|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-526 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 633.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDLDGNLSVFE 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 AVLSSETSTLQIIKHYEQAVQQYtvEQTDRNFQAMMAAQEAMDRHEAWDYNAEIKTILSKLGIH--DTTKQVNSLSGGQQ 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKL--AEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPeeDLDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGNYEDYI 243
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 244 AMRAEKEVIEQKQNDKQRALYKQELAWM-RAGAKAR-STKQQARIHRFNDLEANVKQqqtQDKGELNL---AYSRLGKQV 318
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIrRFRAKARkAKQAQSRIKALEKLEREEPP---RRDKTVEIrfpPPERLGKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 319 YELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEETLNRDIR 398
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIDYLREESEvakekDGTTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTI 478
Cdd:COG0488 396 VLDELRDGAP-----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488422749 479 LEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMMERIVGSFEDYE 526
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYL 518
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-531 |
1.11e-145 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 433.39 E-value: 1.11e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 4 YKIEHLNKSY-ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDLDGNLS 82
Cdd:PRK11819 7 YTMNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETSTLQIIKHYEQAVQQYTVEQTDrnFQAMMAA----QEAMDRHEAWDYNAEIKTILSKLGIHDTTKQVNSL 158
Cdd:PRK11819 87 VRENVEEGVAEVKAALDRFNEIYAAYAEPDAD--FDALAAEqgelQEIIDAADAWDLDSQLEIAMDALRCPPWDAKVTKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGN 238
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 239 YEDYIAMRAEKEVIEQKQNDK-QRALyKQELAWMRAGAKARSTKQQARIHRFNDLeANVKQQQTQDKGELNL-AYSRLGK 316
Cdd:PRK11819 245 YSSWLEQKAKRLAQEEKQEAArQKAL-KRELEWVRQSPKARQAKSKARLARYEEL-LSEEYQKRNETNEIFIpPGPRLGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 317 QVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEETLNRD 396
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 397 IRMIDylreesEVAKEKD-----GTTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:PRK11819 403 KTVWE------EISGGLDiikvgNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 472 DTETLTILEDYIASFGGSVITVSHDRYFLNKVA----------QEYWFihdgmmErivGSFEDYETYKKE 531
Cdd:PRK11819 477 DVETLRALEEALLEFPGCAVVISHDRWFLDRIAthilafegdsQVEWF------E---GNFQEYEEDKKR 537
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-532 |
5.33e-145 |
|
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: 431.67 E-value: 5.33e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 4 YKIEHLNKSY-ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDLDGNLS 82
Cdd:TIGR03719 5 YTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETSTLQIIKHYEQAVQQYTVEQTDRN--FQAMMAAQEAMDRHEAWDYNAEIKTILSKLGIHDTTKQVNSLSG 160
Cdd:TIGR03719 85 VRENVEEGVAEIKDALDRFNEISAKYAEPDADFDklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGNYE 240
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 241 DYIAMRAEKEVIEQKQNDK-QRALyKQELAWMRAGAKARSTKQQARIHRFNDLEANVKQQQTQDK------GElnlaysR 313
Cdd:TIGR03719 245 SWLEQKQKRLEQEEKEESArQKTL-KRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNETAeiyippGP------R 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 314 LGKQVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEETL 393
Cdd:TIGR03719 318 LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRDIRMIDylreesEVAKEKD-----GTTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:TIGR03719 398 DPNKTVWE------EISGGLDiiklgKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 469 NDLDTETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYW-FIHDGMMERIVGSFEDYETYKKEK 532
Cdd:TIGR03719 472 NDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILaFEGDSHVEWFEGNFSEYEEDKKRR 536
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-626 |
8.13e-138 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 416.27 E-value: 8.13e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 12 SYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG---IDD---DFTGDIThpnqyrirYSSQKQDLDGNL--SV 83
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDgriIYEQDLI--------VARLQQDPPRNVegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEAVLSSETSTLQIIKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRHEAWDYNAEIKTILSKLGIhDTTKQVNSLSGGQQ 163
Cdd:PRK11147 84 YDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGL-DPDAALSSLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGNYEDYI 243
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 244 AMRAEKEVIEQKQN---DKQRAlykQELAWMRAGAKARSTKQQARIHRFNDL-EANVKQQQTQDKGELNLA-YSRLGKQV 318
Cdd:PRK11147 243 LEKEEALRVEELQNaefDRKLA---QEEVWIRQGIKARRTRNEGRVRALKALrRERSERREVMGTAKMQVEeASRSGKIV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 319 YELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEETLNRDIR 398
Cdd:PRK11147 320 FEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIDYLRE-ESEVakEKDGTTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLT 477
Cdd:PRK11147 400 VMDNLAEgKQEV--MVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 478 ILEDYIASFGGSVITVSHDRYFL-NKVAQEYWFIHDGMMERIVGSFEDY----ETYKKEKdKQLAIEKQATNTSKTQIKE 552
Cdd:PRK11147 478 LLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRYVGGYHDArqqqAQYLALK-QPAVKKKEEAAAPKAETVK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 553 RKKTGLSYKEKREYESLMSRIEETEIRLSEIEQEMieASADY---------AKIKDLTIEQQQLEQTYDeditRWSELEE 623
Cdd:PRK11147 557 RSSKKLSYKLQRELEQLPQLLEDLEAEIEALQAQV--ADADFfsqpheqtqKVLADLADAEQELEVAFE----RWEELEA 630
|
...
gi 488422749 624 LKE 626
Cdd:PRK11147 631 LKN 633
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-525 |
4.82e-78 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 257.51 E-value: 4.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 16 KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT-HPNQyRIRYSSQKQDLDGNLSVFEAVlssetst 94
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSlDPNE-RLGKLRQDQFAFEEFTVLDTV------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 95 lqIIKHYEQ-AVQQ-----YTV-EQTDRNFqaMMAAQEAMDRHEAWDYNAEIKT--ILSKLGIhdTTKQVNSL----SGG 161
Cdd:PRK15064 86 --IMGHTELwEVKQerdriYALpEMSEEDG--MKVADLEVKFAEMDGYTAEARAgeLLLGVGI--PEEQHYGLmsevAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 162 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGNYED 241
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 242 YiaMRAEKEVIEQKQNDKQRAlyKQELAWM-----RAGAKARSTKQ----QARIHRFNDLEANVKQQQT------QDKge 306
Cdd:PRK15064 240 Y--MTAATQARERLLADNAKK--KAQIAELqsfvsRFSANASKAKQatsrAKQIDKIKLEEVKPSSRQNpfirfeQDK-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 307 lnlaysRLGKQVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYF 386
Cdd:PRK15064 314 ------KLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 387 KQ-TEETLNRDIRMIDYLreeSEVAKEKDGTTVsITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLD 465
Cdd:PRK15064 388 AQdHAYDFENDLTLFDWM---SQWRQEGDDEQA-VRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 466 EPTNDLDTETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMMERIVGSFEDY 525
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-623 |
1.23e-68 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 235.06 E-value: 1.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 16 KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQD-LDgnLSVFEAVLSSETST 94
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPaLP--QPALEYVIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 95 LQIikhyEQAVQQYTvEQTDRNFQAMMAAQeaMDRHEAWDYNAEIKTILSKLGIHDT--TKQVNSLSGGQQKRVVLAKTL 172
Cdd:PRK10636 92 RQL----EAQLHDAN-ERNDGHAIATIHGK--LDAIDAWTIRSRAASLLHGLGFSNEqlERPVSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 173 IEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGNYEDYIAMRAEKEVI 252
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 253 EQK--QNDKQRALYKQELAwMRAGAKARSTKQ-QARIHRFNDLEAnVKQQQTQDKGELNL-AYSRLGKQVYELDSLTKTI 328
Cdd:PRK10636 245 QQAmyESQQERVAHLQSYI-DRFRAKATKAKQaQSRIKMLERMEL-IAPAHVDNPFHFSFrAPESLPNPLLKMEKVSAGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEetlnrdirmIDYLR-EES 407
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ---------LEFLRaDES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 408 EVAKEKDGTTVSITQLLERFLFPSSTHGKKIY----KLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYI 483
Cdd:PRK10636 394 PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTeetrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 484 ASFGGSVITVSHDRYFLNKVAQEYWFIHDGMMERIVGSFEDYETY----KKEKDKQLAIEKQATNTSKTQIKERKKTGLS 559
Cdd:PRK10636 474 IDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWlsdvQKQENQTDEAPKENNANSAQARKDQKRREAE 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 560 YKE-----KREYESLMSRIEETEIRLSEIEQEMIEASA-DYAKIKDLTIEQQQLEQTYdeditrwSELEE 623
Cdd:PRK10636 554 LRTqtqplRKEIARLEKEMEKLNAQLAQAEEKLGDSELyDQSRKAELTACLQQQASAK-------SGLEE 616
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-526 |
4.25e-60 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 213.57 E-value: 4.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMG--GIDDdftgditHPNQYRIRYSSQKQDLDgNLS 82
Cdd:PLN03073 179 HMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDG-------IPKNCQILHVEQEVVGD-DTT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETSTLQIIKHYEQAV-QQYTVEQTDRNFQAMMAAQEAMD-------------RHEAWD-YNAEIK--TILSK 145
Cdd:PLN03073 251 ALQCVLNTDIERTQLLEEEAQLVaQQRELEFETETGKGKGANKDGVDkdavsqrleeiykRLELIDaYTAEARaaSILAG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 146 LGIHD--TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTR 223
Cdd:PLN03073 331 LSFTPemQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTD 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 224 IVELDRGKLTTYPGNYEDYIAMRAEKEVIEQK---QNDKQRALYKQELAWMRAGAKaRSTKQQARIHRFNDLEANVKQQQ 300
Cdd:PLN03073 411 ILHLHGQKLVTYKGDYDTFERTREEQLKNQQKafeSNERSRSHMQAFIDKFRYNAK-RASLVQSRIKALDRLGHVDAVVN 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 301 TQD-KGELNLAYSRLGKQVYEL-DSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIG 378
Cdd:PLN03073 490 DPDyKFEFPTPDDRPGPPIISFsDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 379 QTVKVAYFKQTE-ETLNRDIRMIDYL-REESEVAKEKdgttvsITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLV 456
Cdd:PLN03073 570 AKVRMAVFSQHHvDGLDLSSNPLLYMmRCFPGVPEQK------LRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 457 HQPNVLLLDEPTNDLDTETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMMERIVGSFEDYE 526
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYK 713
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-244 |
1.33e-57 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 202.22 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQD-LDGNLSVF 84
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEeLDPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EAVlssetstlqiikhyeqavQQYTVEQTDRnfqammaaqeamdrheawdynaEIKTILSKLGIH--DTTKQVNSLSGGQ 162
Cdd:COG0488 398 DEL------------------RDGAPGGTEQ----------------------EVRGYLGRFLFSgdDAFKPVGVLSGGE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGNYEDY 242
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
..
gi 488422749 243 IA 244
Cdd:COG0488 518 LE 519
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
321-542 |
5.38e-55 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 195.28 E-value: 5.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 321 LDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQ-TEETLNRDIR- 398
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQePPLDDDLTVLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 -MIDYLREESEVAKEK------------DGTTVS-----------------ITQLLERFLFPSSTHGKKIYKLSGGEQKR 448
Cdd:COG0488 81 tVLDGDAELRALEAELeeleaklaepdeDLERLAelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 449 LYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMMERIVGsfeDYETY 528
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPG---NYSAY 237
|
250
....*....|....
gi 488422749 529 KKEKDKQLAIEKQA 542
Cdd:COG0488 238 LEQRAERLEQEAAA 251
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-513 |
1.25e-53 |
|
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: 179.95 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQteetlnrdirm 399
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 idylreesevakekdgttvsitqllerflfpssthgkkiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTIL 479
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....
gi 488422749 480 EDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-231 |
7.55e-49 |
|
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: 166.86 E-value: 7.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQkqdldgnlsvf 84
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssetstlqiikhyeqavqqytveqtdrnfqammaaqeamdrheawdynaeiktilsklgihdttkqvnsLSGGQQK 164
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 165 RVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-515 |
5.99e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.57 E-value: 5.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQ 388
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 T----EETLnrdirmIDYLREESEVAKEKDGTTVsITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLL 464
Cdd:COG4619 82 EpalwGGTV------RDNLPFPFQLRERKFDRER-ALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 465 DEPTNDLDTETLTILEDYIASF----GGSVITVSHDRYFLNKVAQEYWFIHDGMM 515
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-519 |
1.33e-37 |
|
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: 146.59 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYA--DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLK-VMGGIDD--DFTGDIThpnqyriryssqkqdLDGN 80
Cdd:COG1123 7 VRDLSVRYPggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHggRISGEVL---------------LDGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 --LSVFEAVLSSETSTlqIIKHYEQAVQQYTVEqtdrnFQ-AMMAAQEAMDRHEAWdynAEIKTILSKLGIHDTTKQ-VN 156
Cdd:COG1123 72 dlLELSEALRGRRIGM--VFQDPMTQLNPVTVG-----DQiAEALENLGLSRAEAR---ARVLELLEAVGLERRLDRyPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 233 ttypgnyedyIAMRAEKEVIEQkqndkQRALYKQELAWMRAGAKARSTKQQARIhrfndLEANvkqqqtqdkgelNLAYS 312
Cdd:COG1123 222 ----------VEDGPPEEILAA-----PQALAAVPRLGAARGRAAPAAAAAEPL-----LEVR------------NLSKR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 313 ---RLGKQVYELD--SLTktingrtlfqditqiIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYF 386
Cdd:COG1123 270 ypvRGKGGVRAVDdvSLT---------------LRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLTKLSR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 387 KQTEEtLNRDIRMI---------------DYLREESEVAKEKDGTTVS--ITQLLERFLFPSSTHGKKIYKLSGGEQKRL 449
Cdd:COG1123 335 RSLRE-LRRRVQMVfqdpysslnprmtvgDIIAEPLRLHGLLSRAERRerVAELLERVGLPPDLADRYPHELSGGQRQRV 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 450 YLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD----RYFLNKVAqeywFIHDGmmeRIV 519
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDvsvqAQILNLLRDLQRELGLTYLFISHDlavvRYIADRVA----VMYDG---RIV 484
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
5.08e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 5.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT------HPNQYRIRYSSQK 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 QDLDGN--LSVFEAVLSSETSTLQIIKHYEQAvqqytveqtDRNfqammAAQEAMDRHEAWDYnAEiktilsklgihdtt 152
Cdd:COG1121 84 AEVDWDfpITVRDVVLMGRYGRRGLFRRPSRA---------DRE-----AVDEALERVGLEDL-AD-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 153 KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK---QYPYTVLFVTHDryfLNEVS---TRIVE 226
Cdd:COG1121 135 RPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelrREGKTILVVTHD---LGAVReyfDRVLL 211
|
....*.
gi 488422749 227 LDRGKL 232
Cdd:COG1121 212 LNRGLV 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-244 |
1.86e-35 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 140.41 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 3 AYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLK-VMGGIDDDfTGDITHPNQYRIRYSSQ--KQDLDG 79
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELEPD-SGTVKWSENANIGYYAQdhAYDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 NLSVFEAVlssetstlqiikhyeqavQQYTVEQTDRnfQAmmaaqeamdrheawdynaeIKTILSKL--GIHDTTKQVNS 157
Cdd:PRK15064 398 DLTLFDWM------------------SQWRQEGDDE--QA-------------------VRGTLGRLlfSQDDIKKSVKV 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPG 237
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSG 518
|
....*..
gi 488422749 238 NYEDYIA 244
Cdd:PRK15064 519 TYEEYLR 525
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-232 |
6.85e-35 |
|
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: 132.47 E-value: 6.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---HP-NQYRIR-------YSSQ 73
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlASLSRRelarriaYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 74 KQDLDGNLSVFEAVLSSETStlqiikhYEQAVQQYTVEqtDRNfqammAAQEAMDRheawdynaeiktilskLGIHD-TT 152
Cdd:COG1120 83 EPPAPFGLTVRELVALGRYP-------HLGLFGRPSAE--DRE-----AVEEALER----------------TGLEHlAD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 153 KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDryfLN---EVSTRIV 225
Cdd:COG1120 133 RPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNlaaRYADRLV 209
|
....*..
gi 488422749 226 ELDRGKL 232
Cdd:COG1120 210 LLKDGRI 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-231 |
1.81e-34 |
|
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: 129.89 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD--KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQKQDLDGNLS 82
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-DLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEavlSSETstlQIIKHyeqavqqyTVEQtD-----RNFQammaaqeaMDRHEAWdynAEIKTILSKLGIHDTTKQ-VN 156
Cdd:cd03225 80 VFQ---NPDD---QFFGP--------TVEE-EvafglENLG--------LPEEEIE---ERVEEALELVGLEGLRDRsPF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
318-552 |
1.00e-33 |
|
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: 135.83 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 VYELDSLTKTIN-GRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQtEETLN-- 394
Cdd:TIGR03719 4 IYTMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQ-EPQLDpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIR---------MIDYLREESEVAKEKDGTTVSITQLLERflfpsstHGK----------------------------- 436
Cdd:TIGR03719 83 KTVRenveegvaeIKDALDRFNEISAKYAEPDADFDKLAAE-------QAElqeiidaadawdldsqleiamdalrcppw 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 437 --KIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGGSVITVSHDRYFLNKVAQeyWFIHdgm 514
Cdd:TIGR03719 156 daDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILE--- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488422749 515 MERIVG-SFE-DYETYKKEKDKQLAIE-KQATNTSKTQIKE 552
Cdd:TIGR03719 231 LDRGRGiPWEgNYSSWLEQKQKRLEQEeKEESARQKTLKRE 271
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-232 |
2.56e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---------HPNQYR--IRYSSQ 73
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPEWRrqVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 74 KQDLdgnlsvFEAvlssetstlqiikhyeqavqqyTVEQtdrNFQ-AMMAAQEAMDRHEAwdynaeiKTILSKLGIHDT- 151
Cdd:COG4619 82 EPAL------WGG----------------------TVRD---NLPfPFQLRERKFDRERA-------LELLERLGLPPDi 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 -TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----INWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVE 226
Cdd:COG4619 124 lDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
....*.
gi 488422749 227 LDRGKL 232
Cdd:COG4619 204 LEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-232 |
3.08e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.41 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT--------HPNQYRIR--YSSQKQ 75
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvarDPAEVRRRigYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVlssetstlqiikhyeqavqqytveqtdrnfqAMMAAQEAMDRHEAwdyNAEIKTILSKLGIHDT-TKQ 154
Cdd:COG1131 83 ALYPDLTVRENL-------------------------------RFFARLYGLPRKEA---RERIDELLELFGLTDAaDRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY---PYTVLFVTHDryfLNEV---STRIVELD 228
Cdd:COG1131 129 VGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHY---LEEAerlCDRVAIID 205
|
....
gi 488422749 229 RGKL 232
Cdd:COG1131 206 KGRI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-232 |
2.10e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.49 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT------HPNQYRIRYSSQKQDLD 78
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 79 GN--LSVFEAVLSSETSTLQIIKHYEQAVQQytveqtdrnfqammAAQEAMDRheawdynaeikTILSKLGihdtTKQVN 156
Cdd:cd03235 81 RDfpISVRDVVLMGLYGHKGLFRRLSKADKA--------------KVDEALER-----------VGLSELA----DRQIG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINW---LINYVKQYPYTVLFVTHDryfLNEVST---RIVELDRG 230
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHD---LGLVLEyfdRVLLLNRT 208
|
..
gi 488422749 231 KL 232
Cdd:cd03235 209 VV 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-235 |
9.37e-31 |
|
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: 118.69 E-value: 9.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnlsvf 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL---------------LDG----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssetstlqiikhyeqavqqytveqtdRNFQAMMAAQEAmdRHEAWdynaeIKTILSKLGIHD-TTKQVNSLSGGQQ 163
Cdd:cd03214 61 ------------------------------KDLASLSPKELA--RKIAY-----VPQALELLGLAHlADRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDryfLN---EVSTRIVELDRGKLTTY 235
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD---LNlaaRYADRVILLKDGRIVAQ 179
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-232 |
1.19e-30 |
|
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: 120.35 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG--------IDDDFTGDITHPNQYR--IRYSSQK 74
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsgsILIDGEDVRKEPREARrqIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 QDLDGNLSVFEavlssetstlqIIKHYeqavqqytveqtdrnfqammAAQEAMDRHEAwdyNAEIKTILSKLGIHDTTKQ 154
Cdd:COG4555 83 RGLYDRLTVRE-----------NIRYF--------------------AELYGLFDEEL---KKRIEELIELLGLEEFLDR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 -VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY---PYTVLFVTHDRYFLNEVSTRIVELDRG 230
Cdd:COG4555 129 rVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
..
gi 488422749 231 KL 232
Cdd:COG4555 209 KV 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
318-552 |
1.00e-29 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 123.69 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 VYELDSLTKTING-RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQ-------- 388
Cdd:PRK11819 6 IYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQepqldpek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 ------------TEETLNR--DIRM--------IDYLREESEVAKEK----DGTTvsITQLLERF-----LFPSSThgkK 437
Cdd:PRK11819 86 tvrenveegvaeVKAALDRfnEIYAayaepdadFDALAAEQGELQEIidaaDAWD--LDSQLEIAmdalrCPPWDA---K 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 438 IYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGGSVITVSHDRYFLNKVAQeyWFIHdgmMER 517
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILE---LDR 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 488422749 518 IVG-SFE-DYETYKKEKDKQLAIE-KQATNTSKTQIKE 552
Cdd:PRK11819 236 GRGiPWEgNYSSWLEQKAKRLAQEeKQEAARQKALKRE 273
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-232 |
3.60e-29 |
|
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: 115.28 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD----KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDLDGN 80
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 LS---VFeavlssetstlqiikhyeqavQQY------TVEQtdrnfQAMMAAQeaMDRHEAWDYNAEIKTILSKLGI-HD 150
Cdd:cd03255 82 RHigfVF---------------------QSFnllpdlTALE-----NVELPLL--LAGVPKKERRERAEELLERVGLgDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 151 TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----INWLINYVKQYPYTVLFVTHDRyFLNEVSTRIVE 226
Cdd:cd03255 134 LNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIE 212
|
....*.
gi 488422749 227 LDRGKL 232
Cdd:cd03255 213 LRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
320-500 |
4.92e-29 |
|
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: 114.50 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayfkQTEETLNRDIR 398
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIR-----DAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 midYLREESEV---------------AKEKDGTTVSITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNVLL 463
Cdd:COG4133 79 ---YLGHADGLkpeltvrenlrfwaaLYGLRADREAIDEALEAVGLAGLAD-LPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488422749 464 LDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFL 500
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLEL 194
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-232 |
1.12e-28 |
|
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: 114.35 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD-KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGNlsv 83
Cdd:COG1122 2 ELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL---------------VDGK--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 feavlssETSTLQIIKHYEQA--VQQY--------TVEQtD-----RNFQamMAAQEAMDRheawdynaeIKTILSKLGI 148
Cdd:COG1122 64 -------DITKKNLRELRRKVglVFQNpddqlfapTVEE-DvafgpENLG--LPREEIRER---------VEEALELVGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 149 HD-TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRI 224
Cdd:COG1122 125 EHlADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAELADRV 204
|
....*...
gi 488422749 225 VELDRGKL 232
Cdd:COG1122 205 IVLDDGRI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-232 |
1.22e-28 |
|
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: 112.11 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdithpnqyrIRYSSqkqdldGNLSVF 84
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL---------------LKPDS------GEIKVL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EavlssetstLQIIKHYEQAVQQ-YTVEQTDRNFQAMmaaqeamdrheawdynaeiktilsklgihdTTKQVNSLSGGQQ 163
Cdd:cd03230 61 G---------KDIKKEPEEVKRRiGYLPEEPSLYENL------------------------------TVRENLKLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY---PYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-513 |
3.93e-28 |
|
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: 110.95 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayfKQTEETLnrdiR 398
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIK----KEPEEVK----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIDYLREESevakekdgttvsitqllerFLFPSSThGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTI 478
Cdd:cd03230 74 RIGYLPEEP-------------------SLYENLT-VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 488422749 479 LEDYIASF---GGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03230 134 FWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-231 |
4.29e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.03 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnlsvf 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------------IDG----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssetstlqiikhyeQAVQQYTVEQTDRNFQAMMaaqeamdrheawdynaeiktilsklgihdttkqvnSLSGGQQK 164
Cdd:cd00267 61 ------------------KDIAKLPLEELRRRIGYVP-----------------------------------QLSGGQRQ 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 165 RVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd00267 88 RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAeegRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
320-513 |
4.33e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.03 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGqtvkvayfkqteetlnrdirm 399
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 idylreesevakEKDGTTVSITQLLERFLFpssthgkkIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTIL 479
Cdd:cd00267 60 ------------GKDIAKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 488422749 480 EDYIASF---GGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd00267 120 LELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-231 |
1.25e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 110.65 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyrirySSQKQDLDgnlsVFE 85
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE-----PIRDARED----YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 AVLssetstlqIIKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRHEAWdynaeiktiLSKLGIHD-TTKQVNSLSGGQQK 164
Cdd:COG4133 76 RLA--------YLGHADGLKPELTVRENLRFWAALYGLRADREAIDEA---------LEAVGLAGlADLPVRQLSAGQKR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 165 RVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVstRIVELDRGK 231
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
320-513 |
2.78e-27 |
|
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: 110.72 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYfkqtEETLNRDIRM 399
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE----PREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 I-------------DYLREESEVAKEKDGTTVS-ITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNVLLLD 465
Cdd:COG4555 79 LpderglydrltvrENIRYFAELYGLFDEELKKrIEELIELLGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488422749 466 EPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
320-513 |
1.80e-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: 106.37 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQTEetlnrdiR 398
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLASLSPKELA-------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIDYLREESEVakekdgttVSITQLLERFLFpssthgkkiyKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TE 474
Cdd:cd03214 74 KIAYVPQALEL--------LGLAHLADRPFN----------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488422749 475 TLTILEDYIASFGGSVITVSHDryfLNKVAQ---EYWFIHDG 513
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHD---LNLAARyadRVILLKDG 174
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-513 |
2.81e-26 |
|
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: 105.73 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGqTVKVAYFKQTEETLNRDIRM 399
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 IdylreesevakekdgttvsitqlLERF-LFPSSTHGKKI-YKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLT 477
Cdd:cd03229 81 V-----------------------FQDFaLFPHLTVLENIaLGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488422749 478 ILEDYI----ASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03229 138 EVRALLkslqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
320-503 |
4.14e-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: 106.46 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV-----KVAYFKQTEEtL 393
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLekerkRIGYVPQRRS-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRD-------------IRMIDYLREESEVAKEKdgttvsITQLLER-----FlfpsstHGKKIYKLSGGEQKRLYLLRLL 455
Cdd:cd03235 80 DRDfpisvrdvvlmglYGHKGLFRRLSKADKAK------VDEALERvglseL------ADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488422749 456 VHQPNVLLLDEPTNDLDTET----LTILEDYIASfGGSVITVSHDryfLNKV 503
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTqediYELLRELRRE-GMTILVVTHD---LGLV 195
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-233 |
1.07e-25 |
|
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: 106.04 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSY----ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGn 80
Cdd:COG1124 3 EVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT---------------FDG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 lsvfeavlssETSTLQIIKHYEQAVQ------------QYTVEQTdrnfqamMAaqEAMDRHEAWDYNAEIKTILSKLGI 148
Cdd:COG1124 67 ----------RPVTRRRRKAFRRRVQmvfqdpyaslhpRHTVDRI-------LA--EPLRIHGLPDREERIAELLEQVGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 149 HDT--TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDRYFLNEVST 222
Cdd:COG1124 128 PPSflDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCD 207
|
250
....*....|.
gi 488422749 223 RIVELDRGKLT 233
Cdd:COG1124 208 RVAVMQNGRIV 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-231 |
1.30e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 105.94 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMggidddfTGDI--THPNQY---------------- 66
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-------TGDLppTYGNDVrlfgerrggedvwelr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 67 -RIRYSSQK--QDLDGNLSVFEAVLSSETSTLQIikhyeqaVQQYTVEQTDRnfqammaAQEAMDRheawdynaeiktil 143
Cdd:COG1119 78 kRIGLVSPAlqLRFPRDETVLDVVLSGFFDSIGL-------YREPTDEQRER-------ARELLEL-------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 144 skLGI-HDTTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYV----KQYPYTVLFVTHdryFLN 218
Cdd:COG1119 130 --LGLaHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLdklaAEGAPTLVLVTH---HVE 204
|
250
....*....|....*.
gi 488422749 219 EVS---TRIVELDRGK 231
Cdd:COG1119 205 EIPpgiTHVLLLKDGR 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
320-505 |
5.44e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.02 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV-----KVAYFKQTEEtL 393
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQRAE-V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRD--IRMID---------------YLREESEVAKE--KdgtTVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRL 454
Cdd:COG1121 87 DWDfpITVRDvvlmgrygrrglfrrPSRADREAVDEalE---RVGLEDLADR----------PIGELSGGQQQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488422749 455 LVHQPNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDryfLNKVAQ 505
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTHD---LGAVRE 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
320-519 |
6.28e-25 |
|
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: 103.97 E-value: 6.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQ 388
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 TEETLN----RDI----RM--IDYLREESEVAKEKdgttvsITQLLERFlfpSSTH--GKKIYKLSGGEQKRLYLLRLLV 456
Cdd:COG1120 83 EPPAPFgltvRELvalgRYphLGLFGRPSAEDREA------VEEALERT---GLEHlaDRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 457 HQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHDryfLN---KVAQEYWFIHDGmmeRIV 519
Cdd:COG1120 154 QEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHD---LNlaaRYADRLVLLKDG---RIV 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-232 |
1.84e-24 |
|
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: 101.83 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITH--PNQYRIRYSSQKQ 75
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGeilidgrDVTGvpPERRNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVLSSetstLQIIKHYEQAVQQytveqtdrnfQAMMAAQEAMDRHEAWDYNAEiktilsklgihdttkqv 155
Cdd:cd03259 82 ALFPHLTVAENIAFG----LKLRGVPKAEIRA----------RVRELLELVGLEGLLNRYPHE----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 156 nsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd03259 131 --LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKelqrELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
.
gi 488422749 232 L 232
Cdd:cd03259 209 I 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-231 |
2.30e-24 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 100.34 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDLDGNLS-V 83
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGmV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FeavlssetstlqiikhyeqavQQYTVeqtdrnFQAMmaaqeamdrheawdynaeikTILSKLGIhdttkqvnSLSGGQQ 163
Cdd:cd03229 82 F---------------------QDFAL------FPHL--------------------TVLENIAL--------GLSGGQQ 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd03229 107 QRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-232 |
3.66e-24 |
|
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: 101.59 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG----------IDDDftgDITHPN---QYRIR-- 69
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllrpdsgeilVDGQ---DITGLSekeLYELRrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 ----------YSSqkqdldgnLSVFEAV---LssetstlqiikhyeqavqqytVEQTDrnfqamMAAQEAMDRheawdyn 136
Cdd:COG1127 84 igmlfqggalFDS--------LTVFENVafpL---------------------REHTD------LSEAEIREL------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 137 AEIKtiLSKLGIHDTTKQVNS-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLI-NYVKQYPYTVLFVT 211
Cdd:COG1127 122 VLEK--LELVGLPGAADKMPSeLSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIrELRDELGLTSVVVT 199
|
250 260
....*....|....*....|.
gi 488422749 212 HDRYFLNEVSTRIVELDRGKL 232
Cdd:COG1127 200 HDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-232 |
4.48e-24 |
|
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: 100.68 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnlsvf 84
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII---------------IDG----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EAVLSSETSTLQIIKHYEQAVQQY------TVEQtdrNFqaMMAAQEA--MDRHEAwdyNAEIKTILSKLGIHD-TTKQV 155
Cdd:cd03262 62 LKLTDDKKNINELRQKVGMVFQQFnlfphlTVLE---NI--TLAPIKVkgMSKAEA---EERALELLEKVGLADkADAYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 156 NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAeegMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
320-519 |
9.53e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 100.65 E-value: 9.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTI----NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQteetLN 394
Cdd:COG1124 3 EVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRRRRKA----FR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMI--DY-------------LREESEVAKEKDgTTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQP 459
Cdd:COG1124 79 RRVQMVfqDPyaslhprhtvdriLAEPLRIHGLPD-REERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 460 NVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIV 519
Cdd:COG1124 158 ELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNG---RIV 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
320-513 |
9.88e-24 |
|
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: 99.87 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTING----RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQTEETLN 394
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDISKLSEKELAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDI-------RMIDYL--REESEVAKEKDGTTVS-----ITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPN 460
Cdd:cd03255 82 RHIgfvfqsfNLLPDLtaLENVELPLLLAGVPKKerrerAEELLERVGLGDRLN-HYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 461 VLLLDEPTNDLDTET----LTILEDYIASFGGSVITVSHDRYFLNKVAQEYwFIHDG 513
Cdd:cd03255 161 IILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAEYADRII-ELRDG 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
331-513 |
1.19e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 99.08 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayfKQTEETLNRDI--------RMID 401
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLT----KLSLKELRRKVglvfqnpdDQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 402 YLREESEVA-------KEKDGTTVSITQLLERFLFpSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTE 474
Cdd:cd03225 90 GPTVEEEVAfglenlgLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488422749 475 TLTILEDYIASF---GGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03225 169 GRRELLELLKKLkaeGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
334-469 |
2.16e-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: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 334 FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQtEETLNRDIRMIDY 402
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLtdderkslrkEIGYVFQ-DPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 403 LREESEVAKEKDGT-TVSITQLLERF---LFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTN 469
Cdd:pfam00005 80 LRLGLLLKGLSKREkDARAEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-186 |
2.81e-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: 96.18 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 19 FDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---HPNQYRIRYSSQK------QD--LDGNLSVFEAV 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgQDLTDDERKSLRKeigyvfQDpqLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 88 LSSetstlqiikhyeqavqqytveqtdRNFQAMMAAqeamdrheawDYNAEIKTILSKLGIHDTTKQV-----NSLSGGQ 162
Cdd:pfam00005 81 RLG------------------------LLLKGLSKR----------EKDARAEEALEKLGLGDLADRPvgerpGTLSGGQ 126
|
170 180
....*....|....*....|....
