Cdd:PRK15439 427 VDEPTRGVdvsARNDIYQLI---RSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFGEH 503
|
....*
gi 1314860479 250 HVDIA 254
Cdd:PRK15439 504 QAQEA 508
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
278-480 |
1.27e-17 |
|
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: 81.86 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgigytpenRKEAGIIpwlgv 357
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA--------RRRIGMI----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTNRQKISANGVL-----------QWSTIRRLTEEVmqRMTVKAassETPIGTLSGGNQQKVVIGRWVYAASQIL 426
Cdd:cd03258 88 FQHFNLLSSRTVFENVALpleiagvpkaeIEERVLELLELV--GLEDKA---DAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 427 LLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-227 |
1.59e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 21 PGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAaelgVRAVYQELSLV 100
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ----VALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGlTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQAL--GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:TIGR00958 568 SG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 179 SLaSAEVELVISAvkKMSALGVAVIYVSHRMEEIRRIASCAtVMRDGQV 227
Cdd:TIGR00958 647 AL-DAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQIL-VLKKGSV 691
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-227 |
1.70e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.15 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWigetrLEGDE-ATLTRRAAELGVRAVYQ 95
Cdd:TIGR02203 339 RYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIL-----LDGHDlADYTLASLRRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENLCLGQwPRRNGMIDYLQMAQDAQrcLQALgVDVSPEQL-------VSTLSPAQKQLVEIARVMKGEP 168
Cdd:TIGR02203 414 DVVLFND-TIANNIAYGR-TEQADRAEIERALAAAY--AQDF-VDKLPLGLdtpigenGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 169 RVVILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQV 227
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
265-480 |
1.77e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKR--- 337
Cdd:PRK13548 1 AMLEARNLSvrlgGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 338 -------GIGYTPENRKEAGIIPWLGVDENTvltnrqkisangvlqwstiRRLTEEVMQRMTVkAASSETPIGTLSGGNQ 410
Cdd:PRK13548 81 lpqhsslSFPFTVEEVVAMGRAPHGLSRAED-------------------DALVAAALAQVDL-AHLAGRDYPQLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 411 QKVVIGR-----WVYAASQ-ILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFIsseVEELPLV---CDRILLLQHG 480
Cdd:PRK13548 141 QRVQLARvlaqlWEPDGPPrWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVV---LHDLNLAaryADRIVLLHQG 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-207 |
1.91e-17 |
|
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: 80.61 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQELslve 101
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTT---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 gLTVAENLclgQWPRRNGmidylqmaqDAQRCLQAL------GVDVSPeqlVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:cd03231 88 -LSVLENL---RFWHADH---------SDEQVEEALarvglnGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
265-480 |
1.99e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.93 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpdygdmlkrgiG 340
Cdd:PRK13537 6 APIDFRNVEkrygDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP------------S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 YTPENRKEAGIIPWL-GVDEN-TVLTNRQKISANGVLQWSTIRRLTEEVMQ--RMTVKAassETPIGTLSGGNQQKVVIG 416
Cdd:PRK13537 74 RARHARQRVGVVPQFdNLDPDfTVRENLLVFGRYFGLSAAAARALVPPLLEfaKLENKA---DAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 417 RWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-230 |
2.26e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 16 GNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGdeatltRRAAELGVRAVYQ 95
Cdd:COG1134 32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-----NG------RVSALLELGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 -ElslvegLTVAENLclgqwpRRNGMIdyLQMA-QDAQRCLQA------LG--VDVsPeqlVSTLSPAQKqlveiAR--- 162
Cdd:COG1134 101 pE------LTGRENI------YLNGRL--LGLSrKEIDEKFDEivefaeLGdfIDQ-P---VKTYSSGMR-----ARlaf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 163 --VMKGEPRVVILDEptsslasaevelVIS---------AVKKMSAL---GVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:COG1134 158 avATAVDPDILLVDE------------VLAvgdaafqkkCLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
..
gi 1314860479 229 GD 230
Cdd:COG1134 226 MD 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
275-481 |
2.65e-17 |
|
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: 80.21 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGekitrpdygdmlkrGIGYTPENrkeagiiPW 354
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQE-------PW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LgvdentvltnrqkisangvlQWSTIR-------RLTEEvMQRMTVKAAS-----------SETPIG----TLSGGNQQK 412
Cdd:cd03250 77 I--------------------QNGTIRenilfgkPFDEE-RYEKVIKACAlepdleilpdgDLTEIGekgiNLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 413 VVIGRWVYAASQILLLDEPTRGVDIEAKQQIY-RIVRELAAEGKSVVFISSEVEELPLvCDRILLLQHGT 481
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-214 |
3.11e-17 |
|
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: 80.59 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 21 PGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAaelgVRAVYQELSLV 100
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK----VSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGlTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQ--ALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:cd03248 101 AR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISelASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1314860479 179 SLaSAEVELVISAVKKMSALGVAVIYVSHRMEEIRR 214
Cdd:cd03248 180 AL-DAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
26-227 |
3.57e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.82 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEG-DEATLTRRAAELGVraVYQELSLVEGLT 104
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-----RFHGtDVSRLHARDRKVGF--VFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 105 VAENLCLG--QWPRRN------------GMIDYLQMAQDAQRclqalgvdvSPEQlvstLSPAQKQLVEIARVMKGEPRV 170
Cdd:PRK10851 91 VFDNIAFGltVLPRRErpnaaaikakvtQLLEMVQLAHLADR---------YPAQ----LSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 171 VILDEPTSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK10851 158 LLLDEPFGALdAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
274-481 |
5.99e-17 |
|
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: 79.13 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 274 HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQ--GEIVINGekitRPDYGDMLKRGIGYTPEnrkEAGI 351
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING----RPLDKRSFRKIIGYVPQ---DDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 IPWLGVDENTvltnrqKISANgvlqwstIRRLteevmqrmtvkaassetpigtlSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:cd03213 94 HPTLTVRETL------MFAAK-------LRGL----------------------SGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAEGKSVVFI----SSEVEELplvCDRILLLQHGT 481
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSihqpSSEIFEL---FDKLLLLSQGR 189
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-227 |
6.96e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.03 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQ--ELSLVEGl 103
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLCLGqwPRRNGMIDylQMAQD-AQRCLQALGVdvsPEQLVST----LSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:PRK13641 102 TVLKDVEFG--PKNFGFSE--DEAKEkALKWLKKVGL---SEDLISKspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 179 SLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-227 |
7.88e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.40 E-value: 7.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIG--ETRLEGDEATLTRRAAELGVRA-- 92
Cdd:PRK10619 12 HKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqTINLVRDKDGQLKVADKNQLRLlr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 93 -----VYQELSLVEGLTVAENLClgQWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQ-LVSTLSPAQKQLVEIARVMKG 166
Cdd:PRK10619 92 trltmVFQHFNLWSHMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 167 EPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
26-228 |
7.97e-17 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 79.29 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG-DEATLTRRAAELGVraVYQELSLVEGLT 104
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGaSKKQLVQLRRRIGY--IFQAHNLLGFLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 105 VAENLCLGQWPRRNgmIDYLQMAQDAQRCLQALG----VDVSPEQLvstlSPAQKQLVEIARVMKGEPRVVILDEPTSSL 180
Cdd:TIGR02982 99 ARQNVQMALELQPN--LSYQEARERARAMLEAVGlgdhLNYYPHNL----SGGQKQRVAIARALVHHPKLVLADEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 181 ASAEVELVISAVKKMSA-LGVAVIYVSHRmEEIRRIASCATVMRDGQVA 228
Cdd:TIGR02982 173 DSKSGRDVVELMQKLAKeQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
17-227 |
7.98e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 81.69 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrlEGDEATlTRRAAELGVRAVYQE 96
Cdd:PRK11432 13 TKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-----DGEDVT-HRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGqwprrngmidyLQM-----AQDAQRCLQALG-VDVS--PEQLVSTLSPAQKQLVEIARVMKGEP 168
Cdd:PRK11432 87 YALFPHMSLGENVGYG-----------LKMlgvpkEERKQRVKEALElVDLAgfEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 169 RVVILDEPTSSLasaEVELVISAVKKMSAL----GVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK11432 156 KVLLFDEPLSNL---DANLRRSMREKIRELqqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
276-480 |
9.33e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.42 E-value: 9.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGekitrPDYGDMLKrgigyTPENRKEAGII--- 352
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-----IDTGDFSK-----LQGIRKLVGIVfqn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 PWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:PRK13644 86 PETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314860479 433 RGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPlVCDRILLLQHG 480
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRG 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-289 |
1.00e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.23 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELgvraVYQEL-SLVEGL 103
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL----VFQNPdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLCLGqwPRRNGMiDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASA 183
Cdd:PRK13652 95 TVEQDIAFG--PINLGL-DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 184 EVELVISAVKKMS-ALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHhivSLMLGRDHVDIaPVAPQEIv 262
Cdd:PRK13652 172 GVKELIDFLNDLPeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ---PDLLARVHLDL-PSLPKLI- 246
|
250 260
....*....|....*....|....*..
gi 1314860479 263 dqavlevRALRHKPKLEDISFTLRRGE 289
Cdd:PRK13652 247 -------RSLQAQGIAIDMAYTYQEAE 266
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-227 |
1.02e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 27 DNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWigetrLEGDE-ATLTRR---AAELGVRAVYQELSLVEG 102
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIL-----FDGENiPAMSRSrlyTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 103 LTVAENLClgqWPRRngmiDYLQMAQDAQRC-----LQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PRK11831 99 MNVFDNVA---YPLR----EHTQLPAPLLHStvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 178 SSLASAEVELVISAVKKM-SALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK11831 172 VGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-227 |
1.08e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.28 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGV----- 90
Cdd:PRK13636 12 NYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMvfqdp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 ------RAVYQELSLvegltVAENLclgQWPRRngmidylQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVM 164
Cdd:PRK13636 92 dnqlfsASVYQDVSF-----GAVNL---KLPED-------EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 165 KGEPRVVILDEPTSSLASAEVELVISAVKKMS-ALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-227 |
1.18e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.59 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSeRPDSGDIWIGETRL-EGDEATLTRRAAELGvravyQELSLV 100
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELrELDPESWRKHLSWVG-----QNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGlTVAENLCLGqwprrNGMIDYLQMAQDAQRC-------LQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:PRK11174 436 HG-TLRDNVLLG-----NPDASDEQLQQALENAwvseflpLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEirrIASCAT--VMRDGQV 227
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLED---LAQWDQiwVMQDGQI 561
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
264-481 |
1.22e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 264 QAVLEVRALRHKPK--LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGeKITRPdygdmLKRGIGY 341
Cdd:COG1134 26 ELLLRRRRTRREEFwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL-----LELGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 TPEnrkeagiipwlgvdentvLTNRQKISANGVLQ---WSTIRRLTEEVmqrmtvkAASSE------TPIGTLSGGnqQK 412
Cdd:COG1134 100 HPE------------------LTGRENIYLNGRLLglsRKEIDEKFDEI-------VEFAElgdfidQPVKTYSSG--MR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 413 VvigRWVYAAS-----QILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFIS---SEVEELplvCDRILLLQHGT 481
Cdd:COG1134 153 A---RLAFAVAtavdpDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVShsmGAVRRL---CDRAIWLEKGR 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-227 |
1.30e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrleGDEATLTRRAAELG--VRAVYQELSL 99
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV------AGDDVEALSARAASrrVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 VEGLTVAENLCLGQWPRRnGMIDYLQMAQDA--QRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PRK09536 89 SFEFDVRQVVEMGRTPHR-SRFDTWTETDRAavERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 178 SSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
278-480 |
1.70e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.56 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDM--LKRGIGYTPENRKeagIIPWL 355
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpyLRRRIGVVFQDFR---LLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 GVDENTVLtnrqkisangVLQ-----WSTIRRLTEEVMQR--MTVKAassETPIGTLSGGNQQKVVIGRWVYAASQILLL 428
Cdd:COG2884 95 TVYENVAL----------PLRvtgksRKEIRRRVREVLDLvgLSDKA---KALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 429 DEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSE---VEELPLvcdRILLLQHG 480
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDlelVDRMPK---RVLELEDG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
281-497 |
1.80e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.64 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 281 ISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygdmlkrgigYTPENRKEAGIIpwlgvDEN 360
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------------LPPAERPVSMLF-----QEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 361 TV---LTNRQKISangvLQWSTIRRLTEEvmQRMTVKAASSETPI--------GTLSGGNQQKVVIGRWVYAASQILLLD 429
Cdd:COG3840 81 NLfphLTVAQNIG----LGLRPGLKLTAE--QRAQVEQALERVGLaglldrlpGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 430 EPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGtfsqEFHAPVNVDELMS 497
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADG----RIAADGPTAALLD 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-480 |
1.86e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 14 VAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKS----TLIRML--TGSErPDSGDIWIGETRLEGDEATLTRRAAE 87
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLRRRSRQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 88 LGVRA-----VYQE--LSLVEGLTV----AENLCLGQWPRRNgmidylQMAQDAQRCLQALGVDVSPEQLVS---TLSPA 153
Cdd:PRK10261 99 RHVRGadmamIFQEpmTSLNPVFTVgeqiAESIRLHQGASRE------EAMVEAKRMLDQVRIPEAQTILSRyphQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 154 QKQLVEIARVMKGEPRVVILDEPTSSL---ASAEVELVISAVKKMSALGVavIYVSHRMEEIRRIASCATVMRDGQV--A 228
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALdvtIQAQILQLIKVLQKEMSMGV--IFITHDMGVVAEIADRVLVMYQGEAveT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 229 GDVMLENTSTHHI-----------VSLMLGRDHV---------DIAPVAPQEIVDQAV-----LEVRAL----------- 272
Cdd:PRK10261 251 GSVEQIFHAPQHPytrallaavpqLGAMKGLDYPrrfplisleHPAKQEPPIEQDTVVdgepiLQVRNLvtrfplrsgll 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 273 ----RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKI-TRPDYG-DMLKRGIGYTPENr 346
Cdd:PRK10261 331 nrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKlQALRRDIQFIFQD- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 347 KEAGIIPWLGVDENTVltnrQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQIL 426
Cdd:PRK10261 410 PYASLDPRQTVGDSIM----EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 427 LLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLG 540
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-180 |
2.00e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.16 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVV-ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GE--TRLEGDEATLTRRAAELgvraV 93
Cdd:COG4608 25 GRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdGQdiTGLSGRELRPLRRRMQM----V 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 94 YQE--LSLVEGLTVAEnlCLGQWPRRNGMIDYLQMAQDAQRCLQALGVDVS-----PEQLvstlSPAQKQLVEIARVMKG 166
Cdd:COG4608 101 FQDpyASLNPRMTVGD--IIAEPLRIHGLASKAERRERVAELLELVGLRPEhadryPHEF----SGGQRQRIGIARALAL 174
|
170
....*....|....
gi 1314860479 167 EPRVVILDEPTSSL 180
Cdd:COG4608 175 NPKLIVCDEPVSAL 188
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-227 |
2.24e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.89 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLT----------RRAAELG--V 90
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHElitnpyskkiKNFKELRrrV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 RAVYQ--ELSLVEGlTVAENLCLGqwPRRNGMIDYlQMAQDAQRCLQALGV-----DVSPEQLvstlSPAQKQLVEIARV 163
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFG--PVALGVKKS-EAKKLAKFYLNKMGLddsylERSPFGL----SGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 164 MKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
278-478 |
2.27e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPdygdMLKRGIGYTPENRKEAGIIPWLGv 357
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLVAYVPQSEEVDWSFPVLV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 dENTVLTNRQkisanGVLQWstIRRLTEEVMQRMTVKAASSET------PIGTLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:PRK15056 98 -EDVVMMGRY-----GHMGW--LRRAKKRDRQIVTAALARVDMvefrhrQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQ 478
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-248 |
2.47e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 29 VNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGdiwigetRLEGDEATLTRRAAELGVRAVY-------QELSLVE 101
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAG-------QVYLDGKPIDIRSPRDAIRAGImlcpedrKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GLTVAENL---CLGQWPRRNGMIDYLQMAQDAQRCLQALGVDV-SPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PRK11288 345 VHSVADNInisARRHHLRAGCLINNRWEAENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 178 SSL---ASAEVELVISAvkkMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGR 248
Cdd:PRK11288 425 RGIdvgAKHEIYNVIYE---LAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQALSLALPR 495
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
17-180 |
2.89e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.59 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRL-EGDEATLTRRAAELGvravyQ 95
Cdd:COG4604 8 SKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKRLAILR-----Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQWPRRNG------------MIDYLQMAQDAQRCLqalgvdvspeqlvSTLSPAQKQLVEIARV 163
Cdd:COG4604 83 ENHINSRLTVRELVAFGRFPYSKGrltaedreiideAIAYLDLEDLADRYL-------------DELSGGQRQRAFIAMV 149
|
170
....*....|....*..
gi 1314860479 164 MKGEPRVVILDEPTSSL 180
Cdd:COG4604 150 LAQDTDYVLLDEPLNNL 166
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
278-484 |
2.91e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.13 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmlkRGIGYTPENRkeaGIIPWLGV 357
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---RKVGFVFQHY---ALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DEN-----TVLTNRQKISAngvlqwSTIRRlteEVMQ--RMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:PRK10851 92 FDNiafglTVLPRRERPNA------AAIKA---KVTQllEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELAAEGK-SVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-231 |
3.09e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.59 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGE---TRLegdeaTLTRRAAELGvRaVYQELSL 99
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKL-----PEYKRAKYIG-R-VFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 --VEGLTVAENLCL----GQwpRRNgmidyLQMAQDAQR--------CLQALGVDVSPEQLVSTLSPAQKQLVeiARVMK 165
Cdd:COG1101 92 gtAPSMTIEENLALayrrGK--RRG-----LRRGLTKKRrelfrellATLGLGLENRLDTKVGLLSGGQRQAL--SLLMA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 166 --GEPRVVILDEPTSSLASAEVELVISAVKKM-SALGVAVIYVSHRMEEI-----RRIascatVMRDGQVAGDV 231
Cdd:COG1101 163 tlTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQAldygnRLI-----MMHEGRIILDV 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-438 |
3.58e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 81.13 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 10 VAKVVAGNKRypgvvALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG--------DEATL 81
Cdd:TIGR03719 10 VSKVVPPKKE-----ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGylpqepqlDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 82 TRRAAELGVRAV------YQELSLVEGLTVAE-NLCLGQWPRRNGMIDY---------LQMAQDAQRClqalgvdVSPEQ 145
Cdd:TIGR03719 85 VRENVEEGVAEIkdaldrFNEISAKYAEPDADfDKLAAEQAELQEIIDAadawdldsqLEIAMDALRC-------PPWDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 146 LVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSAlgvAVIYVSH------------------ 207
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHdryfldnvagwileldrg 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 208 ------------------RME---------------EI---------RRIASCATVMRDGQVAGDVMLENTSTHHIvslm 245
Cdd:TIGR03719 235 rgipwegnysswleqkqkRLEqeekeesarqktlkrELewvrqspkgRQAKSKARLARYEELLSQEFQKRNETAEI---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 246 lgrdhvdIAPVAPQeiVDQAVLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVI 321
Cdd:TIGR03719 311 -------YIPPGPR--LGDKVIEAENLTkafgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 322 ngekitrpdyGDMLKrgIGYTPENRKeagiipwlGVDEN-TVLtnrQKIS-ANGVLQWSTIRRLTEEVMQRMTVKAASSE 399
Cdd:TIGR03719 382 ----------GETVK--LAYVDQSRD--------ALDPNkTVW---EEISgGLDIIKLGKREIPSRAYVGRFNFKGSDQQ 438
|
490 500 510
....*....|....*....|....*....|....*....
gi 1314860479 400 TPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIE 438
Cdd:TIGR03719 439 KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
280-480 |
3.62e-16 |
|
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: 79.76 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 280 DISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGE-------KITRPDYgdmlKRGIGYTPEnrkEAGII 352
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsarGIFLPPH----RRRIGYVFQ---EARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 PWLGVDEN------TVLTNRQKISANGVLQWSTIRRLteevMQRMtvkaassetpIGTLSGGNQQKVVIGRWVYAASQIL 426
Cdd:COG4148 90 PHLSVRGNllygrkRAPRAERRISFDEVVELLGIGHL----LDRR----------PATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 427 LLDEPTRGVDIEAKQQIYRIVRELAAEGK-SVVFISSEVEELPLVCDRILLLQHG 480
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDELDiPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
273-480 |
3.80e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 77.91 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 273 RHKPK----LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDyGDMLKRGIGYtpenrke 348
Cdd:cd03252 9 RYKPDgpviLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD-PAWLRRQVGV------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 349 agiipwlgVDENTVLTNRqkisangvlqwsTIRR---LTEEVMQRMTVKAASS---------ETPIG----------TLS 406
Cdd:cd03252 81 --------VLQENVLFNR------------SIRDniaLADPGMSMERVIEAAKlagahdfisELPEGydtivgeqgaGLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 407 GGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAeGKSVVFISSEVEELpLVCDRILLLQHG 480
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV-KNADRIIVMEKG 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
26-212 |
4.02e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.14 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPD---SGDIWIGETRLegdeatlTRRAAELgvRAV---YQELSL 99
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRL-------TALPAEQ--RRIgilFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 VEGLTVAENLCLGQWPRRNGmidylqmAQDAQRCLQAL---GVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:COG4136 88 FPHLSVGENLAFALPPTIGR-------AQRRARVEQALeeaGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1314860479 177 TSSLASA---EV-ELVISAVKkmsALGVAVIYVSHRMEEI 212
Cdd:COG4136 161 FSKLDAAlraQFrEFVFEQIR---QRGIPALLVTHDEEDA 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
25-212 |
4.06e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.49 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRaaELGVraVYQEL-SLVEGL 103
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK--KIGI--IFQNPdNQFIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLCLGQwprRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSL--- 180
Cdd:PRK13632 100 TVEDDIAFGL---ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLdpk 176
|
170 180 190
....*....|....*....|....*....|...
gi 1314860479 181 ASAEV-ELVISAVKKMSAlgvAVIYVSHRMEEI 212
Cdd:PRK13632 177 GKREIkKIMVDLRKTRKK---TLISITHDMDEA 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
276-480 |
4.06e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 81.32 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGdMLKRGIGYTPENrkeagiiPWL 355
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH-TLRQFINYLPQE-------PYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 ---GVDENTVLTNRQKISANGVLQWSTIRRLTEEV--MQRMTVKAASSETpiGTLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:TIGR01193 560 fsgSILENLLLGAKENVSQDEIWAACEIAEIKDDIenMPLGYQTELSEEG--SSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 431 PTRGVDIEAKQQIyrIVRELAAEGKSVVFISSEVEELPLVcDRILLLQHG 480
Cdd:TIGR01193 638 STSNLDTITEKKI--VNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHG 684
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
269-503 |
4.09e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 78.31 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 269 VRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDM--LKRGI------G 340
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRraFRRDVqlvfqdS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 YTPEN-RKEAGIIPWLGVDENTVLT-NRQKISANGVLQWSTIRrltEEVMQRMTVKaassetpigtLSGGNQQKVVIGRW 418
Cdd:TIGR02769 98 PSAVNpRMTVRQIIGEPLRHLTSLDeSEQKARIAELLDMVGLR---SEDADKLPRQ----------LSGGQLQRINIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 419 VYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTFSQE--------FHAP 489
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEEcdvaqllsFKHP 244
|
250
....*....|....