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTN 186
Cdd:pfam00005 127 RQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-213 |
3.69e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 12 SYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDLDGNLSVfeavlsse 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPL-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 92 tstlqiikhyeqavqqyTVEQTdrnfqAMM---AAQEAMDRHEAWDyNAEIKTILSKLGIHDTTK-QVNSLSGGQQKRVV 167
Cdd:NF040873 73 -----------------TVRDL-----VAMgrwARRGLWRRLTRDD-RAAVDDALERVGLADLAGrQLGELSGGQRQRAL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488422749 168 LAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY---PYTVLFVTHD 213
Cdd:NF040873 130 LAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTHD 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-524 |
3.80e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 98.60 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV---------KVAYFKQt 389
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevrrRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EETLNRDIRMIDYLR-------EESEVAKEKdgttvsITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNVL 462
Cdd:COG1131 81 EPALYPDLTVRENLRffarlygLPRKEARER------IDELLELFGLTDAAD-RKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 463 LLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIV--GSFED 524
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKG---RIVadGTPDE 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-233 |
6.59e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.43 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYA-DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGID---------DDFtgDITHPNQYRIRYSSQK 74
Cdd:COG2884 3 RFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEErptsgqvlvNGQ--DLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 -----QD---LDgNLSVFEAVlssetstlqiikhyeqavqqytveqtdrnfqamMAAQEAMDRHEAwDYNAEIKTILSKL 146
Cdd:COG2884 81 igvvfQDfrlLP-DRTVYENV---------------------------------ALPLRVTGKSRK-EIRRRVREVLDLV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 147 GIHDTTKQ-VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----------FESINwlinyvkQYPYTVLFVTHDRY 215
Cdd:COG2884 126 GLSDKAKAlPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDpetsweimelLEEIN-------RRGTTVLIATHDLE 198
|
250
....*....|....*...
gi 488422749 216 FLNEVSTRIVELDRGKLT 233
Cdd:COG2884 199 LVDRMPKRVLELEDGRLV 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-233 |
6.60e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 97.42 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADK----VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGN 80
Cdd:COG1136 6 ELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL---------------IDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 lsvfeavlssETSTLqiiKHYEQAV----------QQY------TVEQtdrnfQAMMAAQEA-MDRHEAwdyNAEIKTIL 143
Cdd:COG1136 71 ----------DISSL---SERELARlrrrhigfvfQFFnllpelTALE-----NVALPLLLAgVSRKER---RERARELL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 144 SKLGIHD-TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----INWLINYVKQYPYTVLFVTHDRyFLN 218
Cdd:COG1136 130 ERVGLGDrLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-ELA 208
|
250
....*....|....*
gi 488422749 219 EVSTRIVELDRGKLT 233
Cdd:COG1136 209 ARADRVIRLRDGRIV 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-232 |
7.21e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 103.38 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 3 AYKIEHLNKSY--ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---------HPNQYR--IR 69
Cdd:COG2274 473 DIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPASLRrqIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSSQKQDL-DG----NLSVFEAVLSSEtstlqiikhyeqavqqytveqtdrnfQAMMAAQEAmdrhEAWD--------YN 136
Cdd:COG2274 553 VVLQDVFLfSGtireNITLGDPDATDE--------------------------EIIEAARLA----GLHDfiealpmgYD 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 137 aeikTILSKLGihdttkqvNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPY--TVLFVTHDR 214
Cdd:COG2274 603 ----TVVGEGG--------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRL 670
|
250
....*....|....*...
gi 488422749 215 YFLNEVStRIVELDRGKL 232
Cdd:COG2274 671 STIRLAD-RIIVLDKGRI 687
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-225 |
1.46e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.47 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYA----DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQY------RIRYssqkq 75
Cdd:COG1116 10 LRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgpDRGV----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 dldgnlsVFeavlssetstlqiikhyeqavQQY------TVEQtdrNfqAMMAAQEA-MDRHEAwdyNAEIKTILSKLGI 148
Cdd:COG1116 85 -------VF---------------------QEPallpwlTVLD---N--VALGLELRgVPKAER---RERARELLELVGL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 149 HDTTKQ-VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIN-WLINYVKQYPYTVLFVTHDryfLNE---V 220
Cdd:COG1116 129 AGFEDAyPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltrERLQdELLRLWQETGKTVLFVTHD---VDEavfL 205
|
....*
gi 488422749 221 STRIV 225
Cdd:COG1116 206 ADRVV 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
329-495 |
2.45e-22 |
|
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: 94.37 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGqtvkvayfkqteetlNRDIRMID--YLREe 406
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID---------------GVDLRDLDleSLRK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 407 sevakekdgtTVS-ITQllERFLFPSSthgkkIYK--LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYI 483
Cdd:cd03228 77 ----------NIAyVPQ--DPFLFSGT-----IREniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL 139
|
170
....*....|....
gi 488422749 484 ASFGG--SVITVSH 495
Cdd:cd03228 140 RALAKgkTVIVIAH 153
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-233 |
2.75e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 95.02 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKV-IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDD------FTGDITHPNQYRIRYSSQKQDLD 78
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKEssgsilLNGKPIKAKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 79 GNL---SVFEAVLssetstlqiikhyeqavqqYTVEQTDrnfqammaaqeamdrheawDYNAEIKTILSKLGIHDTtKQV 155
Cdd:cd03226 82 YQLftdSVREELL-------------------LGLKELD-------------------AGNEQAETVLKDLDLYAL-KER 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 156 N--SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRG 230
Cdd:cd03226 123 HplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
...
gi 488422749 231 KLT 233
Cdd:cd03226 203 AIV 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
318-517 |
2.86e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 95.88 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 VYELDSLTKTI----NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVkvayFKQTEET 392
Cdd:COG1136 4 LLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQDI----SSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 393 L----NRDI-------RMIDYL-------------REESEVAKEKdgttvsITQLLERF-LfpSSTHGKKIYKLSGGEQK 447
Cdd:COG1136 80 LarlrRRHIgfvfqffNLLPELtalenvalplllaGVSRKERRER------ARELLERVgL--GDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 448 RLYLLRLLVHQPNVLLLDEPTNDLDTET----LTILEDYIASFGGSVITVSHDRYFLNKVAQEYwFIHDGMMER 517
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELAARADRVI-RLRDGRIVS 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-232 |
3.47e-22 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 95.83 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSY-ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQ--------------YRIR 69
Cdd:TIGR02315 3 EVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklrRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSSQKQDLDGNLSVFEAVLS---SETSTLQIIkhyeqaVQQYTVEQTDRNFQAmmaaqeamdrheawdynaeiktiLSKL 146
Cdd:TIGR02315 83 MIFQHYNLIERLTVLENVLHgrlGYKPTWRSL------LGRFSEEDKERALSA-----------------------LERV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 147 GIHD-TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHDRYFLNEVS 221
Cdd:TIGR02315 134 GLADkAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKrinkEDGITVIINLHQVDLAKKYA 213
|
250
....*....|.
gi 488422749 222 TRIVELDRGKL 232
Cdd:TIGR02315 214 DRIVGLKAGEI 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
329-527 |
3.64e-22 |
|
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: 95.48 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQ----------------TEE 391
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDITKKNLRElrrkvglvfqnpddqlFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 TLNRDI----RMIDYLREE-----SEVAKEkdgttVSITQLLERFlfpssthgkkIYKLSGGEQKRLYLLRLLVHQPNVL 462
Cdd:COG1122 92 TVEEDVafgpENLGLPREEirervEEALEL-----VGLEHLADRP----------PHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 463 LLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIVGS------FEDYET 527
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLnkeGKTVIIVTHDLDLVAELADRVIVLDDG---RIVADgtprevFSDYEL 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-232 |
3.98e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 95.89 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYA-DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQY--------------RIR 69
Cdd:COG3638 4 ELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalrgralrrlrrRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSSQKQDLDGNLSVFEAVLS---SETSTLQ-IIKHYEQAvqqytveqtDRnfqamMAAQEAMDR----HEAWdynaeikt 141
Cdd:COG3638 84 MIFQQFNLVPRLSVLTNVLAgrlGRTSTWRsLLGLFPPE---------DR-----ERALEALERvglaDKAY-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 142 ilsklgihdttKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----------FESINwlinyvKQYPYTVLFVT 211
Cdd:COG3638 142 -----------QRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDpktarqvmdlLRRIA------REDGITVVVNL 204
|
250 260
....*....|....*....|....*.
gi 488422749 212 HD-----RYFlnevsTRIVELDRGKL 232
Cdd:COG3638 205 HQvdlarRYA-----DRIIGLRDGRV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-232 |
4.53e-22 |
|
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: 95.27 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADK----VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGn 80
Cdd:cd03257 3 EVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII---------------FDG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 lsvfEAVLSSETSTLQIIKHYEQAVQQ---------YTVEQTdrnFQAMMAAQEAMDRHEAwdynAEIKTILSKLGIHDT 151
Cdd:cd03257 67 ----KDLLKLSRRLRKIRRKEIQMVFQdpmsslnprMTIGEQ---IAEPLRIHGKLSKKEA----RKEAVLLLLVGVGLP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 TKQVNS----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTR 223
Cdd:cd03257 136 EEVLNRypheLSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADR 215
|
....*....
gi 488422749 224 IVELDRGKL 232
Cdd:cd03257 216 VAVMYAGKI 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-232 |
4.59e-22 |
|
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: 95.26 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDddftgditHPNQYRIRYssQKQDLDGNlsvfe 85
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL--------RPDSGEVLI--DGEDISGL----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 avlsSETSTLQIIKHYEQAVQQ------YTVEQtdrNFQAMMAAQEAMDRHEawdYNAEIKTILSKLGIHDTTKQVNS-L 158
Cdd:cd03261 68 ----SEAELYRLRRRMGMLFQSgalfdsLTVFE---NVAFPLREHTRLSEEE---IREIVLEKLEAVGLRGAEDLYPAeL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLINYVKQ-YPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-513 |
4.63e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 100.26 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDdftgdiTHPNQYRIRYSS---------QKQ 75
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQ------YEPTSGRIIYHValcekcgyvERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDG-NLSVFEAVLSSETSTL-QIIKHYEQAVQQYTVEQTDRNF-----------------QAMMAAQEAMDRheAWDYN 136
Cdd:TIGR03269 76 SKVGePCPVCGGTLEPEEVDFwNLSDKLRRRIRKRIAIMLQRTFalygddtvldnvlealeEIGYEGKEAVGR--AVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 137 AEIKtiLSklgiHDTTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINW----LINYVKQYPYTVLFVTH 212
Cdd:TIGR03269 154 EMVQ--LS----HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 213 DRYFLNEVSTRIVELDRGklttypgnyedyiamraekEVIEQKQNDKQRALYKQELAWMRagaKARSTKQQARIHRFNDL 292
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENG-------------------EIKEEGTPDEVVAVFMEGVSEVE---KECEVEVGEPIIKVRNV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 293 EanvKQQQTQDKGelnlaysrlgkQVYELDSLTKTINGRTLFqditqiiqsgqriGIVGPNGAGKTTMLNIL-------S 365
Cdd:TIGR03269 286 S---KRYISVDRG-----------VVKAVDNVSLEVKEGEIF-------------GIVGTSGAGKTTLSKIIagvleptS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 366 GE----------DQQFEGTLKIGQTVKVAYFKQTEETL--NRDIrmIDYLREE------SEVAKEKDGTTVSITQLLERf 427
Cdd:TIGR03269 339 GEvnvrvgdewvDMTKPGPDGRGRAKRYIGILHQEYDLypHRTV--LDNLTEAiglelpDELARMKAVITLKMVGFDEE- 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 428 lFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYI----ASFGGSVITVSHDRYFLNKV 503
Cdd:TIGR03269 416 -KAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDV 494
|
570
....*....|
gi 488422749 504 AQEYWFIHDG 513
Cdd:TIGR03269 495 CDRAALMRDG 504
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-302 |
1.04e-21 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 99.64 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 4 YKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVM-GGIDDDfTGDITHPNQYRIRYSSQ-KQDLDGNL 81
Cdd:PRK11147 320 FEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMlGQLQAD-SGRIHCGTKLEVAYFDQhRAELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 82 SVFEAVlssetstlqiikhyeqAVQQYTVEQTDRnfqammaaqeamDRHeawdynaeiktILSKLgihdttkQ------- 154
Cdd:PRK11147 399 TVMDNL----------------AEGKQEVMVNGR------------PRH-----------VLGYL-------Qdflfhpk 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 -----VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTR--IVEL 227
Cdd:PRK11147 433 ramtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcwIFEG 512
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 228 DrGKLTTYPGNYEDYIAMRAEKEVIEQKQNDKQRALYKQELAWMRAGAKARSTKQQARIH----RFNDLEANVKQQQTQ 302
Cdd:PRK11147 513 N-GKIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSKKLSYKLQRELEqlpqLLEDLEAEIEALQAQ 590
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-231 |
1.48e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 94.17 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD-KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHP------------NQYR--IR 69
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdinklkgkalRQLRrqIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSSQKQDLDGNLSVFEAVLS---SETSTLQIIkhyeqaVQQYTVEQTDRNFQAmmaaqeamdrheawdynaeiktiLSKL 146
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSgrlGRRSTWRSL------FGLFPKEEKQRALAA-----------------------LERV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 147 GIHD-TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHDRYFLNEVS 221
Cdd:cd03256 133 GLLDkAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrinrEEGITVIVSLHQVDLAREYA 212
|
250
....*....|
gi 488422749 222 TRIVELDRGK 231
Cdd:cd03256 213 DRIVGLKDGR 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-233 |
3.07e-21 |
|
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: 92.26 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHeKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT--------HPNQYR--IRYSSQK 74
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQKLRrrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 QDLDGNLSVFEAVlssetstlqiikhyeqavqqytveqtdrNFQAmmAAQEAMDRHEawdyNAEIKTILSKLGIHDT-TK 153
Cdd:cd03264 81 FGVYPNFTVREFL----------------------------DYIA--WLKGIPSKEV----KARVDEVLELVNLGDRaKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 154 QVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP--YTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd03264 127 KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
..
gi 488422749 232 LT 233
Cdd:cd03264 207 LV 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-232 |
3.25e-21 |
|
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: 92.89 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRYssQKQDLDGnLSVF 84
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--------LRPTSGSVLF--DGEDITG-LPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EAVLSSETSTLQIIKHYEQAvqqyTVEQtdrNfqAMMAAQ--------EAMDRHEAWDYNAEIKTILSKLGIHD-TTKQV 155
Cdd:cd03219 71 EIARLGIGRTFQIPRLFPEL----TVLE---N--VMVAAQartgsgllLARARREEREARERAEELLERVGLADlADRPA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 156 NSLSGGQQKRVVLAKTLIEQPDLLLLDEPT---NHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:cd03219 142 GELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-232 |
3.35e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.21 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDddftgditHPNQYRIRYSsqKQDLDGNLS--- 82
Cdd:COG1118 5 VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLE--------TPDSGRIVLN--GRDLFTNLPpre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 -----VFeavlssetstlqiikhyeqavQQY------TVEQtdrNFQAMMaaqeamdRHEAWDyNAEIKTILSKL----- 146
Cdd:COG1118 75 rrvgfVF---------------------QHYalfphmTVAE---NIAFGL-------RVRPPS-KAEIRARVEELlelvq 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 147 --GIHDttKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF------ESinWLINYVKQYPYTVLFVTHDR---Y 215
Cdd:COG1118 123 leGLAD--RYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrkelRR--WLRRLHDELGGTTVFVTHDQeeaL 198
|
250
....*....|....*..
gi 488422749 216 flnEVSTRIVELDRGKL 232
Cdd:COG1118 199 ---ELADRVVVMNQGRI 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-497 |
3.55e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 92.20 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVkvayfkQTEETLNRDIR 398
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDV------TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MI--DY-----LREESEVA-------KEKDGTTVSITQLLERFLFpSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLL 464
Cdd:cd03259 76 MVfqDYalfphLTVAENIAfglklrgVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 488422749 465 DEPTNDLDTET----LTILEDYIASFGGSVITVSHDR 497
Cdd:cd03259 155 DEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-225 |
3.76e-21 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 92.15 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADK----VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGn 80
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL---------------VDG- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 lsvfeavlssetstlQIIK--HYEQAV--QQY------TVEQtdrNF-----QAMMAAQEAMDRHEAWdynaeiktiLSK 145
Cdd:cd03293 66 ---------------EPVTgpGPDRGYvfQQDallpwlTVLD---NValgleLQGVPKAEARERAEEL---------LEL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 146 LGI----HDTTKQvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESI-NWLINYVKQYPYTVLFVTHDryfL 217
Cdd:cd03293 119 VGLsgfeNAYPHQ---LSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD---I 192
|
250
....*....|.
gi 488422749 218 NE---VSTRIV 225
Cdd:cd03293 193 DEavfLADRVV 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
324-513 |
4.92e-21 |
|
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: 91.51 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 324 LTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTlkigQTVKVAYFKQTEETLNRDIRMIDY- 402
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE----ITFDGKSYQKNIEALRRIGALIEAp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 403 -------LREESEV-AKEKDGTTVSITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTE 474
Cdd:cd03268 82 gfypnltARENLRLlARLLGIRKKRIDEVLDVVGLKDSAK-KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488422749 475 TLTILEDYI---ASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03268 161 GIKELRELIlslRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-232 |
5.18e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 94.78 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG----------IDDDftgDITH--PNQYRIRYSSQ 73
Cdd:COG3842 8 LENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfetpdsgrilLDGR---DVTGlpPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 74 KQDLDGNLSVFEAV---LSsetstlqiIKHYEQAvqqytvEQTDRnfqammaAQEAMDRHEawdynaeiktiLSKLGihd 150
Cdd:COG3842 85 DYALFPHLTVAENVafgLR--------MRGVPKA------EIRAR-------VAELLELVG-----------LEGLA--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 151 tTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD--------FEsinwLINYVKQYPYTVLFVTHDRyflNE--- 219
Cdd:COG3842 130 -DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklreemrEE----LRRLQRELGITFIYVTHDQ---EEala 201
|
250
....*....|...
gi 488422749 220 VSTRIVELDRGKL 232
Cdd:COG3842 202 LADRIAVMNDGRI 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-232 |
2.75e-20 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 89.99 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---------HPNQYRIRYSSQKQ 75
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILldgkditnlPPHKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVlsseTSTLQIIKHYEQAVQQYTVEQTDrnfqammaaQEAMDRHEAwdynaeiktilsklgihdttKQV 155
Cdd:cd03300 82 ALFPHLTVFENI----AFGLRLKKLPKAEIKERVAEALD---------LVQLEGYAN--------------------RKP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 156 NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINW----LINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd03300 129 SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDmqleLKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
.
gi 488422749 232 L 232
Cdd:cd03300 209 I 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-233 |
8.49e-20 |
|
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: 93.28 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYAD-KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGNlsvf 84
Cdd:COG4988 339 LEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL---------------INGV---- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssETSTLQiikhyEQAVQQYT--VEQTDRNFQA------MMAAQEAMDrheawdynAEIKTILSKLGIHDTTKQVN 156
Cdd:COG4988 400 ------DLSDLD-----PASWRRQIawVPQNPYLFAGtirenlRLGRPDASD--------EELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 S------------LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP--YTVLFVTHDRYFLNEVSt 222
Cdd:COG4988 461 DgldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAkgRTVILITHRLALLAQAD- 539
|
250
....*....|.
gi 488422749 223 RIVELDRGKLT 233
Cdd:COG4988 540 RILVLDDGRIV 550
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-235 |
8.65e-20 |
|
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: 88.39 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG------------DITHPNQYRIRYSS- 72
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkDIYDLDVDVLELRRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 73 -----QKQDLdGNLSVFEAVLssetstlqiikhYEQAVQQYtveqtDRNFQAMMAAQEAMDRHEAWDynaEIKTILSKLG 147
Cdd:cd03260 83 vgmvfQKPNP-FPGSIYDNVA------------YGLRLHGI-----KLKEELDERVEEALRKAALWD---EVKDRLHALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 148 ihdttkqvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQyPYTVLFVTHD-----Ryflne 219
Cdd:cd03260 142 ----------LSGGQQQRLCLARALANEPEVLLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHNmqqaaR----- 205
|
250
....*....|....*.
gi 488422749 220 VSTRIVELDRGKLTTY 235
Cdd:cd03260 206 VADRTAFLLNGRLVEF 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-232 |
9.14e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 88.33 E-value: 9.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD--KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT------HPNQYRIR----YSS 72
Cdd:cd03263 2 QIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysiRTDRKAARqslgYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 73 QKQDLDGNLSVFEAVLssetstlqiikhyeqavqqytveqtdrnFQAMMAAqeamdrHEAWDYNAEIKTILSKLGIHD-T 151
Cdd:cd03263 82 QFDALFDELTVREHLR----------------------------FYARLKG------LPKSEIKEEVELLLRVLGLTDkA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES--INW-LINYVKQYPyTVLFVTHDryfLNEV---STRIV 225
Cdd:cd03263 128 NKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASrrAIWdLILEVRKGR-SIILTTHS---MDEAealCDRIA 203
|
....*..
gi 488422749 226 ELDRGKL 232
Cdd:cd03263 204 IMSDGKL 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-232 |
1.06e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 88.08 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---------THPNQYRIRYSSQKQ 75
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVLSSETstlqiIKHYEQAVQQYTVEQTdrnfqammaaqeamdrheawdynAEIktilskLGI-HDTTKQ 154
Cdd:cd03301 82 ALYPHMTVYDNIAFGLK-----LRKVPKDEIDERVREV-----------------------AEL------LQIeHLLDRK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRG 230
Cdd:cd03301 128 PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
..
gi 488422749 231 KL 232
Cdd:cd03301 208 QI 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
320-474 |
1.58e-19 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 87.25 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQrIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK---------VAYFKQt 389
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EETLNRDIRMIDYLR--------EESEVAKEKDGTtVSITQLLERflfpsstHGKKIYKLSGGEQKRLYLLRLLVHQPNV 461
Cdd:cd03264 80 EFGVYPNFTVREFLDyiawlkgiPSKEVKARVDEV-LELVNLGDR-------AKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170
....*....|...
gi 488422749 462 LLLDEPTNDLDTE 474
Cdd:cd03264 152 LIVDEPTAGLDPE 164
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-232 |
1.58e-19 |
|
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: 87.27 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHpnqyrirYSSQKQDLDGNLSVF 84
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-------DGKSYQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EAVLSSETstlqiikhyeqavqqytveqtdrnFQAMMAAQEAMDRH--EAWDYNAEIKTILSKLGIHDTTKQ-VNSLSGG 161
Cdd:cd03268 75 GALIEAPG------------------------FYPNLTARENLRLLarLLGIRKKRIDEVLDVVGLKDSAKKkVKGFSLG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 162 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINW---LINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKElreLILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-232 |
2.08e-19 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 90.10 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDldgn 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 lsvfeavlssetstlqiikhYEQAVQQYTVeqtdrnFQAMMAAQ--------EAMDRHEAwdyNAEIKTILSKLGIHDTT 152
Cdd:TIGR03265 78 --------------------YGIVFQSYAL------FPNLTVADniayglknRGMGRAEV---AERVAELLDLVGLPGSE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 153 -KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESINWLINYV-KQYPYTVLFVTHDRYFLNEVSTRIVEL 227
Cdd:TIGR03265 129 rKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDArvrEHLRTEIRQLqRRLGVTTIMVTHDQEEALSMADRIVVM 208
|
....*
gi 488422749 228 DRGKL 232
Cdd:TIGR03265 209 NHGVI 213
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
321-547 |
2.16e-19 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 92.62 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 321 LDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGedQQFEGTLKIGQTVKVAYFKQTEET------LN 394
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAM--HAIDGIPKNCQILHVEQEVVGDDTtalqcvLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMIDYLREESEVAK----------------------EKDGTTVSITQLLERF-------------------LFPSST 433
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAqqrelefetetgkgkgankdgvDKDAVSQRLEEIYKRLelidaytaearaasilaglSFTPEM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 434 HGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDg 513
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG- 416
|
250 260 270
....*....|....*....|....*....|....
gi 488422749 514 mmERIVGSFEDYETYKKEKDKQLAIEKQATNTSK 547
Cdd:PLN03073 417 --QKLVTYKGDYDTFERTREEQLKNQQKAFESNE 448
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
318-505 |
2.87e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.90 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 VYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYfkQTEE------ 391
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW--SPAElarrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 ------TLN-----RDI-RM--IDYLREESEVAKEKDG--TTVSITQLLERFlFPSsthgkkiykLSGGEQKRLYLLRLL 455
Cdd:PRK13548 80 vlpqhsSLSfpftvEEVvAMgrAPHGLSRAEDDALVAAalAQVDLAHLAGRD-YPQ---------LSGGEQQRVQLARVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 456 V------HQPNVLLLDEPTNDLDT----ETLTILEDYIASFGGSVITVSHDryfLNKVAQ 505
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD---LNLAAR 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-232 |
3.62e-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: 87.01 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---------HPNQYRIRYSSQKQ 75
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedatdvPVQERNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVlsseTSTLQIiKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRheawdYNAEiktilsklgihdttkqv 155
Cdd:cd03296 84 ALFRHMTVFDNV----AFGLRV-KPRSERPPEAEIRAKVHELLKLVQLDWLADR-----YPAQ----------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 156 nsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd03296 137 --LSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
.