gi 1314860479 490 VnVDELMSAILSVH 503
Cdd:TIGR02769 245 A-GRNLQSAVLPEH 257
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
278-480 |
4.65e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKI---TRPDYGDMLkrgigytpENRKEAGII-- 352
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR--------ELRRNVGMVfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 -----PWLGVDENTVltnRQKISANGVLQWSTIRRlTEEVMQRMTVKAASSETPIgTLSGGNQQKVVIGRWVYAASQILL 427
Cdd:PRK11124 90 qynlwPHLTVQQNLI---EAPCRVLGLSKDQALAR-AEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 428 LDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
276-477 |
4.88e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGekitrpdygdmlKRGIGYTPEnRKEagiipwl 355
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQ-RSE------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 gVDENTVLTNRQKISA-----NGVLQWSTI--RRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAASQILLL 428
Cdd:NF040873 66 -VPDSLPLTVRDLVAMgrwarRGLWRRLTRddRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 429 DEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELpLVCDRILLL 477
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-277 |
5.18e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.15 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 28 NVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDE-----ATLTRRaaelgVRAVYQELSLVEG 102
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclPPEKRR-----IGYVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 103 LTVAENLCLGQWPRRNGMIDYLqmaqdaqrcLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSL-- 180
Cdd:PRK11144 91 YKVRGNLRYGMAKSMVAQFDKI---------VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLdl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 181 ------------ASAEVELVIsavkkmsalgvavIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIvslmlgr 248
Cdd:PRK11144 162 prkrellpylerLAREINIPI-------------LYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA------- 221
|
250 260 270
....*....|....*....|....*....|
gi 1314860479 249 dhvdIAPVAPQEivDQ-AVLEVRALRHKPK 277
Cdd:PRK11144 222 ----MRPWLPKE--EQsSILKVTVLEHHPH 245
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
280-484 |
5.27e-16 |
|
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: 78.07 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 280 DISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDML---KRGIGYTPENrkeAGIIPWLG 356
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRelrRKKISMVFQS---FALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 357 VDENTVLTnrqkISANGVLQWSTIRRlTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVD 436
Cdd:cd03294 119 VLENVAFG----LEVQGVPRAEREER-AAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 437 ----IEAKQQIYRIVRELaaeGKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:cd03294 193 plirREMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-227 |
5.98e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLE-GDEATLTRRaaelgVRAVYQELSlve 101
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSYRSQR-----IRMIFQDPS--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 gltvaenLCLGQWPRRNGMIDY-------LQMAQDAQRCLQAL-GVDVSPEQLV---STLSPAQKQLVEIARVMKGEPRV 170
Cdd:PRK15112 98 -------TSLNPRQRISQILDFplrlntdLEPEQREKQIIETLrQVGLLPDHASyypHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 171 VILDEptsSLASAEVELVISAVKKMSAL----GVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK15112 171 IIADE---ALASLDMSMRSQLINLMLELqekqGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-212 |
6.13e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWigetrLEGDE-ATLTRRAAELGVRAVYQELSLV 100
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLL-----FEGEDiSTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 eGLTVAENLCL-----GQWPRRNGMIDYLQMAQDAQRCLQalgvdvspeQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK10247 94 -GDTVYDNLIFpwqirNQQPDPAIFLDDLERFALPDTILT---------KNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1314860479 176 PTSSLASAEVELVISAVKKM-SALGVAVIYVSHRMEEI 212
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEI 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
278-494 |
7.99e-16 |
|
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: 77.05 E-value: 7.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGlEEY--EQGEIVINGEKITRPDYGDmLKRGIGY-TPEnrkeagIIPW 354
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPptYGNDVRLFGERRGGEDVWE-LRKRIGLvSPA------LQLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDE---NTVLTnrqkisanGVlqWSTI----------RRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYA 421
Cdd:COG1119 91 FPRDEtvlDVVLS--------GF--FDSIglyreptdeqRERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 422 ASQILLLDEPTRGVDIEAKQQIYRIVRELAAEG-KSVVFISSEVEELPLVCDRILLLQHG---------------TFSQE 485
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGrvvaagpkeevltseNLSEA 239
|
....*....
gi 1314860479 486 FHAPVNVDE 494
Cdd:COG1119 240 FGLPVEVER 248
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-268 |
8.26e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 27 DNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEATLTRRAAELGvravyQELSLVEGLTV 105
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQHYASKEVARRIGLLA-----QNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 AENLCLGQWPRRNGMIDYLQMAQDA-QRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSL-ASA 183
Cdd:PRK10253 99 QELVARGRYPHQPLFTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdISH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 184 EVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVagdvmlentsthhivslmlgrdhvdIAPVAPQEIVD 263
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI-------------------------VAQGAPKEIVT 233
|
....*
gi 1314860479 264 QAVLE 268
Cdd:PRK10253 234 AELIE 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
273-480 |
1.03e-15 |
|
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: 76.03 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 273 RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGeKITRPdygdmLKRGIGYTPEnrkeagii 352
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL-----LGLGGGFNPE-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 pwlgvdentvLTNRQKISANGVLQwstiRRLTEEVMQRMTVKAASSE------TPIGTLSGGnqQKVvigRWVYAAS--- 423
Cdd:cd03220 99 ----------LTGRENIYLNGRLL----GLSRKEIDEKIDEIIEFSElgdfidLPVKTYSSG--MKA---RLAFAIAtal 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 424 --QILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03220 160 epDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
278-480 |
1.08e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKI---TRPDYGDMLkrgigytpENRKEAGII-- 352
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR--------LLRQKVGMVfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 -----PWLGVDENTV--------LTNRQ-KISANGVLQwstirRLteevmqRMTVKAASseTPIgTLSGGNQQKVVIGRW 418
Cdd:COG4161 90 qynlwPHLTVMENLIeapckvlgLSKEQaREKAMKLLA-----RL------RLTDKADR--FPL-HLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 419 VYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-227 |
1.19e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 76.02 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 20 YPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEatLTRRAAELGVRA----VYQ 95
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSI-----RLDGED--ITKLPPHERARAgiayVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLG--QWPRRNGMI--DYLQMAQDAQRCLQALGVDvspeqlvstLSPAQKQLVEIARVMKGEPRVV 171
Cdd:TIGR03410 83 GREIFPRLTVEENLLTGlaALPRRSRKIpdEIYELFPVLKEMLGRRGGD---------LSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 172 ILDEPTSSLAS---AEVELVISAVKKMsaLGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:TIGR03410 154 LLDEPTEGIQPsiiKDIGRVIRRLRAE--GGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-250 |
1.39e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.20 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 21 PGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERpdsgDIWIGETRLEGDEATLT--RRAAELGVRAVYQELS 98
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP----GRWEGEIFIDGKPVKIRnpQQAIAQGIAMVPEDRK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 ---LVEGLTVAENLCLGQWPR--RNGMIDYLQMAQDAQRCLQALGVDV-SPEQLVSTLSPAQKQLVEIARVMKGEPRVVI 172
Cdd:PRK13549 349 rdgIVPVMGVGKNITLAALDRftGGSRIDDAAELKTILESIQRLKVKTaSPELAIARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 173 LDEPTSSL---ASAEVELVISAVKKMsalGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVSLMLGRD 249
Cdd:PRK13549 429 LDEPTRGIdvgAKYEIYKLINQLVQQ---GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAALRSE 505
|
.
gi 1314860479 250 H 250
Cdd:PRK13549 506 H 506
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
266-484 |
1.64e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.07 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpdygdmlkrgiGY 341
Cdd:PRK09452 14 LVELRGISksfdGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT------------HV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 TPENR------KEAGIIPWLGVDENTVLTNR-QKISAngvlqwSTIRRLTEEVMqRMTVKAASSETPIGTLSGGNQQKVV 414
Cdd:PRK09452 82 PAENRhvntvfQSYALFPHMTVFENVAFGLRmQKTPA------AEITPRVMEAL-RMVQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 415 IGRWVYAASQILLLDEPTRGVDIEAKQQ----IYRIVRELaaeGKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQmqneLKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQ 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
18-234 |
1.78e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEgdeatltrrAAELGVRAVYQEL 97
Cdd:PRK11247 20 KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA---------EAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAENLCL---GQWprrngmidylqmAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK11247 91 RLLPWKKVIDNVGLglkGQW------------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 175 EPTSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLE 234
Cdd:PRK11247 159 EPLGALdALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
278-484 |
1.80e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 75.74 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR-PDYgdmlKRGIGYTPENRkeaGIIPWLG 356
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPH----KRPVNTVFQNY---ALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 357 VDENTV--LTnRQKISANgvlqwsTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:cd03300 89 VFENIAfgLR-LKKLPKA------EIKERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 435 VDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-235 |
1.94e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 20 YPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGETRLEGDEATLTRRAaelgVRAVYQELS 98
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvFDGKDITDWQTAKIMREA----VAIVPEGRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENLCLGQWprrngMIDYLQMAQDAQRCLqalgvDVSPE------QLVSTLSPAQKQLVEIARVMKGEPRVVI 172
Cdd:PRK11614 91 VFSRMTVEENLAMGGF-----FAERDQFQERIKWVY-----ELFPRlherriQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 173 LDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV----AGDVMLEN 235
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVvledTGDALLAN 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-227 |
2.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.66 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIG--ETRLEGDEATLTRRAAelgvrAVYQ--ELSL 99
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENLWDIRNKAG-----MVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 VEGLtVAENLCLGqwPRRNGmIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSS 179
Cdd:PRK13633 99 VATI-VEEDVAFG--PENLG-IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 180 LASAEVELVISAVKKM-SALGVAVIYVSHRMEEIRRiASCATVMRDGQV 227
Cdd:PRK13633 175 LDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-233 |
2.12e-15 |
|
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: 74.87 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSE--RPDSGDIWigetrLEGD---EATLTRRAAeLGVRAVYQELSLV 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEIL-----FKGEditDLPPEERAR-LGIFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGLTVAenlclgqwprrngmiDYLQmaqdaqrclqalGVDVSpeqlvstLSPAQKQLVEIARVMKGEPRVVILDEPTSSL 180
Cdd:cd03217 90 PGVKNA---------------DFLR------------YVNEG-------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 181 ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRI-ASCATVMRDGQVA--GDVML 233
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVksGDKEL 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-208 |
2.25e-15 |
|
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: 74.51 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTG--SERPDSGDIWIGETRLegDEATLTRRaaelgVRAVYQELSLVEGL 103
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL--DKRSFRKI-----IGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLclgqwprrngmidylqmaqdaqrclqalgvDVSPEqlVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASA 183
Cdd:cd03213 98 TVRETL------------------------------MFAAK--LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180
....*....|....*....|....*
gi 1314860479 184 EVELVISAVKKMSALGVAVIYVSHR 208
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICSIHQ 170
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-232 |
2.63e-15 |
|
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: 75.19 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEatLTRRAAELGVraVYQELSLVEGLTV 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-----ILEGKQ--ITEPGPDRMV--VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 AENLCLGqwprrngmIDYL--QMAQDAQRC-----LQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:TIGR01184 72 RENIALA--------VDRVlpDLSKSERRAiveehIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 179 SL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA--GDVM 232
Cdd:TIGR01184 144 ALdALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAAniGQIL 200
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
278-485 |
3.18e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.56 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKR-GIGY-TPENRKEAGIIPW- 354
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHiGIVFqNPDNQFVGSIVKYd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 --LGVDENTVLTNRQKISANGVLqwstirrltEEVmqRMTVKAASSETpigTLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:PRK13648 105 vaFGLENHAVPYDEMHRRVSEAL---------KQV--DMLERADYEPN---ALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 433 RGVDIEAKQQIYRIVRELAAEgKSVVFIS-----SEVEElplvCDRILLLQHGTFSQE 485
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSE-HNITIISithdlSEAME----ADHVIVMNKGTVYKE 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-229 |
3.46e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.83 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG--DEATLTRRAAELGVraVYQ--ELSLV 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkKNKKLKPLRKKVGI--VFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGlTVAENLCLGqwPRRNGMIDYlQMAQDAQRCLQALGVdvsPEQLVS----TLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:PRK13634 100 EE-TVEKDICFG--PMNFGVSEE-DAKQKAREMIELVGL---PEELLArspfELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 177 TSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAG 229
Cdd:PRK13634 173 TAGLdPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
276-482 |
3.55e-15 |
|
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: 78.90 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrPDYGDmLKRGIGYTPEnrkeagiipWL 355
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISD-VHQNMGYCPQ---------FD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 GVDEntVLTNRQKISAngvlqWSTIRRLTEEVMQRMTVKAASS-------ETPIGTLSGGNQQKVVIGRWVYAASQILLL 428
Cdd:TIGR01257 2022 AIDD--LLTGREHLYL-----YARLRGVPAEEIEKVANWSIQSlglslyaDRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 429 DEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTF 482
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-227 |
3.68e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDiwigETRLEGDEATLTRRAA-----ELGVraVYQ--EL 97
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP----NSKITVDGITLTAKTVwdireKVGI--VFQnpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVeGLTVAENLCLG----QWPRRngmidylQMAQDAQRCLQALG----VDVSPeqlvSTLSPAQKQLVEIARVMKGEPR 169
Cdd:PRK13640 96 QFV-GATVGDDVAFGlenrAVPRP-------EMIKIVRDVLADVGmldyIDSEP----ANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 170 VVILDEPTSSLASAEVELVISAVKK-MSALGVAVIYVSHRMEEIrRIASCATVMRDGQV 227
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
263-481 |
4.53e-15 |
|
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: 75.08 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 263 DQAVLEVRALRhkpK-------LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR--PDygD 333
Cdd:COG0411 1 SDPLLEVRGLT---KrfgglvaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpPH--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 334 MLKRGIGYTPENrkeAGIIPWLGVDEN--TVLTNRQKISANGVL-----QWSTIRRLTEEVMQ-----RMTVKAassETP 401
Cdd:COG0411 76 IARLGIARTFQN---PRLFPELTVLENvlVAAHARLGRGLLAALlrlprARREEREARERAEEllervGLADRA---DEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 402 IGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFIsseveE--LPLV---CDRIL 475
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLI-----EhdMDLVmglADRIV 224
|
....*.
gi 1314860479 476 LLQHGT 481
Cdd:COG0411 225 VLDFGR 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-227 |
4.56e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGETRLEGDEATLT---RRA---AELGV 90
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALSeaeRRRllrTEWGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 raVYQE------LSLVEGLTVAENL-CLGQwprRNgmidYLQMAQDAQRCLQALGVDVSP-EQLVSTLSPAQKQLVEIAR 162
Cdd:PRK11701 94 --VHQHprdglrMQVSAGGNIGERLmAVGA---RH----YGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 163 VMKGEPRVVILDEPTSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLdVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-210 |
5.03e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 77.86 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAaelgVRAVYQELSLVEGlT 104
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF----INYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 105 VAENLCLGQwpRRNGMIDYLQMA-------QDAQRCLQALGVDVSPEQlvSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:TIGR01193 564 ILENLLLGA--KENVSQDEIWAAceiaeikDDIENMPLGYQTELSEEG--SSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190
....*....|....*....|....*....|...
gi 1314860479 178 SSLASAEVELVISAVKKMSAlgVAVIYVSHRME 210
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS 670
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
274-480 |
5.72e-15 |
|
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: 74.19 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 274 HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYgDMLKRGIGYTPENrkeagiip 353
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTL-DSLRRAIGVVPQD-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 wlgvdenTVLTNrQKISANgvlqwstIR--RL--TEEVMQRmTVKAASSETPI--------------GT-LSGGNQQKVV 414
Cdd:cd03253 84 -------TVLFN-DTIGYN-------IRygRPdaTDEEVIE-AAKAAQIHDKImrfpdgydtivgerGLkLSGGEKQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 415 IGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAeGKSVVFISSEVEELpLVCDRILLLQHG 480
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTI-VNADKIIVLKDG 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-227 |
6.02e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.04 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGETRLEGDEATLTRRAAelgVRAVYQE- 96
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlWQGKPLDYSKRGLLALRQQ---VATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 --------------LSLvEGLTVAENlclgQWPRRngmIDYLQMAQDAQRCLQalgvdvspeQLVSTLSPAQKQLVEIAR 162
Cdd:PRK13638 87 eqqifytdidsdiaFSL-RNLGVPEA----EITRR---VDEALTLVDAQHFRH---------QPIQCLSHGQKKRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 163 VMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
267-498 |
6.28e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 6.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEqGEIVINGEKITRPDYGDmLKRGIGYTPENR 346
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAE-LARHRAYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 347 KEAGIIP-WlgvdenTVLTNRQKISANGVLQWSTIRRLTEEVMqrMTVKAassETPIGTLSGGNQQKV-------VIGRW 418
Cdd:PRK03695 79 TPPFAMPvF------QYLTLHQPDKTRTEAVASALNEVAEALG--LDDKL---GRSVNQLSGGEWQRVrlaavvlQVWPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 419 VYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGtfsqEFHAPVNVDELMSA 498
Cdd:PRK03695 148 INPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG----KLLASGRRDEVLTP 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-222 |
6.48e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 75.47 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERP---DSGDIWI-GETRLEGDEATLTR-RAAELGVraVYQE- 96
Cdd:COG0444 18 VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFdGEDLLKLSEKELRKiRGREIQM--IFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 -LSL-----VeGLTVAENLclgqwpRRNGMIDYLQMAQDAQRCLQALGVDvSPEQLVS----TLSPAQKQLVEIARVMKG 166
Cdd:COG0444 96 mTSLnpvmtV-GDQIAEPL------RIHGGLSKAEARERAIELLERVGLP-DPERRLDryphELSGGMRQRVMIARALAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 167 EPRVVILDEPTSSL-AS--AEV-ELVISAVKKmsaLGVAVIYVSHRMEEIRRIASCATVM 222
Cdd:COG0444 168 EPKLLIADEPTTALdVTiqAQIlNLLKDLQRE---LGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
278-484 |
6.93e-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: 73.44 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmlkRGIGYTPENrkeAGIIPWLGV 357
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMVFQN---YALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTNRQKISANgvlqwSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVD- 436
Cdd:cd03301 90 YDNIAFGLKLRKVPK-----DEIDERVREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 437 ---IEAKQQIYRIVRELaaeGKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:cd03301 164 klrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-227 |
9.34e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.40 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRaaELGVraVYQ--ELSLVeG 102
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK--HIGI--VFQnpDNQFV-G 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 103 LTVAENLCLGQwprRNGMIDYLQMAQDAQRCLQALGV----DVSPEqlvsTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:PRK13648 99 SIVKYDVAFGL---ENHAVPYDEMHRRVSEALKQVDMleraDYEPN----ALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 179 SLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRiASCATVMRDGQV 227
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-228 |
1.10e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 73.42 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 21 PGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegDEATLT--RRAaeLGVraVYQELS 98
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDslRRA--IGV--VPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGlTVAENLCLGQWPRRN-GMIDYLQMAQDAQRCLQalgvdvSPEQLVST-------LSPAQKQLVEIARVMKGEPRV 170
Cdd:cd03253 86 LFND-TIGYNIRYGRPDATDeEVIEAAKAAQIHDKIMR------FPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 171 VILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQVA 228
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
265-480 |
1.16e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRAL----RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR-PdygdMLKR-- 337
Cdd:COG1137 2 MTLEAENLvksyGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlP----MHKRar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 338 -GIGYTPEnrkEAGIIPWLGVDENtvltnrqkISAngVLQwstIRRLTEEVMQRmtvKAAS----------SETPIGTLS 406
Cdd:COG1137 78 lGIGYLPQ---EASIFRKLTVEDN--------ILA--VLE---LRKLSKKEREE---RLEElleefgithlRKSKAYSLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 407 GGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEG 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-207 |
1.31e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.30 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGET---RLEGDEATLTRRAaELGVraVYQELSL 99
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDADALAQLRRE-HFGF--IFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 VEGLTVAENLclgQWPRRNGMIDYLQMAQDAQRCLQALG----VDVSPEQLvstlSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK10535 98 LSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGledrVEYQPSQL----SGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190
....*....|....*....|....*....|..
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
275-485 |
1.31e-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: 71.96 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpDYGDMLkrgigytpenrkeagiipw 354
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKAL------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 lgvdentvltnRQKISangVLQwstirrlteevmQRMTVKAASSETPIGT-LSGGNQQKVVIGRWVYAASQILLLDEPTR 433
Cdd:cd03247 74 -----------SSLIS---VLN------------QRPYLFDTTLRNNLGRrFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 434 GVDIEAKQQIYRIVRElAAEGKSVVFISSEVEELPLVcDRILLLQHGTFSQE 485
Cdd:cd03247 128 GLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-225 |
1.38e-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: 76.98 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVV--ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDiwigetrlegdeATLTRRAAELGVRAVYQ 95
Cdd:TIGR01257 1945 KVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD------------ATVAGKSILTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGLTVAENLCLGQ-----WPRRNGmIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRV 170
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGRehlylYARLRG-VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 171 VILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDG 225
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-228 |
1.41e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.62 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEAT--LTRRAaelgVRAVYQE--L 97
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKADPEAqkLLRQK----IQIVFQNpyG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SL-----VeGLTVAENLclgqwprrngMIDY-LQMAQDAQRCLQALG-VDVSPEQ---LVSTLSPAQKQLVEIARVMKGE 167
Cdd:PRK11308 104 SLnprkkV-GQILEEPL----------LINTsLSAAERREKALAMMAkVGLRPEHydrYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 168 PRVVILDEPTSSL---ASAEV-ELVISAVKKMsalGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:PRK11308 173 PDVVVADEPVSALdvsVQAQVlNLMMDLQQEL---GLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
265-480 |
1.81e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRALRHK-------PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmLKR 337
Cdd:PRK13650 3 NIIEVKNLTFKykedqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 338 GIGY---TPENRkeagiipWLGVdenTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVV 414
Cdd:PRK13650 82 KIGMvfqNPDNQ-------FVGA---TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREP-ARLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 415 IGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLvCDRILLLQHG 480
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVAL-SDRVLVMKNG 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-227 |
1.85e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 10 VAKVVAGN--KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETrlegDEATLTRRA-A 86
Cdd:PRK10895 1 MATLTAKNlaKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE----DISLLPLHArA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 87 ELGVRAVYQELSLVEGLTVAENLCLGQWPRRNgmIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKG 166
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDD--LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 167 EPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
275-480 |
2.03e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKItrpDYGdmlKRG----------IGYTPE 344
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYS---KRGllalrqqvatVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 345 NRkeagiIPWLGVDENTVLTNRQKisanGVLQWSTIRRLTEEvmqrMTVKAASS--ETPIGTLSGGNQQKVVIGRWVYAA 422
Cdd:PRK13638 88 QQ-----IFYTDIDSDIAFSLRNL----GVPEAEITRRVDEA----LTLVDAQHfrHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQG 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
278-485 |
2.76e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.69 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpdygdMLKRGIGYTPENRKEA-------- 349
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTIN------LVRDKDGQLKVADKNQlrllrtrl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 350 -------GIIPWLGVDENTVLTNRQKISangvLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAA 422
Cdd:PRK10619 95 tmvfqhfNLWSHMTVLENVMEAPIQVLG----LSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
275-481 |
2.80e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.16 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpDYGDMLKrgigytpENRKEAGII-- 352
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVKLS-------DIRKKVGLVfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 -PWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQ--RMTVKAASSETPIgTLSGGNQQKVVIGRWVYAASQILLLD 429
Cdd:PRK13637 91 yPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPF-ELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 430 EPTRGVDIEAKQQIYRIVRELAAEGK-SVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-228 |
3.05e-14 |
|
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: 71.76 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLI----RMLTgserPDSGDIWIGETRLegdeatltrraAELGVRAVY 94
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILIDGVDI-----------SKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLV-------EGlTVAENLC-LGQWPrrNGMI-DYLQMAQDAQRCLQ---ALGVDVSPEQlvSTLSPAQKQLVEIAR 162
Cdd:cd03244 78 SRISIIpqdpvlfSG-TIRSNLDpFGEYS--DEELwQALERVGLKEFVESlpgGLDTVVEEGG--ENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 163 VMKGEPRVVILDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEI---RRIAscatVMRDGQVA 228
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTIidsDRIL----VLDKGRVV 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
275-480 |
3.12e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpDYGD-MLKRGIGY------TPENRK 347
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS--MLSSrQLARRLALlpqhhlTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 348 -----EAGIIPWLgvdentvlTNRQKISANGvlqwstiRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAA 422
Cdd:PRK11231 93 vrelvAYGRSPWL--------SLWGRLSAED-------NARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-480 |
3.31e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.39 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpdYGDMLKRGIGYtpENRKEAGII-- 352
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLY---FGKDIFQIDAI--KLRKEVGMVfq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 -----PWLGVDENTVLtnrqKISANGVLQWSTIRRLTEEVMQRMTVKAASSE---TPIGTLSGGNQQKVVIGRWVYAASQ 424
Cdd:PRK14246 98 qpnpfPHLSIYDNIAY----PLKSHGIKEKREIKKIVEECLRKVGLWKEVYDrlnSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 425 ILLLDEPTRGVDIEAKQQIYRIVRELAAEgKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
264-481 |
3.40e-14 |
|
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: 74.78 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 264 QAVLEVRAL------RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDyGDMLKR 337
Cdd:COG4618 328 KGRLSVENLtvvppgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD-REELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 338 GIGYTPENrkeagiipwlgVD--ENTVltnRQKISangvlqwstirRLTEEVMQRMtVKAASS--------------ETP 401
Cdd:COG4618 407 HIGYLPQD-----------VElfDGTI---AENIA-----------RFGDADPEKV-VAAAKLagvhemilrlpdgyDTR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 402 IG----TLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPlVCDRILLL 477
Cdd:COG4618 461 IGeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVL 539
|
....
gi 1314860479 478 QHGT 481
Cdd:COG4618 540 RDGR 543
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
276-480 |
3.83e-14 |
|
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: 71.28 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT--RPDYGDMLKRGIGYTPENRKeagIIP 353
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlRGRAIPYLRRKIGVVFQDFR---LLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 WLGVDENTVLTNRqkISANGVLQWstiRRLTEEVMQRMTVKAASSETPIGtLSGGNQQKVVIGRWVYAASQILLLDEPTR 433
Cdd:cd03292 92 DRNVYENVAFALE--VTGVPPREI---RKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314860479 434 GVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-207 |
3.95e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 27 DNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGETRLEGDEAtltrRAAEL-------GVRAVyqels 98
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlWQGEPIRRQRDE----YHQDLlylghqpGIKTE----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 lvegLTVAENLclgQWprrngmidYLQMAQ--DAQRCLQAL------GV-DVspeqLVSTLSPAQKQLVEIARVMKGEPR 169
Cdd:PRK13538 89 ----LTALENL---RF--------YQRLHGpgDDEALWEALaqvglaGFeDV----PVRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1314860479 170 VVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-230 |
3.97e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVV-ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WI------------GETRLEGDEATLT 82
Cdd:PRK13651 13 NKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkdeknkkktkeKEKVLEKLVIQKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 83 RR-----AAELGVR--AVYQ--ELSLVEGlTVAENLCLGqwPRRNGMiDYLQMAQDAQRCLQALGVDV-----SPEQlvs 148
Cdd:PRK13651 93 RFkkikkIKEIRRRvgVVFQfaEYQLFEQ-TIEKDIIFG--PVSMGV-SKEEAKKRAAKYIELVGLDEsylqrSPFE--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 149 tLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVA 228
Cdd:PRK13651 166 -LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
..
gi 1314860479 229 GD 230
Cdd:PRK13651 245 KD 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
266-485 |
4.11e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRALRH-----KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygdmlkrgig 340
Cdd:PRK13652 3 LIETRDLCYsysgsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 yTPENRKEAGIIPWLGVDENTVLTNRQKIS---ANGVLQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGR 417
Cdd:PRK13652 73 -IREVRKFVGLVFQNPDDQIFSPTVEQDIAfgpINLGLDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 418 WVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
276-484 |
4.32e-14 |
|
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: 75.33 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEkitrpdygdmlkrgIGYTPEnrkeagiIPWL 355
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQ-------TSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 ---GVDENTVLtnrqKISANGVLQWSTIR--RLTEEVmqrmTVKAASSETPIG----TLSGGNQQKVVIGRWVYAASQIL 426
Cdd:TIGR01271 499 mpgTIKDNIIF----GLSYDEYRYTSVIKacQLEEDI----ALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 427 LLDEPTRGVDIEAKQQIY-RIVRELAAEgKSVVFISSEVEELPLVcDRILLLQ------HGTFSQ 484
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFeSCLCKLMSN-KTRILVTSKLEHLKKA-DKILLLHegvcyfYGTFSE 633
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
247-498 |
4.32e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 247 GRDHVDIAPVAPQEIVDQAvLEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYeQGEIVINGEKI 326
Cdd:PRK11174 336 QQGEKELASNDPVTIEAED-LEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIEL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 327 TRPDYGDMLKRgigytpenrkeagiIPWLG---------VDENTVLTNRQkisangvlqwstirrLTEEVMQRMTVKAAS 397
Cdd:PRK11174 414 RELDPESWRKH--------------LSWVGqnpqlphgtLRDNVLLGNPD---------------ASDEQLQQALENAWV 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 398 SE----------TPIG----TLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRElAAEGKSVVFISSE 463
Cdd:PRK11174 465 SEflpllpqgldTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQ 543
|
250 260 270
....*....|....*....|....*....|....*
gi 1314860479 464 VEELpLVCDRILLLQHGTFSQEFHapvnVDELMSA 498
Cdd:PRK11174 544 LEDL-AQWDQIWVMQDGQIVQQGD----YAELSQA 573
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
17-207 |
4.49e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.40 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETrlegdeatltrraaelgVRAVYqe 96
Cdd:cd03221 7 SKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------------VKIGY-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 lslvegltvaenlclgqwprrngmidylqmaqdaqrclqalgvdvspeqlVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:cd03221 68 --------------------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 1314860479 177 TSSLASAEVELVISAVKKMSAlgvAVIYVSH 207
Cdd:cd03221 98 TNHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
272-497 |
4.58e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.40 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 272 LRHKPKL----EDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMlkrgigytpenRK 347
Cdd:PLN03232 1242 LRYRPGLppvlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL-----------RR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 348 EAGIIPWLGV-DENTVLTNRQKISA-NGVLQWstirrlteEVMQRMTVKAASSETPIG----------TLSGGNQQKVVI 415
Cdd:PLN03232 1311 VLSIIPQSPVlFSGTVRFNIDPFSEhNDADLW--------EALERAHIKDVIDRNPFGldaevseggeNFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 416 GRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRElaaEGKS--VVFISSEVEELpLVCDRILLLQHGTFsQEFHAPvnvD 493
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIRE---EFKSctMLVIAHRLNTI-IDCDKILVLSSGQV-LEYDSP---Q 1454
|
....
gi 1314860479 494 ELMS 497
Cdd:PLN03232 1455 ELLS 1458
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-241 |
4.97e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRML------------TGSERPDSGDIWIGETrlegDEATLTRraaELGVra 92
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRT----DTVDLRK---EIGM-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 93 VYQELSLVEgLTVAENLCLGQwpRRNGMIDYLQMAQDAQRCLQALGV-DVSPEQLVST---LSPAQKQLVEIARVMKGEP 168
Cdd:PRK14239 91 VFQQPNPFP-MSIYENVVYGL--RLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 169 RVVILDEPTSSL---ASAEVELVISAVKKMSALgvavIYVSHRMEEIRRIASCATVMRDGQvagdvMLENTSTHHI 241
Cdd:PRK14239 168 KIILLDEPTSALdpiSAGKIEETLLGLKDDYTM----LLVTRSMQQASRISDRTGFFLDGD-----LIEYNDTKQM 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
263-491 |
6.35e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.82 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 263 DQAVLEVRALRHK----PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR--PDygdmlK 336
Cdd:COG3842 2 AMPALELENVSKRygdvTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPE-----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 337 RGIGYTPENrkeAGIIPWLGVDENtV---LTNRqKISAngvlqwSTIRRLTEEVMQRmtVK-AASSETPIGTLSGGNQQK 412
Cdd:COG3842 77 RNVGMVFQD---YALFPHLTVAEN-VafgLRMR-GVPK------AEIRARVAELLEL--VGlEGLADRYPHQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 413 VVIGRWVYAASQILLLDEPTRGVDIEAKQQ----IYRIVRELaaeGKSVVFISSEVEELPLVCDRILLLQHGTFSQE--- 485
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEmreeLRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVgtp 220
|
....*....
gi 1314860479 486 ---FHAPVN 491
Cdd:COG3842 221 eeiYERPAT 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-207 |
7.00e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEG--DEAtltrRAAELGVRAVYQ 95
Cdd:TIGR03719 330 KAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAyvDQS----RDALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSlvEGLTVaenLCLG--QWPRRNGMIDYLQMAQDAQrclqalgvdvspeQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:TIGR03719 406 EIS--GGLDI---IKLGkrEIPSRAYVGRFNFKGSDQQ-------------KKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1314860479 174 DEPTSSLasaevelvisAVKKMSAL--------GVAVIyVSH 207
Cdd:TIGR03719 468 DEPTNDL----------DVETLRALeeallnfaGCAVV-ISH 498
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
280-481 |
7.67e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 70.60 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 280 DISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygdmlkrgigytPENR------KEAGIIP 353
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP------------PADRpvsmlfQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 WLGVDENTVLtnrqkisanGVlqwSTIRRLTEEvmQRMTVKAASSETPI--------GTLSGGNQQKVVIGRWVYAASQI 425
Cdd:cd03298 84 HLTVEQNVGL---------GL---SPGLKLTAE--DRQAIEVALARVGLaglekrlpGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 426 LLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
266-480 |
9.47e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.79 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDyGDMLKRgigy 341
Cdd:COG1126 1 MIEIENLHksfgDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK-KDINKL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 tpenRKEAGII-------PWLGVDENTVLTNRQkisangVLQWST--IRRLTEEVMQR--MTVKAASSetPiGTLSGGNQ 410
Cdd:COG1126 76 ----RRKVGMVfqqfnlfPHLTVLENVTLAPIK------VKKMSKaeAEERAMELLERvgLADKADAY--P-AQLSGGQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 411 QKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVE---ElplVCDRILLLQHG 480
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGfarE---VADRVVFMDGG 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
275-480 |
9.55e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.58 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgIGY---TPENRkeagi 351
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ-VGMvfqNPDNQ----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 ipWLG--VDENTV--LTNrqkisaNGVLQWSTIRRLTEEVMQ-RMTVKAasSETPiGTLSGGNQQKVVIGRWVYAASQIL 426
Cdd:PRK13635 94 --FVGatVQDDVAfgLEN------IGVPREEMVERVDQALRQvGMEDFL--NREP-HRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 427 LLDEPTRGVDIEAKQQIYRIVRELAAEGK-SVVFISSEVEElPLVCDRILLLQHG 480
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDE-AAQADRVIVMNKG 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
274-480 |
9.72e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.18 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 274 HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygDMLKrgigytpENRKEAGII- 352
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK----ENLK-------EIRKKIGIIf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 --P---WLGVdenTV-------LTNRQkisangvLQWSTIRRLTEEVMQRMTVKAASSETPIgTLSGGNQQKVVIGRWVY 420
Cdd:PRK13632 90 qnPdnqFIGA---TVeddiafgLENKK-------VPPKKMKDIIDDLAKKVGMEDYLDKEPQ-NLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 421 AASQILLLDEPTRGVDIEAKQQIYRIVRELAAEG-KSVVFISSEVEELpLVCDRILLLQHG 480
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEA-ILADKVIVFSEG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
278-481 |
1.24e-13 |
|
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: 70.38 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYE---QGEIVINGEKITRpdygDMLKRGIGYTPENRKeagIIPW 354
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP----DQFQKCVAYVRQDDI---LLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTNrqkISANGVLQWSTIRRLTEEVMqrmtVKAASSETPIG-----TLSGGNQQKVVIGRWVYAASQILLLD 429
Cdd:cd03234 96 LTVRETLTYTA---ILRLPRKSSDAIRKKRVEDV----LLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 430 EPTRGVDIEAKQQIYRIVRELAAEGKsVVFIS-----SEVEELplvCDRILLLQHGT 481
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNR-IVILTihqprSDLFRL---FDRILLLSSGE 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
266-484 |
1.37e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.18 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRALRH----KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR-PDYgdmlKRGIG 340
Cdd:PRK11607 19 LLEIRNLTKsfdgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPY----QRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 YTPENRkeaGIIPWLGVDENTVLTNRQKISANGvlqwsTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVY 420
Cdd:PRK11607 95 MMFQSY---ALFPHMTVEQNIAFGLKQDKLPKA-----EIASRVNEMLGLVHMQEFAKRKP-HQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 421 AASQILLLDEPTRGVDIEAKQQI-YRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-227 |
1.39e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKST----LIRMLtgserPDSGDIWIGETRLEgdeaTLTRRAAeLGVR----AVYQ 95
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLH----NLNRRQL-LPVRhriqVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 E--LSLVEGLTV----AENLCLGQwprrngmiDYLQMAQDAQRCLQALG-VDVSPE---QLVSTLSPAQKQLVEIARVMK 165
Cdd:PRK15134 370 DpnSSLNPRLNVlqiiEEGLRVHQ--------PTLSAAQREQQVIAVMEeVGLDPEtrhRYPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 166 GEPRVVILDEPTSSLASAEVELVISAVKKMSAL-GVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
267-480 |
1.65e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 69.36 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKPK-LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMlkrgigytpen 345
Cdd:cd03369 12 LSVRYAPDLPPvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 346 RKEAGIIPwlgvDENTVLTNRQKISANGVLQWStirrlTEEVMQRMTVKAASSetpigTLSGGNQQKVVIGRWVYAASQI 425
Cdd:cd03369 81 RSSLTIIP----QDPTLFSGTIRSNLDPFDEYS-----DEEIYGALRVSEGGL-----NLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 426 LLLDEPTRGVDIEAKQQIYRIVRELAAeGKSVVFISSEVEELpLVCDRILLLQHG 480
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTI-IDYDKILVMDAG 199
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
278-481 |
1.76e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.65 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKItrpDYGdmlKRGIgytPENRKEAGIIpwLGV 357
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI---DYS---RKGL---MKLRESVGMV--FQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTNR--QKIS---ANGVLQWSTIRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:PRK13636 91 PDNQLFSASvyQDVSfgaVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 433 RGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-207 |
1.78e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.80 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVV-ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEatltrrAAELGVRAVYQE 96
Cdd:PRK11650 11 KSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE------PADRDIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQRCLQaLG--VDVSPEQlvstLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK11650 85 YALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILE-LEplLDRKPRE----LSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190
....*....|....*....|....*....|....
gi 1314860479 175 EPTSSL-ASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:PRK11650 160 EPLSNLdAKLRVQMRLEIQRLHRRLKTTSLYVTH 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
256-480 |
2.08e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 256 VAPQEIVDQAVLEVRALRHK---------PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQG-----EIVI 321
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYCVfdekqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 322 NGEKITRPDYGDMLKRGIGYTPENRKEAGII---PWLGVDENTVltnRQKIS----ANGVLQwSTIRRLTEEVMQRMTVK 394
Cdd:PRK13631 91 GDKKNNHELITNPYSKKIKNFKELRRRVSMVfqfPEYQLFKDTI---EKDIMfgpvALGVKK-SEAKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 395 AASSE-TPIGtLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDR 473
Cdd:PRK13631 167 DSYLErSPFG-LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADE 245
|
....*..
gi 1314860479 474 ILLLQHG 480
Cdd:PRK13631 246 VIVMDKG 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
278-480 |
2.68e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygdMLKRGIgytPENRKEAGIIpwlgV 357
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITR-----LKNREV---PFLRRQIGMI----F 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTNR---QKISANGVLQWST---IRRLTEEVMQRMTVKAASSETPIgTLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:PRK10908 86 QDHHLLMDRtvyDNVAIPLIIAGASgddIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
275-489 |
3.26e-13 |
|
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: 68.67 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMlkrgigytpenRKEAGIIPw 354
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-----------RSRISIIP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 lgvdENTVL---TNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASS--ETPI----GTLSGGNQQKVVIGRWVYAASQI 425
Cdd:cd03244 85 ----QDPVLfsgTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGglDTVVeeggENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 426 LLLDEPTRGVDIEAKQQIYRIVRElAAEGKSVVFISSEVEELpLVCDRILLLQHGTFsQEFHAP 489
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTI-IDSDRILVLDKGRV-VEFDSP 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
26-208 |
3.29e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAvyqelSLVEGLTV 105
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRS-----GINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 AENlCLgqwprrngmidylqmaQDAQRCLQALGVD-----VSPEQLVS----TLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:PRK13540 92 REN-CL----------------YDIHFSPGAVGITelcrlFSLEHLIDypcgLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 1314860479 177 TSSLASAEVELVISAVKKMSALGVAVIYVSHR 208
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
235-485 |
3.57e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 235 NTSTHHIVSLMLGRDHV-----DIAPVAPQEIVDQAVLEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIV 309
Cdd:PLN03232 585 NVSLQRIEELLLSEERIlaqnpPLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 310 G-LEEYEQGEIVINGEkitrpdygdmlkrgIGYTPEnrkeagiIPWL---GVDENTVLTNRQKISANGvlqwstiRRLTE 385
Cdd:PLN03232 665 GeLSHAETSSVVIRGS--------------VAYVPQ-------VSWIfnaTVRENILFGSDFESERYW-------RAIDV 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 386 EVMQR-MTVKAASSETPIG----TLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFI 460
Cdd:PLN03232 717 TALQHdLDLLPGRDLTEIGergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLV 796
|
250 260
....*....|....*....|....*
gi 1314860479 461 SSEVEELPLVcDRILLLQHGTFSQE 485
Cdd:PLN03232 797 TNQLHFLPLM-DRIILVSEGMIKEE 820
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
276-484 |
3.99e-13 |
|
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: 69.89 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEkitrpdygdmlkrgIGYTPENrkeAGIIPWL 355
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQF---SWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 gVDENTVLtnrqKISANGVLQWSTIRRLTEEvmQRMTVKAASSETPIG----TLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:cd03291 114 -IKENIIF----GVSYDEYRYKSVVKACQLE--EDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 432 TRGVDIEAKQQIY-RIVRELAAEgKSVVFISSEVEELPlVCDRILLLQ------HGTFSQ 484
Cdd:cd03291 187 FGYLDVFTEKEIFeSCVCKLMAN-KTRILVTSKMEHLK-KADKILILHegssyfYGTFSE 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-468 |
4.85e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 30 NFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGdiwigetRLEGDEATLTRRAAELGVRAVYQE--------LSLVE 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG-------ERQSQFSHITRLSFEQLQKLVSDEwqrnntdmLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 ---GLTVAEnlclgqwprrngMIdyLQMAQDAQRCLQ---ALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK10938 96 ddtGRTTAE------------II--QDEVKDPARCEQlaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQvagdvMLENTSTHHIVS------LMLGRD 249
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCT-----LAETGEREEILQqalvaqLAHSEQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 250 HVDIA---PVAPQEIV----DQAVLEvraLRH-------KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGleEYE 315
Cdd:PRK10938 237 LEGVQlpePDEPSARHalpaNEPRIV---LNNgvvsyndRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 316 QG---EIVI------NGEKITRpdygdmLKRGIGY-------------TPENRKEAGIIPWLGVDENTvlTNRQKISANg 373
Cdd:PRK10938 312 QGysnDLTLfgrrrgSGETIWD------IKKHIGYvssslhldyrvstSVRNVILSGFFDSIGIYQAV--SDRQQKLAQ- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 374 vlQWSTIRRLTEEVmqrmtvkaasSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE 453
Cdd:PRK10938 383 --QWLDILGIDKRT----------ADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISE 450
|
490
....*....|....*.