gi 488422749 232 L 232
Cdd:cd03296 215 I 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
329-524 |
3.65e-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: 91.36 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQT-----------VKVAY-------FKQT- 389
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrRQIAWvpqnpylFAGTi 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EETL---NRDI---RMIDYLRE---ESEVAKEKDGTTvsiTQLLERflfpssthGKkiyKLSGGEQKRLYLLRLLVHQPN 460
Cdd:COG4988 428 RENLrlgRPDAsdeELEAALEAaglDEFVAALPDGLD---TPLGEG--------GR---GLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 461 VLLLDEPTNDLDTETLTILEDYIASFGGS--VITVSHDRYFLnKVAQEYWFIHDGmmeRIV--GSFED 524
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALL-AQADRILVLDDG---RIVeqGTHEE 557
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-231 |
4.02e-19 |
|
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: 85.13 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD--KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHpNQYRIRySSQKQDLDGNLS 82
Cdd:cd03228 2 EFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-DGVDLR-DLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VfeavlssetstlqiikhyeqaVQQytveqtdrnfqammaaqeamdrhEAWDYNAeikTILSklgihdttkqvNSLSGGQ 162
Cdd:cd03228 80 Y---------------------VPQ-----------------------DPFLFSG---TIRE-----------NILSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP--YTVLFVTHdRYFLNEVSTRIVELDRGK 231
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAkgKTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-331 |
4.87e-19 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 91.00 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQdldgnlsvf 84
Cdd:PRK10636 314 KMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ--------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssetstLQIIKHYEQAVQQYtveqtdrnfqAMMAAQEamdrheawdYNAEIKTILSKLGIH--DTTKQVNSLSGGQ 162
Cdd:PRK10636 385 ----------LEFLRADESPLQHL----------ARLAPQE---------LEQKLRDYLGGFGFQgdKVTEETRRFSGGE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGNYEDY 242
Cdd:PRK10636 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 243 IAMRAEKEVIEQKQNDKQRAlykqelawmRAGAKARSTKQQARihrfndLEANVKqQQTQdkgELNLAYSRLGKQVYELD 322
Cdd:PRK10636 516 QQWLSDVQKQENQTDEAPKE---------NNANSAQARKDQKR------REAELR-TQTQ---PLRKEIARLEKEMEKLN 576
|
....*....
gi 488422749 323 SLTKTINGR 331
Cdd:PRK10636 577 AQLAQAEEK 585
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-231 |
5.19e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 86.59 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG---IDDdftGDIThpnqyriryssqkqdLDGnl 81
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLleePDS---GTIT---------------VDG-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 82 svfEAVLSSETSTLQIIKHyeqaV----QQY------TVEQtdrNfqAMMAAQEA--MDRHEAwdyNAEIKTILSKLGIH 149
Cdd:COG1126 63 ---EDLTDSKKDINKLRRK----VgmvfQQFnlfphlTVLE---N--VTLAPIKVkkMSKAEA---EERAMELLERVGLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 150 DttkQVNS----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVST 222
Cdd:COG1126 128 D---KADAypaqLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAkegMTMVVVTHEMGFAREVAD 204
|
....*....
gi 488422749 223 RIVELDRGK 231
Cdd:COG1126 205 RVVFMDGGR 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-232 |
5.43e-19 |
|
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: 85.92 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 7 EHLNKSY-ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITHPNQYRIRYSSQK---- 74
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqDVSDLRGRAIPYLRRKigvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 -QD--LDGNLSVFEAVLSSetstLQIIKHYEQAVQqytveqtdrnfQAMMAAQEAMD-RHEAWDYNAEiktilsklgihd 150
Cdd:cd03292 84 fQDfrLLPDRNVYENVAFA----LEVTGVPPREIR-----------KRVPAALELVGlSHKHRALPAE------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 151 ttkqvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVEL 227
Cdd:cd03292 137 -------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIAL 209
|
....*
gi 488422749 228 DRGKL 232
Cdd:cd03292 210 ERGKL 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
320-519 |
5.89e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTlkigqtvkVAYFKQTEETLNRD--- 396
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGE--------VRLNGRPLAAWSPWela 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 397 -IRMIdyLREESEVA-------------------KEKDGT-------TVSITQLLERFlFPSsthgkkiykLSGGEQKRL 449
Cdd:COG4559 75 rRRAV--LPQHSSLAfpftveevvalgraphgssAAQDRQivrealaLVGLAHLAGRS-YQT---------LSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 450 YLLRLL--VHQPN-----VLLLDEPTNDLDT----ETLTILEDYiASFGGSVITVSHDryfLNKVAQeY----WFIHDGm 514
Cdd:COG4559 143 QLARVLaqLWEPVdggprWLFLDEPTSALDLahqhAVLRLARQL-ARRGGGVVAVLHD---LNLAAQ-YadriLLLHQG- 216
|
....*
gi 488422749 515 meRIV 519
Cdd:COG4559 217 --RLV 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-234 |
6.56e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.61 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKqdLDGNLSVF 84
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EAV-LSSETSTLQIIKHYEQAvqQYT-----VEQTDRnfqamMAAQEAMDRHEAwdynaeiktilsklgIHDTTKQVNSL 158
Cdd:PRK11231 82 PQHhLTPEGITVRELVAYGRS--PWLslwgrLSAEDN-----ARVNQAMEQTRI---------------NHLADRRLTDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDfesINW------LINYVKQYPYTVLFVTHDryfLNEVS---TRIVELDR 229
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD---INHqvelmrLMRELNTQGKTVVTVLHD---LNQASrycDHLVVLAN 213
|
....*
gi 488422749 230 GKLTT 234
Cdd:PRK11231 214 GHVMA 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-232 |
8.66e-19 |
|
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: 86.25 E-value: 8.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRYssQKQDLDG----- 79
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--------YRPTSGRILF--DGRDITGlpphr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 -----------------NLSVFEAVLSsetstlqiikhyeqAVQQytveQTDRNFQAMM------AAQEAMDRHEAWDyn 136
Cdd:COG0411 76 iarlgiartfqnprlfpELTVLENVLV--------------AAHA----RLGRGLLAALlrlpraRREEREARERAEE-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 137 aeiktILSKLGIHD-TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPT---NHLDFESINWLINYVKQ-YPYTVLFVT 211
Cdd:COG0411 136 -----LLERVGLADrADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDeRGITILLIE 210
|
250 260
....*....|....*....|.
gi 488422749 212 HDRYFLNEVSTRIVELDRGKL 232
Cdd:COG0411 211 HDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
343-513 |
9.56e-19 |
|
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: 85.04 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 343 SGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTV---------------KVAYFKQtEETL--NRDIRM-IDYLR 404
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQ-QYALfpHLNVREnLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 405 EESEVAKEKDgttvSITQLLERFLFpSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYI- 483
Cdd:cd03297 101 KRKRNREDRI----SVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELk 175
|
170 180 190
....*....|....*....|....*....|...
gi 488422749 484 ---ASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03297 176 qikKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-232 |
1.26e-18 |
|
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: 89.19 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYA-----DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITHPNQYRIRYSS 72
Cdd:COG1123 262 EVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsilfdgkDLTKLSRRSLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 73 QK-----QD----LDGNLSVFEAVlsseTSTLQIikhyeqavqqytveqtdrnfQAMMAAQEAMDRheawdynaeIKTIL 143
Cdd:COG1123 342 RRvqmvfQDpyssLNPRMTVGDII----AEPLRL--------------------HGLLSRAERRER---------VAELL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 144 SKLGIHDTTKQVN--SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDfESI-----NWLINYVKQYPYTVLFVTHDRYF 216
Cdd:COG1123 389 ERVGLPPDLADRYphELSGGQRQRVAIARALALEPKLLILDEPTSALD-VSVqaqilNLLRDLQRELGLTYLFISHDLAV 467
|
250
....*....|....*.
gi 488422749 217 LNEVSTRIVELDRGKL 232
Cdd:COG1123 468 VRYIADRVAVMYDGRI 483
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-233 |
1.52e-18 |
|
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: 89.44 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSY--ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnls 82
Cdd:COG4987 335 ELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT---------------LGG--- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 vfeavlssetstlQIIKHY-EQAVQQYT--VEQTDRNFQA------MMAAQEAMDrheawdynAEIKTILSKLGIHDTTK 153
Cdd:COG4987 397 -------------VDLRDLdEDDLRRRIavVPQRPHLFDTtlrenlRLARPDATD--------EELWAALERVGLGDWLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 154 QVN------------SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY--PYTVLFVTHDRYFLNE 219
Cdd:COG4987 456 ALPdgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLER 535
|
250
....*....|....
gi 488422749 220 VsTRIVELDRGKLT 233
Cdd:COG4987 536 M-DRILVLEDGRIV 548
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-232 |
1.66e-18 |
|
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: 84.73 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADK----VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNqyrIRYSSQKQDLDGNL 81
Cdd:cd03266 4 ADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---FDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 82 SVFEA--VLSSETSTLQIIKHYeqavqqytveqtdrnfqammAAQEAMDRHEAwdyNAEIKTILSKLGIHDT-TKQVNSL 158
Cdd:cd03266 81 GFVSDstGLYDRLTARENLEYF--------------------AGLYGLKGDEL---TARLEELADRLGMEELlDRRVGGF 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:cd03266 138 STGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRalgKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-496 |
2.02e-18 |
|
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: 84.80 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQ------QFEGT------------LKIGQT- 380
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEditglppheiarLGIGRTf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 381 --------------VKVAYFKQTEETLNRDIRMidylREESEVAKEkdgttvsITQLLERF-L-----FPSSThgkkiyk 440
Cdd:cd03219 82 qiprlfpeltvlenVMVAAQARTGSGLLLARAR----REEREARER-------AEELLERVgLadladRPAGE------- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 441 LSGGEQKRLYLLRLLVHQPNVLLLDEPT---NDLDTETLTILEDYIASFGGSVITVSHD 496
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
329-495 |
3.55e-18 |
|
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: 84.37 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEgtlkiGQTVKVAYFKQTEETLnRDIR---------- 398
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY-----GNDVRLFGERRGGEDV-WELRkriglvspal 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 --------------------MIDYLREESEVAKEKdgttvsITQLLERF-LfpssTH--GKKIYKLSGGEQKRLYLLRLL 455
Cdd:COG1119 88 qlrfprdetvldvvlsgffdSIGLYREPTDEQRER------ARELLELLgL----AHlaDRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488422749 456 VHQPNVLLLDEPTNDLDTET----LTILEDYIASFGGSVITVSH 495
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-231 |
4.27e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.16 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLK-VMGGIDDDfTGDIT---HPNQYRIR----------- 69
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRiILGILAPD-SGEVLwdgEPLDPEDRrrigylpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 -YSSQKqdldgnlsvfeaVLssetstlqiikhyEQAVqqYtveqtdrnfqamMAAQEAMDRHEAwdyNAEIKTILSKLGI 148
Cdd:COG4152 82 lYPKMK------------VG-------------EQLV--Y------------LARLKGLSKAEA---KRRADEWLERLGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 149 HD-TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPY---TVLFVTHDryfLNEVST-- 222
Cdd:COG4152 120 GDrANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAkgtTVIFSSHQ---MELVEElc 196
|
250
....*....|
gi 488422749 223 -RIVELDRGK 231
Cdd:COG4152 197 dRIVIINKGR 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-232 |
4.30e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 9 LNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYrIRYSsqkQDLDGNLSVF--EA 86
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQT-INLV---RDKDGQLKVAdkNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 87 VLSSETSTLQIIKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRHEAWDYnaeiktiLSKLGIHDTT--KQVNSLSGGQQK 164
Cdd:PRK10619 87 LRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKY-------LAKVGIDERAqgKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 165 RVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
282-496 |
4.48e-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: 88.35 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 282 QQARIH--RFNDLeanVKQQQTQDKGELNLAYSRLGKQVyELDSLTKTINGRT--LFQDITQIIQSGQRIGIVGPNGAGK 357
Cdd:COG2274 439 QDAKIAleRLDDI---LDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 358 TTMLNILSGEDQQFEGTLKI-GQTVK----------VAYFKQTEETLNRDIR----MIDYLREESEV---AKEkdgttVS 419
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILIdGIDLRqidpaslrrqIGVVLQDVFLFSGTIRenitLGDPDATDEEIieaARL-----AG 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 420 ITQLLERFlfPS------STHGKKiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGG--SVI 491
Cdd:COG2274 590 LHDFIEAL--PMgydtvvGEGGSN---LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVI 664
|
....*
gi 488422749 492 TVSHD 496
Cdd:COG2274 665 IIAHR 669
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
320-517 |
5.54e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.18 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKT-INGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV------KVAYfkqtee 391
Cdd:COG2884 3 RFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrrEIPY------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 tLNRDIRMI--DY---------------LR----EESEVAKEkdgttvsITQLLERF-LfpssthGKKIYK----LSGGE 445
Cdd:COG2884 77 -LRRRIGVVfqDFrllpdrtvyenvalpLRvtgkSRKEIRRR-------VREVLDLVgL------SDKAKAlpheLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 446 QKRLYLLRLLVHQPNVLLLDEPTNDLDTET----LTILEDyIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMMER 517
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETsweiMELLEE-INRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-524 |
5.75e-18 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 83.32 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQtVKVAYFKQTEET-LNRDIR 398
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG-EDISGLSEAELYrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MI-------D----------YLREESEVAKEkdgttvSITQL----LERF-------LFPSSthgkkiykLSGGEQKRLY 450
Cdd:cd03261 81 MLfqsgalfDsltvfenvafPLREHTRLSEE------EIREIvlekLEAVglrgaedLYPAE--------LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 451 LLRLLVHQPNVLLLDEPTNDLDTETLTILEDYI----ASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIV--GSFED 524
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLYDG---KIVaeGTPEE 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
320-497 |
6.88e-18 |
|
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: 86.96 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRT-LFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFK 387
Cdd:TIGR02857 323 EFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QT----EETLNRDIRMidYLREESEVAKEKDGTTVSITQLLERFlfPSSTH---GKKIYKLSGGEQKRLYLLRLLVHQPN 460
Cdd:TIGR02857 403 QHpflfAGTIAENIRL--ARPDASDAEIREALERAGLDEFVAAL--PQGLDtpiGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190
....*....|....*....|....*....|....*....
gi 488422749 461 VLLLDEPTNDLDTETLTILEDYIASF--GGSVITVSHDR 497
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRL 517
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-232 |
6.88e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 83.02 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDdftgdithPNQYRIRY----SSQ--KQDLDGNLSvfeavlssets 93
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK--------PTSGSVLLdgtdIRQldPADLRRNIG----------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 94 tlqiikhyeqavqqyTVEQTDRNFQA------MMAAQEAMDRheawdynaEIKTILSKLGIHDTTK--------QVN--- 156
Cdd:cd03245 82 ---------------YVPQDVTLFYGtlrdniTLGAPLADDE--------RILRAAELAGVTDFVNkhpngldlQIGerg 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 157 -SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY--PYTVLFVTHDRYFLNEVStRIVELDRGKL 232
Cdd:cd03245 139 rGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLVD-RIIVMDSGRI 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-504 |
8.92e-18 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 87.15 E-value: 8.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 32 IGLVGINGTGKSTLLKVMGGIdddftgdithpnqyriryssqkqdLDGNLSVFEavlsSETSTLQIIKHYE-QAVQQYTV 110
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGE------------------------LKPNLGDYD----EEPSWDEVLKRFRgTELQDYFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 111 EQTDRNFQAMMAAQ-----------------EAMDRHEAWDYnaeiktILSKLGI-HDTTKQVNSLSGGQQKRVVLAKTL 172
Cdd:COG1245 154 KLANGEIKVAHKPQyvdlipkvfkgtvrellEKVDERGKLDE------LAEKLGLeNILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 173 IEQPDLLLLDEPTNHLD-FESINW--LINYVKQYPYTVLFVTHDRYFLnevstriveldrgklttypgnyeDYIAmraek 249
Cdd:COG1245 228 LRDADFYFFDEPSSYLDiYQRLNVarLIRELAEEGKYVLVVEHDLAIL-----------------------DYLA----- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 250 EVIEqkqndkqrALYKQELAWMRAgAKARSTK-------------QQARIhRFNDLEANVKQQQTQDKGELNLAYSRLGK 316
Cdd:COG1245 280 DYVH--------ILYGEPGVYGVV-SKPKSVRvginqyldgylpeENVRI-RDEPIEFEVHAPRREKEEETLVEYPDLTK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 317 QvyeLDSLTKTINGRTlfqditqiIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGtlKIGQTVKVAYFKQTEETlNRD 396
Cdd:COG1245 350 S---YGGFSLEVEGGE--------IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKPQYISP-DYD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 397 IRMIDYLReesEVAKEKDGTTVSITQLLERFLFpssthgKKIY-----KLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:COG1245 416 GTVEEFLR---SANTDDFGSSYYKTEIIKPLGL------EKLLdknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
490 500 510
....*....|....*....|....*....|....*..
gi 488422749 472 DTE----TLTILEDYIASFGGSVITVSHDRYFLNKVA 504
Cdd:COG1245 487 DVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLIDYIS 523
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
329-496 |
9.37e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEE-------------TLNR 395
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEvpdslpltvrdlvAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 396 --DIRMIDYLREESEVAKEKDGTTVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDT 473
Cdd:NF040873 83 waRRGLWRRLTRDDRAAVDDALERVGLADLAGR----------QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*.
gi 488422749 474 ETLTILEDYIASF---GGSVITVSHD 496
Cdd:NF040873 153 ESRERIIALLAEEharGATVVVVTHD 178
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
320-495 |
1.02e-17 |
|
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: 80.66 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLT-KTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEetlnrdir 398
Cdd:cd03223 2 ELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 midYLreesevakeKDGTtvsitqLLERFLFPSSThgkkiyKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTI 478
Cdd:cd03223 74 ---YL---------PLGT------LREQLIYPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170
....*....|....*..
gi 488422749 479 LEDYIASFGGSVITVSH 495
Cdd:cd03223 130 LYQLLKELGITVISVGH 146
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-213 |
1.22e-17 |
|
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: 81.96 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 19 FDDLSLAIS---NHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---------------THPNQYRIRYSSQKQDLDGN 80
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 LSVFEAVLSSetstlqiIKHYEQAVQQYTVEQtdrnFQAMMAAQEAMDRHeawdynaeiktilsklgihdttkqVNSLSG 160
Cdd:cd03297 90 LNVRENLAFG-------LKRKRNREDRISVDE----LLDLLGLDHLLNRY------------------------PAQLSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQ----YPYTVLFVTHD 213
Cdd:cd03297 135 GEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHD 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
320-524 |
1.39e-17 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 82.33 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVkvayFKQTEETLNRdIR 398
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdGQDI----TGLSEKELYE-LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 M-----------ID----------YLRE-----ESEV---AKEKdgttvsitqlLERF-------LFPSSthgkkiykLS 442
Cdd:COG1127 82 RrigmlfqggalFDsltvfenvafPLREhtdlsEAEIrelVLEK----------LELVglpgaadKMPSE--------LS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 443 GGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYI----ASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRI 518
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDLDSAFAIADRVAVLADG---KI 220
|
....*...
gi 488422749 519 V--GSFED 524
Cdd:COG1127 221 IaeGTPEE 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
320-496 |
1.55e-17 |
|
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: 82.78 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQ------QFEGT------------LKIGQT- 380
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGRditglpphriarLGIARTf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 381 --------------VKVAYFKQTEETLNRDI-RMIDYLREESEVAKEkdgttvsITQLLERF-LfpSSTHGKKIYKLSGG 444
Cdd:COG0411 86 qnprlfpeltvlenVLVAAHARLGRGLLAALlRLPRARREEREARER-------AEELLERVgL--ADRADEPAGNLSYG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 445 EQKRLYLLRLLVHQPNVLLLDEPT---NDLDTETLT-ILEDYIASFGGSVITVSHD 496
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAaglNPEETEELAeLIRRLRDERGITILLIEHD 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-253 |
1.78e-17 |
|
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: 82.00 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIfDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITH--PNQYRIRYSSQKQ 75
Cdd:cd03299 2 KVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkillngkDITNlpPEKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVlssetstlqiikHYEQAVQQYTVEQTDRnfqammaaqeamdrheawdynaEIKTILSKLGI-HDTTKQ 154
Cdd:cd03299 81 ALFPHMTVYKNI------------AYGLKKRKVDKKEIER----------------------KVLEIAEMLGIdHLLNRK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHDRYFLNEVSTRIVELDRG 230
Cdd:cd03299 127 PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
250 260
....*....|....*....|...
gi 488422749 231 KLTTYpGNYEDYIAMRAEKEVIE 253
Cdd:cd03299 207 KLIQV-GKPEEVFKKPKNEFVAE 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-235 |
1.98e-17 |
|
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: 81.17 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---HPNQY----RIRYSSQKQDL 77
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgKPLDIaarnRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 78 DGNLSVFEavlssetstlqiikhyeqavqqytveqtdrnfQAMMAAQ-EAMDRHEAwdyNAEIKTILSKLGIHD-TTKQV 155
Cdd:cd03269 82 YPKMKVID--------------------------------QLVYLAQlKGLKKEEA---RRRIDEWLERLELSEyANKRV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 156 NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:cd03269 127 EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
...
gi 488422749 233 TTY 235
Cdd:cd03269 207 VLY 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-232 |
2.51e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.98 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDddftgditHPNQYRIRYSSQkqDLDGnlsvfe 85
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLE--------HQTSGHIRFHGT--DVSR------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 aVLSSETSTLQIIKHYeQAVQQYTVeqtdrnFQAMMAAQEAMDRHEAWDyNAEIKTILSKLG-----IHDTTKQVNSLSG 160
Cdd:PRK10851 69 -LHARDRKVGFVFQHY-ALFRHMTV------FDNIAFGLTVLPRRERPN-AAAIKAKVTQLLemvqlAHLADRYPAQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
316-495 |
3.45e-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: 80.29 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 316 KQVYELDSLTKTING------RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGedqQFEGTLKIGqTVKVAYFKQT 389
Cdd:cd03213 1 GVTLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG---RRTGLGVSG-EVLINGRPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EETLNRDIRMI---DYLREESEVAkekdgttvsitqllERFLFPSsthgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:cd03213 77 KRSFRKIIGYVpqdDILHPTLTVR--------------ETLMFAA-----KLRGLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190
....*....|....*....|....*....|...
gi 488422749 467 PTNDLDTET----LTILEDyIASFGGSVITVSH 495
Cdd:cd03213 138 PTSGLDSSSalqvMSLLRR-LADTGRTIICSIH 169
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-233 |
3.77e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 81.22 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 10 NKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT----HPNQYRIRYSS-------QKQDLD 78
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglVPWKRRKKFLRrigvvfgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 79 GNLSVFEavlssetsTLQIIKH-YEQAVQQYTveQTDRNFQAMMAAQEAMDrheawdynaeiktilsklgihdttKQVNS 157
Cdd:cd03267 108 WDLPVID--------SFYLLAAiYDLPPARFK--KRLDELSELLDLEELLD------------------------TPVRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESI-NWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLT 233
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIrNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-504 |
3.91e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.86 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 32 IGLVGINGTGKSTLLKVMGGIdddftgdithpnqyriryssqkqdLDGNLSVFEavlsSETSTLQIIKHYE-QAVQQYTV 110
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGE------------------------LIPNLGDYE----EEPSWDEVLKRFRgTELQNYFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 111 EQTDRNFQAMMAAQ-----------------EAMDRHEAWDYnaeiktILSKLGIHDTTKQ-VNSLSGGQQKRVVLAKTL 172
Cdd:PRK13409 154 KLYNGEIKVVHKPQyvdlipkvfkgkvrellKKVDERGKLDE------VVERLGLENILDRdISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 173 IEQPDLLLLDEPTNHLD-FESINwLINYVKQYpytvlfvTHDRYFLnevstrIVELDRGKLttypgnyeDYIAmraekEV 251
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDiRQRLN-VARLIREL-------AEGKYVL------VVEHDLAVL--------DYLA-----DN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 252 IEqkqndkqralykqeLAWMRAGA-----KARSTK-------------QQARIhRFNDLEANVKQQQTQDKGELNLAYSR 313
Cdd:PRK13409 281 VH--------------IAYGEPGAygvvsKPKGVRvgineylkgylpeENMRI-RPEPIEFEERPPRDESERETLVEYPD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 314 LGKQvyeLDSLTKTINGRTLFQditqiiqsGQRIGIVGPNGAGKTTMLNILSGEDQQFEGtlKIGQTVKVAYFKQTEETl 393
Cdd:PRK13409 346 LTKK---LGDFSLEVEGGEIYE--------GEVIGIVGPNGIGKTTFAKLLAGVLKPDEG--EVDPELKISYKPQYIKP- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRDIRMIDYLREesevAKEKDGTTVSITQLLERFLFPsSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDT 473
Cdd:PRK13409 412 DYDGTVEDLLRS----ITDDLGSSYYKSEIIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
490 500 510
....*....|....*....|....*....|....*
gi 488422749 474 E----TLTILEDYIASFGGSVITVSHDRYFLNKVA 504
Cdd:PRK13409 487 EqrlaVAKAIRRIAEEREATALVVDHDIYMIDYIS 521
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
320-513 |
5.11e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 80.30 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG-EDQQF----EGTLKI-GQTVKVAyfKQTEETL 393
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlNDLIPgapdEGEVLLdGKDIYDL--DVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRDIRM---------------IDY---LREEsevaKEKDGTTVSITQLLERFLFPSSTHGK-KIYKLSGGEQKRLYLLRL 454
Cdd:cd03260 80 RRRVGMvfqkpnpfpgsiydnVAYglrLHGI----KLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 455 LVHQPNVLLLDEPTNDLDTETLTILEDYIASFGG--SVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
320-495 |
6.95e-17 |
|
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: 79.32 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTvkvAYFKQTEETLnrdiRM 399
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT---PLAEQRDEPH----EN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 IDYLREESEV-----AKEK--------DGTTVSITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:TIGR01189 75 ILYLGHLPGLkpelsALENlhfwaaihGGAQRTIEDALAAVGLTGFED-LPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 488422749 467 PTNDLDTETLTILEDYIASF---GGSVITVSH 495
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
320-515 |
9.14e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 79.37 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTI-NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV------KVAYFKQTEE 391
Cdd:cd03292 2 EFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 TLNRDIRMIDYLREESEVAKEKDGTTVS-------ITQLLERfLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLL 464
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPpreirkrVPAALEL-VGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 465 DEPTNDLDTET----LTILEDyIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMM 515
Cdd:cd03292 161 DEPTGNLDPDTtweiMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-496 |
9.82e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKS-TLLKVMGGIDDD----FTGDITHPNQYRIRYSSQK-QDLDGN--LSVFEAVLSSE 91
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTlRGVRGNkiAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 92 TSTLQIIKhyeqavQQYTVeqtdrnfqamMAAQEAMDRHEAwdyNAEIKTILSKLGIHDTTKQVN----SLSGGQQKRVV 167
Cdd:PRK15134 106 NPLHTLEK------QLYEV----------LSLHRGMRREAA---RGEILNCLDRVGIRQAAKRLTdyphQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 168 LAKTLIEQPDLLLLDEPTNHLDFE---SINWLINYVKQ-YPYTVLFVTHDryfLNevstrIVEldrgKLTtypgnyeDYI 243
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSvqaQILQLLRELQQeLNMGLLFITHN---LS-----IVR----KLA-------DRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 244 AMRAEKEVIEQKQNDK-----QRALYKQELAWMRAGAKARSTKQQARIHRFNDLEANVKQQQtqdkgelnlaysrlgkqv 318
Cdd:PRK15134 228 AVMQNGRCVEQNRAATlfsapTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRK------------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 319 yelDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTT----MLNILSGEDQ-QFEGT----------LKIGQTVKV 383
Cdd:PRK15134 290 ---GILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEiWFDGQplhnlnrrqlLPVRHRIQV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 384 AyFKQTEETLNRDIRMIDYLREESEV------AKEKDGTTVSITQllERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVH 457
Cdd:PRK15134 367 V-FQDPNSSLNPRLNVLQIIEEGLRVhqptlsAAQREQQVIAVME--EVGLDPETRH-RYPAEFSGGQRQRIAIARALIL 442
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 488422749 458 QPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:PRK15134 443 KPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHD 485
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-232 |
1.00e-16 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 80.24 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDD------DFTGDITHPNQYRIR-----YSSQ 73
Cdd:TIGR03873 3 RLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpdagtvDLAGVDLHGLSRRARarrvaLVEQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 74 KQDLDGNLSVFEAVLSSETStlqiikhyeqavqqytveqtdrnFQAMMAAQEAMDrHEAWDYnaeiktILSKLGI-HDTT 152
Cdd:TIGR03873 83 DSDTAVPLTVRDVVALGRIP-----------------------HRSLWAGDSPHD-AAVVDR------ALARTELsHLAD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 153 KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPY---TVLFVTHDRYFLNEVSTRIVELDR 229
Cdd:TIGR03873 133 RDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDG 212
|
...
gi 488422749 230 GKL 232
Cdd:TIGR03873 213 GRV 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
321-496 |
1.11e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 321 LDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQtvkvAYFKQTEEtlnrDIRM- 399
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT----APLAEARE----DTRLm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 ------------IDYL--------REESEVAKEKDGttvsitqLLERFL-FPSSthgkkiykLSGGEQKRLYLLRLLVHQ 458
Cdd:PRK11247 87 fqdarllpwkkvIDNVglglkgqwRDAALQALAAVG-------LADRANeWPAA--------LSGGQKQRVALARALIHR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488422749 459 PNVLLLDEPTNDLDTETLTILEDYIASF----GGSVITVSHD 496
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLwqqhGFTVLLVTHD 193
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
327-515 |
1.44e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 327 TINGRtlFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEdQQFEGTLKIGQT-----------VKVAYFKQTEETLNr 395
Cdd:COG4138 7 AVAGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRplsdwsaaelaRHRAYLSQQQSPPF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 396 DIRMIDYLR--EESEVAKEKDGTTVSitQLLERF----LFPSSTHgkkiyKLSGGEQKRLYLLR--LLVH-----QPNVL 462
Cdd:COG4138 83 AMPVFQYLAlhQPAGASSEAVEQLLA--QLAEALgledKLSRPLT-----QLSGGEWQRVRLAAvlLQVWptinpEGQLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 463 LLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDryfLN---KVAQEYWFIHDGMM 515
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD---LNhtlRHADRVWLLKQGKL 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-231 |
1.57e-16 |
|
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: 79.02 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITH-PNQYRIR----YSS 72
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrDITGlPPHERARagigYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 73 QKQDLDGNLSVFEavlssetstlqiikhyeqavqqytveqtdrNFQamMAAQEAMDRHEAWDYnAEIKTILSKLgiHDTT 152
Cdd:cd03224 82 EGRRIFPELTVEE------------------------------NLL--LGAYARRRAKRKARL-ERVYELFPRL--KERR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 153 KQ-VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESINWLinyvKQYPYTVLFVTHDRYFLNEVSTRI 224
Cdd:cd03224 127 KQlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLApkiveeiFEAIREL----RDEGVTILLVEQNARFALEIADRA 202
|
....*..
gi 488422749 225 VELDRGK 231
Cdd:cd03224 203 YVLERGR 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-235 |
1.95e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVM-------------GGIDDDFTgdiTHPNQYRIRYS 71
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdsgqlniAGHQFDFS---QKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 72 SQKQDLdgnlsVFeavlssetstlqiikhyeqavQQY------TVEQtdrNFQAM------MAAQEAMDRheawdynaeI 139
Cdd:COG4161 81 RQKVGM-----VF---------------------QQYnlwphlTVME---NLIEApckvlgLSKEQAREK---------A 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 140 KTILSKLGIHDTTKQV-NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SINWLINYVKQYPYTVLFVTHDRY 215
Cdd:COG4161 123 MKLLARLRLTDKADRFpLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIVTHEVE 202
|
250 260
....*....|....*....|
gi 488422749 216 FLNEVSTRIVELDRGKLTTY 235
Cdd:COG4161 203 FARKVASQVVYMEKGRIIEQ 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
329-524 |
2.31e-16 |
|
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: 82.51 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQtvkVAYFKQTEETLNRDIRMID---YL-- 403
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG---VDLRDLDEDDLRRRIAVVPqrpHLfd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 404 ---REESEVAKEkDGTTVSITQLLER-----FL--FPSS------THGKKiykLSGGEQKRLYLLRLLVHQPNVLLLDEP 467
Cdd:COG4987 423 ttlRENLRLARP-DATDEELWAALERvglgdWLaaLPDGldtwlgEGGRR---LSGGERRRLALARALLRDAPILLLDEP 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 468 TNDLDTET-LTILEDYIASFGG-SVITVSHDRYFLNKVAQEYwFIHDGmmeRIV--GSFED 524
Cdd:COG4987 499 TEGLDAATeQALLADLLEALAGrTVLLITHRLAGLERMDRIL-VLEDG---RIVeqGTHEE 555
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-233 |
2.32e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.98 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 11 KSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnLSVfeavLSS 90
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI---------------VDG-LKV----NDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 91 ETSTLQIIKHYEQAVQQYTVeqtdrnFQAMMAAQEAM---------DRHEAwdyNAEIKTILSKLGIHDTTKQVNS-LSG 160
Cdd:PRK09493 69 KVDERLIRQEAGMVFQQFYL------FPHLTALENVMfgplrvrgaSKEEA---EKQARELLAKVGLAERAHHYPSeLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVELDRGKLT 233
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeegMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-232 |
2.83e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 79.42 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIF-----DDLSLAISNHEKIGLVGINGTGKSTLLKVMGG----------IDDDftgDITHPNQYRIR 69
Cdd:TIGR04521 2 KLKNVSYIYQPGTPFekkalDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGllkptsgtvtIDGR---DITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSSQKQDLdgnlsVF---EAVLSSETstlqIIKhyeqavqqytveqtD-----RNFQamMAAQEAMDRheawdynaeIKT 141
Cdd:TIGR04521 79 DLRKKVGL-----VFqfpEHQLFEET----VYK--------------DiafgpKNLG--LSEEEAEER---------VKE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 142 ILSKLGIHDTTKQVN--SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----INWLINYVKQYPYTVLFVTHDry 215
Cdd:TIGR04521 125 ALELVGLDEEYLERSpfELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGrkeiLDLFKRLHKEKGLTVILVTHS-- 202
|
250 260
....*....|....*....|
gi 488422749 216 fLNEV---STRIVELDRGKL 232
Cdd:TIGR04521 203 -MEDVaeyADRVIVMHKGKI 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-520 |
3.05e-16 |
|
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: 78.38 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTI-NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEETLNRDIR 398
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MI--DY-LREESEVAKE----KDGTTVSITQLLErfLFP----------------SSTHGKKIYKLSGGEQKRLYLLRLL 455
Cdd:cd03256 82 MIfqQFnLIERLSVLENvlsgRLGRRSTWRSLFG--LFPkeekqralaalervglLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 456 VHQPNVLLLDEPTNDLDTETLTILEDYIA----SFGGSVITVSHDryfLNkVAQEYwfihdgmMERIVG 520
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKrinrEEGITVIVSLHQ---VD-LAREY-------ADRIVG 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-232 |
3.13e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMggidddfTGDIThPNQYRIRYssQKQDLdgnlsvfe 85
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-------SGELS-PDSGEVRL--NGRPL-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 avlsSETSTLQIIKHyeQAV--QQ------YTVEQ---------TDRNFQAMMAAQEAMDRHEAWDYnaeiktilsklgi 148
Cdd:PRK13548 67 ----ADWSPAELARR--RAVlpQHsslsfpFTVEEvvamgraphGLSRAEDDALVAAALAQVDLAHL------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 149 hdTTKQVNSLSGGQQKRVVLAKTLI------EQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHD----- 213
Cdd:PRK13548 128 --AGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaa 205
|
250
....*....|....*....
gi 488422749 214 RYflnevSTRIVELDRGKL 232
Cdd:PRK13548 206 RY-----ADRIVLLHQGRL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
320-496 |
3.56e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.59 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKT----INGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVkvayfkqteETLN 394
Cdd:COG1116 9 ELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdGKPV---------TGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMI--DY---------------LREESEVAKEKDGTtvsITQLLERF-LfpSSTHGKKIYKLSGGEQKRLYLLRLLV 456
Cdd:COG1116 80 PDRGVVfqEPallpwltvldnvalgLELRGVPKAERRER---ARELLELVgL--AGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488422749 457 HQPNVLLLDEPTNDLDTETLTILEDYI----ASFGGSVITVSHD 496
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-472 |
3.75e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIE--HLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGI--DDDFTGDIThpnqyriryssqkqd 76
Cdd:PRK13549 1 MMEYLLEmkNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEII--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 77 LDGNLSVFEAVLSSETSTLQIIkHYEQA-VQQYTVEQTdrnfqaMMAAQEAMdRHEAWDYNA---EIKTILSKLGIH-DT 151
Cdd:PRK13549 66 FEGEELQASNIRDTERAGIAII-HQELAlVKELSVLEN------IFLGNEIT-PGGIMDYDAmylRAQKLLAQLKLDiNP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYV---KQYPYTVLFVTHDryfLNEV---STRIV 225
Cdd:PRK13549 138 ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIrdlKAHGIACIYISHK---LNEVkaiSDTIC 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 226 ELDRGK-LTTYPG---NYEDYIAMRAEKEVieqkqndkqRALYKQElawmragakarstkqqarihrfndlEANVkqqqt 301
Cdd:PRK13549 215 VIRDGRhIGTRPAagmTEDDIITMMVGREL---------TALYPRE-------------------------PHTI----- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 302 qdkgelnlaysrlGKQVYELDSLT---KTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQ-QFEGTLKI 377
Cdd:PRK13549 256 -------------GEVILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 378 -GQTVKVayfKQTEETLNRDIRMIDYLREESEV--------------------------AKEKDgttvSITQLLERFLFP 430
Cdd:PRK13549 323 dGKPVKI---RNPQQAIAQGIAMVPEDRKRDGIvpvmgvgknitlaaldrftggsriddAAELK----TILESIQRLKVK 395
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 488422749 431 SSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD 472
Cdd:PRK13549 396 TASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-522 |
5.27e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.02 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGI--DDDFTGDIThpnqyriryssqkqdLDGNLS 82
Cdd:TIGR02633 3 EMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIY---------------WSGSPL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETSTLQIIKHYEQAVQQYTVEQTdrnfqaMMAAQEAMDRHEAWDYNAEI---KTILSKLGIHDT--TKQVNS 157
Cdd:TIGR02633 68 KASNIRDTERAGIVIIHQELTLVPELSVAEN------IFLGNEITLPGGRMAYNAMYlraKNLLRELQLDADnvTRPVGD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYV---KQYPYTVLFVTHDryfLNEVS----TRIVELDRG 230
Cdd:TIGR02633 142 YGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIrdlKAHGVACVYISHK---LNEVKavcdTICVIRDGQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 231 KLTTYPG---NYEDYIAMRAEKEVieqkqndkqRALYKQELawmragakarstkqqarihrfndleanvkqqqtqdkgel 307
Cdd:TIGR02633 219 HVATKDMstmSEDDIITMMVGREI---------TSLYPHEP--------------------------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 308 nlaySRLGKQVYELDSLT--KTIN-GRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGE-DQQFEGTLKIGQtvKV 383
Cdd:TIGR02633 251 ----HEIGDVILEARNLTcwDVINpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFING--KP 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 384 AYFKQTEETLNRDIRMIDYLREESEV--------------------------AKEKDGTTVSITQLLERFLFPSSThgkk 437
Cdd:TIGR02633 325 VDIRNPAQAIRAGIAMVPEDRKRHGIvpilgvgknitlsvlksfcfkmridaAAELQIIGSAIQRLKVKTASPFLP---- 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 438 IYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET---LTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGm 514
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG- 479
|
....*...
gi 488422749 515 meRIVGSF 522
Cdd:TIGR02633 480 --KLKGDF 485
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
330-514 |
5.47e-16 |
|
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: 76.91 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 330 GRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIG-------QTVKVAYF-------KQTEETLNR 395
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakERRKSIGYvmqdvdyQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 396 DIRMIDYLREESEVAKEKDGTTVSITQLLERflFPSSthgkkiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:cd03226 92 ELLLGLKELDAGNEQAETVLKDLDLYALKER--HPLS--------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488422749 476 LTILEDYI---ASFGGSVITVSHDRYFLNKVAQEYWFIHDGM 514
Cdd:cd03226 162 MERVGELIrelAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
335-513 |
5.89e-16 |
|
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: 77.76 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTV----KVAYFKQ------TEETLNRDIRMIDYLR 404
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRRigvvfgQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 405 --------EESEVAKEKDGttvsITQLL--ERFLFpssthgKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTE 474
Cdd:cd03267 118 llaaiydlPPARFKKRLDE----LSELLdlEELLD------TPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488422749 475 T-LTI---LEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03267 188 AqENIrnfLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-231 |
6.38e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.88 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnlsvf 84
Cdd:PRK11607 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM---------------LDG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssetSTLQIIKHYEQAV----QQY------TVEQTdrnfQAMMAAQEAMDRHEAwdyNAEIKTILSKLGIHDTTK- 153
Cdd:PRK11607 81 --------VDLSHVPPYQRPInmmfQSYalfphmTVEQN----IAFGLKQDKLPKAEI---ASRVNEMLGLVHMQEFAKr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 154 QVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL----INYVKQYPYTVLFVTHDRYFLNEVSTRIVELDR 229
Cdd:PRK11607 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
..
gi 488422749 230 GK 231
Cdd:PRK11607 226 GK 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-232 |
6.40e-16 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 81.45 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRyssqkqdLDGnlsvfeavlsseTSTLQI-- 97
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGL--------YQPTEGSVL-------LDG------------VDIRQIdp 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 98 --IKHYEQAVQQYTveqtdRNFQAMMAAQEAMDRHEAWDynAEIKTILSKLGIHDTTK--------QVN----SLSGGQQ 163
Cdd:TIGR03375 535 adLRRNIGYVPQDP-----RLFYGTLRDNIALGAPYADD--EEILRAAELAGVTEFVRrhpdgldmQIGergrSLSGGQR 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP--YTVLFVTHDRYFLNEVsTRIVELDRGKL 232
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLagKTLVLVTHRTSLLDLV-DRIIVMDNGRI 677
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-229 |
6.76e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.80 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIthpnqyriryssqkqdLDGNLSVFE 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----------------LAGTAPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 AvlssetstlqiikhyeqavqqytveqtdRNFQAMMAaQEAmdRHEAW-------------DYNAEIKTILSKLGIHD-T 151
Cdd:PRK11247 79 A----------------------------REDTRLMF-QDA--RLLPWkkvidnvglglkgQWRDAALQALAAVGLADrA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDryflneVSTRIVEL 227
Cdd:PRK11247 128 NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD------VSEAVAMA 201
|
..
gi 488422749 228 DR 229
Cdd:PRK11247 202 DR 203
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
320-474 |
6.90e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.36 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV--------KVAYFKQtE 390
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQ-H 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 391 ETLNRDIRMIDYL-----------REESEVAKEKdgttvsITQLLE---------RflFPSsthgkkiyKLSGGEQKRLY 450
Cdd:PRK10851 83 YALFRHMTVFDNIafgltvlprreRPNAAAIKAK------VTQLLEmvqlahladR--YPA--------QLSGGQKQRVA 146
|
170 180
....*....|....*....|....
gi 488422749 451 LLRLLVHQPNVLLLDEPTNDLDTE 474
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQ 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
329-495 |
1.19e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 74.95 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayfkQTEETLNRDirMIDYLREES 407
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADIS-----QWDPNELGD--HVGYLPQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 408 EvakekdgttvsitqllerfLFPSSThGKKIykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIAS-- 485
Cdd:cd03246 86 E-------------------LFSGSI-AENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlk 143
|
170
....*....|.
gi 488422749 486 -FGGSVITVSH 495
Cdd:cd03246 144 aAGATRIVIAH 154
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-495 |
1.94e-15 |
|
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: 75.39 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV------KVAYFKQtEET 392
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLdiaarnRIGYLPE-ERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 393 LNRDIRMIDYLR--------EESEVAKEkdgttvsITQLLERFLFpSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLL 464
Cdd:cd03269 81 LYPKMKVIDQLVylaqlkglKKEEARRR-------IDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190
....*....|....*....|....*....|....
gi 488422749 465 DEPTNDLDTETLTILEDYI---ASFGGSVITVSH 495
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIrelARAGKTVILSTH 186
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-232 |
2.02e-15 |
|
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: 75.87 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKST-------LLKVMGGIDDDFTGDIT-HPNQYR--IRYSSQKQ 75
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRATVAGHDVVrEPREVRrrIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVLssetstlqiikhYEQAVQQYTVEQTDRNfqammaAQEAMDRHEAWDYnaeiktilsklgihdTTKQV 155
Cdd:cd03265 83 SVDDELTGWENLY------------IHARLYGVPGAERRER------IDELLDFVGLLEA---------------ADRLV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 156 NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQ----YPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:cd03265 130 KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKlkeeFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
.
gi 488422749 232 L 232
Cdd:cd03265 210 I 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
320-496 |
2.41e-15 |
|
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: 75.55 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGR----TLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVkvayfkqteETLN 394
Cdd:COG4181 10 ELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDL---------FALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMIdyLREES------------------------EVAKEKDGTTVSiTQLLERF-L------FPSsthgkkiyKLSG 443
Cdd:COG4181 81 EDARAR--LRARHvgfvfqsfqllptltalenvmlplELAGRRDARARA-RALLERVgLghrldhYPA--------QLSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 444 GEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET----LTILEDYIASFGGSVITVSHD 496
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHD 206
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-228 |
3.19e-15 |
|
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: 75.52 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 26 ISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQkqdldgnlsvfeavlssetstlQIIKHYEQAV 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQ----------------------YIKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 106 QQYTVEQTDrnfqammaaqeamDRHEAWDYNAEIKTILSKLGIHDttKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPT 185
Cdd:cd03237 79 RDLLSSITK-------------DFYTHPYFKTEIAKPLQIEQILD--REVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488422749 186 NHLDFES-------INWLINYVKQypyTVLFVTHDRYFLNEVSTRIVELD 228
Cdd:cd03237 144 AYLDVEQrlmaskvIRRFAENNEK---TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-232 |
3.45e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.44 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSY-ADKVIFDdLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYriryssqkqdldgnlsv 83
Cdd:PRK11124 4 QLNGINCFYgAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEavLSSETSTLQIIKhYEQAV----QQY------TVEQtdrNF-QAMMAAQeAMDRHEAwdyNAEIKTILSKLGIHDTT 152
Cdd:PRK11124 66 FD--FSKTPSDKAIRE-LRRNVgmvfQQYnlwphlTVQQ---NLiEAPCRVL-GLSKDQA---LARAEKLLERLRLKPYA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 153 KQVN-SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK---QYPYTVLFVTHDRYFLNEVSTRIVELD 228
Cdd:PRK11124 136 DRFPlHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRelaETGITQVIVTHEVEVARKTASRVVYME 215
|
....
gi 488422749 229 RGKL 232
Cdd:PRK11124 216 NGHI 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
322-467 |
3.65e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 75.39 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 322 DSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK-----------VAYFKQt 389
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIThlpmherarlgIGYLPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EETLNRDIRMIDYLREESEVAKE--KDGTTVSITQLLERFlfpSSTH--GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLD 465
Cdd:TIGR04406 84 EASIFRKLTVEENIMAVLEIRKDldRAEREERLEALLEEF---QISHlrDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
..
gi 488422749 466 EP 467
Cdd:TIGR04406 161 EP 162
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-495 |
3.92e-15 |
|
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: 74.45 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVkvayFKQTEETLNRDIRM 399
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP----LDFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 IDYLR--------EESEVAKEKDGTTVSITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:cd03231 78 LGHAPgikttlsvLENLRFWHADHSDEQVEEALARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 488422749 472 DTETLTILEDYIASF---GGSVITVSH 495
Cdd:cd03231 157 DKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-468 |
3.98e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGNLSVF 84
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL---------------LDGEPVRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EAVLSSETSTLQIIkHYEQA-VQQYTVEQtdrNfqaMMAAQEA-----MDRHEAwdyNAEIKTILSKLGIH-DTTKQVNS 157
Cdd:COG1129 71 RSPRDAQAAGIAII-HQELNlVPNLSVAE---N---IFLGREPrrgglIDWRAM---RRRARELLARLGLDiDPDTPVGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHdryFLNEV---STRIVELDRGK 231
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriIRRLKAQGVAIIYISH---RLDEVfeiADRVTVLRDGR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 232 L-TTYPgnyedyIAMRAEKEVIEQkqndkqralykqelawM--RAGAKARSTKQQARihrfndleanvkqqqtqdkgeln 308
Cdd:COG1129 218 LvGTGP------VAELTEDELVRL----------------MvgRELEDLFPKRAAAP----------------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 309 laysrlGKQVYELDSLTktinGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK----- 382
Cdd:COG1129 253 ------GEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPVRirspr 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 383 ------VAYFkqTEE------TLNRDIR---------------MIDyLREESEVAKEkdgttvsitqLLERFLFPSSTHG 435
Cdd:COG1129 323 dairagIAYV--PEDrkgeglVLDLSIRenitlasldrlsrggLLD-RRRERALAEE----------YIKRLRIKTPSPE 389
|
490 500 510
....*....|....*....|....*....|...
gi 488422749 436 KKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:COG1129 390 QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
320-514 |
4.03e-15 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 74.59 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTL-FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV------KVAYFKQTEE 391
Cdd:TIGR02673 3 EFHNVSKAYPGGVAaLHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIaGEDVnrlrgrQLPLLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 TLNRDIRMIDYLREESEVA---------KEKDGTTVSIT----QLLER-FLFPSSthgkkiykLSGGEQKRLYLLRLLVH 457
Cdd:TIGR02673 83 VVFQDFRLLPDRTVYENVAlplevrgkkEREIQRRVGAAlrqvGLEHKaDAFPEQ--------LSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 458 QPNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLNKVAQEYWFIHDGM 514
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-214 |
4.38e-15 |
|
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: 78.48 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADK-VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnlsvf 84
Cdd:TIGR02857 324 FSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA---------------VNG----- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssetstlQIIKHYEQAVQQYT---VEQTDRNFQAMMAAQEAMDRHEAWDynAEIKTILSKLGIHDTTKQV------ 155
Cdd:TIGR02857 384 -----------VPLADADADSWRDQiawVPQHPFLFAGTIAENIRLARPDASD--AEIREALERAGLDEFVAALpqgldt 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 156 ------NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP--YTVLFVTHDR 214
Cdd:TIGR02857 451 pigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAqgRTVLLVTHRL 517
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-496 |
5.05e-15 |
|
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: 74.43 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKT----INGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTlkigqtvkVAYFKQTEETLNR 395
Cdd:cd03293 2 EVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE--------VLVDGEPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 396 DIRMI---DYL---------------------REESEVAKEkdgttvsitqLLERF-LfpSSTHGKKIYKLSGGEQKRLY 450
Cdd:cd03293 74 DRGYVfqqDALlpwltvldnvalglelqgvpkAEARERAEE----------LLELVgL--SGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488422749 451 LLRLLVHQPNVLLLDEPTNDLDTETLTILEDYI----ASFGGSVITVSHD 496
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-225 |
6.00e-15 |
|
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: 77.90 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 30 EKIGLVGINGTGKSTLLKVMGGIDDDFTGDIthPNQYRIRYSSQ--KQDLDGnlsvfeavlssetstlqiikhyeqavqq 107
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQyiSPDYDG---------------------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 108 yTVEQTDRNfqammAAQEAMDrhEAWdYNAEIktiLSKLGIHDT-TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTN 186
Cdd:COG1245 417 -TVEEFLRS-----ANTDDFG--SSY-YKTEI---IKPLGLEKLlDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488422749 187 HLDFE---SINWLI-NYVKQYPYTVLFVTHDRYFLNEVSTRIV 225
Cdd:COG1245 485 HLDVEqrlAVAKAIrRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-189 |
6.51e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 22 LSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgditHPNQYRIRYSSQK-QDLDGN-LSVFEAVLSSETSTLQIIK 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL---------LPGQGEILLNGRPlSDWSAAeLARHRAYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 100 hyeqaVQQYtveqtdrnfqaMMAAQEAMDRHEAWDynAEIKTILSKLGIHDT-TKQVNSLSGGQQKRVVLAKTLIE---- 174
Cdd:COG4138 86 -----VFQY-----------LALHQPAGASSEAVE--QLLAQLAEALGLEDKlSRPLTQLSGGEWQRVRLAAVLLQvwpt 147
|
170
....*....|....*...
gi 488422749 175 ---QPDLLLLDEPTNHLD 189
Cdd:COG4138 148 inpEGQLLLLDEPMNSLD 165
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
320-513 |
7.38e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITqiIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV--------KVAYFKQ-- 388
Cdd:COG3840 3 RLDDLTYRYGDFPLRFDLT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLtalppaerPVSMLFQen 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 ------TEET-----LNRDIRMIDYLREESEVAKEKdgttVSITQLLERFlfPSSthgkkiykLSGGEQKRLYLLRLLVH 457
Cdd:COG3840 81 nlfphlTVAQniglgLRPGLKLTAEQRAQVEQALER----VGLAGLLDRL--PGQ--------LSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 458 QPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:COG3840 147 KRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-219 |
1.16e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT--------HPNQYRIRYS--SQKQ 75
Cdd:PRK13537 10 FRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsRARHARQRVGvvPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEavlssetsTLQIIKHYeqavqqytveqtdrnFQamMAAQEAMDRheawdynaeIKTIL--SKLGiHDTTK 153
Cdd:PRK13537 90 NLDPDFTVRE--------NLLVFGRY---------------FG--LSAAAARAL---------VPPLLefAKLE-NKADA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488422749 154 QVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTN-------HLDFESINWLINYVKqypyTVLFVTHdryFLNE 219
Cdd:PRK13537 135 KVGELSGGMKRRLTLARALVNDPDVLVLDEPTTgldpqarHLMWERLRSLLARGK----TILLTTH---FMEE 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-233 |
1.18e-14 |
|
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: 72.08 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRyssqkqdLDGnlsvf 84
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL--------YKPDSGEIL-------VDG----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssetstlqiikhyeQAVQQYTVeqtdrnfqammaaqeamdrHEAWDynaeiktilskLGIhdTTkqVNSLSGGQQK 164
Cdd:cd03216 62 ------------------KEVSFASP-------------------RDARR-----------AGI--AM--VYQLSVGERQ 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 165 RVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHdryFLNEV---STRIVELDRGKLT 233
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRaqgVAVIFISH---RLDEVfeiADRVTVLRDGRVV 161
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-234 |
1.24e-14 |
|
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: 73.62 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADK----VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGn 80
Cdd:COG4181 10 ELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR---------------LAG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 lsvfeavlsSETSTLQiikhyEQA-----------VQQytveqtdrNFQ---AMMA------------AQEAMDRHEAWd 134
Cdd:COG4181 74 ---------QDLFALD-----EDArarlrarhvgfVFQ--------SFQllpTLTAlenvmlplelagRRDARARARAL- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 135 ynaeiktiLSKLG----IHDTTKQvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----INWLINYVKQYPYT 206
Cdd:COG4181 131 --------LERVGlghrLDHYPAQ---LSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTT 199
|
250 260
....*....|....*....|....*...
gi 488422749 207 VLFVTHDRYfLNEVSTRIVELDRGKLTT 234
Cdd:COG4181 200 LVLVTHDPA-LAARCDRVLRLRAGRLVE 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-226 |
1.24e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 11 KSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT-----HPNQYR-----IRYSSQKQDLDGN 80
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpVPARARlararIGVVPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 LSVFEAVLssetstlqiikhyeqaVQQYTVEQTDRNFQAMMAAQEAMDRHEawdynaeiktilSKLgihDTtkQVNSLSG 160
Cdd:PRK13536 129 FTVRENLL----------------VFGRYFGMSTREIEAVIPSLLEFARLE------------SKA---DA--RVSDLSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTN-------HLDFESINWLINYVKqypyTVLFVTH---------DRYFLNEVSTRI 224
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTgldpharHLIWERLRSLLARGK----TILLTTHfmeeaerlcDRLCVLEAGRKI 251
|
..
gi 488422749 225 VE 226
Cdd:PRK13536 252 AE 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
320-496 |
1.24e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.49 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVkVAyfkqTEETLNRDIRM 399
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-VT----DLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 I--DY---------------LR------EE-----SEVAKekdgtTVSITQLLERflFPSsthgkkiyKLSGGEQKRLYL 451
Cdd:COG3839 80 VfqSYalyphmtvyeniafpLKlrkvpkAEidrrvREAAE-----LLGLEDLLDR--KPK--------QLSGGQRQRVAL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488422749 452 LRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
331-475 |
1.46e-14 |
|
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: 73.46 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQ---FEGTLKI-GQTVKVAYFKQTEETLNRDIRMIDYL--- 403
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFnGQPRKPDQFQKCVAYVRQDDILLPGLtvr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 404 ------------REESEVAKEKDGTTVSITQLLERFLfpsstHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:cd03234 100 etltytailrlpRKSSDAIRKKRVEDVLLRDLALTRI-----GGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
....
gi 488422749 472 DTET 475
Cdd:cd03234 175 DSFT 178
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-538 |
1.93e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 315 GKQVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQtvKVAYFkqteetlN 394
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYF-------G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMIDYLREESEVAKE-KDGTTVSITQLLERFLFPSSTHG---------------------KKIY--------KLSGG 444
Cdd:PRK14246 78 KDIFQIDAIKLRKEVGMVfQQPNPFPHLSIYDNIAYPLKSHGikekreikkiveeclrkvglwKEVYdrlnspasQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 445 EQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGG--SVITVSHDRYFLNKVAQEYWFIHDGMMERIVGSF 522
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237
|
250
....*....|....*.
gi 488422749 523 EDYETYKKEKDKQLAI 538
Cdd:PRK14246 238 EIFTSPKNELTEKYVI 253
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
321-496 |
2.01e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 321 LDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQT---EETLNRDI 397
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlylDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RMIDYLREEsevAKEKDgttvsITQLLERfLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLT 477
Cdd:PRK09544 87 NRFLRLRPG---TKKED-----ILPALKR-VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180
....*....|....*....|...
gi 488422749 478 ILEDYI----ASFGGSVITVSHD 496
Cdd:PRK09544 158 ALYDLIdqlrRELDCAVLMVSHD 180
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
329-495 |
2.10e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.21 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKigqtvkvayFKQTEETLNRDIRMIDYL----- 403
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK---------LDGGDIDDPDVAEACHYLghrna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 404 -------REESEV-AKEKDGTTVSITQLLERFLFPSSTHGKKIYkLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:PRK13539 84 mkpaltvAENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY-LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|...
gi 488422749 476 LTILEDYIASF---GGSVITVSH 495
Cdd:PRK13539 163 VALFAELIRAHlaqGGIVIAATH 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
329-495 |
2.28e-14 |
|
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: 72.64 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK----------VAYFKQTEETLNRDI 397
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIRdisrkslrsmIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 R-MIDYLREESEVAKEKD-GTTVSITQLLERflfpsSTHGKKIY------KLSGGEQKRLYLLRLLVHQPNVLLLDEPTN 469
Cdd:cd03254 94 MeNIRLGRPNATDEEVIEaAKEAGAHDFIMK-----LPNGYDTVlgenggNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180
....*....|....*....|....*...