gi 1314860479 454 GKS-VVFISSEVEELP 468
Cdd:PRK10938 451 GETqLLFVSHHAEDAP 466
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
266-480 |
5.49e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.34 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRALRHK-PK----LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKItRPDYGDMLKRgig 340
Cdd:PRK13639 1 ILETRDLKYSyPDgteaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 ytpenRKEAGIIPWLGVDENTVLTNRQKIS---ANGVLQWSTIRRLTEEVMQRMTVKAaSSETPIGTLSGGNQQKVVIGR 417
Cdd:PRK13639 77 -----RKTVGIVFQNPDDQLFAPTVEEDVAfgpLNLGLSKEEVEKRVKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 418 WVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
267-480 |
5.86e-13 |
|
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: 68.36 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKPK----LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQ-----GEIVINGEKITRPDYGDMlkr 337
Cdd:cd03260 1 IELRDLNVYYGdkhaLKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 338 gigytpENRKEAGII---P---WLGVDENTVLTNRqkisANGVLQWSTIRRLTEEVMQRMTVKA-ASSETPIGTLSGGNQ 410
Cdd:cd03260 78 ------ELRRRVGMVfqkPnpfPGSIYDNVAYGLR----LHGIKLKEELDERVEEALRKAALWDeVKDRLHALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 411 QKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEgKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
275-480 |
6.13e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.96 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygdmlkrgigYTPEN-RKEAGIIP 353
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD------------LTLESlRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 wlgvdENTVLTNRqkisangvlqwsTIR---RL-----TEEVMQRMTVKAASSE----------TPIG----TLSGGNQQ 411
Cdd:COG1132 421 -----QDTFLFSG------------TIReniRYgrpdaTDEEVEEAAKAAQAHEfiealpdgydTVVGergvNLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 412 KVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAeGKSVVFIS---SEVEElplvCDRILLLQHG 480
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAhrlSTIRN----ADRILVLDDG 550
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-227 |
6.18e-13 |
|
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: 66.95 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRaaelgVRAVYQELSLVEGl 103
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL-----ISVLNQRPYLFDT- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLclgqwPRRngmidylqmaqdaqrclqalgvdvspeqlvstLSPAQKQLVEIARVMKGEPRVVILDEPTSSL--- 180
Cdd:cd03247 90 TLRNNL-----GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLdpi 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 181 -ASAEVELVISAVKkmsalGVAVIYVSHR---MEEIRRIascaTVMRDGQV 227
Cdd:cd03247 133 tERQLLSLIFEVLK-----DKTLIWITHHltgIEHMDKI----LFLENGKI 174
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
276-481 |
6.27e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 68.23 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEK----ITRPDYGDML---KRGIGYT------ 342
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPREILalrRRTIGYVsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 343 -PenRKEAGII---PWL--GVDEntvltnrqkisangvlqwSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIG 416
Cdd:COG4778 105 iP--RVSALDVvaePLLerGVDR------------------EEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 417 RWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-227 |
6.54e-13 |
|
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: 70.87 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSErPDSGDIWIGETRLEG-DEATLTRRAAELGVraVYQE 96
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGlSRRALRPLRRRMQV--VFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 ----LS--------LVEGLTVaenlclgQWPRRNGmidylqmAQDAQRCLQALgVDVSpeqlvstLSPA----------- 153
Cdd:COG4172 371 pfgsLSprmtvgqiIAEGLRV-------HGPGLSA-------AERRARVAEAL-EEVG-------LDPAarhryphefsg 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 154 -QKQLVEIARVMKGEPRVVILDEPTSSL-AS--AEV-ELVISAVKKmsaLGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:COG4172 429 gQRQRIAIARALILEPKLLVLDEPTSALdVSvqAQIlDLLRDLQRE---HGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-254 |
6.68e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEG-----DEATLTRRaaelgvravyqeL 97
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-----RVLGyvpfkRRKEFARR------------I 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEG--------LTVAENLCLgqwprrNGMIDYLQMAQDAQR---CLQALGVDvspEQL---VSTLSPAQKqlveiarv 163
Cdd:COG4586 98 GVVFGqrsqlwwdLPAIDSFRL------LKAIYRIPDAEYKKRldeLVELLDLG---ELLdtpVRQLSLGQR-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 164 MKGE--------PRVVILDEPTSSL-ASAEVElVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQVA--GDV 231
Cdd:COG4586 161 MRCElaaallhrPKILFLDEPTIGLdVVSKEA-IREFLKEYNReRGTTILLTSHDMDDIEALCDRVIVIDHGRIIydGSL 239
|
250 260
....*....|....*....|....*
gi 1314860479 232 --MLENTSTHHIVSLMLGRDHVDIA 254
Cdd:COG4586 240 eeLKERFGPYKTIVLELAEPVPPLE 264
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
275-469 |
7.52e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT--RPDYGDMLKRgIGYtpenrkEAGII 352
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdLCTYQKQLCF-VGH------RSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 PWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVmqrmtvkaassETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPT 432
Cdd:PRK13540 87 PYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLI-----------DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1314860479 433 RGVDIEAKQQIYRIVRELAAEGKSVVFISSevEELPL 469
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSH--QDLPL 190
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-228 |
8.36e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.44 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAaeLGVraVYQELSLVEGlT 104
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS--LTI--IPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 105 VAENLclgqwprrngmiDYLQMAQDAQrCLQALGVDVSPeqlvSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAE 184
Cdd:cd03369 98 IRSNL------------DPFDEYSDEE-IYGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314860479 185 VELvISAVKKMSALGVAVIYVSHRmeeIRRIASCAT--VMRDGQVA 228
Cdd:cd03369 161 DAL-IQKTIREEFTNSTILTIAHR---LRTIIDYDKilVMDAGEVK 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-227 |
8.58e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.99 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQ--ELSLVEG 102
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 103 lTVAENLCLGqwPRRNGmIDYLQMAQDAQRCLQALGVDVSP-EQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSL- 180
Cdd:PRK13643 101 -TVLKDVAFG--PQNFG-IPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLd 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314860479 181 ASAEVELvISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13643 177 PKARIEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-227 |
1.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQ--ELSLVEG 102
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 103 lTVAENLCLGqwPRRNGmIDYLQMAQDAQRCLQALGVDvspEQLVST----LSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:PRK13649 102 -TVLKDVAFG--PQNFG-VSQEEAEALAREKLALVGIS---ESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 179 SLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-178 |
1.11e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEAtlTRRaaelgvRAVY--QELSLV 100
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQPVDAGDIA--TRR------RVGYmsQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGLTVAENLCL---------GQWPRRngmidylqMAQDAQRC-LQALgVDVSPEQlvstLSPAQKQLVEIARVMKGEPRV 170
Cdd:NF033858 352 GELTVRQNLELharlfhlpaAEIAAR--------VAEMLERFdLADV-ADALPDS----LPLGIRQRLSLAVAVIHKPEL 418
|
....*...
gi 1314860479 171 VILDEPTS 178
Cdd:NF033858 419 LILDEPTS 426
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
278-479 |
1.20e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGeivingeKITRPDygdmlKRGIGYTPENrkeagiipwLGV 357
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------VIKRNG-----KLRIGYVPQK---------LYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTnrqkISANGVLQWSTIRRLTEEVMQRmtVKAAS-SETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVD 436
Cdd:PRK09544 79 DTTLPLT----VNRFLRLRPGTKKEDILPALKR--VQAGHlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314860479 437 IEAKQQIYRIVRELAAEGKSVVFISSevEELPLV---CDRILLLQH 479
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVS--HDLHLVmakTDEVLCLNH 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-227 |
1.41e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGD-----EATLTRRaaELGVRAVYQELSL 99
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikEVKRLRK--EIGLVFQFPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 VEGlTVAENLCLGQwprrngmIDYLQMAQDAQRCLQALGVDVS-PEQLVS----TLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK13645 104 FQE-TIEKDIAFGP-------VNLGENKQEAYKKVPELLKLVQlPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-207 |
1.53e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 66.91 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPD---SGDIWI-GETRlegDEATLTRRAAElgvraVYQELSLVE 101
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFnGQPR---KPDQFQKCVAY-----VRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GLTVAENL-----CLGQWPRRNGMIDylqmAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:cd03234 95 GLTVRETLtytaiLRLPRKSSDAIRK----KRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|.
gi 1314860479 177 TSSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
246-480 |
1.69e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 246 LGRDHVDIaPVAPQEIVDQAVLEVRALRhKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYE---QGEIVIN 322
Cdd:TIGR00955 11 FGRVAQDG-SWKQLVSRLRGCFCRERPR-KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 323 GEKITRpdygDMLKRGIGYTpenRKEAGIIPWLGVDENTVLTNRQKISANgvLQWSTIRRLTEEVMQRMTVKAAsSETPI 402
Cdd:TIGR00955 89 GMPIDA----KEMRAISAYV---QQDDLFIPTLTVREHLMFQAHLRMPRR--VTKKEKRERVDEVLQALGLRKC-ANTRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 403 GT------LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFI----SSEVEELplvCD 472
Cdd:TIGR00955 159 GVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFEL---FD 235
|
....*...
gi 1314860479 473 RILLLQHG 480
Cdd:TIGR00955 236 KIILMAEG 243
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-233 |
2.46e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.07 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYP-GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATL-TRRAAELGVRAVYQE 96
Cdd:PRK13647 13 RYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV-----KVMGREVNAeNEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LS-LVEGLTVAENLCLGqwPRRNGMiDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK13647 88 PDdQVFSSTVWDDVAFG--PVNMGL-DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV--AGDVML 233
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVlaEGDKSL 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
270-481 |
3.06e-12 |
|
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: 66.20 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 270 RALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEkitRP-DYGDMLKRGIGYTPENRKE 348
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPwKRRKKFLRRIGVVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 349 agiIPW--------------LGVDENTVLTNRQKISAngVLQwstirrLTEEVmqrmtvkaassETPIGTLSGGNQQKVV 414
Cdd:cd03267 106 ---LWWdlpvidsfyllaaiYDLPPARFKKRLDELSE--LLD------LEELL-----------DTPVRQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 415 IGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISS----EVEELplvCDRILLLQHGT 481
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTShymkDIEAL---ARRVLVIDKGR 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-208 |
4.09e-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: 68.16 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG-VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEATLTRRaaelgVRAVYQE 96
Cdd:TIGR02868 343 GYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdGVPVSSLDQDEVRRR-----VSVCAQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVeGLTVAENLCLGQwP-----------RRNGMIDYLQMAQDaqrclqalGVDVSPEQLVSTLSPAQKQLVEIARVMK 165
Cdd:TIGR02868 418 AHLF-DTTVRENLRLAR-PdatdeelwaalERVGLADWLRALPD--------GLDTVLGEGGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314860479 166 GEPRVVILDEPTSSL-ASAEVELVISAVKKMSalGVAVIYVSHR 208
Cdd:TIGR02868 488 ADAPILLLDEPTEHLdAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-476 |
4.20e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIgetrLEGDEATLTRRAAE----------L 88
Cdd:NF033858 10 RYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV----LGGDMADARHRRAVcpriaympqgL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 89 GvRAVYQELSlvegltVAENL----CL-GQWPR-RNGMIDYLqmaqdaqrcLQALGVDVSPEQLVSTLSPAQKQ------ 156
Cdd:NF033858 86 G-KNLYPTLS------VFENLdffgRLfGQDAAeRRRRIDEL---------LRATGLAPFADRPAGKLSGGMKQklglcc 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 157 -LVEiarvmkgEPRVVILDEPTSS---LASAEV-ELvISAVKK----MSALgVAVIYvshrMEEIRRIASCAtVMRDGQV 227
Cdd:NF033858 150 aLIH-------DPDLLILDEPTTGvdpLSRRQFwEL-IDRIRAerpgMSVL-VATAY----MEEAERFDWLV-AMDAGRV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 228 --AG--DVMLENTSTHHI----VSLM---LGRDH--VDIAPVAPQEIvDQAVLEVRALRHK----PKLEDISFTLRRGEV 290
Cdd:NF033858 216 laTGtpAELLARTGADTLeaafIALLpeeKRRGHqpVVIPPRPADDD-DEPAIEARGLTMRfgdfTAVDHVSFRIRRGEI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 291 LGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKItrpDYGDM-LKRGIGYTP-------EnrkeagiipwLGVDENTV 362
Cdd:NF033858 295 FGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIaTRRRVGYMSqafslygE----------LTVRQNLE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 363 LTNRQ-KISANgvlqwsTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKV-----VIGRwvyaaSQILLLDEPTRGVD 436
Cdd:NF033858 362 LHARLfHLPAA------EIAARVAEMLERFDLADVADALP-DSLPLGIRQRLslavaVIHK-----PELLILDEPTSGVD 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1314860479 437 IEAKQQIYRIVRELAAEGKSVVFIS----SEVEElplvCDRILL 476
Cdd:NF033858 430 PVARDMFWRLLIELSREDGVTIFISthfmNEAER----CDRISL 469
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-227 |
4.47e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRL-EGDEATLtrRAAelgVRAVYQ 95
Cdd:PRK11160 347 TYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIaDYSEAAL--RQA---ISVVSQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENLCLGQwPRrngmidylqmAQDAQrcLQALGVDVSPEQLVST--------------LSPAQKQLVEIA 161
Cdd:PRK11160 422 RVHLFSA-TLRDNLLLAA-PN----------ASDEA--LIEVLQQVGLEKLLEDdkglnawlgeggrqLSGGEQRRLGIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 162 RVMKGEPRVVILDEPTSSLaSAEVELVISAVKKMSALGVAVIYVSHR---MEEIRRIAscatVMRDGQV 227
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGL-DAETERQILELLAEHAQNKTVLMITHRltgLEQFDRIC----VMDNGQI 551
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
254-461 |
4.83e-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: 68.16 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 254 APVAPQEIVDQAVLEVRALRHK-----PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR 328
Cdd:TIGR02868 322 APAAGAVGLGKPTLELRDLSAGypgapPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 329 PDyGDMLKRGIGYTPENRKeagiipwlgVDENTVLTN-------------RQKISANGVLQWstIRRLTEEVMQRMTVKA 395
Cdd:TIGR02868 402 LD-QDEVRRRVSVCAQDAH---------LFDTTVRENlrlarpdatdeelWAALERVGLADW--LRALPDGLDTVLGEGG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 396 ASsetpigtLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRElAAEGKSVVFIS 461
Cdd:TIGR02868 470 AR-------LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLIT 527
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-72 |
4.93e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 4.93e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGET 72
Cdd:PRK11819 332 KSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET 386
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
275-485 |
5.03e-12 |
|
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: 65.71 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVING---EKITRpdygDMLKRGIGYTPENrkeagi 351
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISR----KSLRSMIGVVLQD------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 iPWL---GVDENTVLtNRQKISANGVLQWSTIRRLTEEVMQRmtvkAASSETPIG----TLSGGNQQKVVIGRWVYAASQ 424
Cdd:cd03254 86 -TFLfsgTIMENIRL-GRPNATDEEVIEAAKEAGAHDFIMKL----PNGYDTVLGenggNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 425 ILLLDEPTRGVDIEAKQQIYRIVRELaAEGKSVVFIS---SEVEElplvCDRILLLQHGTFSQE 485
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAhrlSTIKN----ADKILVLDDGKIIEE 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-227 |
5.37e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.27 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 7 AVPVAKVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAA 86
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 87 ELGVRA--VYQELSLVEgLTVAENLCLGQwpRRNGMIDYLQMAQDAQRCLQALGV-DVSPEQLVST---LSPAQKQLVEI 160
Cdd:PRK14271 98 EFRRRVgmLFQRPNPFP-MSIMDNVLAGV--RAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 161 ARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMsALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-216 |
5.52e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGE----TRLEGD-----EATLTRRAAElGVRAV--- 93
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivARLQQDpprnvEGTVYDFVAE-GIEEQaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 94 ---YQELSLVEGLTVAENLcLGQWPRRNGMIDYL---QMAQDAQRCLQALGVDvsPEQLVSTLSPAQKQLVEIARVMKGE 167
Cdd:PRK11147 98 lkrYHDISHLVETDPSEKN-LNELAKLQEQLDHHnlwQLENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 168 PRVVILDEPTSSLASAEVELVISAVKKMSAlgvAVIYVSHRMEEIRRIA 216
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHDRSFIRNMA 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
275-485 |
6.62e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygdmlkrgigYTPEnrkeagiipw 354
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST------------LKPE---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 lgvdentvlTNRQKIS--------------ANGVLQWStIRRLTEEvMQRMTVKAASSETP-------IGTLSGGNQQKV 413
Cdd:PRK10247 78 ---------IYRQQVSycaqtptlfgdtvyDNLIFPWQ-IRNQQPD-PAIFLDDLERFALPdtiltknIAELSGGEKQRI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 414 VIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINHADKVITLQPHAGEMQE 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
263-480 |
6.75e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 263 DQAVLEVRALRH----KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMlkrg 338
Cdd:PRK11701 3 DQPLLSVRGLTKlygpRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 339 igytPE-NRKEAGIIPWLGVDENTVLTNRQKISA----------NGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSG 407
Cdd:PRK11701 79 ----SEaERRRLLRTEWGFVHQHPRDGLRMQVSAggnigerlmaVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 408 GNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
278-480 |
6.78e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKrgigytpENRKEAGII---PW 354
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK-------PVRKKVGVVfqfPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:PRK13643 95 SQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314860479 435 VDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
277-485 |
7.19e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.88 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 277 KLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmLKRGIGYTPENRKEAGIIPWLG 356
Cdd:PRK13642 22 QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRKIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 357 VDENTVLTNRqkisanGVLQWSTIRRLTEEVMQRMTVKAASSETpiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVD 436
Cdd:PRK13642 101 DDVAFGMENQ------GIPREEMIKRVDEALLAVNMLDFKTREP--ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 437 IEAKQQIYRIVRELAAEGK-SVVFISSEVEElPLVCDRILLLQHGTFSQE 485
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQlTVLSITHDLDE-AASSDRILVMKAGEIIKE 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-256 |
9.34e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQELSLVEGL 103
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLCLGQWPRRNGMIDYLQMAQDAqrcLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLAS- 182
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDA---LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPl 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 183 AEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAG----DVMLENTSTHHIVSLMLGrdhVDIAPV 256
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQvgtpDEILNNPANDYVRTFFRG---VDISQV 273
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
268-480 |
1.04e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 66.25 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 268 EVRALRhkpkleDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDM--LKRGIGYTPE- 344
Cdd:COG1135 17 PVTALD------DVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraARRKIGMIFQh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 345 ----NRKeagiipwlgvdenTVLTN------RQKISAngvlqwSTIRRLTEEVMQR--MTVKAAS--SEtpigtLSGGNQ 410
Cdd:COG1135 91 fnllSSR-------------TVAENvalpleIAGVPK------AEIRKRVAELLELvgLSDKADAypSQ-----LSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 411 QKVVIGRwvyA-ASQ--ILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSE---VEElplVCDRILLLQHG 480
Cdd:COG1135 147 QRVGIAR---AlANNpkVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEmdvVRR---ICDRVAVLENG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
26-207 |
1.06e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetrlegdeatltRRAAELGVRAVYQELSL--VEGL 103
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------------KRNGKLRIGYVPQKLYLdtTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLCLGQWPRRNGMIDYLQMAQdAQRCLQAlgvdvsPEQlvsTLSPAQKQLVEIARVMKGEPRVVILDEPTSSL-AS 182
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDILPALKRVQ-AGHLIDA------PMQ---KLSGGETQRVLLARALLNRPQLLVLDEPTQGVdVN 154
|
170 180
....*....|....*....|....*..
gi 1314860479 183 AEVEL--VISAVKKmsALGVAVIYVSH 207
Cdd:PRK09544 155 GQVALydLIDQLRR--ELDCAVLMVSH 179
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
272-491 |
1.08e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.84 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 272 LRHKPKL----EDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMlkrgigytpenRK 347
Cdd:PLN03130 1245 LRYRPELppvlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL-----------RK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 348 EAGIIPWLGV-DENTVLTNRQKISA-NGVLQWSTIRRL-TEEVMQRMTVKAASSETPIG-TLSGGNQQKVVIGRWVYAAS 423
Cdd:PLN03130 1314 VLGIIPQAPVlFSGTVRFNLDPFNEhNDADLWESLERAhLKDVIRRNSLGLDAEVSEAGeNFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 424 QILLLDEPTRGVDIEAKQQIYRIVRElaaEGKS--VVFISSEVEELpLVCDRILLLQHGTFsQEFHAPVN 491
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIRE---EFKSctMLIIAHRLNTI-IDCDRILVLDAGRV-VEFDTPEN 1458
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
275-499 |
1.50e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.50 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPK----LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLkrgigytpENRKEAG 350
Cdd:PRK15079 30 PPKtlkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWR--------AVRSDIQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 351 II---------PWLGVDE---NTVLTNRQKISAngvlqwstirrltEEVMQRmtVKAASseTPIGTL-----------SG 407
Cdd:PRK15079 102 MIfqdplaslnPRMTIGEiiaEPLRTYHPKLSR-------------QEVKDR--VKAMM--LKVGLLpnlinryphefSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 408 GNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILL--LQH----G 480
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVmyLGHavelG 244
|
250 260
....*....|....*....|.
gi 1314860479 481 TFSQEFHAPVN--VDELMSAI 499
Cdd:PRK15079 245 TYDEVYHNPLHpyTKALMSAV 265
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
268-481 |
1.63e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.49 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 268 EVRALRhkpkleDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINgekitrpdygdmlkrgiGYTP-ENR 346
Cdd:COG4586 34 EVEAVD------DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----------------GYVPfKRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 347 KE-AGIIpwlGVdentVLTNRQ-------------------KISANGVLQwsTIRRLTE-----EVMQrmtvkaasseTP 401
Cdd:COG4586 91 KEfARRI---GV----VFGQRSqlwwdlpaidsfrllkaiyRIPDAEYKK--RLDELVElldlgELLD----------TP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 402 IGTLSGGNQQKVVIgrwvyAAS-----QILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISS----EVEELplvCD 472
Cdd:COG4586 152 VRQLSLGQRMRCEL-----AAAllhrpKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTShdmdDIEAL---CD 223
|
....*....