gi 488422749 470 DLDTETLTILEDYIASF--GGSVITVSH 495
Cdd:cd03254 169 NIDTETEKLIQEALEKLmkGRTSIIIAH 196
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-232 |
2.48e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.72 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG----------IDDDftgDITH--PNQYRI 68
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGledptsgeilIGGR---DVTDlpPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 69 RYSSQKQDLDGNLSVFEAVLSSetstLQIIKHYEQAVQQytveqtdrnfqammAAQEAmdrheawdynAEIktilskLGI 148
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFP----LKLRKVPKAEIDR--------------RVREA----------AEL------LGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 149 HDT-TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF--------EsinwLINYVKQYPYTVLFVTHDryfLNE 219
Cdd:COG3839 124 EDLlDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAklrvemraE----IKRLHRRLGTTTIYVTHD---QVE 196
|
250
....*....|....*.
gi 488422749 220 VST---RIVELDRGKL 232
Cdd:COG3839 197 AMTladRIAVMNDGRI 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-232 |
2.50e-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: 72.14 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 21 DLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITH--PNQYRIRYSSQKQDLDGNLSVFEAVLSSE 91
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGrvlingvDVTAapPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 92 TSTLQIikhyeQAVQQytveqtdrnfQAmmaaqeamdrheawdynaeIKTILSKLGIHDTTKQV-NSLSGGQQKRVVLAK 170
Cdd:cd03298 96 SPGLKL-----TAEDR----------QA-------------------IEVALARVGLAGLEKRLpGELSGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 171 TLIEQPDLLLLDEPTNHLDFESINWLINYV----KQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVldlhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
225-293 |
2.58e-14 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 68.37 E-value: 2.58e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 225 VELDRGKLTTYPGNYEDYIAMRAEKEVIEQKQNDKQRALYKQELAWM-RAGAKARSTKQ-QARIHRFNDLE 293
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKQaQSRIKALEKME 71
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-232 |
2.60e-14 |
|
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: 71.09 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 14 ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRyssqkqdLDGnlsvfeavlssets 93
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGL--------LRPTSGRVR-------LDG-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 94 tlqiikhyeQAVQQYTVEQTDRNFQAMMaaQEAMdrheawdynaeiktiLSKLGIHDttkqvNSLSGGQQKRVVLAKTLI 173
Cdd:cd03246 64 ---------ADISQWDPNELGDHVGYLP--QDDE---------------LFSGSIAE-----NILSGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488422749 174 EQPDLLLLDEPTNHLDFE---SINWLINYVKQYPYTVLFVTHDRYFLNEVStRIVELDRGKL 232
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEgerALNQAIAALKAAGATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
320-495 |
2.94e-14 |
|
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: 70.92 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayFKQTEETLNRDIR 398
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVS---FASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIdylreesevakekdgttvsitqllerflfpssthgkkiYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTI 478
Cdd:cd03216 79 MV--------------------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180
....*....|....*....|
gi 488422749 479 LEDYIASF---GGSVITVSH 495
Cdd:cd03216 121 LFKVIRRLraqGVAVIFISH 140
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-213 |
3.40e-14 |
|
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: 75.47 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD-KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnLSV 83
Cdd:TIGR02868 336 ELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT---------------LDG-VPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEAvlsSETSTLQIIKHYEQavQQYTVEQTDRNfQAMMAAQEAMDrheawdynAEIKTILSKLGIHD------------T 151
Cdd:TIGR02868 400 SSL---DQDEVRRRVSVCAQ--DAHLFDTTVRE-NLRLARPDATD--------EELWAALERVGLADwlralpdgldtvL 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 152 TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP--YTVLFVTHD 213
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALsgRTVVLITHH 529
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
320-526 |
4.04e-14 |
|
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: 72.23 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGR----TLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIgQTVKVAYFKQTE-ETLN 394
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-DGTDLTLLSGKElRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMI----DYLREES---------EVAK-EKDGTTVSITQLLErflFPSSTHGKKIY--KLSGGEQKRLYLLRLLVHQ 458
Cdd:cd03258 82 RRIGMIfqhfNLLSSRTvfenvalplEIAGvPKAEIEERVLELLE---LVGLEDKADAYpaQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 459 PNVLLLDEPTNDLDTET----LTILEDYIASFGGSVITVSHD----RYFLNKVAqeywFIHDGmmeRIVGSFEDYE 526
Cdd:cd03258 159 PKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEmevvKRICDRVA----VMEKG---EVVEEGTVEE 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
318-504 |
4.37e-14 |
|
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: 71.77 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 VYELDSLTKTINGRTLF----QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEETL 393
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRDIRMI---------------DYLREESEVAKEKDGTT---VSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLL 455
Cdd:cd03257 81 RKEIQMVfqdpmsslnprmtigEQIAEPLRIHGKLSKKEarkEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 456 VHQPNVLLLDEPTNDLDT----ETLTILEDYIASFGGSVITVSHD----RYFLNKVA 504
Cdd:cd03257 161 ALNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDlgvvAKIADRVA 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-233 |
4.87e-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: 70.42 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSY--ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDG-NLS 82
Cdd:cd03247 3 INNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---------------LDGvPVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETSTLQiikhyeQAVQQYTVeqtdrnfqammaaqeamdrheawdynaeikTILSKLGIHdttkqvnsLSGGQ 162
Cdd:cd03247 68 DLEKALSSLISVLN------QRPYLFDT------------------------------TLRNNLGRR--------FSGGE 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY--PYTVLFVTHdRYFLNEVSTRIVELDRGKLT 233
Cdd:cd03247 104 RQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITH-HLTGIEHMDKILFLENGKII 175
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-252 |
4.92e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.15 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 18 IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGdithpnQYRIRySSQKQDLDGNLSvfeAVLSSEtstlqi 97
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG------TYRVA-GQDVATLDADAL---AQLRRE------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 98 ikHYEQAVQQY------TVEQtDRNFQAMMAAQEAMDRHEawdynaEIKTILSKLGIHDTTK-QVNSLSGGQQKRVVLAK 170
Cdd:PRK10535 87 --HFGFIFQRYhllshlTAAQ-NVEVPAVYAGLERKQRLL------RAQELLQRLGLEDRVEyQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 171 TLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEvSTRIVELDRGKLTTYPGNYEDYIAMRA 247
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdrgHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAGG 236
|
....*
gi 488422749 248 EKEVI 252
Cdd:PRK10535 237 TEPVV 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-225 |
5.12e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.23 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 26 ISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpNQYRIRYSSQKQDLDGNLSVfEAVLSSETSTLqiikhyeqav 105
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYIKPDYDGTV-EDLLRSITDDL---------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 106 qqytveqtdrnfqammaaqeamdrHEAWdYNAEIktiLSKLGIHDT-TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEP 184
Cdd:PRK13409 429 ------------------------GSSY-YKSEI---IKPLQLERLlDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488422749 185 TNHLDFE-------SINwliNYVKQYPYTVLFVTHDRYFLNEVSTRIV 225
Cdd:PRK13409 481 SAHLDVEqrlavakAIR---RIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-213 |
5.29e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDLDGNLSVfe 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 avlssetsTLQIIKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRheawdynaeiktilsklgihdttkqvnsLSGGQQKR 165
Cdd:PRK09544 85 --------TVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK----------------------------LSGGETQR 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488422749 166 VVLAKTLIEQPDLLLLDEPTNHLDFE---SINWLINYVK-QYPYTVLFVTHD 213
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNgqvALYDLIDQLRrELDCAVLMVSHD 180
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
320-519 |
5.53e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQtvkvaYFKQTEETLNRDIRM 399
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGD-----ITIDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 IDYLREESE------------------------VAKEKDGttvSITQLLERFLFPSSTHGKK-IY--KLSGGEQKRLYLL 452
Cdd:PRK11264 80 IRQLRQHVGfvfqnfnlfphrtvleniiegpviVKGEPKE---EATARARELLAKVGLAGKEtSYprRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488422749 453 RLLVHQPNVLLLDEPTNDLDTETL-----TILEdyIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIV 519
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVgevlnTIRQ--LAQEKRTMVIVTHEMSFARDVADRAIFMDQG---RIV 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
320-497 |
5.76e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.64 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV---------KVAY---- 385
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLnGRDLftnlpprerRVGFvfqh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 386 ---FKQteetLN-RD-----IRMIDYLREEsevAKEKdgttvsITQLLERF-L------FPSsthgkkiyKLSGGEQKRL 449
Cdd:COG1118 84 yalFPH----MTvAEniafgLRVRPPSKAE---IRAR------VEELLELVqLegladrYPS--------QLSGGQRQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488422749 450 YLLRLLVHQPNVLLLDEPTNDLDTETLTILE----DYIASFGGSVITVSHDR 497
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRrwlrRLHDELGGTTVFVTHDQ 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-238 |
6.97e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---------THPNQYRIRYS 71
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 72 SQKQDLDGNLSVFEavlssetstlqiikhyeqavqqytveqtDRNFQAMMAAQEAMDRHEAWDYNAEIKtilsKLGiHDT 151
Cdd:PRK11000 81 FQSYALYPHLSVAE----------------------------NMSFGLKLAGAKKEEINQRVNQVAEVL----QLA-HLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-FESINWLINYV---KQYPYTVLFVTHDRYFLNEVSTRIVEL 227
Cdd:PRK11000 128 DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaALRVQMRIEISrlhKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
250 260
....*....|....*....|
gi 488422749 228 DRGK---------LTTYPGN 238
Cdd:PRK11000 208 DAGRvaqvgkpleLYHYPAN 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-233 |
7.09e-14 |
|
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: 73.22 E-value: 7.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 21 DLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDItHPNQYRIRYSSQKQDLdgnlsvfeavlSSETSTLQIIkh 100
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-VLNGRTLFDSRKGIFL-----------PPEKRRIGYV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 101 YEQA--VQQYTVEQtdrNFQAMMAAQEAMDRHEAWDynaeikTILSKLGI-HDTTKQVNSLSGGQQKRVVLAKTLIEQPD 177
Cdd:TIGR02142 81 FQEArlFPHLSVRG---NLRYGMKRARPSERRISFE------RVIELLGIgHLLGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 178 LLLLDEPTNHLDFESINWLINYVK------QYPytVLFVTHDryfLNEV---STRIVELDRGKLT 233
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLErlhaefGIP--ILYVSHS---LQEVlrlADRVVVLEDGRVA 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
320-496 |
7.13e-14 |
|
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: 71.13 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVkVAYFKQTEetlnRDIRM 399
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKD----RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 I-----------------------DYLREE-----SEVAKekdgtTVSITQLLERflfpssthgkKIYKLSGGEQKRLYL 451
Cdd:cd03301 77 VfqnyalyphmtvydniafglklrKVPKDEidervREVAE-----LLQIEHLLDR----------KPKQLSGGQRQRVAL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488422749 452 LRLLVHQPNVLLLDEPTNDLDT----ETLTILEDYIASFGGSVITVSHD 496
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-494 |
7.14e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNqyrIRYSSQKQDLDGNLSVF 84
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 ----EAVLSSETSTLQ---IIKHYEQAVqqYTVEQTDRNFqamMAAQEAMdrheawdynaeiktILSKLGIH-DTTKQVN 156
Cdd:PRK09700 84 iiyqELSVIDELTVLEnlyIGRHLTKKV--CGVNIIDWRE---MRVRAAM--------------MLLRVGLKvDLDEKVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKlt 233
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 234 typgnyedYIAMRAEKEVieqkQNDkqralykqELAWMRAGAKARStkqqarihRFNDLEANVKQQQtqdkgelnlaysr 313
Cdd:PRK09700 223 --------SVCSGMVSDV----SND--------DIVRLMVGRELQN--------RFNAMKENVSNLA------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 314 lGKQVYELDSLTKTINGRTlfQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVayfKQTEET 392
Cdd:PRK09700 262 -HETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISP---RSPLDA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 393 LNRDIRMIDYLREESEVAKEKD-GTTVSITQLLERF-------LFPSSTHGK------------------KIYKLSGGEQ 446
Cdd:PRK09700 336 VKKGMAYITESRRDNGFFPNFSiAQNMAISRSLKDGgykgamgLFHEVDEQRtaenqrellalkchsvnqNITELSGGNQ 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 488422749 447 KRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDyIASFGGSVITVS 494
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQ-LADDGKVILMVS 466
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
283-495 |
8.42e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.46 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 283 QARIHRFNDLEANVKQQQTQDKGELNLAYSRlGKQVyELDSLT-KTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTML 361
Cdd:COG4178 329 RATVDRLAGFEEALEAADALPEAASRIETSE-DGAL-ALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 362 NILSG--------------EDQQF--------EGTLKiGQtvkVAYfKQTEETLNRDiRMIDYLREesevakekdgttVS 419
Cdd:COG4178 407 RAIAGlwpygsgriarpagARVLFlpqrpylpLGTLR-EA---LLY-PATAEAFSDA-ELREALEA------------VG 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 420 ITQLLERFlfpsSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIAS--FGGSVITVSH 495
Cdd:COG4178 469 LGHLAERL----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-256 |
8.48e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAY--KIEHLNKSYADKV-IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQkqdl 77
Cdd:PRK13636 1 MEDYilKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 78 dGNLSVFEA---VLSSETSTLqiikhYEQAVQQytveqtDRNFQAMMAAQEAMDRHEawdynaEIKTILSKLGI-HDTTK 153
Cdd:PRK13636 76 -GLMKLRESvgmVFQDPDNQL-----FSASVYQ------DVSFGAVNLKLPEDEVRK------RVDNALKRTGIeHLKDK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 154 QVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDR 229
Cdd:PRK13636 138 PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE 217
|
250 260
....*....|....*....|....*..
gi 488422749 230 GKLTTYPGNYEdyiaMRAEKEVIEQKQ 256
Cdd:PRK13636 218 GRVILQGNPKE----VFAEKEMLRKVN 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
320-513 |
9.25e-14 |
|
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: 70.86 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKT--INGRTL--FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG----------------EDQQFEGTLKIG- 378
Cdd:cd03266 3 TADALTKRfrDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllepdagfatvdgfdvVKEPAEARRRLGf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 379 ----------QTVK--VAYFKqteetlnrdiRMIDYLREESEVAKEKDGTTVSITQLLERflfpssthgkKIYKLSGGEQ 446
Cdd:cd03266 83 vsdstglydrLTARenLEYFA----------GLYGLKGDELTARLEELADRLGMEELLDR----------RVGGFSTGMR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 447 KRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYI---ASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIrqlRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
558-623 |
1.18e-13 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 65.95 E-value: 1.18e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 558 LSYKEKREYESLMSRIEETEIRLSEIEQEMIEAS--ADYAKIKDLTIEQQQLEQTYDEDITRWSELEE 623
Cdd:pfam16326 2 LSYKEQRELEELEAEIEKLEEEIAELEAQLADPElySDYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-230 |
1.23e-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: 70.54 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYA-----DKVI--FDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGidddftgdiTH-PNQYRIRYSSQKQD 76
Cdd:COG4778 6 EVENLSKTFTlhlqgGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG---------NYlPDSGSILVRHDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 77 LDgnlsvfeaVLSSETStlQIIkhyeqAVQQYT---VEQ--------TDRNFQAMMAAQEAMDRHEAwdyNAEIKTILSK 145
Cdd:COG4778 77 VD--------LAQASPR--EIL-----ALRRRTigyVSQflrviprvSALDVVAEPLLERGVDREEA---RARARELLAR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 146 LGIHDTTKQV--NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQYPYTVLFVTHDRYFLNEV 220
Cdd:COG4778 139 LNLPERLWDLppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravVVELIEEAKARGTAIIGIFHDEEVREAV 218
|
250
....*....|
gi 488422749 221 STRIVELDRG 230
Cdd:COG4778 219 ADRVVDVTPF 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-231 |
1.45e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.67 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITH--PNQYRIRYSSQKQD 76
Cdd:PRK09452 17 LRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGrimldgqDITHvpAENRHVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 77 LDGNLSVFEAVlsseTSTLQIIKHYEQavqqytvEQTDRNFQAMMAAQeamdrheawdynaeiktiLSKLGihdtTKQVN 156
Cdd:PRK09452 97 LFPHMTVFENV----AFGLRMQKTPAA-------EITPRVMEALRMVQ------------------LEEFA----QRKPH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYklrkQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-231 |
1.50e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 70.99 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 2 EAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDdftgdithPNQYRIRYSSQ----KQDL 77
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLET--------PDSGEIRVGGEeirlKPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 78 DGNLS----------------VFEAV-LSSETSTLQ-IIkhyEQAVQqytVEQTDRnfqammaaQEAMDRHEAwdynaei 139
Cdd:COG4598 79 DGELVpadrrqlqrirtrlgmVFQSFnLWSHMTVLEnVI---EAPVH---VLGRPK--------AEAIERAEA------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 140 ktILSKLGIHDTTKQV-NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRY 215
Cdd:COG4598 138 --LLAKVGLADKRDAYpAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAeegRTMLVVTHEMG 215
|
250
....*....|....*.
gi 488422749 216 FLNEVSTRIVELDRGK 231
Cdd:COG4598 216 FARDVSSHVVFLHQGR 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-232 |
1.57e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDddftgditHPNQYRIRYssqkqdldGN 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLE--------QPEAGTIRV--------GD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 LSVFEAVLSSETSTLqiIKHYEQAVQqyTVEQTDRNFQAMMAAQEAMD---------RHEAwdyNAEIKTILSKLGIH-D 150
Cdd:PRK11264 65 ITIDTARSLSQQKGL--IRQLRQHVG--FVFQNFNLFPHRTVLENIIEgpvivkgepKEEA---TARARELLAKVGLAgK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 151 TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVEL 227
Cdd:PRK11264 138 ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqekRTMVIVTHEMSFARDVADRAIFM 217
|
....*
gi 488422749 228 DRGKL 232
Cdd:PRK11264 218 DQGRI 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
320-496 |
1.89e-13 |
|
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: 70.09 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKigqtvkVAYFKQTEETlnRDIR- 398
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT------VAGHDVVREP--REVRr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIDYLREESEVAKEKDGT-----------------TVSITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNV 461
Cdd:cd03265 74 RIGIVFQDLSVDDELTGWenlyiharlygvpgaerRERIDELLDFVGLLEAAD-RLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 488422749 462 LLLDEPTNDLDTETLTILEDYI----ASFGGSVITVSHD 496
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIeklkEEFGMTILLTTHY 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-184 |
2.11e-13 |
|
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: 69.88 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG----------IDDdftGDITHPNQYR-----IR 69
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvkpdsgkilLDG---QDITKLPMHKrarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSSQKQdldgnlSVFEavlssetstlqiikhyeqavqQYTVEQTdrnfqaMMAAQEAM--DRHEAwdyNAEIKTILSKLG 147
Cdd:cd03218 79 YLPQEA------SIFR---------------------KLTVEEN------ILAVLEIRglSKKER---EEKLEELLEEFH 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 488422749 148 IHDTTKQV-NSLSGGQQKRVVLAKTLIEQPDLLLLDEP 184
Cdd:cd03218 123 ITHLRKSKaSSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-230 |
2.20e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.92 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 15 DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDL-DGNLsvFEAVLssets 93
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLpLGTL--REALL----- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 94 tlqiikhYEQAVQQYTveqtdrnfqammaaqeamdrheawdyNAEIKTILSKLGIHDTTKQV-------NSLSGGQQKRV 166
Cdd:COG4178 448 -------YPATAEAFS--------------------------DAELREALEAVGLGHLAERLdeeadwdQVLSLGEQQRL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 167 VLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPY--TVLFVTHdRYFLNEVSTRIVELDRG 230
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPgtTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-233 |
2.20e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSY--ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdldgnlsV 83
Cdd:PRK13635 8 VEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT---------------------V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEAVLSSETsTLQIIKHYEQAVQ----QYtVEQTDRNFQAMMAAQEAMDRHEAwdynaeIKTIlsklgiHDTTKQVN--- 156
Cdd:PRK13635 67 GGMVLSEET-VWDVRRQVGMVFQnpdnQF-VGATVQDDVAFGLENIGVPREEM------VERV------DQALRQVGmed 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 -------SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESINWLinyVKQYPYTVLFVTHDryfLNEV-- 220
Cdd:PRK13635 133 flnrephRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQL---KEQKGITVLSITHD---LDEAaq 206
|
250
....*....|...
gi 488422749 221 STRIVELDRGKLT 233
Cdd:PRK13635 207 ADRVIVMNKGEIL 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-230 |
2.44e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddFTGDITHPNQYR---------------IR 69
Cdd:PRK09984 6 RVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHIEllgrtvqregrlardIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSS-------QKQDLDGNLSVFEAVLsseTSTLQIIKHYEQAVQQYTVEQTDRNFQAmmaaqeamdrheawdynaeikti 142
Cdd:PRK09984 83 KSRantgyifQQFNLVNRLSVLENVL---IGALGSTPFWRTCFSWFTREQKQRALQA----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 143 LSKLGI-HDTTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP----YTVLFVTHDRYFL 217
Cdd:PRK09984 137 LTRVGMvHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndgITVVVTLHQVDYA 216
|
250
....*....|...
gi 488422749 218 NEVSTRIVELDRG 230
Cdd:PRK09984 217 LRYCERIVALRQG 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-235 |
2.78e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.48 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 10 NKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGNLS-VFEAvl 88
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT---------------VRGRVSsLLGL-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 89 sseTSTLQiikhyeqavQQYTVEQTDRnfqaMMAAQEAMDRHEAWDYNAEIKTiLSKLG--IHdttKQVNSLSGGQQKRV 166
Cdd:cd03220 92 ---GGGFN---------PELTGRENIY----LNGRLLGLSRKEIDEKIDEIIE-FSELGdfID---LPVKTYSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 167 VLAKTLIEQPDLLLLDEPTNHLD-------FESINWLINYVKqypyTVLFVTHDRYFLNEVSTRIVELDRGKLTTY 235
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDaafqekcQRRLRELLKQGK----TVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
320-496 |
2.81e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQ 388
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDVealsaraasrRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 -TEETLNRDIRMI------------DYLREESEVAKEKDGTTVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLL 455
Cdd:PRK09536 85 dTSLSFEFDVRQVvemgrtphrsrfDTWTETDRAAVERAMERTGVAQFADR----------PVTSLSGGERQRVLLARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488422749 456 VHQPNVLLLDEPTNDLD----TETLTILEDyIASFGGSVITVSHD 496
Cdd:PRK09536 155 AQATPVLLLDEPTASLDinhqVRTLELVRR-LVDDGKTAVAAIHD 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
320-472 |
3.01e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV---------KVAYFKQT 389
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EeTLNRDIRMIDYLREESEVAKEKDGTTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTN 469
Cdd:PRK13537 89 D-NLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
...
gi 488422749 470 DLD 472
Cdd:PRK13537 168 GLD 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
334-496 |
3.03e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 72.39 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 334 FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGqTVKVAYFKQTEET-----LNRDIRMIDY-LREES 407
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-GVPVSSLDQDEVRrrvsvCAQDAHLFDTtVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 408 EVAKEkDGTTVSITQLLER-------------FLFPSSTHGKKiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTE 474
Cdd:TIGR02868 430 RLARP-DATDEELWAALERvgladwlralpdgLDTVLGEGGAR---LSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....
gi 488422749 475 T-LTILEDYIASFGG-SVITVSHD 496
Cdd:TIGR02868 506 TaDELLEDLLAALSGrTVVLITHH 529
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-213 |
4.31e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.66 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGI-DDDFTG---------DITH--PNQYRIRYSS 72
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlSPAFSAsgevllngrRLTAlpAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 73 QKQDLDGNLSVFEAVLssetstlqiikhyeqavqqytveqtdrnfqamMAAQEAMDRHEAwdyNAEIKTILSKLGIHD-T 151
Cdd:COG4136 83 QDDLLFPHLSVGENLA--------------------------------FALPPTIGRAQR---RARVEQALEEAGLAGfA 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 152 TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD------FESinWLINYVKQYPYTVLFVTHD 213
Cdd:COG4136 128 DRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDaalraqFRE--FVFEQIRQRGIPALLVTHD 193
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-189 |
4.31e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT------HPNQYRI---RYSSQKQD 76
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvEALSARAasrRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 77 ldgnlsvfeAVLSSETSTLQIIK--HYEQAVQQYTVEQTDRNfqammAAQEAMDRHEAWDYNAeiktilsklgihdttKQ 154
Cdd:PRK09536 86 ---------TSLSFEFDVRQVVEmgRTPHRSRFDTWTETDRA-----AVERAMERTGVAQFAD---------------RP 136
|
170 180 190
....*....|....*....|....*....|....*
gi 488422749 155 VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
341-519 |
4.32e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 68.67 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQtVKVAyfkqTEETLNRDIRMID------------------- 401
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVT----AAPPADRPVSMLFqennlfahltveqnvglgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 402 ----YLREESEVAKEKDGTTVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----T 473
Cdd:cd03298 96 spglKLTAEDRQAIEVALARVGLAGLEKR----------LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488422749 474 ETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIV 519
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG---RIA 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-513 |
4.33e-13 |
|
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: 68.71 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTvKVAYFKQTEETLNRDIRM 399
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGL-KLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 I--------------------DYLREESEVAKEKDGTtvsitQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQP 459
Cdd:cd03262 81 VfqqfnlfphltvlenitlapIKVKGMSKAEAEERAL-----ELLEKVGLADKAD-AYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 460 NVLLLDEPTNDLDTET----LTILEDyIASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:cd03262 155 KVMLFDEPTSALDPELvgevLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
320-496 |
5.13e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.14 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTT----MLNILSGEdqqfEGTLKI-GQTVKVAyfkqteetln 394
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTtiriILGILAPD----SGEVLWdGEPLDPE---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 rDIRMIDYLREE-----------------------SEVAKEKdgttvsITQLLERFLFPSSThGKKIYKLSGGEQKRLYL 451
Cdd:COG4152 69 -DRRRIGYLPEErglypkmkvgeqlvylarlkglsKAEAKRR------ADEWLERLGLGDRA-NKKVEELSKGNQQKVQL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488422749 452 LRLLVHQPNVLLLDEPTNDLD---TETL-TILEDYIASfGGSVITVSHD 496
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDpvnVELLkDVIRELAAK-GTTVIFSSHQ 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-244 |
6.83e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADK--VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVmggidddftgdITH---PNQYRIRyssqkqdLDG- 79
Cdd:PRK11160 341 LNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL-----------LTRawdPQQGEIL-------LNGq 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 NLSVF-EAVLSSETSTLqiikhyEQAVqqYTVEQTDR-NFQamMAAQEAMDrheawdynAEIKTILSKLGIH---DTTKQ 154
Cdd:PRK11160 403 PIADYsEAALRQAISVV------SQRV--HLFSATLRdNLL--LAAPNASD--------EALIEVLQQVGLEkllEDDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 VNS--------LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQYPyTVLFVTHDRYFLNEVStR 223
Cdd:PRK11160 465 LNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILELLAEHAQNK-TVLMITHRLTGLEQFD-R 542
|
250 260
....*....|....*....|.
gi 488422749 224 IVELDRGKLTTYpGNYEDYIA 244
Cdd:PRK11160 543 ICVMDNGQIIEQ-GTHQELLA 562
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-234 |
7.44e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 21 DLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQ-KQDLDGNlsvfeavlssetsTLQIIK 99
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAaKAELRNQ-------------KLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 100 HYEQAVQQYTVEQTdrnfQAMMAAQEAMDRHEAwdyNAEIKTILSKLGIHDTTKQVNS-LSGGQQKRVVLAKTLIEQPDL 178
Cdd:PRK11629 94 QFHHLLPDFTALEN----VAMPLLIGKKKPAEI---NSRALEMLAAVGLEHRANHRPSeLSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 179 LLLDEPTNHLDF---ESINWLINYVKQYPYTV-LFVTHDRYFLNEVStRIVELDRGKLTT 234
Cdd:PRK11629 167 VLADEPTGNLDArnaDSIFQLLGELNRLQGTAfLVVTHDLQLAKRMS-RQLEMRDGRLTA 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-251 |
7.55e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGI-----------DDDFTGDITHPNQYR-I 68
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprdagniiidDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 69 RYSSQKQDLDGNLSVFEAVLssetSTLQIIKHYEQAvqqytvEQTDRnfqammaAQEAMDRHeawdynaEIKTILSKLGi 148
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLM----AVLQIRDDLSAE------QREDR-------ANELMEEF-------HIEHLRDSMG- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 149 hdttkqvNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQYPYTVLFVTHDRYFLNEVSTRIV 225
Cdd:PRK10895 136 -------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISvidIKRIIEHLRDSGLGVLITDHNVRETLAVCERAY 208
|
250 260
....*....|....*....|....*.
gi 488422749 226 ELDRGKLTTYpGNYEDYIAMRAEKEV 251
Cdd:PRK10895 209 IVSQGHLIAH-GTPTEILQDEHVKRV 233
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-472 |
7.83e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 23 SLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSsqkqdldgnlsvfeavlssetstlqiikhYE 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-----------------------------FE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 103 QavQQYTVEQT-DRNFQAMM----------AAQEAMDRHEAwdyNAEIKTILSKLGI-HDTTKQVNSLSGGQQKRVVLAK 170
Cdd:PRK10938 74 Q--LQKLVSDEwQRNNTDMLspgeddtgrtTAEIIQDEVKD---PARCEQLAQQFGItALLDRRFKYLSTGETRKTLLCQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 171 TLIEQPDLLLLDEPTNHLDFESINWLINYVKQypytvlfVTHDRYFLNEVSTRIVELdrgklttyPgNYEDYIAMRAEKE 250
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLAS-------LHQSGITLVLVLNRFDEI--------P-DFVQFAGVLADCT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 251 VIEQ--KQNDKQRALYkqelawmragakarstKQQARIHRFNDL---EANVKQQQTQDKGELNLaysrlgkqvYELDSLT 325
Cdd:PRK10938 213 LAETgeREEILQQALV----------------AQLAHSEQLEGVqlpEPDEPSARHALPANEPR---------IVLNNGV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 326 KTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQfegtlkiGQTVKVAYFKQ---TEETLnRDI-RMID 401
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQ-------GYSNDLTLFGRrrgSGETI-WDIkKHIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 402 Y----LREESEVAkekdgTTV----------SI--------------TQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLR 453
Cdd:PRK10938 340 YvsssLHLDYRVS-----TSVrnvilsgffdSIgiyqavsdrqqklaQQWLDILGIDKRTADAPFHSLSWGQQRLALIVR 414
|
490
....*....|....*....
gi 488422749 454 LLVHQPNVLLLDEPTNDLD 472
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLD 433
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
320-497 |
8.78e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQ 388
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 TEETLNRDIRmiDYLREESEVAKEKDGTTvSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:PRK10247 89 TPTLFGDTVY--DNLIFPWQIRNQQPDPA-IFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|...
gi 488422749 469 NDLDTETLTILEDYIASF----GGSVITVSHDR 497
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYvreqNIAVLWVTHDK 198
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
320-483 |
9.07e-13 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 68.09 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVA----------YFKQ 388
Cdd:TIGR03864 3 EVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVaGHDLRRApraalarlgvVFQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 TeeTLNRDIRMIDYLREE-------SEVAKEKdgttvsITQLLERFLFpSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNV 461
Cdd:TIGR03864 83 P--TLDLDLSVRQNLRYHaalhglsRAEARAR------IAELLARLGL-AERADDKVRELNGGHRRRVEIARALLHRPAL 153
|
170 180
....*....|....*....|..
gi 488422749 462 LLLDEPTNDLDTETLTILEDYI 483
Cdd:TIGR03864 154 LLLDEPTVGLDPASRAAITAHV 175
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
320-497 |
1.16e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.86 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK-VAYFKQTEETLNRDI 397
Cdd:PRK11607 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLShVPPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RMIDYLREESEVA---KEKDGTTVSITQLLERFLfpSSTH-----GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTN 469
Cdd:PRK11607 101 ALFPHMTVEQNIAfglKQDKLPKAEIASRVNEML--GLVHmqefaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 488422749 470 DLDT--------ETLTILEdyiaSFGGSVITVSHDR 497
Cdd:PRK11607 179 ALDKklrdrmqlEVVDILE----RVGVTCVMVTHDQ 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-231 |
1.29e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.09 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDLDGNLSVFEAV-LSSETSTLQII 98
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVrLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 99 khyeqAVQQYTveQTDRNFQAMM--------AAQEAMDRHEAWdynaeiktiLSKLGIHD-TTKQVNSLSGGQQKRVVLA 169
Cdd:PRK11300 102 -----LVAQHQ--QLKTGLFSGLlktpafrrAESEALDRAATW---------LERVGLLEhANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 170 KTLIEQPDLLLLDEPT---NHLDFESINWLINYVK-QYPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:PRK11300 166 RCMVTQPEILMLDEPAaglNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
320-496 |
1.34e-12 |
|
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: 67.65 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV-KVAYFKQTEETLNRDI 397
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdGKDItNLPPHKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RMIDYLREESEVA-------------KEKDGTTVSITQLLERflfpsstHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLL 464
Cdd:cd03300 82 ALFPHLTVFENIAfglrlkklpkaeiKERVAEALDLVQLEGY-------ANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 488422749 465 DEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:cd03300 155 DEPLGALDlklrKDMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-467 |
1.51e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 67.57 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQT------------VKVAYFK 387
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QtEETLNRDIRMIDYLREESEVAKE-KDGTTVSITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:cd03218 82 Q-EASIFRKLTVEENILAVLEIRGLsKKEREEKLEELLEEFHITHLRK-SKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
.
gi 488422749 467 P 467
Cdd:cd03218 160 P 160
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-243 |
1.58e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 67.75 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 3 AYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDD-----FTGDIT---------------- 61
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILldgediydpdvdvvel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 62 ---------HPNQ------------YRIRYSSQKQDLDgnlsvfEAVlssetstlqiikhyEQAVQQytveqtdrnfqam 120
Cdd:COG1117 91 rrrvgmvfqKPNPfpksiydnvaygLRLHGIKSKSELD------EIV--------------EESLRK------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 121 mAAQeamdrheaWDynaEIKTILSKLGihdttkqvNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLI 197
Cdd:COG1117 138 -AAL--------WD---EVKDRLKKSA--------LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakIEELI 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 198 NYVKQYpYTVLFVTH---------DR--YFLNevsTRIVELDR-GKLTTYPGNY--EDYI 243
Cdd:COG1117 198 LELKKD-YTIVIVTHnmqqaarvsDYtaFFYL---GELVEFGPtEQIFTNPKDKrtEDYI 253
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
320-504 |
1.84e-12 |
|
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: 67.07 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKT-----INGRTL--FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI---GQTVKVAyfkQT 389
Cdd:COG4778 6 EVENLSKTftlhlQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVDLA---QA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EEtlnRDI-----RMIDY----LR-------------------EESEVAKEKDGttvsitQLLERF--------LFPSSt 433
Cdd:COG4778 83 SP---REIlalrrRTIGYvsqfLRviprvsaldvvaepllergVDREEARARAR------ELLARLnlperlwdLPPAT- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 434 hgkkiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET----LTILEDYIASfGGSVITVSHDRYFLNKVA 504
Cdd:COG4778 153 -------FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR-GTAIIGIFHDEEVREAVA 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
321-475 |
2.11e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 321 LDSLTKTI-NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK-------VAYFKQTEE 391
Cdd:PRK15056 9 VNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPTRqalqknlVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 T------LNRDIRMID------YLReeseVAKEKDGTTVsiTQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQP 459
Cdd:PRK15056 89 VdwsfpvLVEDVVMMGryghmgWLR----RAKKRDRQIV--TAALARVDMVEFRH-RQIGELSGGQKKRVFLARAIAQQG 161
|
170
....*....|....*.
gi 488422749 460 NVLLLDEPTNDLDTET 475
Cdd:PRK15056 162 QVILLDEPFTGVDVKT 177
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
318-496 |
2.14e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 VYELDSLTKTI----NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLK-IGQTVKvayfKQTEE- 391
Cdd:PRK10584 6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlVGQPLH----QMDEEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 --------------------TLN--RDIRMIDYLREESEvAKEKDGTTVSITQLlerflfpssTHGKKIY----KLSGGE 445
Cdd:PRK10584 82 raklrakhvgfvfqsfmlipTLNalENVELPALLRGESS-RQSRNGAKALLEQL---------GLGKRLDhlpaQLSGGE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 446 QKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIAS----FGGSVITVSHD 496
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSlnreHGTTLILVTHD 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-232 |
2.23e-12 |
|
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: 70.15 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYA-DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThPNQYRIryssqkQDLDgnlsvf 84
Cdd:TIGR01193 476 INDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL-LNGFSL------KDID------ 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 eavlssETSTLQIIKHYEQAVQQYTVEQTDrnfQAMMAAQEAMDRHEAWDYN--AEIKTILSK--LGIH-DTTKQVNSLS 159
Cdd:TIGR01193 543 ------RHTLRQFINYLPQEPYIFSGSILE---NLLLGAKENVSQDEIWAACeiAEIKDDIENmpLGYQtELSEEGSSIS 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 160 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLI-NYVKQYPYTVLFVTHdRYFLNEVSTRIVELDRGKL 232
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVnNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
335-475 |
2.28e-12 |
|
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: 66.84 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTvkvayfkqteetlnrDIRMID---------YLRE 405
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT---------------DIRQLDpadlrrnigYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 406 ESEV--AKEKDGTTVS-----------------ITQLLER----FLFPSSTHGkkiYKLSGGEQKRLYLLRLLVHQPNVL 462
Cdd:cd03245 86 DVTLfyGTLRDNITLGapladderilraaelagVTDFVNKhpngLDLQIGERG---RGLSGGQRQAVALARALLNDPPIL 162
|
170
....*....|...
gi 488422749 463 LLDEPTNDLDTET 475
Cdd:cd03245 163 LLDEPTSAMDMNS 175
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
320-513 |
2.37e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.04 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAyfKQTEETLNRDIR 398
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVNDP--KVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MID---YL---------------------REESE-VAKE---KDGttvsitqLLERF-LFPSsthgkkiyKLSGGEQKRL 449
Cdd:PRK09493 81 MVFqqfYLfphltalenvmfgplrvrgasKEEAEkQAREllaKVG-------LAERAhHYPS--------ELSGGQQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 450 YLLRLLVHQPNVLLLDEPTNDLDT----ETLTILEDyIASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPelrhEVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
320-497 |
2.39e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.59 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGqtvkvayfkqtEETLN----- 394
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-----------GRDVTglppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 -RDIRMI--DY---------------LREESEVAKEKDGTT------VSITQLLERflfpssthgkKIYKLSGGEQKRLY 450
Cdd:COG3842 76 kRNVGMVfqDYalfphltvaenvafgLRMRGVPKAEIRARVaellelVGLEGLADR----------YPHQLSGGQQQRVA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 451 LLRLLVHQPNVLLLDEPTNDLD--------TETLTILEDyiasFGGSVITVSHDR 497
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDaklreemrEELRRLQRE----LGITFIYVTHDQ 196
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-225 |
2.40e-12 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 68.16 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIF----DDLSLAISNHEKIGLVGINGTGKSTLLK-VMGgidddftgdITHPNQY---RIRYssQKQD 76
Cdd:COG0444 3 EVRNLKVYFPTRRGVvkavDGVSFDVRRGETLGLVGESGSGKSTLARaILG---------LLPPPGItsgEILF--DGED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 77 LDGnlsvfeavLSSETstLQIIKHYE-QAVQQ---------YTVEQTdrnFQAMMAAQEAMDRHEAWdynAEIKTILSKL 146
Cdd:COG0444 72 LLK--------LSEKE--LRKIRGREiQMIFQdpmtslnpvMTVGDQ---IAEPLRIHGGLSKAEAR---ERAIELLERV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 147 GIHDTTKQVNS----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDfESI-----NWLINYVKQYPYTVLFVTHDRYFL 217
Cdd:COG0444 136 GLPDPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALD-VTIqaqilNLLKDLQRELGLAILFITHDLGVV 214
|
....*...
gi 488422749 218 NEVSTRIV 225
Cdd:COG0444 215 AEIADRVA 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
329-495 |
2.47e-12 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 65.80 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLkigqtvkvayfkqteeTLNrdirmidylreESE 408
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI----------------TLD-----------GVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 409 VAKEKDGTTVSITQLLER-FLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASF- 486
Cdd:cd03247 66 VSDLEKALSSLISVLNQRpYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVl 145
|
170
....*....|
gi 488422749 487 -GGSVITVSH 495
Cdd:cd03247 146 kDKTLIWITH 155
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
2.48e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 67.58 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSY----ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqd 76
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 77 LDGnlsvfEAVLSSETstlqiikhyEQAVqqytVEQTD-----RN------FQAMMAAQEAMDRHEAWDYNaeiktiLSK 145
Cdd:COG4525 66 LDG-----VPVTGPGA---------DRGV----VFQKDallpwLNvldnvaFGLRLRGVPKAERRARAEEL------LAL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488422749 146 LGIHDT-TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESINWLINYVKQYPY-TVLFVTHD 213
Cdd:COG4525 122 VGLADFaRRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTGkGVFLITHS 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-213 |
3.12e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADK----VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdldgn 80
Cdd:PRK10584 8 EVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVS------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 lsvfeaVLSSETSTLQiikhyEQAVQQYTVEQTDRNFQAMM-----AAQE-----AMDRHEA-WDYNAEIKTILSKLGIH 149
Cdd:PRK10584 69 ------LVGQPLHQMD-----EEARAKLRAKHVGFVFQSFMliptlNALEnvelpALLRGESsRQSRNGAKALLEQLGLG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 150 DTTKQVNS-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----INWLINYVKQYPYTVLFVTHD 213
Cdd:PRK10584 138 KRLDHLPAqLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILVTHD 206
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-232 |
3.29e-12 |
|
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: 67.14 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 4 YKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQ--YRIRYSSQK------- 74
Cdd:TIGR02769 12 YRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlYQLDRKQRRafrrdvq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 ---QDldgNLSVFEAVLSSETSTLQIIKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRHEAwdynaeiktilsklgihdt 151
Cdd:TIGR02769 92 lvfQD---SPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPR------------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 tkqvnSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESINWLINYVKQ-YPYTVLFVTHDRYFLNEVSTRIVEL 227
Cdd:TIGR02769 150 -----QLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQaFGTAYLFITHDLRLVQSFCQRVAVM 224
|
....*
gi 488422749 228 DRGKL 232
Cdd:TIGR02769 225 DKGQI 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
334-495 |
3.30e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.47 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 334 FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYfkqTEETLNRDIRMI--------DYLRE 405
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY---SEAALRQAISVVsqrvhlfsATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 406 ESEVAKEKDG--------TTVSITQLLErflfpsSTHGKKIY------KLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:PRK11160 433 NLLLAAPNASdealievlQQVGLEKLLE------DDKGLNAWlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180
....*....|....*....|....*...
gi 488422749 472 DTET----LTILEDYIAsfGGSVITVSH 495
Cdd:PRK11160 507 DAETerqiLELLAEHAQ--NKTVLMITH 532
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
319-496 |
5.36e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 319 YELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTV-----------KVAYFK 387
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 Q----TEETLNRDIRMID----------YLREESEVAKEKDgTTVSITQLLERFlfpssthgkkIYKLSGGEQKRLYLLR 453
Cdd:PRK10575 92 QqlpaAEGMTVRELVAIGrypwhgalgrFGAADREKVEEAI-SLVGLKPLAHRL----------VDSLSGGERQRAWIAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488422749 454 LLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
320-531 |
5.47e-12 |
|
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: 65.24 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGedqqFEGTLKIGQTVkvaYFKqteetlNRDIRM 399
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEVTEGEI---LFK------GEDITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 IdylrEESEVAKEkdGTTVSitqllerFLFPSSTHGKKI--------YKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:cd03217 69 L----PPEERARL--GIFLA-------FQYPPEIPGVKNadflryvnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 472 DTETLTILEDYIASF---GGSVITVSHDRYFLNKVAQEYWFI-HDGmmeRIV--GSFEDYETYKKE 531
Cdd:cd03217 136 DIDALRLVAEVINKLreeGKSVLIITHYQRLLDYIKPDRVHVlYDG---RIVksGDKELALEIEKK 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-232 |
5.59e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.44 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITHPnqyrirySSQKQDLd 78
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgeDVTHR-------SIQQRDI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 79 gnLSVFEA-VLSSETStlqIIKHYEQAVQQYTVEQTDRNfQAMMAAQEAMDrheawdynaeiktiLSklGIHDttKQVNS 157
Cdd:PRK11432 81 --CMVFQSyALFPHMS---LGENVGYGLKMLGVPKEERK-QRVKEALELVD--------------LA--GFED--RYVDQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF-------ESINWLinyVKQYPYTVLFVTHDRYFLNEVSTRIVELDRG 230
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIREL---QQQFNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
..
gi 488422749 231 KL 232
Cdd:PRK11432 214 KI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
318-519 |
5.80e-12 |
|
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: 68.39 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 VYELDSLTKTINGRTLF--QDITQIIQSGQRIGIVGPNGAGKTTMLNILSG---EDQQFEGTLKIGQTVKVAYfkqTEET 392
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLEL---SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 393 LNRDIRMI--------DYLREESEVAKEKDGTTVS-------ITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVH 457
Cdd:COG1123 81 RGRRIGMVfqdpmtqlNPVTVGDQIAEALENLGLSraeararVLELLEAVGLERRLD-RYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 458 QPNVLLLDEPTNDLDT----ETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIV 519
Cdd:COG1123 160 DPDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG---RIV 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-233 |
7.12e-12 |
|
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: 65.62 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITH-PNQYRIR----YSS 72
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGsirldgeDITKlPPHERARagiaYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 73 QKQDLDGNLSVFEavlssetstlqiikhyeqavqqytveqtdrNFQAMMAAQEAMDRH---EAWDYNAEIKTILSKLGih 149
Cdd:TIGR03410 82 QGREIFPRLTVEE------------------------------NLLTGLAALPRRSRKipdEIYELFPVLKEMLGRRG-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 150 dttkqvNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTnhldfESI---------NWLINYVKQYPYTVLFVTHDRYFLNEV 220
Cdd:TIGR03410 130 ------GDLSGGQQQQLAIARALVTRPKLLLLDEPT-----EGIqpsiikdigRVIRRLRAEGGMAILLVEQYLDFAREL 198
|
250
....*....|...
gi 488422749 221 STRIVELDRGKLT 233
Cdd:TIGR03410 199 ADRYYVMERGRVV 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-496 |
7.60e-12 |
|
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: 68.17 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKS-TLLKVMGGIDDDftgdITHPnQYRIRYssQKQDLdgnLSVFEAVLssetstlqii 98
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDP----AAHP-SGSILF--DGQDL---LGLSEREL---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 99 khyeQAV---------QQ--------YTVEQtdrnfQAM--MAAQEAMDRHEAWdynAEIKTILSKLGIHDTTKQVNS-- 157
Cdd:COG4172 87 ----RRIrgnriamifQEpmtslnplHTIGK-----QIAevLRLHRGLSGAAAR---ARALELLERVGIPDPERRLDAyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 --LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDryfLNEVStriveldrgk 231
Cdd:COG4172 155 hqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqaQILDLLKDLQRELGMALLLITHD---LGVVR---------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 232 lttypgNYEDYIA-MRA----E----KEVIEQKQNDKQRALykqeLAWMRAGAKARSTKQQARIhrfndLEANvkqqqtq 302
Cdd:COG4172 222 ------RFADRVAvMRQgeivEqgptAELFAAPQHPYTRKL----LAAEPRGDPRPVPPDAPPL-----LEAR------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 303 dkgELNLAYSR----LGKQVYELDSLtktingrtlfQDITQIIQSGQRIGIVGPNGAGKTT----MLNILSGEDQ-QFEG 373
Cdd:COG4172 280 ---DLKVWFPIkrglFRRTVGHVKAV----------DGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIPSEGEiRFDG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 374 T-------------------------------LKIGQTV----KVAYFKQTEETlnRDIRMIDYLREesevakekdgttV 418
Cdd:COG4172 347 QdldglsrralrplrrrmqvvfqdpfgslsprMTVGQIIaeglRVHGPGLSAAE--RRARVAEALEE------------V 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 419 SIT-QLLERflFPsstHgkkiyKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITV 493
Cdd:COG4172 413 GLDpAARHR--YP---H-----EFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILDLLRDLQREHGLAYLFI 482
|
...
gi 488422749 494 SHD 496
Cdd:COG4172 483 SHD 485
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
341-495 |
8.07e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.37 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK--------VAYFKQ--------TEET-----LNRDIR 398
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTttppsrrpVSMLFQennlfshlTVAQniglgLNPGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIDYLREE-SEVAKEkdgttVSITQLLERFlfPSsthgkkiyKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----T 473
Cdd:PRK10771 102 LNAAQREKlHAIARQ-----MGIEDLLARL--PG--------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQ 166
|
170 180
....*....|....*....|..
gi 488422749 474 ETLTILEDYIASFGGSVITVSH 495
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMVSH 188
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-232 |
8.89e-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: 64.98 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 10 NKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDD---FTGDIT--------HPNQYRIRYSSQKQDLD 78
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILfngqprkpDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 79 GNLSVFEAVLSSETSTLQiiKHYEQAVQQytveqtdrnfqaMMAAQEAMdRHEAwdynaeiktiLSKLGihdtTKQVNSL 158
Cdd:cd03234 94 PGLTVRETLTYTAILRLP--RKSSDAIRK------------KRVEDVLL-RDLA----------LTRIG----GNLVKGI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPY---TVLFVTHD-RYFLNEVSTRIVELDRGKL 232
Cdd:cd03234 145 SGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARrnrIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
330-495 |
9.09e-12 |
|
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: 65.33 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 330 GRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILsgedqqF------EGTLKI-GQTVKvayfKQTEETLNRDIRM--- 399
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL------FrfydvsSGSILIdGQDIR----EVTLDSLRRAIGVvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 ------------IDYLREE-SEVAKEKDGTTVSITQLLERFLFPSSTH-GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLD 465
Cdd:cd03253 83 dtvlfndtigynIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIvGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190
....*....|....*....|....*....|..
gi 488422749 466 EPTNDLDTETLTILEDYIASF--GGSVITVSH 495
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-254 |
1.00e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.80 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 13 YADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRYSSQKQDLD--GNLSVFEavlss 90
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--------LRPQKGAVLWQGKPLDYSkrGLLALRQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 91 etstlQIIKHYEQAVQQ--YTVEQTDRNF--QAMMAAQEAMDRheawdynaEIKTILSKLGIHDTTKQ-VNSLSGGQQKR 165
Cdd:PRK13638 78 -----QVATVFQDPEQQifYTDIDSDIAFslRNLGVPEAEITR--------RVDEALTLVDAQHFRHQpIQCLSHGQKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 166 VVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK---QYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTY--PGNye 240
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRrivAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHgaPGE-- 222
|
250
....*....|....
gi 488422749 241 dyiaMRAEKEVIEQ 254
Cdd:PRK13638 223 ----VFACTEAMEQ 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
330-495 |
1.10e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 330 GRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK---VAYFKQT---------------E 390
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRrqrDEYHQDLlylghqpgikteltaL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 391 ETLNRDIRMIDYLREES-EVAKEKDGttvsitqLLERFLFPSSThgkkiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTN 469
Cdd:PRK13538 93 ENLRFYQRLHGPGDDEAlWEALAQVG-------LAGFEDVPVRQ-------LSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 488422749 470 DLDTETLTILEDYI---ASFGGSVITVSH 495
Cdd:PRK13538 159 AIDKQGVARLEALLaqhAEQGGMVILTTH 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-232 |
1.17e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 8 HLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGdithpnqyrIRYSSQKqdLDGNLSVFeav 87
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG---------YRYSGDV--LLGGRSIF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 88 lsSETSTLQIIKHYEQAVQQ---YTVEQTDrNFQAMMAAQEAMDRHEawdYNAEIKTILSKLGIHDTTKQVNS-----LS 159
Cdd:PRK14271 92 --NYRDVLEFRRRVGMLFQRpnpFPMSIMD-NVLAGVRAHKLVPRKE---FRGVAQARLTEVGLWDAVKDRLSdspfrLS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 160 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP--YTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:PRK14271 166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAdrLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-496 |
1.21e-11 |
|
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: 64.45 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLF--QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQtvkvaYFKQTEEtlnRDI 397
Cdd:cd03263 2 QIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-----YSIRTDR---KAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RM-----------------IDYLREESEV-AKEKDGTTVSITQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQP 459
Cdd:cd03263 74 RQslgycpqfdalfdeltvREHLRFYARLkGLPKSEIKEEVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 488422749 460 NVLLLDEPTNDLDTETLTILEDYIASFGG--SVITVSHD 496
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-232 |
1.26e-11 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 64.50 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 13 YADKVIFDD------LSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---------THPNQYRIRYSSQKQDL 77
Cdd:TIGR01277 2 ALDKVRYEYehlpmeFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIkvndqshtgLAPYQRPVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 78 DGNLSVFEAVLSSETSTLQIikhyeQAVQQYTVEQtdrnfqammAAQEamdrheawdynaeiktilskLGIHDTTKQV-N 156
Cdd:TIGR01277 82 FAHLTVRQNIGLGLHPGLKL-----NAEQQEKVVD---------AAQQ--------------------VGIADYLDRLpE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:TIGR01277 128 QLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
296-495 |
1.32e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 296 VKQQQTQDkGELNLAYSRLGKQvyeldsLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDqqfEGTL 375
Cdd:TIGR00955 10 VFGRVAQD-GSWKQLVSRLRGC------FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS---PKGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 376 KIGQTVKV--------------AYFKQ---------TEETLNRDIRmidyLREESEVAKEKDGTTVSitQLLERFLFPSS 432
Cdd:TIGR00955 80 KGSGSVLLngmpidakemraisAYVQQddlfiptltVREHLMFQAH----LRMPRRVTKKEKRERVD--EVLQALGLRKC 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488422749 433 TH-----GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDT----ETLTILEDyIASFGGSVITVSH 495
Cdd:TIGR00955 154 ANtrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSfmaySVVQVLKG-LAQKGKTIICTIH 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-189 |
1.32e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.10 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnLSVF 84
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL---------------VDG-LDVA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 E---AVLSsetSTLQIIKHYEQAVQQYTVEQ--------------TDRNFQAMmaaQEAMDRheawdynaeiktilskLG 147
Cdd:COG4604 67 TtpsRELA---KRLAILRQENHINSRLTVRElvafgrfpyskgrlTAEDREII---DEAIAY----------------LD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488422749 148 IHD-TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:COG4604 125 LEDlADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
330-472 |
1.33e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.81 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 330 GRTLFqDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQT-------------------- 389
Cdd:PRK13634 20 RRALY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplrkkvgivfqfpehql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 -EETLNRDIRM--IDYLREESEvAKEKDGTTVSITQLLERFLFPSSthgkkiYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:PRK13634 99 fEETVEKDICFgpMNFGVSEED-AKQKAREMIELVGLPEELLARSP------FELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
....*.
gi 488422749 467 PTNDLD 472
Cdd:PRK13634 172 PTAGLD 177
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-232 |
1.39e-11 |
|
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: 64.41 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 15 DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---HP-NQYRIRYSSQKQDLDGNlsvfEAVLSS 90
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPiSQYEHKYLHSKVSLVGQ----EPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 91 ETSTLQIikhyeqavqQYTVEQTdrnfqAMMAAQEAMDRHEAWDYNAEIKtilskLGIH-DTTKQVNSLSGGQQKRVVLA 169
Cdd:cd03248 102 RSLQDNI---------AYGLQSC-----SFECVKEAAQKAHAHSFISELA-----SGYDtEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 170 KTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP--YTVLFVTHdRYFLNEVSTRIVELDRGKL 232
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPerRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
320-527 |
1.41e-11 |
|
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: 64.67 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIG---------QTVKVAYFKQtE 390
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVFQ-H 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 391 ETLNRDIRMIDYL--------REESEVAKEKDGTTVSITQL--LERFL--FPSsthgkkiyKLSGGEQKRLYLLRLLVHQ 458
Cdd:cd03296 83 YALFRHMTVFDNVafglrvkpRSERPPEAEIRAKVHELLKLvqLDWLAdrYPA--------QLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 459 PNVLLLDEPTNDLDTETLTILEDYIASF----GGSVITVSHDRYFLNKVAQEYWFIHDGMMERiVGSFED-YET 527
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ-VGTPDEvYDH 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-232 |
1.50e-11 |
|
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: 64.52 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADK----VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT--------------HPNQY 66
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 67 RIRYSSQKQDLDGNLSVFEAVlsseTSTLQIiKHYEQAVQQYTVEQTdRNFQAMMaaqeamDRHEAwdYNAEiktilskl 146
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENV----ALPLEI-AGVPKAEIEERVLEL-LELVGLE------DKADA--YPAQ-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 147 gihdttkqvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SINWL---INyvKQYPYTVLFVTHDRYFLNEV 220
Cdd:cd03258 141 -----------LSGGQKQRVGIARALANNPKVLLCDEATSALDPEttqSILALlrdIN--RELGLTIVLITHEMEVVKRI 207
|
250
....*....|..
gi 488422749 221 STRIVELDRGKL 232
Cdd:cd03258 208 CDRVAVMEKGEV 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-189 |
1.84e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.58 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 12 SYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMggidddfTGDitHPNQY----------------------RIR 69
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGD--HPQGYsndltlfgrrrgsgetiwdikkHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSSQKQDLDG--NLSVFEAVLSSETSTLQIikhYeQAVqqytveqTDRnfQAMMAAQeamdrheaWdynaeiktiLSKLG 147
Cdd:PRK10938 340 YVSSSLHLDYrvSTSVRNVILSGFFDSIGI---Y-QAV-------SDR--QQKLAQQ--------W---------LDILG 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488422749 148 IHDTT--KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:PRK10938 390 IDKRTadAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.86e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSY-ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGD-------ITHPNQYRIRyss 72
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlirgepITKENIREVR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 73 qkqdldgnlsvfeavlssETSTLqIIKHYEQAVQQYTVEQtDRNFQAM-MAAQEAMDRHEawdynaeIKTILSKLGIHDT 151
Cdd:PRK13652 78 ------------------KFVGL-VFQNPDDQIFSPTVEQ-DIAFGPInLGLDEETVAHR-------VSSALHMLGLEEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 TKQV-NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYV----KQYPYTVLFVTHDRYFLNEVSTRIVE 226
Cdd:PRK13652 131 RDRVpHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLndlpETYGMTVIFSTHQLDLVPEMADYIYV 210
|
....*....