gi 1314860479 473 RILLLQHGT 481
Cdd:COG4586 224 RVIVIDHGR 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-216 |
1.75e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.29 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 20 YPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLI----RM--LTGSERPdSGDIWIGETRLEG---DEATLTRRaaelgV 90
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMndLIPGARV-EGEILLDGEDIYDpdvDVVELRRR-----V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 RAVYQE-----LSlvegltVAENLCLGqwPRRNGMIDYLQMAQDAQRCLQALGV--DVSP--EQLVSTLSPAQKQLVEIA 161
Cdd:COG1117 95 GMVFQKpnpfpKS------IYDNVAYG--LRLHGIKSKSELDEIVEESLRKAALwdEVKDrlKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 162 RVMKGEPRVVILDEPTSSL---ASAEVELVISAVKKmsalGVAVIYVSHRMEEIRRIA 216
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALdpiSTAKIEELILELKK----DYTIVIVTHNMQQAARVS 220
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-230 |
1.88e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRM----LTGSERPD----SGDIWI-GETRLEGDEATLTRRAAELGvravy 94
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRgarvTGDVTLnGEPLAAIDAPRLARLRAVLP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 95 QELSLVEGLTVAENLCLGQWP--RRNGMIDYlQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVM-------- 164
Cdd:PRK13547 90 QAAQPAFAFSAREIVLLGRYPhaRRAGALTH-RDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 165 -KGEPRVVILDEPTSSLASAEVELVISAVKKMS---ALGVAVIYvsHRMEEIRRIASCATVMRDGQVAGD 230
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLArdwNLGVLAIV--HDPNLAARHADRIAMLADGAIVAH 236
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-203 |
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 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLtgSERPDSGDIwIGETRLEGD--EATLTRRAAelgvrAVYQELSLVEGL 103
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVL--AGRKTAGVI-TGEILINGRplDKNFQRSTG-----YVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENLCLGQWPRrngmidylqmaqdaqrclqalgvdvspeqlvsTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASA 183
Cdd:cd03232 95 TVREALRFSALLR--------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|
gi 1314860479 184 EVELVISAVKKMSALGVAVI 203
Cdd:cd03232 143 AAYNIVRFLKKLADSGQAIL 162
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-236 |
2.24e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.09 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGsERPDSGDIWIGETRLEG-DEATLTRRAAEL-------GVRAVYQEL 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDwSAAELARHRAYLsqqqsppFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SL-VEGLTVAENLClgqwprrnGMIDYLqmaqdaqrcLQALGVDVSPEQLVSTLSPAQKQLVEIARVM-------KGEPR 169
Cdd:COG4138 91 ALhQPAGASSEAVE--------QLLAQL---------AEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 170 VVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV-----AGDVMLENT 236
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLvasgeTAEVMTPEN 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-212 |
2.59e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.89 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVR--------------ALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDE-ATLTRRAA 86
Cdd:PRK10790 339 GRIDIDNVSFAYRDDNLVlqninlsvpsrgfvALVGHTGSGKSTLASLLMGYYPLTEGEI-----RLDGRPlSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 87 ELGVRAVYQElSLVEGLTVAENLCLGQWPRRNGMIDYLQMAQDAQ--RCLQA-----LGvdvspEQlVSTLSPAQKQLVE 159
Cdd:PRK10790 414 RQGVAMVQQD-PVVLADTFLANVTLGRDISEEQVWQALETVQLAElaRSLPDglytpLG-----EQ-GNNLSVGQKQLLA 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 160 IARVMKGEPRVVILDEPTSSLASA---EVELVISAVKKMSALgvavIYVSHRMEEI 212
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGteqAIQQALAAVREHTTL----VVIAHRLSTI 538
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-211 |
2.68e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLegdEATLTRRAAELGVraVYQELSLVE 101
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGM--CPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GLTVAENLCL-GQWPRRNGMIDYLQMaqdaQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSL 180
Cdd:TIGR01257 1017 HLTVAEHILFyAQLKGRSWEEAQLEM----EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190
....*....|....*....|....*....|.
gi 1314860479 181 ASAEVELVISAVKKMSAlGVAVIYVSHRMEE 211
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRS-GRTIIMSTHHMDE 1122
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
275-480 |
2.87e-11 |
|
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: 63.40 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDmLKRGIGYTPENrkeagIIPW 354
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQD-----VFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQrmtvKAASSETPIG----TLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:cd03251 89 NDTVAENIAYGRPGATREEVEEAARAANAHEFIME----LPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELaAEGKSVVFIS---SEVEElplvCDRILLLQHG 480
Cdd:cd03251 165 ATSALDTESERLVQAALERL-MKNRTTFVIAhrlSTIEN----ADRIVVLEDG 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
275-480 |
3.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.67 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGL---EEYEQGEIVINGEKITRPDYGDMLKR-GIGY-TPENRKEA 349
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIREKvGIVFqNPDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 350 GIIpwlGVDENTVLTNRQkISANGVLqwSTIRRLTEEVMQRMTVKAASSetpigTLSGGNQQKVVIGRWVYAASQILLLD 429
Cdd:PRK13640 100 ATV---GDDVAFGLENRA-VPRPEMI--KIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 430 EPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVcDRILLLQHG 480
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMA-DQVLVLDDG 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-227 |
5.31e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLT-------GSERPDSGDIWIGETRLEGDEATLTRraaELGVraVYQELS 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLRK---EVGM--VFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENLClgqWP-RRNGMIDYLQMAQDAQRCLQALG----VDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:PRK14246 101 PFPHLSIYDNIA---YPlKSHGIKEKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 174 DEPTSSL---ASAEVELVISAVKKMsalgVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK14246 178 DEPTSMIdivNSQAIEKLITELKNE----IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
264-480 |
6.26e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.72 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 264 QAVLEVRAL----RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGL---EEYEQGEIVINGEKITRpdyGDMLK 336
Cdd:PRK09984 2 QTIIRVEKLaktfNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQR---EGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 337 RGIgytPENRKEAGII--PWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAAS-------SETPIGTLSG 407
Cdd:PRK09984 79 RDI---RKSRANTGYIfqQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTrvgmvhfAHQRVSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 408 GNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVREL-AAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
276-481 |
7.66e-11 |
|
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: 61.96 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRG---IGYTPENrkeagii 352
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQK------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 PWL---GVDENTVLT---NRQKISAngVLQWSTIRrlteevmQRMTVKAASSETPIG----TLSGGNQQKVVIGRWVYAA 422
Cdd:cd03290 88 PWLlnaTVEENITFGspfNKQRYKA--VTDACSLQ-------PDIDLLPFGDQTEIGergiNLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYR--IVRELAAEGKSVVFISSEVEELPLVcDRILLLQHGT 481
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHA-DWIIAMKDGS 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
276-484 |
7.91e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEkitrpdygdmlkrgIGYTPENrkeagiiPWL 355
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQ-------AWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 gvdENTVLtnRQKISANGVLQWSTIRRLTEE--VMQRMTVKAASSETPIG----TLSGGNQQKVVIGRWVYAASQILLLD 429
Cdd:TIGR00957 711 ---QNDSL--RENILFGKALNEKYYQQVLEAcaLLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 430 EPTRGVDIEAKQQIYRIV--RELAAEGKSVVFISSEVEELPLVcDRILLLQHGTFSQ 484
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEHVigPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISE 841
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
177-480 |
8.02e-11 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 64.35 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 177 TSSLASAEVELVISavkkmSALGVAVIYVSHR---------------------MEEIRRIASCATVMRDGQVAGDvmlen 235
Cdd:TIGR02203 236 AGSISSPITQLIAS-----LALAVVLFIALFQaqagsltagdftafitamialIRPLKSLTNVNAPMQRGLAAAE----- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 236 tsthHIVSLMLGRDHVDIAPVAPQEIvdQAVLEVRALRHK------PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIV 309
Cdd:TIGR02203 306 ----SLFTLLDSPPEKDTGTRAIERA--RGDVEFRNVTFRypgrdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 310 GLEEYEQGEIVINGEKITrpDYG-DMLKRGIGYtpenrkeagiipwlgVDENTVLTNrQKISANgvLQWSTIRRLTEEVM 388
Cdd:TIGR02203 380 RFYEPDSGQILLDGHDLA--DYTlASLRRQVAL---------------VSQDVVLFN-DTIANN--IAYGRTEQADRAEI 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 389 QRMTVKAASSE----------TPIGT----LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELaAEG 454
Cdd:TIGR02203 440 ERALAAAYAQDfvdklplgldTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQG 518
|
330 340
....*....|....*....|....*....
gi 1314860479 455 KSVVFIS---SEVEElplvCDRILLLQHG 480
Cdd:TIGR02203 519 RTTLVIAhrlSTIEK----ADRIVVMDDG 543
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
267-461 |
8.69e-11 |
|
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: 60.63 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGeivingeKITRPDYGDMLkrgigYTPENr 346
Cdd:cd03223 6 LSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-------RIGMPEGEDLL-----FLPQR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 347 keagiiPWLgvdenTVLTNRQKIsangVLQWSTIrrlteevmqrmtvkaassetpigtLSGGNQQKVVIGRWVYAASQIL 426
Cdd:cd03223 73 ------PYL-----PLGTLREQL----IYPWDDV------------------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*
gi 1314860479 427 LLDEPTRGVDIEAKQQIYRIVRElaaEGKSVVFIS 461
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE---LGITVISVG 145
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
265-480 |
9.55e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.07 E-value: 9.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRALRHKPK----LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQG-----EIVINGEKITRPDYGDM- 334
Cdd:PRK11264 2 SAIEVKNLVKKFHgqtvLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKGLIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 335 -LKRGIGYTPENrkeAGIIPWLGVDENTVltnRQKISANGVLQWSTIRRlTEEVMQRMTVKAASSETPiGTLSGGNQQKV 413
Cdd:PRK11264 82 qLRQHVGFVFQN---FNLFPHRTVLENII---EGPVIVKGEPKEEATAR-ARELLAKVGLAGKETSYP-RRLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 414 VIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
278-484 |
1.00e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.56 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEeYEQGEIVING---EKITRPDYgdmlkrgigytpenRKEAGIIPw 354
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGvswNSVPLQKW--------------RKAFGVIP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 lgvdeNTVL----TNRQKISANGvlQWS--TIRRLTEEVMQRMTVKAASSETPIG------TLSGGNQQKVVIGRWVYAA 422
Cdd:cd03289 84 -----QKVFifsgTFRKNLDPYG--KWSdeEIWKVAEEVGLKSVIEQFPGQLDFVlvdggcVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRElAAEGKSVVFISSEVEELpLVCDRILLLQHGTFSQ 484
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAM-LECQRFLVIEENKVRQ 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-180 |
1.02e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.72 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGE--TRLEgDEATLTRRAAELGVraVYQELSLVEG 102
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQplHQMD-EEARAKLRAKHVGF--VFQSFMLIPT 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 103 LTVAENLCLGQWPRrnGMIDYlQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSL 180
Cdd:PRK10584 103 LNALENVELPALLR--GESSR-QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
278-458 |
1.10e-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: 60.97 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygDMLKRGIGYTPEnrkEAGIIPWLGV 357
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR--DSIARGLLYLGH---APGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENtvltnrqkisangvLQWSTIRRLTEEVMQRM-TVKAASSE-TPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGV 435
Cdd:cd03231 91 LEN--------------LRFWHADHSDEQVEEALaRVGLNGFEdRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|...
gi 1314860479 436 DIEAKQQIYRIVRELAAEGKSVV 458
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVV 179
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-227 |
1.15e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 10 VAKVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAaelg 89
Cdd:PRK13642 7 VENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 90 VRAVYQEL-SLVEGLTVAENLCLGQwprRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEP 168
Cdd:PRK13642 83 IGMVFQNPdNQFVGATVEDDVAFGM---ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 169 RVVILDEPTSSL---ASAEVELVISAVKKMSALgvAVIYVSHRMEEIRRiASCATVMRDGQV 227
Cdd:PRK13642 160 EIIILDESTSMLdptGRQEIMRVIHEIKEKYQL--TVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-226 |
1.24e-10 |
|
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: 60.95 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLtgserpdsgdiwIGETRLEGDEATLTRRAAelgvravY--Q 95
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL------------LGELEKLSGSVSVPGSIA-------YvsQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENLCLGQwprrngmiDYlqmaqDAQR-------ClqALGVDVspEQLV-----------STLSPAQKQL 157
Cdd:cd03250 74 EPWIQNG-TIRENILFGK--------PF-----DEERyekvikaC--ALEPDL--EILPdgdlteigekgINLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 158 VEIARVMKGEPRVVILDEPTSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRiASCATVMRDGQ 226
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVdAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-227 |
1.25e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.85 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 11 AKVVAGNKR--YPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTG-----SERPDSGDIWI-GETRLEGDEATLT 82
Cdd:PRK14247 2 NKIEIRDLKvsFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLdGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 83 RRaaelgVRAVYQELSLVEGLTVAENLCLGqwPRRNGMIDYLQMAQdaQRCLQALGVDVSPEQL-------VSTLSPAQK 155
Cdd:PRK14247 82 RR-----VQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQ--ERVRWALEKAQLWDEVkdrldapAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 156 QLVEIARVMKGEPRVVILDEPTSSL---ASAEVELVISAVKKmsalGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLdpeNTAKIESLFLELKK----DMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-475 |
1.49e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 35 KGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigETRLEGDEAtLTR-RAAELG----------VRAVY-----QELS 98
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEV-LKRfRGTELQdyfkklangeIKVAHkpqyvDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENLclgqwpRRN---GMIDYLqmaqdaqrcLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:COG1245 174 KVFKGTVRELL------EKVderGKLDEL---------AEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 176 PTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRdGQ--VAGdvmlentsthhIVSLMLGrdhvdi 253
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILY-GEpgVYG-----------VVSKPKS------ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 254 APVA---------PQE---IVDQAV-LEVRALRHKPKLEDI-----------SFTL-------RRGEVLGIAGLLGAGRS 302
Cdd:COG1245 301 VRVGinqyldgylPEEnvrIRDEPIeFEVHAPRREKEEETLveypdltksygGFSLeveggeiREGEVLGIVGPNGIGKT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 303 ELLKAIVGLEEYEQGEiVINGEKIT-RPDYgdmLKRGIGYTpenrkeagiipwlgVDENTVLTNRQKISANgvlqWstir 381
Cdd:COG1245 381 TFAKILAGVLKPDEGE-VDEDLKISyKPQY---ISPDYDGT--------------VEEFLRSANTDDFGSS----Y---- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 382 rLTEEVMQRMTVKAAsSETPIGTLSGGNQQKVVIgrwvyAAS-----QILLLDEPTRGVDIEAKQQIYRIVRELAAEGKS 456
Cdd:COG1245 435 -YKTEIIKPLGLEKL-LDKNVKDLSGGELQRVAI-----AAClsrdaDLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGK 507
|
490 500
....*....|....*....|...
gi 1314860479 457 VVFIsseVEE----LPLVCDRIL 475
Cdd:COG1245 508 TAMV---VDHdiylIDYISDRLM 527
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
255-482 |
1.55e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.31 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 255 PVAPQEIVDQAVLEVRAL------RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITr 328
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVsftypdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 329 pDYG-DMLKRGIgytpenrkeagiipwlgvdenTVLTNRQKISANgvlqwsTIR-------------RLTEEVMQRMTVK 394
Cdd:PRK11160 406 -DYSeAALRQAI---------------------SVVSQRVHLFSA------TLRdnlllaapnasdeALIEVLQQVGLEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 395 AASSETP----IG----TLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAeGKSVVFISSEVEE 466
Cdd:PRK11160 458 LLEDDKGlnawLGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTG 536
|
250
....*....|....*.
gi 1314860479 467 LPLVcDRILLLQHGTF 482
Cdd:PRK11160 537 LEQF-DRICVMDNGQI 551
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
278-484 |
1.67e-10 |
|
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: 63.78 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEqGEIVING---EKITRPDYgdmlkrgigytpenRKEAGIIPw 354
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQTW--------------RKAFGVIP- 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 lgvDENTVLTNRQKISANGVLQWS--TIRRLTEEVMQRMTVKAASSETPIG------TLSGGNQQKVVIGRWVYAASQIL 426
Cdd:TIGR01271 1299 ---QKVFIFSGTFRKNLDPYEQWSdeEIWKVAEEVGLKSVIEQFPDKLDFVlvdggyVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 427 LLDEPTRGVDIEAKQQIYRIVRELAAEGkSVVFISSEVEELpLVCDRILLLQHGTFSQ 484
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNC-TVILSEHRVEAL-LECQQFLVIEGSSVKQ 1431
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-213 |
1.83e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.06 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETrlegDEATLTRRAAELGVRAVYQELSLVEgLT 104
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT----DIRTVTRASLRRNIAVVFQDAGLFN-RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 105 VAENLCLGQWPRRNG-MIDYLQMAQDAQRCL-QALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLAS 182
Cdd:PRK13657 425 IEDNIRVGRPDATDEeMRAAAERAQAHDFIErKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190
....*....|....*....|....*....|....
gi 1314860479 183 ---AEVELVISAVKKmsalGVAVIYVSHRMEEIR 213
Cdd:PRK13657 505 eteAKVKAALDELMK----GRTTFIIAHRLSTVR 534
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
249-481 |
2.24e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.90 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 249 DHVDIAPVAPQEI--VDQAVLEVRALR-----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGeivi 321
Cdd:COG4178 343 EAADALPEAASRIetSEDGALALEDLTlrtpdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG---- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 322 ngeKITRPDYGDM-------------LKRGIGY--TPENRKEAGIIPWL---GVDEntvLTNRQKISANgvlqWSTIrrl 383
Cdd:COG4178 419 ---RIARPAGARVlflpqrpylplgtLREALLYpaTAEAFSDAELREALeavGLGH---LAERLDEEAD----WDQV--- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 384 teevmqrmtvkaassetpigtLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRElaaEGKSVVFIS-S 462
Cdd:COG4178 486 ---------------------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELPGTTVISvG 541
|
250
....*....|....*....
gi 1314860479 463 EVEELPLVCDRILLLQHGT 481
Cdd:COG4178 542 HRSTLAAFHDRVLELTGDG 560
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
278-485 |
3.02e-10 |
|
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: 62.51 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYE--QGEIVIN------GEKITRPDYG----------------D 333
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIYHvalcekCGYVERPSKVgepcpvcggtlepeevD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 334 MLKRGIGYTPENRKEAGII---PWLGVDENTVLTN----RQKISANGVLQWSTIRRLTEEVM--QRMTVKAASsetpigt 404
Cdd:TIGR03269 96 FWNLSDKLRRRIRKRIAIMlqrTFALYGDDTVLDNvleaLEEIGYEGKEAVGRAVDLIEMVQlsHRITHIARD------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 405 LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELA-AEGKSVVFISSEVEELPLVCDRILLLQHGTFS 483
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
..
gi 1314860479 484 QE 485
Cdd:TIGR03269 249 EE 250
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-207 |
3.28e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.37 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPD---SGDIWIGETRLEGDEatLTRRAAelgvrAVYQELSLVEG 102
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKE--MRAISA-----YVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 103 LTVAENLCLG---QWPRRNGMIDYLQMAQDAqrcLQALGvdvspeqlvstLSPAQKQLVEIARVMKG------------- 166
Cdd:TIGR00955 114 LTVREHLMFQahlRMPRRVTKKEKRERVDEV---LQALG-----------LRKCANTRIGVPGRVKGlsggerkrlafas 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1314860479 167 ----EPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSH 207
Cdd:TIGR00955 180 elltDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-236 |
3.66e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDN----VNFTLNKGEVRALLGKNGAGKSTLIRMLTGSeRPDSGDIWIGETRLEgdeatlTRRAAELGVRAVYqelsl 99
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLE------AWSAAELARHRAY----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 vegltvaenLCLGQWPRRNgM--IDYLQMAQDAQRCL-----------QALGVDVSPEQLVSTLSPAQKQLVEIARVM-- 164
Cdd:PRK03695 74 ---------LSQQQTPPFA-MpvFQYLTLHQPDKTRTeavasalnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlq 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 165 ---KGEP--RVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV-----AGDVMLE 234
Cdd:PRK03695 144 vwpDINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLlasgrRDEVLTP 223
|
..
gi 1314860479 235 NT 236
Cdd:PRK03695 224 EN 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
264-480 |
3.71e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.57 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 264 QAVLEVRAL-------------RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPD 330
Cdd:PRK15112 2 ETLLEVRNLsktfryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 331 YGDMLKRgigytpenrkeagiIPWLGVDENTVLTNRQKISA--------NGVLQWSTIRRLTEEVMQRMTVKAASSETPI 402
Cdd:PRK15112 82 YSYRSQR--------------IRMIFQDPSTSLNPRQRISQildfplrlNTDLEPEQREKQIIETLRQVGLLPDHASYYP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 403 GTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVREL-AAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
278-480 |
3.73e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.36 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGD--MLKRGIG-----------YTpe 344
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQIGmifqhfnllssRT-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 345 nrkeagiipwlgVDENTVL------TNRQKISANgvlqwstirrlTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRW 418
Cdd:PRK11153 99 ------------VFDNVALplelagTPKAEIKAR-----------VTELLELVGLSDKADRYP-AQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 419 VYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
277-480 |
4.33e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.98 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 277 KLEDI-----------SFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygdmlkrgigyTPEN 345
Cdd:PRK10771 3 KLTDItwlyhhlpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-------------TPPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 346 RKEAGIIpwlgVDENTV---LTNRQKIS---ANGVLQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWV 419
Cdd:PRK10771 70 RRPVSML----FQENNLfshLTVAQNIGlglNPGLKLNAAQREKLHAIARQMGIEDLLARLP-GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 420 YAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGK-SVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
269-500 |
5.88e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.09 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 269 VRALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygdmLKRGigytpENRKE 348
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK------LNRA-----QRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 349 AGIIPWLGVDENTVLTNRQKISA------NGVLQWSTIRRL--TEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVY 420
Cdd:PRK10419 88 RRDIQMVFQDSISAVNPRKTVREiireplRHLLSLDKAERLarASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 421 AASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG--------TFSQEFHAPVN 491
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGqivetqpvGDKLTFSSPAG 247
|
....*....
gi 1314860479 492 vDELMSAIL 500
Cdd:PRK10419 248 -RVLQNAVL 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-194 |
6.10e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.73 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 32 TLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetrlEGDEATLTRRAaelgvravyQELSlvegltvaenlcl 111
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------EIELDTVSYKP---------QYIK------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 112 gqwPRRNGMIDYLQMAQDAQRC---------LQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLAS 182
Cdd:cd03237 72 ---ADYEGTVRDLLSSITKDFYthpyfkteiAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170
....*....|..
gi 1314860479 183 AEVELVISAVKK 194
Cdd:cd03237 149 EQRLMASKVIRR 160
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
275-481 |
6.23e-10 |
|
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: 57.46 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVInGEKITrpdygdmlkrgIGYTPEnrkeagiipw 354
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK-----------IGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 lgvdentvltnrqkisangvlqwstirrlteevmqrmtvkaassetpigtLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314860479 435 VDIEAKQQiyrIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:cd03221 101 LDLESIEA---LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-210 |
6.24e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTG--SERPDSGdiwigetrlegdeatltrrAAELGVRAVYQELSLVEGL 103
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAG-------------------CVDVPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TvaenlclgqwprRNGMIDylqmaqDAQRCLQALG-VDVspeQL----VSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:COG2401 107 G------------RKGDFK------DAVELLNAVGlSDA---VLwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|...