gi 488422749 227 LDRGKLTTY 235
Cdd:PRK13652 211 MDKGRIVAY 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-233 |
2.08e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSY-ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDddftgditHPNQYRIRYSSQkqdldgNLSV 83
Cdd:PRK10908 3 RFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE--------RPSAGKIWFSGH------DITR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEavlSSETSTLQiiKHYEQAVQQYTVeQTDRNFQAMMAAQEAMDRHEAWDYNAEIKTILSKLGIHDTTKQVN-SLSGGQ 162
Cdd:PRK10908 69 LK---NREVPFLR--RQIGMIFQDHHL-LMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPiQLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLT 233
Cdd:PRK10908 143 QQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
329-524 |
2.10e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGedqqF---EGTLKI-GQTVkvayfkqteetlnRDIRMIDYLR 404
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG----FlpyQGSLKInGIEL-------------RELDPESWRK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 405 EESEVAKE----------------KDGTTVSITQLLER-----FLfPSSTHG------KKIYKLSGGEQKRLYLLRLLVH 457
Cdd:PRK11174 424 HLSWVGQNpqlphgtlrdnvllgnPDASDEQLQQALENawvseFL-PLLPQGldtpigDQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488422749 458 QPNVLLLDEPTNDLDTET----LTILEDyiASFGGSVITVSHDRYFLNKVaQEYWFIHDGmmeRIV--GSFED 524
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSeqlvMQALNA--ASRRQTTLMVTHQLEDLAQW-DQIWVMQDG---QIVqqGDYAE 569
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-213 |
2.22e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.01 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVI-FDdlsLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---------THPNQYRIRYSSQK 74
Cdd:COG3840 3 RLDDLTYRYGDFPLrFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltaLPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 QDLDGNLSVFEAV---LSSETstlqiikhyeqavqQYTVEQTDRnfqammaaqeamdrheawdynaeIKTILSKLGIHD- 150
Cdd:COG3840 80 NNLFPHLTVAQNIglgLRPGL--------------KLTAEQRAQ-----------------------VEQALERVGLAGl 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 151 TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHD 213
Cdd:COG3840 123 LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
320-496 |
2.35e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.65 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG---EDQQFEGTLKIGQTV---------KVAYFK 387
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlsPAFSASGEVLLNGRRltalpaeqrRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QTE-----------------ETLNRDIRmidylREESEVAKEKdgttVSITQLLERFlfPSSthgkkiykLSGGEQKRLY 450
Cdd:COG4136 83 QDDllfphlsvgenlafalpPTIGRAQR-----RARVEQALEE----AGLAGFADRD--PAT--------LSGGQRARVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488422749 451 LLRLLVHQPNVLLLDEPTNDLDTE-TLTILE---DYIASFGGSVITVSHD 496
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAAlRAQFREfvfEQIRQRGIPALLVTHD 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
9-227 |
2.38e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 9 LNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---THPNQY--RIRYSSQKQDLDGnlsv 83
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTATRgdRSRFMAYLGHLPG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 feavLSSETSTLQIIkHYEQAVQQYTVEQTDRNfqammaaqeAMdrheawdynaeikTILSKLGIHDTTkqVNSLSGGQQ 163
Cdd:PRK13543 93 ----LKADLSTLENL-HFLCGLHGRRAKQMPGS---------AL-------------AIVGLAGYEDTL--VRQLSAGQK 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYT---VLFVTHDRYFLNEVSTRIVEL 227
Cdd:PRK13543 144 KRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGggaALVTTHGAYAAPPVRTRMLTL 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-231 |
2.59e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYA-----DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG----------IDDDftgDITHPNQY-RI 68
Cdd:COG1101 3 ELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslppdsgsilIDGK---DVTKLPEYkRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 69 RYSSQK-QD-LDG---NLSVFE----AVLSSETSTLQIikhyeqavqqytveqtdrnfqammaaqeAMDRHEAWDYNAEI 139
Cdd:COG1101 80 KYIGRVfQDpMMGtapSMTIEEnlalAYRRGKRRGLRR----------------------------GLTKKRRELFRELL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 140 KTIlsKLGIHD--TTKqVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLINY-VKQYPYTVLFVTHD 213
Cdd:COG1101 132 ATL--GLGLENrlDTK-VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAALVLELTEKiVEENNLTTLMVTHN 208
|
250
....*....|....*....
gi 488422749 214 -RYFLnEVSTRIVELDRGK 231
Cdd:COG1101 209 mEQAL-DYGNRLIMMHEGR 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-232 |
2.85e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYA-----DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPN----QYRIRYSSQKQ 75
Cdd:TIGR00958 478 LIEFQDVSFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvQYDHHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNlsvfEAVLSSETSTLQIIkhyeqavqqYTVEQTDRNfQAMMAAQEAMdrheAWDYNAEI-KTILSKLGIHDttkq 154
Cdd:TIGR00958 558 ALVGQ----EPVLFSGSVRENIA---------YGLTDTPDE-EIMAAAKAAN----AHDFIMEFpNGYDTEVGEKG---- 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 155 vNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHdRYFLNEVSTRIVELDRGKL 232
Cdd:TIGR00958 616 -SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSV 691
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-233 |
2.86e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 22 LSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDdFTGDIT----------HPNQYRIR-YSSQKQDLDGNLSVFeavlss 90
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQfagqpleawsAAELARHRaYLSQQQTPPFAMPVF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 91 etstlqiikHYeqavqqYTVEQTDRnfqammaAQEAMDRHeAWDYNAEIKTILSKLGIHdttkqVNSLSGGQQKRVVLAK 170
Cdd:PRK03695 88 ---------QY------LTLHQPDK-------TRTEAVAS-ALNEVAEALGLDDKLGRS-----VNQLSGGEWQRVRLAA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 171 TLIE-----QPD--LLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHDryfLNEV---STRIVELDRGKLT 233
Cdd:PRK03695 140 VVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALdrlLSELCQQGIAVVMSSHD---LNHTlrhADRVWLLKQGKLL 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-252 |
3.27e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 7 EHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG----DITHPNQY-------RIRYSSQKQ 75
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwlDGEHIQHYaskevarRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVLSSETStlqiikhYEQAVQQYTVEQTDRNFQAMMAAqeamdrheawdynaeiktilsklGIHDTTKQ- 154
Cdd:PRK10253 91 TTPGDITVQELVARGRYP-------HQPLFTRWRKEDEEAVTKAMQAT-----------------------GITHLADQs 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDryfLNEV---STRIVEL 227
Cdd:PRK10253 141 VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD---LNQAcryASHLIAL 217
|
250 260
....*....|....*....|....*
gi 488422749 228 DRGKLttypgnyedyIAMRAEKEVI 252
Cdd:PRK10253 218 REGKI----------VAQGAPKEIV 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-220 |
3.33e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKV-MGgidddftgditHPNqYRIrySSQKQDLDGnlsv 83
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVlMG-----------HPK-YEV--TSGSILLDG---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 fEAVLSSETstlqiikhYEQAVQ------QYTVE---QTDRNFqaMMAAQEAMDRHE--AWDYNAEIKTILSKLGIHDT- 151
Cdd:COG0396 64 -EDILELSP--------DERARAgiflafQYPVEipgVSVSNF--LRTALNARRGEElsAREFLKLLKEKMKELGLDEDf 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 152 -TKQVN-SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPY---TVLFVTHDRYFLNEV 220
Cdd:COG0396 133 lDRYVNeGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRILDYI 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
329-495 |
4.12e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 65.96 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGedqqF----EGTLKI-GQTVK----------VAYFKQT---- 389
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR----FydptSGRILIdGVDIRdltleslrrqIGVVPQDtflf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EETLnRD-IRM--IDYLREE-SEVAKekdgtTVSITQLLERflFPS--STH-GKKIYKLSGGEQKRLYLLRLLVHQPNVL 462
Cdd:COG1132 427 SGTI-REnIRYgrPDATDEEvEEAAK-----AAQAHEFIEA--LPDgyDTVvGERGVNLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190
....*....|....*....|....*....|....*
gi 488422749 463 LLDEPTNDLDTETLTILEDYIASF--GGSVITVSH 495
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERLmkGRTTIVIAH 533
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
335-468 |
4.39e-11 |
|
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: 62.84 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIG----------QTVK--VAYFKQT---------EETL 393
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglpphERARagIGYVPEGrrifpeltvEENL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 394 nrdiRMIDYLREESEVAKEKDgttvsitQLLErfLFP--SSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:cd03224 97 ----LLGAYARRRAKRKARLE-------RVYE--LFPrlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
320-472 |
4.44e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.85 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK------------VAYF 386
Cdd:PRK13536 43 DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVPararlararigvVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 387 KQTEETLNRDIRMIDYLREESEVAKEKDGTtvsITQLLErFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:PRK13536 123 DNLDLEFTVRENLLVFGRYFGMSTREIEAV---IPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
....*.
gi 488422749 467 PTNDLD 472
Cdd:PRK13536 199 PTTGLD 204
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
158-232 |
4.66e-11 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 64.44 E-value: 4.66e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:TIGR01187 101 LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiqeQLGITFVFVTHDQEEAMTMSDRIAIMRKGKI 179
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
331-495 |
4.83e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFqDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEETLNRDIRMIDYLREESEVA 410
Cdd:PRK13643 20 RALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 411 KE----------------KDGTTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD-- 472
Cdd:PRK13643 99 EEtvlkdvafgpqnfgipKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpk 178
|
170 180
....*....|....*....|....*
gi 488422749 473 --TETLTILEDyIASFGGSVITVSH 495
Cdd:PRK13643 179 arIEMMQLFES-IHQSGQTVVLVTH 202
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-184 |
4.99e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKST-------LLKVMGG---IDDDftgDITHPNQYR-----IR 69
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVKPDSGrifLDGE---DITHLPMHKrarlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 70 YSSQKQdldgnlSVFeavlssetstlqiikhyeqavQQYTVEQtdrNFQAMMAAQEaMDRHEAwdyNAEIKTILSKLGIH 149
Cdd:COG1137 82 YLPQEA------SIF---------------------RKLTVED---NILAVLELRK-LSKKER---EERLEELLEEFGIT 127
|
170 180 190
....*....|....*....|....*....|....*.
gi 488422749 150 DTTKQV-NSLSGGQQKRVVLAKTLIEQPDLLLLDEP 184
Cdd:COG1137 128 HLRKSKaYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
320-467 |
5.03e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK-----------VAYFK 387
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QtEETLNRD------IRMIDYLREES-EVAKEKdgttvsITQLLERFlfpSSTH--GKKIYKLSGGEQKRLYLLRLLVHQ 458
Cdd:COG1137 85 Q-EASIFRKltvednILAVLELRKLSkKEREER------LEELLEEF---GITHlrKSKAYSLSGGERRRVEIARALATN 154
|
....*....
gi 488422749 459 PNVLLLDEP 467
Cdd:COG1137 155 PKFILLDEP 163
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-235 |
5.18e-11 |
|
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: 63.09 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD-KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVmggIDDDFTgdithPNQYRIRyssqkqdldgnlsv 83
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKM---INRLIE-----PTSGEIF-------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEAVLSSETSTLQIIKHYEQAVQQ------YTVEQtdrNFqAMMAAQEAMDRHEawdYNAEIKTILSKLGIHDTT---KQ 154
Cdd:cd03295 60 IDGEDIREQDPVELRRKIGYVIQQiglfphMTVEE---NI-ALVPKLLKWPKEK---IRERADELLALVGLDPAEfadRY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----------FESINWLINyvkqypYTVLFVTHDryfLNE---VS 221
Cdd:cd03295 133 PHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpitrdqlqeeFKRLQQELG------KTIVFVTHD---IDEafrLA 203
|
250
....*....|....
gi 488422749 222 TRIVELDRGKLTTY 235
Cdd:cd03295 204 DRIAIMKNGEIVQV 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-214 |
5.74e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---------THPNQYR--IRYSSQK 74
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedistLKPEIYRqqVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 QDLDGnlsvfEAVLSSETSTLQIikhyeqavqqytveqtdrnfqammaaqeamdRHEAWDYNAEIKTiLSKLGIHDTT-- 152
Cdd:PRK10247 90 PTLFG-----DTVYDNLIFPWQI-------------------------------RNQQPDPAIFLDD-LERFALPDTIlt 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 153 KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLIN-YVKQYPYTVLFVTHDR 214
Cdd:PRK10247 133 KNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnKHNVNEIIHrYVREQNIAVLWVTHDK 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-227 |
7.32e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.99 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 17 VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI----THPNQYR------IRYSSQKQDLDGNLSVFEa 86
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngTPLAEQRdephenILYLGHLPGLKPELSALE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 87 vlssetsTLQIIKHYEQAvQQYTVEQtdrnfqammaAQEAMDrheawdynaeiktiLSklGIHDTTkqVNSLSGGQQKRV 166
Cdd:TIGR01189 93 -------NLHFWAAIHGG-AQRTIED----------ALAAVG--------------LT--GFEDLP--AAQLSAGQQRRL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 167 VLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPYT---VLFVTHDRyfLNEVSTRIVEL 227
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARggiVLLTTHQD--LGLVEARELRL 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
315-472 |
7.61e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.20 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 315 GKQVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV------------ 381
Cdd:PRK09452 11 LSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDIthvpaenrhvnt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 382 ---------------KVAYFKQTEETLNRDI--RMIDYLReesevakekdgtTVSITQLLERflfpssthgkKIYKLSGG 444
Cdd:PRK09452 91 vfqsyalfphmtvfeNVAFGLRMQKTPAAEItpRVMEALR------------MVQLEEFAQR----------KPHQLSGG 148
|
170 180
....*....|....*....|....*...
gi 488422749 445 EQKRLYLLRLLVHQPNVLLLDEPTNDLD 472
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
336-496 |
8.04e-11 |
|
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: 63.98 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 336 DITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTV---------------KVAYFKQtEETL------- 393
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQ-EARLfphlsvr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 -NRDIRMIDYLREESEVAKEKDGTTVSITQLLERFlfPSsthgkkiyKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD 472
Cdd:TIGR02142 94 gNLRYGMKRARPSERRISFERVIELLGIGHLLGRL--PG--------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180
....*....|....*....|....*...
gi 488422749 473 ----TETLTILEDYIASFGGSVITVSHD 496
Cdd:TIGR02142 164 dprkYEILPYLERLHAEFGIPILYVSHS 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-540 |
8.36e-11 |
|
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: 64.82 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQ--QFEGTL-----------------KIGQT 380
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 381 VKV---------AYFKQTEETLNRDI-RMIDYLREESEVAKEKDGTTVSITQLLERFLFPSSTHGKKIYKL--------- 441
Cdd:TIGR03269 82 CPVcggtlepeeVDFWNLSDKLRRRIrKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLiemvqlshr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 442 --------SGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTI----LEDYIASFGGSVITVSHDRYFLNKVAQEYWF 509
Cdd:TIGR03269 162 ithiardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAIW 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 488422749 510 IHDGMMERIVGSFEDYETYKK-----EKDKQLAIEK 540
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVAVFMEgvsevEKECEVEVGE 277
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
340-496 |
8.57e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 8.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 340 IIQSGQRIGIVGPNGAGKTTMLNILSGEDQ----QFEGTLKIGQTVKvaYFKQTE-----ETL-NRDIR------MIDYL 403
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPSWDEVLK--RFRGTElqnyfKKLyNGEIKvvhkpqYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 404 ReesevaKEKDGTTVsitQLLER------------FLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:PRK13409 173 P------KVFKGKVR---ELLKKvdergkldevveRLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180
....*....|....*....|....*..
gi 488422749 472 DTETLTILEDYIASF--GGSVITVSHD 496
Cdd:PRK13409 244 DIRQRLNVARLIRELaeGKYVLVVEHD 270
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
341-504 |
8.74e-11 |
|
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: 62.35 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV--------KVAYFKQT-----EETLNRDIR--MIDYLR 404
Cdd:cd03299 22 VERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQNyalfpHMTVYKNIAygLKKRKV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 405 EESEVAKEKDGTT--VSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET----LTI 478
Cdd:cd03299 102 DKKEIERKVLEIAemLGIDHLLNR----------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREE 171
|
170 180 190
....*....|....*....|....*....|
gi 488422749 479 LEDYIASFGGSVITVSHD----RYFLNKVA 504
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-232 |
9.23e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYAD---------KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDddftgditHPNQYRIRYssQKQD 76
Cdd:PRK10419 6 VSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLE--------SPSQGNVSW--RGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 77 LdgnlsvfeAVLSSETstlqiIKHYEQAVQQYtveqtdrnFQAMMAA-----------QEAMdRH----EAWDYNAEIKT 141
Cdd:PRK10419 76 L--------AKLNRAQ-----RKAFRRDIQMV--------FQDSISAvnprktvreiiREPL-RHllslDKAERLARASE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 142 ILSKLGIHDT--TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDRY 215
Cdd:PRK10419 134 MLRAVDLDDSvlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLR 213
|
250
....*....|....*..
gi 488422749 216 FLNEVSTRIVELDRGKL 232
Cdd:PRK10419 214 LVERFCQRVMVMDNGQI 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
319-505 |
1.00e-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: 62.43 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 319 YELDSLTKTINGRTLfqDITQ-IIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIgQTVKVAYFKQTEETlNRDI 397
Cdd:cd03237 1 YTYPTMKKTLGEFTL--EVEGgSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKA-DYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RMIDYLRE-----------ESEVAKekdgtTVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:cd03237 77 TVRDLLSSitkdfythpyfKTEIAK-----PLQIEQILDR----------EVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488422749 467 PTNDLDTETLTILEDYIASFG----GSVITVSHDRYFLNKVAQ 505
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAenneKTAFVVEHDIIMIDYLAD 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-228 |
1.00e-10 |
|
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: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 14 ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQKQDL-DGNLSvfEAVLsset 92
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLpLGTLR--EQLI---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 93 stlqiikhyeqavqqYtveqtdrnfqammaaqeamdrheAWDynaeiktilsklgihdttkqvNSLSGGQQKRVVLAKTL 172
Cdd:cd03223 86 ---------------Y-----------------------PWD---------------------DVLSGGEQQRLAFARLL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 173 IEQPDLLLLDEPTNHLDFESINWLINYVKQYPYTVLFVTHdRYFLNEVSTRIVELD 228
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
322-472 |
1.02e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 322 DSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQT------------VKVAYFKQt 389
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGYLPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 EETLNRDIRMIDYLREESEVAKE--KDGTTVSITQLLERFLFpSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEP 467
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIRDDlsAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
....*
gi 488422749 468 TNDLD 472
Cdd:PRK10895 165 FAGVD 169
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
342-516 |
1.05e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.68 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 342 QSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI------------GQtVKVAYFKQ--------------------- 388
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkdGQ-LKVADKNQlrllrtrltmvfqhfnlwshm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 --TEETLNRDIRMIDYLREESEVAKEKDGTTVSITQllerflfpsSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:PRK10619 108 tvLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE---------RAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488422749 467 PTNDLDT----ETLTILEDyIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMME 516
Cdd:PRK10619 179 PTSALDPelvgEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
335-513 |
1.06e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.75 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVkvayfkqteETLNRD----IR----------- 398
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVaGQDV---------ATLDADalaqLRrehfgfifqry 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 -MIDYLREESEV-------AKEKDGTTVSITQLLERFLFpssthGKKIY----KLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:PRK10535 96 hLLSHLTAAQNVevpavyaGLERKQRLLRAQELLQRLGL-----EDRVEyqpsQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488422749 467 PTNDLDT----ETLTILEDyIASFGGSVITVSHDRYFLNKvAQEYWFIHDG 513
Cdd:PRK10535 171 PTGALDShsgeEVMAILHQ-LRDRGHTVIIVTHDPQVAAQ-AERVIEIRDG 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-232 |
1.31e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.54 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 3 AYKIEHLNKSYA-----DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSSQK--Q 75
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLS-VF---EAVLSSETstlqIIKhyeqavqqyTVEQTDRNFQAmmAAQEAMDRHEAWdynaeiktiLSKLGIHDT 151
Cdd:PRK13641 82 KLRKKVSlVFqfpEAQLFENT----VLK---------DVEFGPKNFGF--SEDEAKEKALKW---------LKKVGLSED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 --TKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHDRYFLNEVSTRIVE 226
Cdd:PRK13641 138 liSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTVILVTHNMDDVAEYADDVLV 217
|
....*.
gi 488422749 227 LDRGKL 232
Cdd:PRK13641 218 LEHGKL 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
329-475 |
1.55e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.83 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILS-GEDQQFeGTLKI-GQ---TVKVAYFKQTEET-------LNRD 396
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQS-GRILIdGTdirTVTRASLRRNIAVvfqdaglFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 397 IRmiDYLReeseVAKEkDGTTVSITQLLER-----FLFPSS----TH-GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:PRK13657 425 IE--DNIR----VGRP-DATDEEMRAAAERaqahdFIERKPdgydTVvGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
....*....
gi 488422749 467 PTNDLDTET 475
Cdd:PRK13657 498 ATSALDVET 506
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-230 |
1.66e-10 |
|
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: 61.33 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITHPNQYRIrYSSQKQDLDGNLSVFEAVLSSET 92
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGgvilegkQITEPGPDRM-VVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 93 STLqiiKHYEQAVQQYTVEQTdrnfQAMMAAQEAMDrheawdynaeiktilsklgihdttKQVNSLSGGQQKRVVLAKTL 172
Cdd:TIGR01184 81 RVL---PDLSKSERRAIVEEH----IALVGLTEAAD------------------------KRPGQLSGGMKQRVAIARAL 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 173 IEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDryfLNE---VSTRIVELDRG 230
Cdd:TIGR01184 130 SIRPKVLLLDEPFGALDAltrgNLQEELMQIWEEHRVTVLMVTHD---VDEallLSDRVVMLTNG 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-213 |
1.73e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 9 LNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKST-------LLKVMGGIDddFTGDITH--------PNQYRIRYSSQ 73
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglallrLINSQGEIW--FDGQPLHnlnrrqllPVRHRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 74 kqdlDGNLSvfeavLSSETSTLQIIKHYEQaVQQYTVEQTDRNFQAMMAAQE----AMDRHEawdYNAEiktilsklgih 149
Cdd:PRK15134 370 ----DPNSS-----LNPRLNVLQIIEEGLR-VHQPTLSAAQREQQVIAVMEEvgldPETRHR---YPAE----------- 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 150 dttkqvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHD 213
Cdd:PRK15134 426 --------FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKslqqKHQLAYLFISHD 485
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
320-496 |
1.79e-10 |
|
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: 61.55 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTING-RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFK 387
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QT-----EETLNRDIRMIDYLREESEVAKEKdgttvSITQLLERF-LFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNV 461
Cdd:cd03295 82 QQiglfpHMTVEENIALVPKLLKWPKEKIRE-----RADELLALVgLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 488422749 462 LLLDEPTNDLDTETLTILEDYIA----SFGGSVITVSHD 496
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlqqELGKTIVFVTHD 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
320-495 |
1.80e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayFKQTEETLNRDIR 398
Cdd:COG3845 7 ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVR---IRSPRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 M-------IDYL---------REES--------EVAKEkdgttvsITQLLERFLF---PSsthgKKIYKLSGGEQKRLYL 451
Cdd:COG3845 84 MvhqhfmlVPNLtvaenivlgLEPTkggrldrkAARAR-------IRELSERYGLdvdPD----AKVEDLSVGEQQRVEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488422749 452 LRLLVHQPNVLLLDEPTNDL---DTETL-TILEDYIASfGGSVITVSH 495
Cdd:COG3845 153 LKALYRGARILILDEPTAVLtpqEADELfEILRRLAAE-GKSIIFITH 199
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
321-583 |
1.85e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.33 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 321 LDSLTKTINGRTLFQ----DITQIIQSGQRIG-IVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEET--L 393
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfkalNNTSLTFKKNKVTcVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRDIRMIDYLRE--------ESEVA-------KEKDGTTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQ 458
Cdd:PRK13645 89 RKEIGLVFQFPEyqlfqetiEKDIAfgpvnlgENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 459 PNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMMERIVGSFEDYEtykkekDK 534
Cdd:PRK13645 169 GNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS------NQ 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488422749 535 QLaiekqatnTSKTQIKERKKTGLSYKEKREYESLMSR----IEETEIRLSEI 583
Cdd:PRK13645 243 EL--------LTKIEIDPPKLYQLMYKLKNKGIDLLNKnirtIEEFAKELAKV 287
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-230 |
2.23e-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: 60.58 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 16 KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQ--YRIRYSSQKQDL-DGNLSVFEAVLSSEt 92
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGplDFQRDSIARGLLyLGHAPGIKTTLSVL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 93 STLQIIkhyeqavqqytveqtdRNFQAMMAAQEAMDRheawdynaeiktiLSKLGIHDTTkqVNSLSGGQQKRVVLAKTL 172
Cdd:cd03231 92 ENLRFW----------------HADHSDEQVEEALAR-------------VGLNGFEDRP--VAQLSAGQQRRVALARLL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 173 IEQPDLLLLDEPTNHLDFESINWLINYVKQYPY---TVLFVTHDRyfLNEVSTRIVELDRG 230
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCArggMVVLTTHQD--LGLSEAGARELDLG 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-496 |
2.24e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 21 DLSLAISNHEKIGLVGINGTGKS-TLLKVMGGIDDdfTGDITHPNQYRIRYSSQKQDLDGNLSVFE---------AVLSS 90
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--AGGLVQCDKMLLRRRSRQVIELSEQSAAQmrhvrgadmAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 91 E--TSTLQIIKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRHEAwdynAEIKTILSKLGihdttkqvNSLSGGQQKRVVL 168
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI----PEAQTILSRYP--------HQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 169 AKTLIEQPDLLLLDEPTNHLDF---ESINWLINYVKQ-YPYTVLFVTHDRYFLNEVSTRIVELDRGKlTTYPGNYEdyia 244
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVtiqAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGE-AVETGSVE---- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 245 mraekEVIEQKQNDKQRALYKqelAWMRAGAkarsTKQQARIHRFNDLEANVKQQQTQDKGELNLAYsrlGKQVYELDSL 324
Cdd:PRK10261 255 -----QIFHAPQHPYTRALLA---AVPQLGA----MKGLDYPRRFPLISLEHPAKQEPPIEQDTVVD---GEPILQVRNL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 325 TKTINGRT-LFQDITQIIQS----------GQRIGIVGPNGAGKTT----MLNILsgEDQQFEGTLKiGQTVKVAYFKQT 389
Cdd:PRK10261 320 VTRFPLRSgLLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTtgraLLRLV--ESQGGEIIFN-GQRIDTLSPGKL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 eETLNRDIRMI---------------DYLREESEVAKEKDGTTVS--ITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLL 452
Cdd:PRK10261 397 -QALRRDIQFIfqdpyasldprqtvgDSIMEPLRVHGLLPGKAAAarVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488422749 453 RLLVHQPNVLLLDEPTNDLDT----ETLTILEDYIASFGGSVITVSHD 496
Cdd:PRK10261 476 RALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHD 523
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-233 |
2.27e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIE--HLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRYSSQKQDLD 78
Cdd:COG3845 1 MMPPALElrGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL--------YQPDSGEILIDGKPVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 79 G--------------------NLSVFE-AVLSSETSTLQIIkhyeqavqqytveqtdrnfqammaaqeamDRHEAwdyNA 137
Cdd:COG3845 73 SprdaialgigmvhqhfmlvpNLTVAEnIVLGLEPTKGGRL-----------------------------DRKAA---RA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 138 EIKTILSKLGIH-DTTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESINWLinyVKQyPYTVLF 209
Cdd:COG3845 121 RIRELSERYGLDvDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTpqeadelFEILRRL---AAE-GKSIIF 196
|
250 260
....*....|....*....|....*..
gi 488422749 210 VTHDryfLNEV---STRIVELDRGKLT 233
Cdd:COG3845 197 ITHK---LREVmaiADRVTVLRRGKVV 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-232 |
2.28e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 60.26 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 12 SYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG--IDDDFTGDI------THPNQYR--IRYSSQKQDLDGNL 81
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlingrpLDKRSFRkiIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 82 SVFEAVlssetstlqiikhyeqavqqytveqtdrnfqammaaqeamdrheawDYNAEIKtilsklgihdttkqvnSLSGG 161
Cdd:cd03213 98 TVRETL----------------------------------------------MFAAKLR----------------GLSGG 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 162 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP---YTVLFVTHD-RYFLNEVSTRIVELDRGKL 232
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdtgRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
320-531 |
2.31e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.24 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG---------------ED---------------- 368
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyevtsgsilldgEDilelspderaragifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 369 --QQ---FEGtlkigqtVKVAYFKQTEETLNRD--IRMIDYLREESEVAKEkdgttVSITQ-LLERFLFpssthgkkiYK 440
Cdd:COG0396 82 afQYpveIPG-------VSVSNFLRTALNARRGeeLSAREFLKLLKEKMKE-----LGLDEdFLDRYVN---------EG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 441 LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLNKVAQEywFIH---DGm 514
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRILDYIKPD--FVHvlvDG- 217
|
250 260
....*....|....*....|....*..
gi 488422749 515 meRIV--GSFE--------DYETYKKE 531
Cdd:COG0396 218 --RIVksGGKElaleleeeGYDWLKEE 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
2.42e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGI-----------------DDDFTGDITHP 63
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypearvsgevyldgQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 64 NQyRIRYSSQKQDLDGNLSVFEAVlssetstlqiikhyEQAVQQYTVEQTDRNFQAMMaaQEAMDRHEAWDynaEIKTIL 143
Cdd:PRK14247 81 RR-RVQMVFQIPNPIPNLSIFENV--------------ALGLKLNRLVKSKKELQERV--RWALEKAQLWD---EVKDRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 144 SKlgihdttkQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQyPYTVLFVTHDRYFLNEV 220
Cdd:PRK14247 141 DA--------PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELKK-DMTIVLVTHFPQQAARI 211
|
250
....*....|..
gi 488422749 221 STRIVELDRGKL 232
Cdd:PRK14247 212 SDYVAFLYKGQI 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
334-495 |
2.53e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.59 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 334 FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQTEETLNRDIR---- 398
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLvqydhhylhrQVALVGQEPVLFSGSVRenia 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 --MIDYLREESEVAKEKDGTTVSITQllerflFPSSTH---GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDT 473
Cdd:TIGR00958 577 ygLTDTPDEEIMAAAKAANAHDFIME------FPNGYDtevGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180
....*....|....*....|..
gi 488422749 474 ETLTILEDYIASFGGSVITVSH 495
Cdd:TIGR00958 651 ECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-189 |
2.75e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.27 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 15 DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQ--------YRIRYSSQKQDLDGNLSVFEa 86
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvaEACHYLGHRNAMKPALTVAE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 87 vlssetsTLQiikhyeqavqqytveqtdrnFQAMMAAQEAMDRHEAwdynaeiktiLSKLGIHD-TTKQVNSLSGGQQKR 165
Cdd:PRK13539 93 -------NLE--------------------FWAAFLGGEELDIAAA----------LEAVGLAPlAHLPFGYLSAGQKRR 135
|
170 180
....*....|....*....|....