gi 1314860479 179 SLASAEVELVISAVKKMS-ALGVAVIYVSHRME 210
Cdd:COG2401 166 HLDRQTAKRVARNLQKLArRAGITLVVATHHYD 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
270-480 |
6.37e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 270 RALRHKPKLEDISFTLRR-------------GEVLGIAGLLGAGRSELLKAIVGLEEYE--QGEIVINGEKITRPdygdM 334
Cdd:PLN03211 63 RILGHKPKISDETRQIQErtilngvtgmaspGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ----I 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 335 LKRgIGYTPENRKeagIIPWLGVDENTVLTNRQKISANGVLQWSTirRLTEEVMQRMTVkAASSETPIGT-----LSGGN 409
Cdd:PLN03211 139 LKR-TGFVTQDDI---LYPHLTVRETLVFCSLLRLPKSLTKQEKI--LVAESVISELGL-TKCENTIIGNsfirgISGGE 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 410 QQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFI----SSEVEELplvCDRILLLQHG 480
Cdd:PLN03211 212 RKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmhqpSSRVYQM---FDSVLVLSEG 283
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
278-458 |
6.48e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYG---------DMLKrgigytpenrke 348
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachylghrNAMK------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 349 agiiPWLGVDENtvltnrqkisangvLQ-WSTIR----RLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAAS 423
Cdd:PRK13539 86 ----PALTVAEN--------------LEfWAAFLggeeLDIAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLLVSNR 146
|
170 180 190
....*....|....*....|....*....|....*
gi 1314860479 424 QILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVV 458
Cdd:PRK13539 147 PIWILDEPTAALDAAAVALFAELIRAHLAQGGIVI 181
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
280-502 |
7.10e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.66 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 280 DISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVING-------EKITRPDYgdmlKRGIGYTpenRKEAGII 352
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPE----KRRIGYV---FQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 PWLGVDENTVLTNRQKISAngvlQWSTIRRL--TEEVMQRMtvkaassetPIgTLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:PRK11144 89 PHYKVRGNLRYGMAKSMVA----QFDKIVALlgIEPLLDRY---------PG-SLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELAAEGK-SVVFISSEVEELPLVCDRILLLQHGTF-----------SQEFHAPVNVDELmSA 498
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINiPILYVSHSLDEILRLADRVVVLEQGKVkafgpleevwaSSAMRPWLPKEEQ-SS 233
|
....
gi 1314860479 499 ILSV 502
Cdd:PRK11144 234 ILKV 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
281-481 |
7.64e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 59.62 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 281 ISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRGIGYTPENRKeagIIPWLGVDEN 360
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVR---LFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 361 TVLTNRQKISAN---GVLQWSTIRRLTEEVMQRmtvkAAS----------SETPIGTLSGGNQQKVVIGRWVYAASQILL 427
Cdd:PRK11300 101 LLVAQHQQLKTGlfsGLLKTPAFRRAESEALDR----AATwlervgllehANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 428 LDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
272-492 |
1.07e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.11 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 272 LRHKPKLE----DISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMlkrgigytpenRK 347
Cdd:TIGR00957 1292 LRYREDLDlvlrHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL-----------RF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 348 EAGIIPwlgvDENTVLTNRQKISANGVLQWStirrlTEEV---MQRMTVKAASSETPIG----------TLSGGNQQKVV 414
Cdd:TIGR00957 1361 KITIIP----QDPVLFSGSLRMNLDPFSQYS-----DEEVwwaLELAHLKTFVSALPDKldhecaeggeNLSVGQRQLVC 1431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 415 IGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRElAAEGKSVVFISsevEELPLVCD--RILLLQHGTFsQEFHAPVNV 492
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIA---HRLNTIMDytRVIVLDKGEV-AEFGAPSNL 1506
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-216 |
1.40e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.89 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 5 TEAVPVAKVVAGNKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDsgdiwiGETRLEG-----DEA 79
Cdd:PRK14258 2 SKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE------SEVRVEGrveffNQN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 80 TLTRRaaeLGVRAVYQELSLVEG------LTVAENLCLG----QWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLvsT 149
Cdd:PRK14258 76 IYERR---VNLNRLRRQVSMVHPkpnlfpMSVYDNVAYGvkivGWRPKLEIDDIVESALKDADLWDEIKHKIHKSAL--D 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 150 LSPAQKQLVEIARVMKGEPRVVILDEPTSSL---ASAEVELVISAVKKMSALgvAVIYVSHRMEEIRRIA 216
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLdpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLS 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
278-485 |
1.56e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.02 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDyGDMLKRGIgytpenRKEAGII---PW 354
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKT-KDKYIRPV------RKRIGMVfqfPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVltNRQKI--SANGVLQWSTIR-RLTEEVMQRMTVKAASSETPIgTLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:PRK13646 96 SQLFEDTV--EREIIfgPKNFKMNLDEVKnYAHRLLMDLGFSRDVMSQSPF-QMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-188 |
1.58e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 29 VNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI-GETRLEGDEatlTRRAAELG-VRAVYQELSLVEGLTVA 106
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDR---SRFMAYLGhLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 107 ENLcLGQWPRrngmidylQMAQDAqrcLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVE 186
Cdd:PRK13543 107 CGL-HGRRAK--------QMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT 174
|
..
gi 1314860479 187 LV 188
Cdd:PRK13543 175 LV 176
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-222 |
1.85e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.33 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGETRLEGDEAtlTRRAAELGVRAVYQE--LSLVE 101
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGKDLLGMKDD--EWRAVRSDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GLTVAENLClgqWPRRngmIDYLQM-AQDAQRCLQALGVDVS-PEQLVS----TLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK15079 114 RMTIGEIIA---EPLR---TYHPKLsRQEVKDRVKAMMLKVGlLPNLINryphEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1314860479 176 PTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRMEEIRRIASCATVM 222
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-460 |
2.25e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 32 TLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-----WigETRLE---GDE-ATLTRRAAELGVRAV----YQEL- 97
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepsW--DEVLKrfrGTElQNYFKKLYNGEIKVVhkpqYVDLi 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 -SLVEGlTVAENLclgqwpRRN---GMIDYLqmaqdaqrcLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:PRK13409 173 pKVFKG-KVRELL------KKVderGKLDEV---------VERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMeeirriascaTVMrdgqvagDVMLENT-------STHHIVSLML 246
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEHDL----------AVL-------DYLADNVhiaygepGAYGVVSKPK 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 247 GrdhvdiAPVA---------PQE---IVDQAV-LEVRALRHKPKLEDI-----------SFTL-------RRGEVLGIAG 295
Cdd:PRK13409 299 G------VRVGineylkgylPEEnmrIRPEPIeFEERPPRDESERETLveypdltkklgDFSLeveggeiYEGEVIGIVG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 296 LLGAGRSELLKAIVGLEEYEQGEIVINgekitrpdygdmLKrgIGYTPEnrkeagiipWLGVD-ENTV---LTNRQKISA 371
Cdd:PRK13409 373 PNGIGKTTFAKLLAGVLKPDEGEVDPE------------LK--ISYKPQ---------YIKPDyDGTVedlLRSITDDLG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 372 NGVLQWSTIRRLT-EEVMQRmtvkaassetPIGTLSGGNQQKVVIgrwvyAAS-----QILLLDEPTRGVDIEAKQQIYR 445
Cdd:PRK13409 430 SSYYKSEIIKPLQlERLLDK----------NVKDLSGGELQRVAI-----AAClsrdaDLYLLDEPSAHLDVEQRLAVAK 494
|
490
....*....|....*
gi 1314860479 446 IVRELAAEGKSVVFI 460
Cdd:PRK13409 495 AIRRIAEEREATALV 509
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
265-492 |
2.30e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 58.93 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 265 AVLEVRALRHK----PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITR--PDygdmlKRG 338
Cdd:COG3839 2 ASLELENVSKSyggvEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlpPK-----DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 339 IGYTPENrkeAGIIPWLGVDENTV--LTNRqKISAngvlqwSTIRRLTEEV---------MQRMtvkaassetPiGTLSG 407
Cdd:COG3839 77 IAMVFQS---YALYPHMTVYENIAfpLKLR-KVPK------AEIDRRVREAaellgledlLDRK---------P-KQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 408 GNQQKVVIGRWVYAASQILLLDEPTRGVD----IEAKQQIYRIVRELaaeGKSVVFISSEVEELPLVCDRILLLQHGTFS 483
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
250
....*....|....*
gi 1314860479 484 QE------FHAPVNV 492
Cdd:COG3839 214 QVgtpeelYDRPANL 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
264-436 |
2.51e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 264 QAVLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGL-----EEYEQGEIVINGEKITRPDYGdm 334
Cdd:PRK14239 3 EPILQVSDLSvyynKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 335 lkrgigyTPENRKEAGII-----PW-LGVDENTVLTNRqkisANGVLQWSTIRRLTEEVMQRMT----VKAASSETPIGt 404
Cdd:PRK14239 81 -------TVDLRKEIGMVfqqpnPFpMSIYENVVYGLR----LKGIKDKQVLDEAVEKSLKGASiwdeVKDRLHDSALG- 148
|
170 180 190
....*....|....*....|....*....|..
gi 1314860479 405 LSGGNQQKVVIGRWVYAASQILLLDEPTRGVD 436
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-243 |
2.66e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.76 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSerpdSGDIW-IGETRLEGDEATLT------RRA---AELGVra 92
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI----TKDNWhVTADRFRWNGIDLLklspreRRKiigREIAM-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 93 VYQE--LSLVEGLTVAENLC-----------LGQWP--RRNGMIDYLQMA--QDAQRCLQALgvdvsPEQlvstLSPAQK 155
Cdd:COG4170 94 IFQEpsSCLDPSAKIGDQLIeaipswtfkgkWWQRFkwRKKRAIELLHRVgiKDHKDIMNSY-----PHE----LTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 156 QLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSAL-GVAVIYVSHRMEEIRRIASCATVMRDGQvagdvMLE 234
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQ-----TVE 239
|
....*....
gi 1314860479 235 NTSTHHIVS 243
Cdd:COG4170 240 SGPTEQILK 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
280-491 |
2.70e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 280 DISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEkitRPDYGDMLKRGIGYTPENRkeaGIIPWLGVDE 359
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAERGVGMVFQSY---ALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 360 NTV----LTNRQKISANG-VLQWSTIRRLtEEVMQRMTvKAassetpigtLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:PRK11000 95 NMSfglkLAGAKKEEINQrVNQVAEVLQL-AHLLDRKP-KA---------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 435 VD----IEAKQQIYRIVRELaaeGKSVVFIS-SEVEELPLVcDRILLLQHGTFSQE------FHAPVN 491
Cdd:PRK11000 164 LDaalrVQMRIEISRLHKRL---GRTMIYVThDQVEAMTLA-DKIVVLDAGRVAQVgkplelYHYPAN 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
274-480 |
2.94e-09 |
|
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: 57.48 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 274 HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYgDMLKRGIGYtpenrkeagiip 353
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH-KYLHSKVSL------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 wlgVDENTVLTNR--QKISANGVLQWSTIRrlTEEVMQRMTVKAASSETPIG----------TLSGGNQQKVVIGRWVYA 421
Cdd:cd03248 93 ---VGQEPVLFARslQDNIAYGLQSCSFEC--VKEAAQKAHAHSFISELASGydtevgekgsQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 422 ASQILLLDEPTRGVDIEAKQQIYRIVRElAAEGKSVVFIS---SEVEElplvCDRILLLQHG 480
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAhrlSTVER----ADQILVLDGG 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
267-481 |
2.97e-09 |
|
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: 56.77 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYE--QGEIVINGEKITrpdygDMlkrgig 340
Cdd:cd03217 1 LEIKDLHvsvgGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDIT-----DL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 341 yTPENRKEAGI---------IPwlGVDENTVLtnrqkisangvlqwstiRRLTEevmqrmtvkaassetpigTLSGGNQQ 411
Cdd:cd03217 70 -PPEERARLGIflafqyppeIP--GVKNADFL-----------------RYVNE------------------GFSGGEKK 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 412 KVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLV-CDRILLLQHGT 481
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGR 182
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
26-233 |
3.17e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGseRPD----SGDI-WIGETRLegdEATLTRRaAELGVRAVYQELSLV 100
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDIlFKGESIL---DLEPEER-AHLGIFLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGLTVAenlclgqwprrngmiDYLQMAQDAQRCLQALgVDVSPEQLVSTLSP----------------------AQKQLV 158
Cdd:CHL00131 97 PGVSNA---------------DFLRLAYNSKRKFQGL-PELDPLEFLEIINEklklvgmdpsflsrnvnegfsgGEKKRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 159 EIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHR---MEEIrrIASCATVMRDGQV--AGDVML 233
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYI--KPDYVHVMQNGKIikTGDAEL 238
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-208 |
3.33e-09 |
|
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: 56.01 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLtgserpdsgdiwigetrlegdeatltrraAELgvravyqelslvegltv 105
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-----------------------------AGL----------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 aenlclgqWPRRNGMIDYLQMAQD---AQRCLQALGVdvSPEQLV----STLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:cd03223 51 --------WPWGSGRIGMPEGEDLlflPQRPYLPLGT--LREQLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190
....*....|....*....|....*....|.
gi 1314860479 179 SLaSAEVEL-VISAVKKMsalGVAVIYVSHR 208
Cdd:cd03223 121 AL-DEESEDrLYQLLKEL---GITVISVGHR 147
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
274-484 |
4.41e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.96 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 274 HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKR--GIGYTP--ENRKEA 349
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRlaVVSQTPflFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 350 GIIPwLGVDENTvltnRQKISANGVLQ--WSTIRRLTE----EVMQRMTVkaassetpigtLSGGNQQKVVIGRWVYAAS 423
Cdd:PRK10789 407 NNIA-LGRPDAT----QQEIEHVARLAsvHDDILRLPQgydtEVGERGVM-----------LSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 424 QILLLDEPTRGVDIEAKQQIYRIVRELaAEGKSVVfISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQW-GEGRTVI-ISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-227 |
7.62e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETR---LEGDEATLTRRAAELGVRAVYQELS- 98
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidtLSPGKLQALRRDIQFIFQDPYASLDp 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 -LVEGLTVAENLclgqwpRRNGMIDYLQMAQDAQRCLQALGVdvSPE---QLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PRK10261 417 rQTVGDSIMEPL------RVHGLLPGKAAAARVAWLLERVGL--LPEhawRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 175 EPTSSL-ASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:PRK10261 489 EAVSALdVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
276-489 |
8.39e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVI--------NGEKITRPDYGDMLKRGIgytpENRK 347
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrSRQVIELSEQSAAQMRHV----RGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 348 EAGIIPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRM--TVKAASSETPIG----TLSGGNQQKVVIGRWVYA 421
Cdd:PRK10261 106 MAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMldQVRIPEAQTILSryphQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 422 ASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLL------QHGTFSQEFHAP 489
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMyqgeavETGSVEQIFHAP 260
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
278-498 |
1.04e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDyGDMLKRGIGYTPENRKEA-------- 349
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQQLPAAegmtvrel 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 350 ---GIIPWLGVDENTVLTNRQKIsangvlqwstirrltEEVMQRMTVKAASSETpIGTLSGGNQQKVVIGRWVYAASQIL 426
Cdd:PRK10575 106 vaiGRYPWHGALGRFGAADREKV---------------EEAISLVGLKPLAHRL-VDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 427 LLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGtfsqEFHAPVNVDELMSA 498
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGG----EMIAQGTPAELMRG 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-244 |
1.18e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDE----------------ATLTRRAAel 88
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI-----TLHGKKinnhnaneainhgfalVTEERRST-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 89 gvrAVYQELSlVEGLTVAENLclGQWPRRNGMIDYLQMAQDAQRCLQALGVDV-SPEQLVSTLSPAQKQLVEIARVMKGE 167
Cdd:PRK10982 336 ---GIYAYLD-IGFNSLISNI--RNYKNKVGLLDNSRMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 168 PRVVILDEPTSSL---ASAEV-ELVISAVKKmsalGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVMLENTSTHHIVS 243
Cdd:PRK10982 410 PEILMLDEPTRGIdvgAKFEIyQLIAELAKK----DKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILR 485
|
.
gi 1314860479 244 L 244
Cdd:PRK10982 486 L 486
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
280-489 |
1.40e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 280 DISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYE---QGEIVINGEKITRpdygdmlkrgigyTPE---NRKEAGIIP 353
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILN-------------LPEkelNKLRAEQIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 WLGVDENTVLTNRQKISAngvlqwstirRLTEEVMQ--------------RM--TVKAASSETPIGT----LSGGNQQKV 413
Cdd:PRK09473 101 MIFQDPMTSLNPYMRVGE----------QLMEVLMLhkgmskaeafeesvRMldAVKMPEARKRMKMypheFSGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 414 VIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILL------LQHGTFSQEF 486
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVmyagrtMEYGNARDVF 250
|
...
gi 1314860479 487 HAP 489
Cdd:PRK09473 251 YQP 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
275-480 |
1.48e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.72 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygDMLKRGIGYTPENRKeagIIPW 354
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL--DAVRQSLGMCPQHNI---LFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTNRQKISAngvlqWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRS-----WEEAQLEMEAMLEDTGLHHKRNEEA-QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314860479 435 VDIEAKQQIYRIVRELAAeGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
278-461 |
1.94e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.13 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGD--MLKRGIGYTPEN-------RKE 348
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkLLRQKIQIVFQNpygslnpRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 349 AGIIPWLGVDENTVLTNRQKisangvlqwstiRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLL 428
Cdd:PRK11308 111 VGQILEEPLLINTSLSAAER------------REKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190
....*....|....*....|....*....|....
gi 1314860479 429 DEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFIS 461
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQElGLSYVFIS 212
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-86 |
2.18e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 2.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRAA 86
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-----LLDGKPVTAEQPED 394
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
278-484 |
2.28e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.20 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVING---EKITRPDYGDMLKRGIGYTPENrkeAGIIPW 354
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQS---FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLtnrqKISANGVLQwSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:PRK10070 121 MTVLDNTAF----GMELAGINA-EERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 435 VDIEAKQQIY-RIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:PRK10070 195 LDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
275-485 |
2.44e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVG-LEEYEQGEIVINGEkitrpdygdmlkrgIGYTPEnrkeagiIP 353
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT--------------VAYVPQ-------VS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 354 WL---GVDENTVLTNrqkiSANGVLQWSTIRrlTEEVMQRMTVKAASSETPIG----TLSGGNQQKVVIGRWVYAASQIL 426
Cdd:PLN03130 689 WIfnaTVRDNILFGS----PFDPERYERAID--VTALQHDLDLLPGGDLTEIGergvNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 427 LLDEPTRGVDIEAKQQIYR--IVRELaaEGKSVVFISSEVEELPLVcDRILLLQHGTFSQE 485
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDkcIKDEL--RGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEE 820
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
264-485 |
2.97e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.53 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 264 QAVLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGL-EEYEQ----GEIVINGEKITRPDYGDM 334
Cdd:PRK14247 1 MNKIEIRDLKvsfgQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLiELYPEarvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 335 LKR--GIGYTPENrkeagiIPWLGVDENTVL---TNR---QKISANGVLQWSTIR-RLTEEVMQRMtvkaassETPIGTL 405
Cdd:PRK14247 81 RRRvqMVFQIPNP------IPNLSIFENVALglkLNRlvkSKKELQERVRWALEKaQLWDEVKDRL-------DAPAGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 406 SGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEgKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-213 |
3.32e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 28 NVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDeATLTRRAAELGVRAV-------------- 93
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKD-INLKWWRSKIGVVSQdpllfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 94 YQELSLVE-----------GLTVAENLCLGQWPRRNGMIDYLQMAQ--DAQRCLQALG----------VDVSPEQLV--- 147
Cdd:PTZ00265 482 YSLYSLKDlealsnyynedGNDSQENKNKRNSCRAKCAGDLNDMSNttDSNELIEMRKnyqtikdsevVDVSKKVLIhdf 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 148 ----------------STLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSA-LGVAVIYVSHRME 210
Cdd:PTZ00265 562 vsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLS 641
|
...
gi 1314860479 211 EIR 213
Cdd:PTZ00265 642 TIR 644
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
266-459 |
3.33e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRAL---R-HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT--RPDY-GDMLKrg 338
Cdd:PRK13538 1 MLEARNLaceRdERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqRDEYhQDLLY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 339 IGYTPenrkeaGIIPWLGVDENtvLTNRQKISangvlqwstiRRLTEEVMQRMTVK---AASSETPIGTLSGGNQQKVVI 415
Cdd:PRK13538 79 LGHQP------GIKTELTALEN--LRFYQRLH----------GPGDDEALWEALAQvglAGFEDVPVRQLSAGQQRRVAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314860479 416 GRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVF 459
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-77 |
3.42e-08 |
|
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: 55.96 E-value: 3.42e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1314860479 29 VNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGD 77
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD 399
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-208 |
4.57e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 55.58 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEvRALL-GKNGAGKSTLIRMLTGserpdsgdIW-IGE---TRLEGDEAT-LTRRAaelgvravYqelsL 99
Cdd:COG4178 379 LEDLSLSLKPGE-RLLItGPSGSGKSTLLRAIAG--------LWpYGSgriARPAGARVLfLPQRP--------Y----L 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 VEGlTVAENLCLgqwPRRNGMIDylqmAQDAQRCLQALGVDVSPEQL------VSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:COG4178 438 PLG-TLREALLY---PATAEAFS----DAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190
....*....|....*....|....*....|....*
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHR 208
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELP-GTTVISVGHR 543
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
278-485 |
6.51e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPD---YGDMLKRGIGYTPENRKeagIIPW 354
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRAKHVGFVFQSFM---LIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVL--------TNRQKISANGVL-QWSTIRRLTEEVMQrmtvkaassetpigtLSGGNQQKVVIGRWVYAASQI 425
Cdd:PRK10584 103 LNALENVELpallrgesSRQSRNGAKALLeQLGLGKRLDHLPAQ---------------LSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 426 LLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-216 |
6.57e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.63 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 20 YPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRM------LTGSERPDsGDIWIGETRLEG---DEATLTRRaaelgV 90
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGKNLYApdvDPVEVRRR-----I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 91 RAVYQELSLVEGlTVAENLCLGqwPRRNGMidYLQMAQDAQRCL-QALGVDVSPEQLV---STLSPAQKQLVEIARVMKG 166
Cdd:PRK14243 94 GMVFQKPNPFPK-SIYDNIAYG--ARINGY--KGDMDELVERSLrQAALWDEVKDKLKqsgLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 167 EPRVVILDEPTSSL---ASAEVELVISAVKKMsalgVAVIYVSHRMEEIRRIA 216
Cdd:PRK14243 169 QPEVILMDEPCSALdpiSTLRIEELMHELKEQ----YTIIIVTHNMQQAARVS 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
274-480 |
6.87e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 52.63 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 274 HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEE--YEQGEIVINGEKITrpdygDMLKRGIGYTPENRKEagi 351
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD-----KNFQRSTGYVEQQDVH--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 IPWLGVDENTvltnrqKISANgvlqwstIRRLTEEvmQRmtvkaassetpigtlsggnqQKVVIGRWVYAASQILLLDEP 431
Cdd:cd03232 91 SPNLTVREAL------RFSAL-------LRGLSVE--QR--------------------KRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAEGKSVV-FISSEVEELPLVCDRILLLQHG 480
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKLADSGQAILcTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
278-491 |
7.47e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEqGEIVINGekitRPDY--GDMLKRGIGYTPENRKEAGIIPWL 355
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEG----RVEFfnQNIYERRVNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 GVDENTVLTN----------RQKISANGVLQwSTIR--RLTEEVMQRMTVKAASsetpigtLSGGNQQKVVIGRWVYAAS 423
Cdd:PRK14258 98 NLFPMSVYDNvaygvkivgwRPKLEIDDIVE-SALKdaDLWDEIKHKIHKSALD-------LSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 424 QILLLDEPTRGVDIEAKQQIYRIVRELAAEGK-SVVFISSEVEELPLVCD----------RI-LLLQHGTFSQEFHAPVN 491
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDftaffkgnenRIgQLVEFGLTKKIFNSPHD 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
278-450 |
8.45e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.90 E-value: 8.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGE---KITRPDYGDMLKRGIGYTPENRKeagIIPw 354
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNQKLGFIYQFHH---LLP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 lgvdENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:PRK11629 101 ----DFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170
....*....|....*.
gi 1314860479 435 VDIEAKQQIYRIVREL 450
Cdd:PRK11629 176 LDARNADSIFQLLGEL 191
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
266-461 |
9.76e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYE--QGEIVINGEKITRPDygdmlkrgi 339
Cdd:CHL00131 7 ILEIKNLHasvnENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLE--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 340 gytPENRKEAGI---------IPwlGVDE----NTVLTNRQKisANGVLQWSTIRRLtEEVMQRMTVkAASSETPIGT-- 404
Cdd:CHL00131 78 ---PEERAHLGIflafqypieIP--GVSNadflRLAYNSKRK--FQGLPELDPLEFL-EIINEKLKL-VGMDPSFLSRnv 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 405 ---LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFIS 461
Cdd:CHL00131 149 negFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIT 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
279-438 |
9.83e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 279 EDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVIngekitrpdyGDMLKrgIGYTPENRkeAGIIPwlgvd 358
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI----------GETVK--LAYVDQSR--DALDP----- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 359 ENTVLtnrQKISaNGVlqwSTIRRLTEEVMQRMTV-----KAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTR 433
Cdd:PRK11819 402 NKTVW---EEIS-GGL---DIIKVGNREIPSRAYVgrfnfKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTN 474
|
....*
gi 1314860479 434 GVDIE 438
Cdd:PRK11819 475 DLDVE 479
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-227 |
1.06e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.25 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 20 YPG--VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEgdEATLT--RRAAELgvraVYQ 95
Cdd:PRK11176 351 YPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR--DYTLAslRNQVAL----VSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 96 ELSLVEGlTVAENL---CLGQWPRRNgMIDYLQMAQdAQRCLQAL--GVD-VSPEQLVStLSPAQKQLVEIARVMKGEPR 169
Cdd:PRK11176 425 NVHLFND-TIANNIayaRTEQYSREQ-IEEAARMAY-AMDFINKMdnGLDtVIGENGVL-LSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 170 VVILDEPTSSLASaEVELVISAV-----KKMSALGVAviyvsHRMEEIRRiASCATVMRDGQV 227
Cdd:PRK11176 501 ILILDEATSALDT-ESERAIQAAldelqKNRTSLVIA-----HRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
278-453 |
1.07e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQ-----GEIVINGEKITRPDYGDMlkrgigytpENRKEAGII 352
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPI---------EVRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 -------PWLGVDENTVL------TNRQKISANGVLQWSTIRR-LTEEVMQRMTVKAassetpiGTLSGGNQQKVVIGRW 418
Cdd:PRK14267 91 fqypnpfPHLTIYDNVAIgvklngLVKSKKELDERVEWALKKAaLWDEVKDRLNDYP-------SNLSGGQRQRLVIARA 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1314860479 419 VYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE 453
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE 198
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-228 |
1.25e-07 |
|
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: 54.06 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETrlegDEATLT----RRAaeLGVraVYQELSLVE 101
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ----DIRDVTqaslRAA--IGI--VPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GlTVAENLCLGQWprRNGMIDYLQMAQDAQrcLQALgVDVSPEQLVST-------LSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:COG5265 446 D-TIAYNIAYGRP--DASEEEVEAAARAAQ--IHDF-IESLPDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1314860479 175 EPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQVA 228
Cdd:COG5265 520 EATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-207 |
1.29e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 18 KRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGEtrlegdeatltrrAAELGVRAVYQEL 97
Cdd:PRK15064 327 KGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE-------------NANIGYYAQDHAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGLTVAEnlclgqWprrngMIDYLQMAQDAQRCLQALGV------DVspEQLVSTLSPAQKQLVEIARVMKGEPRVV 171
Cdd:PRK15064 394 DFENDLTLFD------W-----MSQWRQEGDDEQAVRGTLGRllfsqdDI--KKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190
....*....|....*....|....*....|....*.
gi 1314860479 172 ILDEPTSSLASAEVELVISAVKKMSAlgvAVIYVSH 207
Cdd:PRK15064 461 VMDEPTNHMDMESIESLNMALEKYEG---TLIFVSH 493
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
278-480 |
1.37e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.76 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT--RPDYGDMLKrgigytpenrkEAGIIPWL 355
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAeaREDTRLMFQ-----------DARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 GVDENTVLTNRQKisangvlqWstiRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGV 435
Cdd:PRK11247 97 KVIDNVGLGLKGQ--------W---RDAALQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 436 D----IEAKQQIYRIVRElaaEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK11247 165 DaltrIEMQDLIESLWQQ---HGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-214 |
1.41e-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: 51.55 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIrmltgserpdsgdiwigetrLEGDEATLTRRAAELGVRAVYQELSLVEGLT 104
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV--------------------NEGLYASGKARLISFLPKFSRNKLIFIDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 105 VAENLCLGqwprrngmidYLqmaqdaqrclqalgvdvSPEQLVSTLSPAQKQLVEIARVMKGEPR--VVILDEPTSSLAS 182
Cdd:cd03238 70 FLIDVGLG----------YL-----------------TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190
....*....|....*....|....*....|..
gi 1314860479 183 AEVELVISAVKKMSALGVAVIYVSHRMEEIRR 214
Cdd:cd03238 123 QDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
284-460 |
1.49e-07 |
|
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: 52.41 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 284 TLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpdygdmlkrgigYTPenrkeagiipwlgvdentvl 363
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKP-------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 364 tnrQKISANgvlQWSTIRRLTEEVMQRMTVKAA-SSE--TPIG----------TLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:cd03237 68 ---QYIKAD---YEGTVRDLLSSITKDFYTHPYfKTEiaKPLQieqildrevpELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190
....*....|....*....|....*....|
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELAAEGKSVVFI 460
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFV 171
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-207 |
3.23e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 20 YPG-VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWigetrlegdeatltrRAAELGVrAVYQElS 98
Cdd:PLN03073 518 YPGgPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---------------RSAKVRM-AVFSQ-H 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENLCLGQWPRRNGMIDylqmaQDAQRCLQALGVDVS-PEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPT 177
Cdd:PLN03073 581 HVDGLDLSSNPLLYMMRCFPGVPE-----QKLRAHLGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190
....*....|....*....|....*....|
gi 1314860479 178 SSLASAEVELVISAVKKMSAlgvAVIYVSH 207
Cdd:PLN03073 656 NHLDLDAVEALIQGLVLFQG---GVLMVSH 682
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-207 |
3.32e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 32 TLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetrlegdeatltrraaELGVRAVY--QELSLVEGLTVAENL 109
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------------DEDLKISYkpQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 110 clgqwprRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVI 189
Cdd:COG1245 423 -------RSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
170
....*....|....*....
gi 1314860479 190 SAVKKMSAL-GVAVIYVSH 207
Cdd:COG1245 496 KAIRRFAENrGKTAMVVDH 514
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-485 |
3.78e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEE----YE-QGEIVINGEKITrpDYGDMLkrgigytpENRKEA 349
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgYRySGDVLLGGRSIF--NYRDVL--------EFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 350 GII-----PW-LGVDENTVLTNR-QKISANGVLQWSTIRRLTEeVMQRMTVKAASSETPIgTLSGGNQQKVVIGRWVYAA 422
Cdd:PRK14271 104 GMLfqrpnPFpMSIMDNVLAGVRaHKLVPRKEFRGVAQARLTE-VGLWDAVKDRLSDSPF-RLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELaAEGKSVVFISSEVEELPLVCDRILLLQHGTFSQE 485
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
266-472 |
4.25e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 266 VLEVRALR----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygdmLKRGIGY 341
Cdd:PRK11831 7 LVDMRGVSftrgNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPA------MSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 342 TPENR-----KEAGIIPWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSEtpigtLSGGNQQKVVIG 416
Cdd:PRK11831 81 TVRKRmsmlfQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSE-----LSGGMARRAALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 417 RWVYAASQILLLDEPTRGVDIEAKQQIYRIVREL-AAEGKSVVFISSEVEELPLVCD 472
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIAD 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-238 |
4.26e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRlegdeatlTRRAAELGVRAVY---QELS 98
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP--------TRQALQKNLVAYVpqsEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 99 LVEGLTVAENLCLGqwprRNGMIDYLQM--AQDAQRCLQALG-VDVSP--EQLVSTLSPAQKQLVEIARVMKGEPRVVIL 173
Cdd:PRK15056 91 WSFPVLVEDVVMMG----RYGHMGWLRRakKRDRQIVTAALArVDMVEfrHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 174 DEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIAScATVMRDGQVAGDVMLENTST 238
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
278-484 |
4.27e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.03 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpdygdmlKRGIgytpENR------KEAGI 351
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--------HRSI----QQRdicmvfQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 IPWLGVDENTVLTNR-QKISAngvlqwstirrltEEVMQRmtVKAASS--------ETPIGTLSGGNQQKVVIGRWVYAA 422
Cdd:PRK11432 90 FPHMSLGENVGYGLKmLGVPK-------------EERKQR--VKEALElvdlagfeDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHGTFSQ 484
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQ 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
272-481 |
4.34e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 272 LRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIvingekitrpdygdMLKRGIGYTPENrkeagi 351
Cdd:PTZ00243 670 LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERSIAYVPQQ------ 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 iPWL---GVDENTVLTNRQKISAngvLQwSTIR--RLTEEVMQRmtvkAASSETPIG----TLSGGNQQKVVIGRWVYAA 422
Cdd:PTZ00243 730 -AWImnaTVRGNILFFDEEDAAR---LA-DAVRvsQLEADLAQL----GGGLETEIGekgvNLSGGQKARVSLARAVYAN 800
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 423 SQILLLDEPTRGVDIEAKQqiyRIVREL---AAEGKSVVFISSEVEELPLVcDRILLLQHGT 481
Cdd:PTZ00243 801 RDVYLLDDPLSALDAHVGE---RVVEECflgALAGKTRVLATHQVHVVPRA-DYVVALGDGR 858
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-67 |
5.08e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 5.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 2 FTATEAVP-----VAKVVAGnkrYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI 67
Cdd:PRK10636 302 FRAPESLPnpllkMEKVSAG---YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
271-481 |
5.56e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 271 ALRHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVG-LEEYE-------QGEIVINGEKITRPDyGDMLKRGIGYT 342
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAID-APRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 343 PENRKEAgiIPWlGVDENTVLTNRQKISANGVLQwstirRLTEEVMQRMTVKAASSE---TPIGTLSGGNQQKVVIGR-- 417
Cdd:PRK13547 89 PQAAQPA--FAF-SAREIVLLGRYPHARRAGALT-----HRDGEIAWQALALAGATAlvgRDVTTLSGGELARVQFARvl 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 418 ---WVYAASQI----LLLDEPTRGVDIEAKQQIYRIVRELAAEGK-SVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:PRK13547 161 aqlWPPHDAAQppryLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAARHADRIAMLADGA 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
278-480 |
5.83e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.16 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPdygdmLKRgIGYTPENRKEAGII---PW 354
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAN-----LKK-IKEVKRLRKEIGLVfqfPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTNRQ----KISANGVLQWSTIRRLTEEV-MQRMTVKAASSEtpigtLSGGNQQKVVIGRWVYAASQILLLD 429
Cdd:PRK13645 101 YQLFQETIEKDIAfgpvNLGENKQEAYKKVPELLKLVqLPEDYVKRSPFE-----LSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1314860479 430 EPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-227 |
8.86e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.57 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTG----SERPdSGDIWIGEtrLEGDEATLTRRAaelgvRAVY--QELSL 99
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSV-EGDIHYNG--IPYKEFAEKYPG-----EIIYvsEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 100 VEGLTVAENLclgqwprrngmiDYlqmaqdAQRCLQalgvdvspEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSS 179
Cdd:cd03233 95 FPTLTVRETL------------DF------ALRCKG--------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 180 LASAEVELVISAVKKMS-ALG-VAVIYVSHRMEEIRRIASCATVMRDGQV 227
Cdd:cd03233 149 LDSSTALEILKCIRTMAdVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-180 |
9.50e-07 |
|
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: 49.64 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 21 PGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQELSLV 100
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGlTVAENLCLGQwP----RRNGMIDYLQMAQDAQrcLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEP 176
Cdd:cd03290 92 NA-TVEENITFGS-PfnkqRYKAVTDACSLQPDID--LLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
....
gi 1314860479 177 TSSL 180
Cdd:cd03290 168 FSAL 171
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
273-480 |
9.84e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.17 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 273 RHKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRpdygdmlkrgigYTPEN-RKEAGI 351
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD------------YTLASlRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 ipwlgVDENTVLTNrqKISANGVLQWSTIRRLTEEVMQRMTVKAASS---------ETPIG----TLSGGNQQKVVIGRW 418
Cdd:PRK11176 422 -----VSQNVHLFN--DTIANNIAYARTEQYSREQIEEAARMAYAMDfinkmdnglDTVIGengvLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 419 VYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEgKSVVFIS---SEVEElplvCDRILLLQHG 480
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAhrlSTIEK----ADEILVVEDG 554
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
279-453 |
1.06e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.98 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 279 EDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgIGYTPENRKEAGIIpwlgvd 358
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGDI------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 359 enTVltnrQKISANG-------VLQWstiRRLTEEVM---QRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAASQILLL 428
Cdd:PRK10253 97 --TV----QELVARGryphqplFTRW---RKEDEEAVtkaMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180
....*....|....*....|....*
gi 1314860479 429 DEPTRGVDIEAKQQIYRIVRELAAE 453
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNRE 192
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-67 |
1.38e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 1.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI 67
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-75 |
1.43e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 1.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 17 NKRYPGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGeTRLE 75
Cdd:PRK11147 326 NYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-TKLE 383
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
275-461 |
1.61e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.80 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVG-LEEYEQ--GEIVINGekITRPDYGDMLKRGIGYTPENrkeagi 351
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrTEGNVSveGDIHYNG--IPYKEFAEKYPGEIIYVSEE------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 ipwlgvDE-NTVLTNRQKISANGVLQWSTIRRlteevmqrmtvkaassetpigTLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:cd03233 92 ------DVhFPTLTVRETLDFALRCKGNEFVR---------------------GISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190
....*....|....*....|....*....|.
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELAAEGKSVVFIS 461
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
276-461 |
1.63e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKIT--------RPDYG---DMLKRGIGYTPE 344
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVarlqqdppRNVEGtvyDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 345 NRKE-AGIIPWLGVDENTVLTNR-QKISAngVLQWSTIRRLTEEVMQRMTVKAASSETPIGTLSGGNQQKVVIGRWVYAA 422
Cdd:PRK11147 97 YLKRyHDISHLVETDPSEKNLNElAKLQE--QLDHHNLWQLENRINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1314860479 423 SQILLLDEPTRGVDIEAKQQIYRIVRELAAegkSVVFIS 461
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFIS 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
275-484 |
1.72e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.49 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPD-----------------YGDMLKR 337
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhrqvalvgqepvlFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 338 GIGY----TPENR-----KEAGIIPWLGVDENTVLTNrqkISANGVLqwstirrlteevmqrmtvkaassetpigtLSGG 408
Cdd:TIGR00958 574 NIAYgltdTPDEEimaaaKAANAHDFIMEFPNGYDTE---VGEKGSQ-----------------------------LSGG 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 409 NQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYrivRELAAEGKSVVFISsevEELPLV--CDRILLLQHGTFSQ 484
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ---ESRSRASRTVLLIA---HRLSTVerADQILVLKKGSVVE 693
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-214 |
1.73e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 17 NKRY---PGVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTG-----------SERPDSGDIwIGETRLEGDEA--- 79
Cdd:PTZ00265 1172 NFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivFKNEHTNDM-TNEQDYQGDEEqnv 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 80 --------TLTRRAAELGVRAVYQELS--LVEGLTVAE-------NL--CLGQWPRRNGMIDYLQMA--------QDAQR 132
Cdd:PTZ00265 1251 gmknvnefSLTKEGGSGEDSTVFKNSGkiLLDGVDICDynlkdlrNLfsIVSQEPMLFNMSIYENIKfgkedatrEDVKR 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 133 CLQALGVDVSPEQLVS-----------TLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAE---VELVISAVKKMSal 198
Cdd:PTZ00265 1331 ACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeklIEKTIVDIKDKA-- 1408
|
250
....*....|....*.
gi 1314860479 199 GVAVIYVSHRMEEIRR 214
Cdd:PTZ00265 1409 DKTIITIAHRIASIKR 1424
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-215 |
1.88e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLtgSERPDSGDIWIGETRLEGDE--ATLTRRAAelgvrAVYQELSLVE 101
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVITGGDRLVNGRPldSSFQRSIG-----YVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 102 GLTVAENLCLGQWPRR-------------NGMIDYLQMAQDAQRCLQALGVDVSPEQlvstlspaQKQL---VEIArvmk 165
Cdd:TIGR00956 850 TSTVRESLRFSAYLRQpksvsksekmeyvEEVIKLLEMESYADAVVGVPGEGLNVEQ--------RKRLtigVELV---- 917
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 166 GEPRVVI-LDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHR-----MEEIRRI 215
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsailFEEFDRL 973
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
278-461 |
2.67e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.11 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDyGDMLKRgigytpENRKEAGIIpWLGV 357
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD-ADALAQ------LRREHFGFI-FQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTNRQKISANGV---LQWSTIRRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:PRK10535 96 HLLSHLTAAQNVEVPAVyagLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180
....*....|....*....|....*..
gi 1314860479 435 VDIEAKQQIYRIVRELAAEGKSVVFIS 461
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDRGHTVIIVT 201
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
275-480 |
2.94e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.96 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGE---KITRPDygdmLKRGIGYTpenRKEAGi 351
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirTVTRAS----LRRNIAVV---FQDAG- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 352 ipwlgvdentvLTNRQkISANgvlqwstIR----RLTEEVMQRMTVKAASSE----------TPIG----TLSGGNQQKV 413
Cdd:PRK13657 420 -----------LFNRS-IEDN-------IRvgrpDATDEEMRAAAERAQAHDfierkpdgydTVVGergrQLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 414 VIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELaAEGKSVVFIS---SEVEElplvCDRILLLQHG 480
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAhrlSTVRN----ADRILVFDNG 545
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
278-480 |
2.94e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEkitrpdygdmlkrgigytpenrkeAGIIPwLGV 357
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS------------------------AALIA-ISS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 358 DENTVLTNRQKISANGVLQWST---IRRLTEEVMQRMTVKAASSEtPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRG 434
Cdd:PRK13545 95 GLNGQLTGIENIELKGLMMGLTkekIKEIIPEIIEFADIGKFIYQ-PVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314860479 435 VDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13545 174 GDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-227 |
3.47e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTL----IRMLTgserpDSGDIWIgeTRLEGDEATLTRRAAELGVraVYQEL 97
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQI--DGVSWNSVPLQKWRKAFGV--IPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 98 SLVEGlTVAENL-CLGQWPRRngmiDYLQMAQDAQrcLQALgVDVSPEQLVSTL-------SPAQKQLVEIARVMKGEPR 169
Cdd:cd03289 87 FIFSG-TFRKNLdPYGKWSDE----EIWKVAEEVG--LKSV-IEQFPGQLDFVLvdggcvlSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 170 VVILDEPTSSLASAEVElVISAVKKMSALGVAVIYVSHRMEEIRRIAScATVMRDGQV 227
Cdd:cd03289 159 ILLLDEPSAHLDPITYQ-VIRKTLKQAFADCTVILSEHRIEAMLECQR-FLVIEENKV 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
267-481 |
3.56e-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: 47.32 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 267 LEVRALRHKpKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVgleeYEQGEIVINGekiTRPDYGD-----------ML 335
Cdd:cd03238 1 LTVSGANVH-NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLIS---FLPKFSRnklifidqlqfLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 336 KRGIGYTPENRkeagiipwlgvdentvltnrqkisangvlqwstirrlteevmqrmtvkaassetPIGTLSGGNQQKVVI 415
Cdd:cd03238 73 DVGLGYLTLGQ------------------------------------------------------KLSTLSGGELQRVKL 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 416 GRWVYAASQ--ILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLvCDRILLLQHGT 481
Cdd:cd03238 99 ASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
276-480 |
3.92e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.59 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKrgigytpENRKEAGII--- 352
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIK-------QIRKKVGLVfqf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 PWLGVDENTVLTNRQKISAN-GVLQWSTIRRLTEEVMQRMTVKAASSETPIgTLSGGNQQKVVIGRWVYAASQILLLDEP 431
Cdd:PRK13649 94 PESQLFEETVLKDVAFGPQNfGVSQEEAEALAREKLALVGISESLFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 432 TRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-298 |
7.52e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 23 VVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERpdsgDIW-IGETRLEGDEATLTRRAAELGVRAVYQELSLV- 100
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK----DNWrVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 ----EGLTVAENLCL------------GQWPRRNGMidylqMAQDAQRCLQALGVDVSPEQLVS---TLSPAQKQLVEIA 161
Cdd:PRK15093 96 qepqSCLDPSERVGRqlmqnipgwtykGRWWQRFGW-----RKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 162 RVMKGEPRVVILDEPTSSLAS---AEVELVISAVKKMSalGVAVIYVSHRMEEIRRIASCATVMRDGQVagdvmLENTST 238
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPttqAQIFRLLTRLNQNN--NTTILLISHDLQMLSQWADKINVLYCGQT-----VETAPS 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1314860479 239 HHIVslmlgrdhvdiapVAPQEIVDQAVLEV-----RALRHKPKLEDISFTLRRGEVLGIAGLLG 298
Cdd:PRK15093 244 KELV-------------TTPHHPYTQALIRAipdfgSAMPHKSRLNTLPGAIPLLEHLPIGCRLG 295
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
28-207 |
9.74e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 28 NVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRlegdeatlTRRAAELGVRAVYQELSLVEGLTVAE 107
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCN--------INNIAKPYCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 108 NLCLgqWPRRNGMIDYLQMAQDAQRCLQALgvdvspEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVEL 187
Cdd:PRK13541 90 NLKF--WSEIYNSAETLYAAIHYFKLHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|
gi 1314860479 188 VISAVKKMSALGVAVIYVSH 207
Cdd:PRK13541 162 LNNLIVMKANSGGIVLLSSH 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-211 |
1.05e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGS-------------ERPDSGD-IW-----IG--ETRLEGDEATLTRr 84
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgRRRGSGEtIWdikkhIGyvSSSLHLDYRVSTS- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 85 aaelgVRAV-----------YQELSlvegltvaenlclgqwprrngmiDYLQmaQDAQRCLQALGVDV----SPEQlvsT 149
Cdd:PRK10938 355 -----VRNVilsgffdsigiYQAVS-----------------------DRQQ--KLAQQWLDILGIDKrtadAPFH---S 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 150 LSPAQKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALG-VAVIYVSHRMEE 211
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGeTQLLFVSHHAED 464
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
405-489 |
1.25e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 405 LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVFISSEVEELPLVCDRILLLQHG--- 480
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGrcv 236
|
90
....*....|..
gi 1314860479 481 ---TFSQEFHAP 489
Cdd:PRK15134 237 eqnRAATLFSAP 248
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-228 |
1.25e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.78 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RYPGVV--ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetRLEGDEATLTRRAAELGVRAVYQE 96
Cdd:PRK10789 322 TYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI-----RFHDIPLTKLQLDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGLTVAENLCLGQWPRRNGMIDYL-QMA---QDAQRCLQALGVDVSpEQLVsTLSPAQKQLVEIARVMKGEPRVVI 172
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDATQQEIEHVaRLAsvhDDILRLPQGYDTEVG-ERGV-MLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 173 LDEPTSSLASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRRiASCATVMRDGQVA 228
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHGHIA 528
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
276-478 |
1.33e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGdmlkRGIGYTpenrkeaGIIPWL 355
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS----RFMAYL-------GHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 GVDENTvLTNRQKISAngvLQWSTIRRLTEEVMQRMTVkAASSETPIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGV 435
Cdd:PRK13543 94 KADLST-LENLHFLCG---LHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314860479 436 DIEAKQQIYRIVR-ELAAEGKSVVFISSEVEELPlVCDRILLLQ 478
Cdd:PRK13543 169 DLEGITLVNRMISaHLRGGGAALVTTHGAYAAPP-VRTRMLTLE 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
286-474 |
1.57e-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: 46.59 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 286 RRGEVLGIAGLLGAGRSELLKAIVG------------------LEEYEQGEI------VINGE--KITRPDYGDMLKRGI 339
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEFRGSELqnyftkLLEGDvkVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 340 -GYTPENRKEagiipwlgVDENTVLtnrqkisangvlqwstirrltEEVMQRMTVKAASsETPIGTLSGGNQQKVVIGRW 418
Cdd:cd03236 104 kGKVGELLKK--------KDERGKL---------------------DELVDQLELRHVL-DRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 419 VYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRI 474
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
254-480 |
1.70e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.51 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 254 APVAPQEIVDQAVLEVRALR-----HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITr 328
Cdd:COG5265 345 APDAPPLVVGGGEVRFENVSfgydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 329 pdygdmlkrgiGYTPEN-RKEAGIIPwlgvdENTVLTNrqkisangvlqwSTIR------RLT---EEVMQrmTVKAAS- 397
Cdd:COG5265 424 -----------DVTQASlRAAIGIVP-----QDTVLFN------------DTIAyniaygRPDaseEEVEA--AARAAQi 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 398 ----------SETPIG----TLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRElAAEGKSVVFI--- 460
Cdd:COG5265 474 hdfieslpdgYDTRVGerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIahr 552
|
250 260
....*....|....*....|.
gi 1314860479 461 -SSEVEelplvCDRILLLQHG 480
Cdd:COG5265 553 lSTIVD-----ADEILVLEAG 568
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-69 |
2.05e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 2.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1314860479 25 ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWI 69
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-238 |
2.09e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 4 ATEAVPVAKVVagnKRYPGVVALDNVNFTLNKGEVRALLGKNGAG--KSTLIRMLTGSE---RPDSGDIWIGETRlegde 78
Cdd:NF000106 10 ARNAVEVRGLV---KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 79 aTLTR-----RAAELGVRavyqelslvEGLTVAENLCLgqwPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLVSTLSPA 153
Cdd:NF000106 82 -ALRRtig*hRPVR*GRR---------ESFSGRENLYM---IGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 154 QKQLVEIARVMKGEPRVVILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIRRIASCATVMRDGQVAGDVML 233
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
....*
gi 1314860479 234 ENTST 238
Cdd:NF000106 229 DELKT 233
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-328 |
2.76e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 141 VSPEQLVSTLSPAQKQLVEIARVMKGEPRVV--ILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHrmeEIRRIASC 218
Cdd:PRK00635 468 LTPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH---DEQMISLA 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 219 ATVM----RDGQVAGDVMLENT------STHHIVSLMLGRD-HVDIaPVAPQEIVDQAVLEvRALRHkpKLEDISFTLRR 287
Cdd:PRK00635 545 DRIIdigpGAGIFGGEVLFNGSpreflaKSDSLTAKYLRQElTIPI-PEKRTNSLGTLTLS-KATKH--NLKDLTISLPL 620
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1314860479 288 GEVLGIAGLLGAGRSELLK--AIVGLEEYEQGE----IVINGEKITR 328
Cdd:PRK00635 621 GRLTVVTGVSGSGKSSLINdtLVPAVEEFIEQGfcsnLSIQWGAISR 667
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
278-481 |
3.27e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.78 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGDMLKRgigytpeNRKEAGII---PW 354
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKP-------LRKKVGIVfqfPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDENTVLTNRQKISAN-GVLQWSTIRR---------LTEEVMQRmtvkaasseTPIgTLSGGNQQKVVIGRWVYAASQ 424
Cdd:PRK13634 96 HQLFEETVEKDICFGPMNfGVSEEDAKQKaremielvgLPEELLAR---------SPF-ELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 425 ILLLDEPTRGVDIEAKQQI----YRIVRElaaEGKSVVFISSEVEELPLVCDRILLLQHGT 481
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMmemfYKLHKE---KGLTTVLVTHSMEDAARYADQIVVMHKGT 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-214 |
3.41e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 45.62 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetrlegdeatltrraAELGVRAVYQELSLVEGLTV 105
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------------KHSGRISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 AENLCLG---QWPRRNGMIDYLQMAQDAQRCLQALGVDVSPEQLvsTLSPAQKQLVEIARVMKGEPRVVILDEPTSSL-A 181
Cdd:cd03291 115 KENIIFGvsyDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGI--TLSGGQRARISLARAVYKDADLYLLDSPFGYLdV 192
|
170 180 190
....*....|....*....|....*....|...
gi 1314860479 182 SAEVELVISAVKKMSAlGVAVIYVSHRMEEIRR 214
Cdd:cd03291 193 FTEKEIFESCVCKLMA-NKTRILVTSKMEHLKK 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
255-480 |
4.41e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 255 PVAPQEIVDQAVLEVRALRHKPK---LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVG-LEEYE---QGEIVINGekIT 327
Cdd:TIGR00956 51 PNALLKILTRGFRKLKKFRDTKTfdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHigvEGVITYDG--IT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 328 RPDYGDMLKRGIGYTPENRKEagiIPWLGVDENTVLTNRQKISAN---GVLQWSTIRRLTEEVMQRMTVkAASSETPIGT 404
Cdd:TIGR00956 129 PEEIKKHYRGDVVYNAETDVH---FPHLTVGETLDFAARCKTPQNrpdGVSREEYAKHIADVYMATYGL-SHTRNTKVGN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 405 -----LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFI-----SSEVEELplvCDRI 474
Cdd:TIGR00956 205 dfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaiyqcSQDAYEL---FDKV 281
|
....*.
gi 1314860479 475 LLLQHG 480
Cdd:TIGR00956 282 IVLYEG 287
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
381-499 |
6.17e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 381 RRLTEEVMQRMTVKAASSETPiGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFI 460
Cdd:NF000106 122 RARADELLERFSLTEAAGRAA-AKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|....*....
gi 1314860479 461 SSEVEELPLVCDRILLLQHGtfsqEFHAPVNVDELMSAI 499
Cdd:NF000106 201 TQYMEEAEQLAHELTVIDRG----RVIADGKVDELKTKV 235
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-92 |
6.20e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 6.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 33 LNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI-WIGET--------RLEGDEATLTRRAAELGVRA 92
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDeWDGITpvykpqyiDLSGGELQRVAIAAALLRNA 90
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
278-480 |
6.63e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 44.73 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITrpdygdmlkrgigytPEN----RKEAGII- 352
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---------------AENekwvRSKVGLVf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 353 --PWLGVDENTVLTNRQKISANGVLQWSTIRRLTEEVMQRMTVKAASSETPIgTLSGGNQQKVVIGRWVYAASQILLLDE 430
Cdd:PRK13647 86 qdPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPY-HLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1314860479 431 PTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-214 |
8.60e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.29 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIwigetrlegdeatltrraAELGVRAVYQELSLVEGLTV 105
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------------KHSGRISFSPQTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 AENLCLG---QWPRRNGMIDYLQMAQDaqrclqalgVDVSPEQLVS-------TLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:TIGR01271 504 KDNIIFGlsyDEYRYTSVIKACQLEED---------IALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1314860479 176 PTSSL-ASAEVELVISAVKKMSAlGVAVIYVSHRMEEIRR 214
Cdd:TIGR01271 575 PFTHLdVVTEKEIFESCLCKLMS-NKTRILVTSKLEHLKK 613
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
405-477 |
1.04e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1314860479 405 LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLL 477
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-190 |
1.05e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDS--GDIWIGETRLEgdEATLTRRAAelgvraVYQELSLVEGL 103
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQILKRTGF------VTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 104 TVAENL---CLGQWPRRNGMIDYLQMAQD--AQRCLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:PLN03211 156 TVRETLvfcSLLRLPKSLTKQEKILVAESviSELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170
....*....|...
gi 1314860479 179 SL-ASAEVELVIS 190
Cdd:PLN03211 236 GLdATAAYRLVLT 248
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-67 |
1.16e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDI 67
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSY 58
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
263-480 |
1.56e-04 |
|
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: 44.29 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 263 DQAVLEVRALR--------HKPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGL----EEYEQGEIVINGEKITRPD 330
Cdd:COG4172 3 SMPLLSVEDLSvafgqgggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 331 YGDMLK-RGigytpenrKEAGII---PwlgvdentvLTnrqkiSANGVLqwsTIRRLTEEVM---QRMTVKAASS----- 398
Cdd:COG4172 83 ERELRRiRG--------NRIAMIfqeP---------MT-----SLNPLH---TIGKQIAEVLrlhRGLSGAAARAralel 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 399 ---------ETPIGT----LSGGNQQKVVIgrwvyAAS-----QILLLDEPTRGVDIEAKQQIYRIVRELAAE-GKSVVF 459
Cdd:COG4172 138 lervgipdpERRLDAyphqLSGGQRQRVMI-----AMAlanepDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLL 212
|
250 260
....*....|....*....|....
gi 1314860479 460 ISsevEELPLV---CDRILLLQHG 480
Cdd:COG4172 213 IT---HDLGVVrrfADRVAVMRQG 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
278-480 |
1.91e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 278 LEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVI---NGEKITRPDYGDML----------KRGIGYTPE 344
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVleklviqktrFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 345 NRKEAGII--------------------PW-LGVDENTVLTNRQK-ISANGvlqwstirrLTEEVMQRmtvkaasseTPI 402
Cdd:PRK13651 103 IRRRVGVVfqfaeyqlfeqtiekdiifgPVsMGVSKEEAKKRAAKyIELVG---------LDESYLQR---------SPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1314860479 403 GtLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFISSEVEELPLVCDRILLLQHG 480
Cdd:PRK13651 165 E-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
275-480 |
2.41e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.55 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 275 KPKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDYGdMLKRGIGYTPENrkeagiiPW 354
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQGVAMVQQD-------PV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 355 LGVDenTVLTN---RQKISANGVlqWSTIrrlteEVMQRMTVKAASSE---TPIG----TLSGGNQQKVVIGRWVYAASQ 424
Cdd:PRK10790 426 VLAD--TFLANvtlGRDISEEQV--WQAL-----ETVQLAELARSLPDglyTPLGeqgnNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1314860479 425 ILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVF---ISSEVEelplvCDRILLLQHG 480
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIahrLSTIVE-----ADTILVLHRG 550
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
385-498 |
3.28e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 385 EEVMQRMTVKAASSETPIG-TLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEG-KSVVFISS 462
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVGPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAH 1417
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1314860479 463 EVEELPLvCDRILLLQH----GTFSQefhAPVNVDELMSA 498
Cdd:PTZ00265 1418 RIASIKR-SDKIVVFNNpdrtGSFVQ---AHGTHEELLSV 1453
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-180 |
3.48e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGdiwigetrlegdeATLTRRaaelGVRAVYQELSLVEGLTV 105
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-------------ASVVIR----GTVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 AENLCLG---QWPRRNGMIDYLQMAQDaqrcLQAL-GVDVSP--EQLVStLSPAQKQLVEIARVMKGEPRVVILDEPTSS 179
Cdd:PLN03130 696 RDNILFGspfDPERYERAIDVTALQHD----LDLLpGGDLTEigERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
.
gi 1314860479 180 L 180
Cdd:PLN03130 771 L 771
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-216 |
3.61e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLT-----GSERPDSGDIWIGETRLEGDEATLTRRAAELGVraVYQELSLV 100
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLFGRNIYSPDVDPIEVRREVGM--VFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 101 EGLTVAENLCLGQwpRRNGMI-DYLQMAQDAQRCLQ--ALGVDVSP--EQLVSTLSPAQKQLVEIARVMKGEPRVVILDE 175
Cdd:PRK14267 98 PHLTIYDNVAIGV--KLNGLVkSKKELDERVEWALKkaALWDEVKDrlNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1314860479 176 PTSSL---ASAEVELVISAVKKmsalGVAVIYVSHRMEEIRRIA 216
Cdd:PRK14267 176 PTANIdpvGTAKIEELLFELKK----EYTIVLVTHSPAQAARVS 215
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
405-484 |
4.92e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 405 LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEG-KSVVFISSEVEELPLVCDRILLLQ----- 478
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVFEgepgv 151
|
....*.
gi 1314860479 479 HGTFSQ 484
Cdd:cd03222 152 YGIASQ 157
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
405-477 |
6.40e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.81 E-value: 6.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1314860479 405 LSGGNQQKVVIGRWVyaASQ--ILLLDEPTRGVDIEAKQQIYRIVRELAA-EGKSVVFISSEVEELPLVCDRILLL 477
Cdd:COG4170 159 LTEGECQKVMIAMAI--ANQprLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
281-489 |
9.79e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 281 ISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEqGEIVINGEKITRPDYGDMLKRgigytpENRKEAGI-IPWLGVDE 359
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNGQDLQRISEK------ERRNLVGAeVAMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 360 NTVLT-----NRQKISANGVLQW---STIRRLTEEVMQRMTVKAASSETPI--GTLSGGNQQKVVIGRWVYAASQILLLD 429
Cdd:PRK11022 99 MTSLNpcytvGFQIMEAIKVHQGgnkKTRRQRAIDLLNQVGIPDPASRLDVypHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 430 EPTRGVDIEAKQQIYRIVRELA-AEGKSVVFISSEVEELPLVCDRILLL------QHGTFSQEFHAP 489
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMyagqvvETGKAHDIFRAP 245
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
276-497 |
1.58e-03 |
|
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: 40.22 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 276 PKLEDISFTLRRGEVLGIAGLLGAGRSELLKAIVGLEEYEQGEIVINGEKITRPDygdmlkrgigytpenrkeagiIPWL 355
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---------------------LRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 356 gvdentvltnRQKI---SANGVLQWSTIR--------RLTEEVMQRMTVKAASSE----------TPIG----TLSGGNQ 410
Cdd:cd03249 76 ----------RSQIglvSQEPVLFDGTIAenirygkpDATDEEVEEAAKKANIHDfimslpdgydTLVGergsQLSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 411 QKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVrELAAEGKSVVFIS---SEVEElplvCDRILLLQHGTFSQE-F 486
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAhrlSTIRN----ADLIAVLQNGQVVEQgT 220
|
250
....*....|.
gi 1314860479 487 HapvnvDELMS 497
Cdd:cd03249 221 H-----DELMA 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
405-486 |
1.64e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.89 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 405 LSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRElaaegKSVVFISseveelplVCDRILLLQHGTFSQ 484
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE-----FGITLFS--------VSHRKSLWKYHEYLL 649
|
..
gi 1314860479 485 EF 486
Cdd:TIGR00954 650 YM 651
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
401-482 |
1.71e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 401 PIGTLSGGNQQKVVIGRWVYAASQILLLDEPTRGVDIEAkqqIYRIVRELAAEGKSVV-------FISSEVEELPLVCDR 473
Cdd:PLN03073 624 PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQGGVLmvshdehLISGSVDELWVVSEG 700
|
....*....
gi 1314860479 474 ILLLQHGTF 482
Cdd:PLN03073 701 KVTPFHGTF 709
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-208 |
2.28e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.50 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 22 GVVALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLtgserpdsGDIW--IGETRLEGDEATL------------TRR--- 84
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELWpvYGGRLTKPAKGKLfyvpqrpymtlgTLRdqi 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 85 ----AAELGVRAVYQELSLVEGLtvaENLCLGQWPRRNGMIDYLQMAQDaqrclqalgvdvspeqlvsTLSPAQKQLVEI 160
Cdd:TIGR00954 536 iypdSSEDMKRRGLSDKDLEQIL---DNVQLTHILEREGGWSAVQDWMD-------------------VLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1314860479 161 ARVMKGEPRVVILDEPTSSLaSAEVELVI-SAVKKMsalGVAVIYVSHR 208
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAV-SVDVEGYMyRLCREF---GITLFSVSHR 638
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-243 |
2.36e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.73 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 19 RY-PGVV-ALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDIWIGETRLEGDEATLTRRAAELgvraVYQE 96
Cdd:PLN03232 1243 RYrPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSI----IPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 97 LSLVEGlTVAENLCLGQWPRRNGMIDYLQMA--QDAQRcLQALGVDVSPEQLVSTLSPAQKQLVEIARVMKGEPRVVILD 174
Cdd:PLN03232 1319 PVLFSG-TVRFNIDPFSEHNDADLWEALERAhiKDVID-RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1314860479 175 EPTSSLaSAEVELVISAVKKMSALGVAVIYVSHRMEEirrIASC--ATVMRDGQVagdvmLENTSTHHIVS 243
Cdd:PLN03232 1397 EATASV-DVRTDSLIQRTIREEFKSCTMLVIAHRLNT---IIDCdkILVLSSGQV-----LEYDSPQELLS 1458
|
|
| SiR |
cd06199 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
61-211 |
4.12e-03 |
|
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain.
Pssm-ID: 99796 [Multi-domain] Cd Length: 360 Bit Score: 39.52 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 61 RPDSGDIWIGETRLEGDEATLTRRAAELGVRAVYQE--------LSLVEG-------LTVAENLCLGQWPRRNGMIDYLQ 125
Cdd:cd06199 44 DPALVDELLAALGLSGDEPVSTVGGGTLPLREALIKhyeittllLALLESyaadtgaLELLALAALEAVLAFAELRDVLD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 126 MaqdaqrcLQALGVDVSPEQLVSTLSPAQKQLVEIArvmkgeprvvildeptSSLASA--EVELVISAVKKMSA----LG 199
Cdd:cd06199 124 L-------LPIPPARLTAEELLDLLRPLQPRLYSIA----------------SSPKAVpdEVHLTVAVVRYESHgrerKG 180
|
170
....*....|..
gi 1314860479 200 VAVIYVSHRMEE 211
Cdd:cd06199 181 VASTFLADRLKE 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-213 |
4.54e-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: 38.78 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSErpdsgdiwiGETR-LEGDEATLTRRAAELGVRAVyqelSLVEGLT 104
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAE---------GQRRyVESLSAYARQFLGQMDKPDV----DSIEGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 105 VA---ENLCLGQWPRRN-----GMIDYLQM--AQDAQRC----LQALGVD-VSPEQLVSTLSPAQKQLVEIARVMKGEPR 169
Cdd:cd03270 78 PAiaiDQKTTSRNPRSTvgtvtEIYDYLRLlfARVGIRErlgfLVDVGLGyLTLSRSAPTLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1314860479 170 VV--ILDEPTSSLASAEVELVISAVKKMSALGVAVIYVSHRMEEIR 213
Cdd:cd03270 158 GVlyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR 203
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
24-108 |
4.70e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 38.50 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 24 VALDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPDSGDiWIGetrLEGDeatltrrAAELGVRAVyqelsLVEGL 103
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGD-FIG---LRGD-------ALPLGANSF-----ILPGL 64
|
....*
gi 1314860479 104 TVAEN 108
Cdd:PRK15177 65 TGEEN 69
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-60 |
4.92e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.62 E-value: 4.92e-03
10 20 30
....*....|....*....|....*....|....*
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSE 60
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE 51
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-209 |
5.27e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 26 LDNVNFTLNKGEVRALLGKNGAGKSTLIRMLTGSERPdsgdiwigetrleGDEATLTRRaaelGVRAVYQELSLVEGLTV 105
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-------------AETSSVVIR----GSVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 106 AENLCLGQ--WPRRNG-MIDYLQMAQD----AQRCLQALGvdvspEQLVStLSPAQKQLVEIARVMKGEPRVVILDEPTS 178
Cdd:PLN03232 696 RENILFGSdfESERYWrAIDVTALQHDldllPGRDLTEIG-----ERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190
....*....|....*....|....*....|.
gi 1314860479 179 SLASAEVELVISAVKKMSALGVAVIYVSHRM 209
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQL 800
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
394-468 |
6.47e-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: 37.34 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314860479 394 KAASSETPIGT---LSGGNQQKV----VIGRWVYAASQILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVVFIS--SEV 464
Cdd:cd03227 64 VAAVSAELIFTrlqLSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIThlPEL 143
|
....
gi 1314860479 465 EELP 468
Cdd:cd03227 144 AELA 147
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
425-480 |
7.64e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.94 E-value: 7.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1314860479 425 ILLLDEPTRGVDIEAKQQIYRIVRELAAEGKSVV-FISSEVEELPLVCDRILLLQHG 480
Cdd:TIGR00956 923 LLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILcTIHQPSAILFEEFDRLLLLQKG 979
|
|
| |