gi 488422749 166 VVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALD 159
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-240 |
3.09e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.79 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 17 VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIthpnQYRIRYSSQKQDLDGNLSvfeAVLSSETSTLQ 96
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI----QVGDIYIGDKKNNHELIT---NPYSKKIKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 97 IIKHYEQAVQQY--------TVEQtDRNFQAMMAAQEAMDRHEawdynaEIKTILSKLGIHDTTKQVN--SLSGGQQKRV 166
Cdd:PRK13631 113 ELRRRVSMVFQFpeyqlfkdTIEK-DIMFGPVALGVKKSEAKK------LAKFYLNKMGLDDSYLERSpfGLSGGQKRRV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 167 VLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYPGNYE 240
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGeheMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
334-495 |
3.14e-10 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 60.63 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 334 FQDITQIIQSGQRIGIVGPNGAGKTTMLNILsgedQQF----EGTLKI-GQTVK----------VAYFKQT----EETLN 394
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLL----ERFydptSGEILLdGVDIRdlnlrwlrsqIGLVSQEpvlfDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMIDYLREESEV--AKEKDGTTVSITQLLERFlfpsSTH-GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:cd03249 95 ENIRYGKPDATDEEVeeAAKKANIHDFIMSLPDGY----DTLvGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180
....*....|....*....|....*.
gi 488422749 472 DTETLTILEDYI--ASFGGSVITVSH 495
Cdd:cd03249 171 DAESEKLVQEALdrAMKGRTTIVIAH 196
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
333-519 |
3.20e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 333 LFqDITQIIQSGQRIGIVGPNGAGKTTMLNIL-------SGE----DQQFEGTLKIG--------QTVKVAyFKQ----- 388
Cdd:PRK11124 18 LF-DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTlniaGNHFDFSKTPSdkairelrRNVGMV-FQQynlwp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 ----TEETLNRDIRMIDYLREESEVAKEKDGTTVSITQLLERFlfPssthgkkiYKLSGGEQKRLYLLRLLVHQPNVLLL 464
Cdd:PRK11124 96 hltvQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRF--P--------LHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 465 DEPTNDLDTETLTILEDYIASFGGSVIT---VSHDRYFLNKVAQEYWFIHDGmmeRIV 519
Cdd:PRK11124 166 DEPTAALDPEITAQIVSIIRELAETGITqviVTHEVEVARKTASRVVYMENG---HIV 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
320-497 |
3.33e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.04 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVkvayfkqTEETL-NRDI 397
Cdd:PRK11432 8 VLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDV-------THRSIqQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RM----------------IDYLREESEVAKEKDGTTVSITQLL-------ERFlfpssthgkkIYKLSGGEQKRLYLLRL 454
Cdd:PRK11432 81 CMvfqsyalfphmslgenVGYGLKMLGVPKEERKQRVKEALELvdlagfeDRY----------VDQISGGQQQRVALARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488422749 455 LVHQPNVLLLDEPTNDLDTETLTILEDYI----ASFGGSVITVSHDR 497
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIrelqQQFNITSLYVTHDQ 197
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
316-481 |
3.80e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 316 KQVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG---EDQQFEGTLK-IGQTVkvayfkQTEE 391
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIElLGRTV------QREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 TLNRDIR--------------MIDYLREESEVAKEKDGTT---------------VSITQLLERFLFPSSTHgKKIYKLS 442
Cdd:PRK09984 76 RLARDIRksrantgyifqqfnLVNRLSVLENVLIGALGSTpfwrtcfswftreqkQRALQALTRVGMVHFAH-QRVSTLS 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 488422749 443 GGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILED 481
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMD 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-472 |
4.35e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQKQDLDGNLSVFE 85
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 AVLSsetstlqiikhyeqAVQQYTVEQT----DRNFQAMMAAQEAMDRheawdynaEIKTILSKLGIH-DTTKQVNSLSG 160
Cdd:PRK10982 80 QELN--------------LVLQRSVMDNmwlgRYPTKGMFVDQDKMYR--------DTKAIFDELDIDiDPRAKVATLSV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKlttypg 237
Cdd:PRK10982 138 SQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLftiIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 238 nyedYIAMRAEKEvieqkqndkqraLYKQELAWMRAGakaRSTKQqarihRFNDleanvkqqQTQDKGELNLaysrlgkq 317
Cdd:PRK10982 212 ----WIATQPLAG------------LTMDKIIAMMVG---RSLTQ-----RFPD--------KENKPGEVIL-------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 vyELDSLTkTINGRTLfQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKV---------AYFK 387
Cdd:PRK10982 252 --EVRNLT-SLRQPSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKINNhnaneainhGFAL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QTEE------------TLNRDIRMIDYLREESEVAKEKDgtTVSITQ-LLERFLFPSSTHGKKIYKLSGGEQKRLYLLRL 454
Cdd:PRK10982 328 VTEErrstgiyayldiGFNSLISNIRNYKNKVGLLDNSR--MKSDTQwVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRW 405
|
490
....*....|....*...
gi 488422749 455 LVHQPNVLLLDEPTNDLD 472
Cdd:PRK10982 406 LLTQPEILMLDEPTRGID 423
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
320-519 |
4.83e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.41 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNIL-------SGE----DQQFEGTLKIGQTVKVAY--- 385
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQlniaGHQFDFSQKPSEKAIRLLrqk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 386 ----FKQ---------TEETLNRDIRMIDYLREESEVAKEKDGTTVSITQLLERFlfPssthgkkiYKLSGGEQKRLYLL 452
Cdd:COG4161 84 vgmvFQQynlwphltvMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF--P--------LHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 453 RLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGGSVIT---VSHDRYFLNKVAQEYWFIHDGmmeRIV 519
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITqviVTHEVEFARKVASQVVYMEKG---RII 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-246 |
4.93e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDD-----DFTGDITHpNQYRIrYSSQKQDLDG 79
Cdd:PRK14239 7 QVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVY-NGHNI-YSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 N--------------LSVFEAVLSSetstLQIIKHYEQAVQQYTVEqtdrnfqammaaqEAMDRHEAWDynaEIKTILsk 145
Cdd:PRK14239 85 RkeigmvfqqpnpfpMSIYENVVYG----LRLKGIKDKQVLDEAVE-------------KSLKGASIWD---EVKDRL-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 146 lgiHDTTKqvnSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESI----NWLINYVKQypYTVLFVTHDRYFLNEVS 221
Cdd:PRK14239 143 ---HDSAL---GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAgkieETLLGLKDD--YTMLLVTRSMQQASRIS 214
|
250 260 270
....*....|....*....|....*....|....*.
gi 488422749 222 TRIVELDRGKLTTY---------PGNYE--DYIAMR 246
Cdd:PRK14239 215 DRTGFFLDGDLIEYndtkqmfmnPKHKEteDYISGK 250
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-232 |
5.28e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 12 SYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGidddF---TGDIT---------HPNQYRIRYSSQKQdldg 79
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG----FlpyQGSLKingielrelDPESWRKHLSWVGQ---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 NLSVFEAVLSsETSTLqiikhyeqAVQQYTVEQTDrnfQAMMAAQeamdrheawdynaeIKTILSKL--GIHDTTKQVNS 157
Cdd:PRK11174 431 NPQLPHGTLR-DNVLL--------GNPDASDEQLQ---QALENAW--------------VSEFLPLLpqGLDTPIGDQAA 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 158 -LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYPY--TVLFVTHDRYFLNEVSTrIVELDRGKL 232
Cdd:PRK11174 485 gLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRrqTTLMVTHQLEDLAQWDQ-IWVMQDGQI 561
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
327-495 |
5.40e-10 |
|
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: 62.46 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 327 TINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQTEETLNRDIR-MIDYlRE 405
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRdQIIY-PD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 406 ESEVAKEKDGT---------TVSITQLLERFLFPSSTHGKKiYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTEtl 476
Cdd:TIGR00954 540 SSEDMKRRGLSdkdleqildNVQLTHILEREGGWSAVQDWM-DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD-- 616
|
170 180
....*....|....*....|...
gi 488422749 477 tiLEDYIAS----FGGSVITVSH 495
Cdd:TIGR00954 617 --VEGYMYRlcreFGITLFSVSH 637
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
341-468 |
6.46e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.89 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYfkQTEETLNRDIRMID-----YLREESEVAKEKDG 415
Cdd:PRK11614 28 INQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW--QTAKIMREAVAIVPegrrvFSRMTVEENLAMGG 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 416 TTVSITQLLERF-----LFPsSTHGKKIYK---LSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:PRK11614 106 FFAERDQFQERIkwvyeLFP-RLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-248 |
7.13e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 2 EAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdithpnqyrIRYSSQKQDLDGNL 81
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRL---------------IEIYDSKIKVDGKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 82 SVFEAVLSsETSTLQIIKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRHEAWDYNAEIKTILSKLG----IHDTTKQ-VN 156
Cdd:PRK14246 74 LYFGKDIF-QIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGlwkeVYDRLNSpAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESINWLINYVKQyPYTVLFVTHDRYFLNEVSTRIVELDRGKLT 233
Cdd:PRK14246 153 QLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
250
....*....|....*
gi 488422749 234 TYPGNYEDYIAMRAE 248
Cdd:PRK14246 232 EWGSSNEIFTSPKNE 246
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
329-495 |
7.67e-10 |
|
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: 59.81 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIG----QTVKVAYFK-------QTEETLNRDI 397
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlALADPAWLRrqvgvvlQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RMIDYL------REESEVAKEKDGTTVSITQLLERFlfpSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDL 471
Cdd:cd03252 93 RDNIALadpgmsMERVIEAAKLAGAHDFISELPEGY---DTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180
....*....|....*....|....*.
gi 488422749 472 DTETLTILEDYIASF--GGSVITVSH 495
Cdd:cd03252 170 DYESEHAIMRNMHDIcaGRTVIIIAH 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-256 |
8.11e-10 |
|
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: 59.42 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 17 VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRyssqkqdLDGNLSvfeAVLSSETSTLQ 96
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--------YVPENGRVL-------VDGHDL---ALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 97 IikhyeQAVQQYTVEQTDRNFQAMMAAQEAMDRHE---------AWDYNAEIK----TILSKLGIhdttkqvnSLSGGQQ 163
Cdd:cd03252 78 V-----GVVLQENVLFNRSIRDNIALADPGMSMERvieaaklagAHDFISELPegydTIVGEQGA--------GLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY--PYTVLFVTHdRYFLNEVSTRIVELDRGKLTTyPGNYED 241
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVE-QGSHDE 222
|
250
....*....|....*
gi 488422749 242 YIAMRAEKEVIEQKQ 256
Cdd:cd03252 223 LLAENGLYAYLYQLQ 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-232 |
8.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.13 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 15 DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGNLSVFEAVLSSETST 94
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII---------------IDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 95 LQIIKHYEQAVQQYTVEQtDRNF---QAMMAAQEAMDR-HEAwdynaeiktiLSKLGIHD-TTKQVNSLSGGQQKRVVLA 169
Cdd:PRK13650 84 GMVFQNPDNQFVGATVED-DVAFgleNKGIPHEEMKERvNEA----------LELVGMQDfKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 170 KTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHDryfLNEV--STRIVELDRGKL 232
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKgirdDYQMTVISITHD---LDEValSDRVLVMKNGQV 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-496 |
9.71e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 33 GLVGINGTGKSTLLKVMGGIDDDFTGdithpnqyRIRYSSQKQDLDGNLSVFEAVLSsetstlqIIkHYE-QAVQQYTVE 111
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAG--------SILYLGKEVTFNGPKSSQEAGIG-------II-HQElNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 112 QT---DRNFQAMMAAQEamdrheaWD-YNAEIKTILSKLGI-HDTTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTN 186
Cdd:PRK10762 98 ENiflGREFVNRFGRID-------WKkMYAEADKLLARLNLrFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 187 HL---DFESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKlttypgnyedYIAMRAEKEVIEQKqndkqral 263
Cdd:PRK10762 171 ALtdtETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ----------FIAEREVADLTEDS-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 264 ykqeLAWMRAGAKARstKQQARIHrfndleanvkqqqtQDKGELNLAYSRL-GKQVyeldsltktingrtlfQDITQIIQ 342
Cdd:PRK10762 233 ----LIEMMVGRKLE--DQYPRLD--------------KAPGEVRLKVDNLsGPGV----------------NDVSFTLR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 343 SGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVayfKQTEETLNRDIRMIdylreeSEVAKeKDG------ 415
Cdd:PRK10762 277 KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVT---RSPQDGLANGIVYI------SEDRK-RDGlvlgms 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 416 --TTVSITQL------------------LERF--LF----PSstHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTN 469
Cdd:PRK10762 347 vkENMSLTALryfsraggslkhadeqqaVSDFirLFniktPS--MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
490 500 510
....*....|....*....|....*....|
gi 488422749 470 DLDTETLTILEDYIASF---GGSVITVSHD 496
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFkaeGLSIILVSSE 454
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-232 |
1.03e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.76 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyriRYSSQ-KQDLDGNLS-VFEavlSSETSTLQI 97
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDnFEKLRKHIGiVFQ---NPDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 98 IKHYEQAVqqytveqtdrNFQAMMAAQEAMDRheawdynaEIKTILSKLGIHD-TTKQVNSLSGGQQKRVVLAKTLIEQP 176
Cdd:PRK13648 100 IVKYDVAF----------GLENHAVPYDEMHR--------RVSEALKQVDMLErADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488422749 177 DLLLLDEPTNHLD---FESINWLINYVKQ-YPYTVLFVTHDryfLNEV--STRIVELDRGKL 232
Cdd:PRK13648 162 SVIILDEATSMLDpdaRQNLLDLVRKVKSeHNITIISITHD---LSEAmeADHVIVMNKGTV 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
333-507 |
1.09e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 333 LFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK---VAYFKQTEETLNRD-IRMIDYLREES 407
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlCTYQKQLCFVGHRSgINPYLTLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 408 EVAKEKDGTTVSITQL-----LERFL-FPSSThgkkiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILED 481
Cdd:PRK13540 96 LYDIHFSPGAVGITELcrlfsLEHLIdYPCGL-------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170 180 190
....*....|....*....|....*....|
gi 488422749 482 YIASF---GGSVITVSHDRYFLNKV-AQEY 507
Cdd:PRK13540 169 KIQEHrakGGAVLLTSHQDLPLNKAdYEEY 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
7-232 |
1.22e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 7 EHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGiddDFTGDIThPNQYRIRyssQKQDLDGN------ 80
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGA-PRGARVT---GDVTLNGEplaaid 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 ---LSVFEAVLSSET------STLQII--KHYEQAVQQYTVEQTDRNFqammaAQEAMDRHEAwdynaeiktilSKLGIH 149
Cdd:PRK13547 78 aprLARLRAVLPQAAqpafafSAREIVllGRYPHARRAGALTHRDGEI-----AWQALALAGA-----------TALVGR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 150 DTTkqvnSLSGGQQKRVVLAKTL---------IEQPDLLLLDEPTNHLDFESINWLINYV----KQYPYTVLFVTHDRYF 216
Cdd:PRK13547 142 DVT----TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNL 217
|
250
....*....|....*.
gi 488422749 217 LNEVSTRIVELDRGKL 232
Cdd:PRK13547 218 AARHADRIAMLADGAI 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-233 |
1.24e-09 |
|
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: 60.50 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 21 DLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRyssqkqdLDGnlsvfeAVLSSETSTLQIIKH 100
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGL--------ERPDSGRIR-------LGG------EVLQDSARGIFLPPH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 101 -----YeqaVQQ-------YTVEQtdrNFQAMMAAQEAMDRHEAWDYnaeiktILSKLGI-HDTTKQVNSLSGGQQKRVV 167
Cdd:COG4148 76 rrrigY---VFQearlfphLSVRG---NLLYGRKRAPRAERRISFDE------VVELLGIgHLLDRRPATLSGGERQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 168 LAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY------PytVLFVTHDryfLNEV---STRIVELDRGKLT 233
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLrdeldiP--ILYVSHS---LDEVarlADHVVLLEQGRVV 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
331-498 |
1.31e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 59.26 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTvkvAYFKQTEETLNRDI------------- 397
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK---PISMLSSRQLARRLallpqhhltpegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 ---RMIDYLR---------------EESEVAKEKDGttvsITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQP 459
Cdd:PRK11231 92 tvrELVAYGRspwlslwgrlsaednARVNQAMEQTR----INHLADR----------RLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488422749 460 NVLLLDEPTNDLD----TETLTILEDyIASFGGSVITVSHD-----RY 498
Cdd:PRK11231 158 PVVLLDEPTTYLDinhqVELMRLMRE-LNTQGKTVVTVLHDlnqasRY 204
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
320-472 |
1.51e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTL-FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVkVayfkQTEETLNRDIR 398
Cdd:PRK11650 5 KLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV-V----NELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MI--DY---------------LR----EESEVAK--EKDGTTVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLL 455
Cdd:PRK11650 80 MVfqNYalyphmsvrenmaygLKirgmPKAEIEErvAEAARILELEPLLDR----------KPRELSGGQRQRVAMGRAI 149
|
170
....*....|....*..
gi 488422749 456 VHQPNVLLLDEPTNDLD 472
Cdd:PRK11650 150 VREPAVFLFDEPLSNLD 166
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-53 |
1.52e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.94 E-value: 1.52e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488422749 11 KSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGID 53
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIL 76
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
325-495 |
1.66e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 325 TKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQ--QFEGTLKIG------QTVKVAYFKQTEE----- 391
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANnrkptkQILKRTGFVTQDDilyph 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 -TLNRDIRMIDYLREESEVAK-EKDGTTVSITQLLERFLFPSSTHGKK-IYKLSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:PLN03211 155 lTVRETLVFCSLLRLPKSLTKqEKILVAESVISELGLTKCENTIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|
gi 488422749 469 NDLDTETLTILEDYIASF---GGSVITVSH 495
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLaqkGKTIVTSMH 264
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
334-377 |
1.67e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 58.31 E-value: 1.67e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488422749 334 FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI 377
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV 81
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
332-519 |
2.21e-09 |
|
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: 58.66 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 332 TLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQtEETLNRDIRMI---------- 400
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQDLYQLDRKQ-RRAFRRDVQLVfqdspsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 401 ------------DYLREESEVAKEKdgttvSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:TIGR02769 104 rmtvrqiigeplRHLTSLDESEQKA-----RIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 469 NDLD----TETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIV 519
Cdd:TIGR02769 179 SNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG---QIV 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
2.27e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.59 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 3 AYKIEHLNKSYADKV-IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITHPNQYRIRysSQK 74
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrvkvmgrEVNAENEKWVR--SKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 75 ----QDLDGNL---SVFEAVLSSETStlqiikhyeqavQQYTVEQTDRNfqammaAQEAMDRHEAWDYNaeiktilsklg 147
Cdd:PRK13647 82 glvfQDPDDQVfssTVWDDVAFGPVN------------MGLDKDEVERR------VEEALKAVRMWDFR----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 148 ihdtTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRI 224
Cdd:PRK13647 133 ----DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQV 208
|
250
....*....|....
gi 488422749 225 VELDRGKLTTYPGN 238
Cdd:PRK13647 209 IVLKEGRVLAEGDK 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
320-496 |
2.28e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.56 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQ 388
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLDVattpsrelakRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 tEETLN-----RDI----------------------RMIDYLreesevakekdgttvSITQLLERFLfpssthgkkiYKL 441
Cdd:COG4604 83 -ENHINsrltvRELvafgrfpyskgrltaedreiidEAIAYL---------------DLEDLADRYL----------DEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 442 SGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-244 |
2.34e-09 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 60.05 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 16 KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdithpnqyrIRYSSQKQDLDGnlsvfeAVLSS-ETST 94
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGI---------------WPPTSGSVRLDG------ADLKQwDRET 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 95 L-QIIKHYEQAVQQY--TVEQT----DRNF--QAMMAAQEAMDRHEawdynaeikTILSKLGIHDTTKQVN--SLSGGQQ 163
Cdd:TIGR01842 390 FgKHIGYLPQDVELFpgTVAENiarfGENAdpEKIIEAAKLAGVHE---------LILRLPDGYDTVIGPGgaTLSGGQR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 164 KRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLIN---YVKQYPYTVLFVTHdRYFLNEVSTRIVELDRGKLTTYpGNYE 240
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDEEGEQALANaikALKARGITVVVITH-RPSLLGCVDKILVLQDGRIARF-GERD 538
|
....
gi 488422749 241 DYIA 244
Cdd:TIGR01842 539 EVLA 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
340-496 |
3.29e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.80 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 340 IIQSGQRIGIVGPNGAGKTTMLNILSGE--------------D---QQFEGT--------LKIGQtVKVAY--------- 385
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswDevlKRFRGTelqdyfkkLANGE-IKVAHkpqyvdlip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 386 --FKQT-EETLNR-DIR-MIDYLREEsevakekdgttVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQPN 460
Cdd:COG1245 174 kvFKGTvRELLEKvDERgKLDELAEK-----------LGLENILDR----------DISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488422749 461 VLLLDEPTNDLD-TETLT----ILEdyIASFGGSVITVSHD 496
Cdd:COG1245 233 FYFFDEPSSYLDiYQRLNvarlIRE--LAEEGKYVLVVEHD 271
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-185 |
3.59e-09 |
|
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: 57.68 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLK-VMGgidddftgdITHPNQYRIRYssQKQDLDGnLSV 83
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG---------LLPPRSGSIRF--DGEDITG-LPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEAV-----LSSET----STLqiikhyeqavqqyTVEQtdrNFqaMMAAQEAMDRHE-AWDYnAEI-------KTILSKL 146
Cdd:COG0410 73 HRIArlgigYVPEGrrifPSL-------------TVEE---NL--LLGAYARRDRAEvRADL-ERVyelfprlKERRRQR 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 488422749 147 GihdttkqvNSLSGGQQKRVVLAKTLIEQPDLLLLDEPT 185
Cdd:COG0410 134 A--------GTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
333-496 |
4.88e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 333 LFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQTEETLNRDIRMI--------DYL 403
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMSKLSSAAKAELRNQKLGFIyqfhhllpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 404 REESeVA--------KEKDGTTVSITQLLERFLFPSSTHgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:PRK11629 104 ALEN-VAmplligkkKPAEINSRALEMLAAVGLEHRANH--RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180
....*....|....*....|....*
gi 488422749 476 ----LTILEDYIASFGGSVITVSHD 496
Cdd:PRK11629 181 adsiFQLLGELNRLQGTAFLVVTHD 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
331-475 |
4.98e-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: 57.10 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQTEETLNRDIR- 398
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhsKVSLVGQEPVLFARSLQd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 -----MIDYLREESEVAKEKDGTTVSITQLLERflfPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDT 473
Cdd:cd03248 107 niaygLQSCSFECVKEAAQKAHAHSFISELASG---YDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
..
gi 488422749 474 ET 475
Cdd:cd03248 184 ES 185
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-530 |
5.24e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.35 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSgEDQQFEGTLKIGQtvKVAYFKQT----EETLNR 395
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEG--RVEFFNQNiyerRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 396 DIRMIDYLREESEV--------------------AKEKDGTTVSITQLLErfLFPSSTHgkKIYK----LSGGEQKRLYL 451
Cdd:PRK14258 86 LRRQVSMVHPKPNLfpmsvydnvaygvkivgwrpKLEIDDIVESALKDAD--LWDEIKH--KIHKsaldLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 452 LRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFG----GSVITVSHDRYFLNKVAQEYWFIHDGmmERIVGSFEDYET 527
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLSDFTAFFKGN--ENRIGQLVEFGL 239
|
...
gi 488422749 528 YKK 530
Cdd:PRK14258 240 TKK 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
326-475 |
5.99e-09 |
|
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: 56.50 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 326 KTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGedqQFEGTLKIGQTVKvaY----FKQTEETLNRDIRMID 401
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIH--YngipYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 402 ylREESEVAkekdgtTVSITQLLErflFPSSTHGKKIYK-LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:cd03233 90 --EEDVHFP------TLTVRETLD---FALRCKGNEFVRgISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-196 |
6.37e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 15 DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIthpnqyriRYSSQK---------QDL-------- 77
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV--------LWQGEPirrqrdeyhQDLlylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 78 -DGNLSVFEavlssetstlqiikhyeqavqqytveqtdrNFQAMMAAQEAMDRHEAWDynaeiktILSKLGIH---DTTk 153
Cdd:PRK13538 85 iKTELTALE------------------------------NLRFYQRLHGPGDDEALWE-------ALAQVGLAgfeDVP- 126
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488422749 154 qVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL 196
Cdd:PRK13538 127 -VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
320-519 |
6.58e-09 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 56.93 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG-EDQQfEGTLKIGqtvkvayfkqtEETLNRDIR 398
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPD-SGTITVD-----------GEDLTDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIDYLREES-----------------------------------EVAKEkdgttvsitqLLERF-------LFPSSthgk 436
Cdd:COG1126 71 DINKLRRKVgmvfqqfnlfphltvlenvtlapikvkkmskaeaeERAME----------LLERVgladkadAYPAQ---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 437 kiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET----LTILEDyIASFGGSVITVSHDRYFLNKVAQEYWFIHD 512
Cdd:COG1126 137 ----LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELvgevLDVMRD-LAKEGMTMVVVTHEMGFAREVADRVVFMDG 211
|
....*..
gi 488422749 513 GmmeRIV 519
Cdd:COG1126 212 G---RIV 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
335-496 |
6.58e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 56.71 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV------KVAYFK----------QTEETLNRDI 397
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQItepgpdRMVVFQnysllpwltvRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RMIDYLREESEVAKEKDGTTVSITQLLErflfpssthgKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLT 477
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGLTEAAD----------KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 488422749 478 ILEDYIASF----GGSVITVSHD 496
Cdd:TIGR01184 152 NLQEELMQIweehRVTVLMVTHD 174
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-254 |
6.62e-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: 56.00 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGidddftgditHPNqYR-----IRYssQKQDLDg 79
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----------HPK-YEvtegeILF--KGEDIT- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 NLSVfeavlssetstlqiikhYEQAVQQYTVeqtdrnfqammaaqeamdrheAWDYNAEIKTIlsKLGihDTTKQVN-SL 158
Cdd:cd03217 68 DLPP-----------------EERARLGIFL---------------------AFQYPPEIPGV--KNA--DFLRYVNeGF 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHDRYFLNEV-STRIVELDRGKltt 234
Cdd:cd03217 106 SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVaevINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGR--- 182
|
250 260
....*....|....*....|
gi 488422749 235 ypgnyedyIAMRAEKEVIEQ 254
Cdd:cd03217 183 --------IVKSGDKELALE 194
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
340-496 |
6.69e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 340 IIQSGQRIGIVGPNGAGKTTMLNILSGEDQ-----------------QFEGT-LKIgqtvkvaYFKQTEETLNRDIRMID 401
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKpnlgkfddppdwdeildEFRGSeLQN-------YFTKLLEGDVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 402 YLRE--------ESEVAKEKDGT--------TVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLD 465
Cdd:cd03236 95 YVDLipkavkgkVGELLKKKDERgkldelvdQLELRHVLDR----------NIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....
gi 488422749 466 EPTNDLDTE---TLTILEDYIASFGGSVITVSHD 496
Cdd:cd03236 165 EPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
309-515 |
6.72e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 309 LAYSRLGKQVYELD-----------SLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI 377
Cdd:PRK14271 1 MACERLGGQSGAADvdaaapamaavNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 378 GQTV----KVAYFKQTEETLNR-----------DIRMIDYLR---EESEVAKEKDGTTVSITQLLERFLFPSSTH--GKK 437
Cdd:PRK14271 81 GDVLlggrSIFNYRDVLEFRRRvgmlfqrpnpfPMSIMDNVLagvRAHKLVPRKEFRGVAQARLTEVGLWDAVKDrlSDS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 438 IYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGG--SVITVSHDRYFLNKVAQEYWFIHDGMM 515
Cdd:PRK14271 161 PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-232 |
7.04e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 57.31 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 3 AYKIEHLNKSY--ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdithpnqyrirYSSQKqdldGN 80
Cdd:PRK13632 7 MIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL-----------------LKPQS----GE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 LSVFEAVLSSETSTlQIIKHYEQAVQ----QY---TVEQtDRNFQAmmaAQEAMDRHEAWDYnaeIKTILSKLGIHD-TT 152
Cdd:PRK13632 66 IKIDGITISKENLK-EIRKKIGIIFQnpdnQFigaTVED-DIAFGL---ENKKVPPKKMKDI---IDDLAKKVGMEDyLD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 153 KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDryfLNEV--STRIVE 226
Cdd:PRK13632 138 KEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD---MDEAilADKVIV 214
|
....*.
gi 488422749 227 LDRGKL 232
Cdd:PRK13632 215 FSEGKL 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
331-475 |
7.69e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGE--DQQFEGTLKIgqtvkvayfkqTEETLNRDIRMIDYLreese 408
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDV-----------PDNQFGREASLIDAI----- 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 409 vakEKDGTTVSITQLLER------FLFpssthgKKIYK-LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:COG2401 107 ---GRKGDFKDAVELLNAvglsdaVLW------LRRFKeLSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
336-573 |
8.17e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 336 DITQIIQSGQRIGIVGPNGAGKTTM---LNIL--------------------SGEDQQFEGTLKIGQTV--KVAYFKQT- 389
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkkTKEKEKVLEKLVIQKTRfkKIKKIKEIr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 ---------------EETLNRDIRM--IDYLREESEvAKEKDGTTVSITQLLERFLFPSSthgkkiYKLSGGEQKRLYLL 452
Cdd:PRK13651 105 rrvgvvfqfaeyqlfEQTIEKDIIFgpVSMGVSKEE-AKKRAAKYIELVGLDESYLQRSP------FELSGGQKRRVALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 453 RLLVHQPNVLLLDEPTNDLDTE-TLTILE--DYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIVgsfEDYETYK 529
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG---KII---KDGDTYD 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 488422749 530 KEKDKQLAIEKQATNTSKTQIKER-KKTGLSYKEKREYESLMSRI 573
Cdd:PRK13651 252 ILSDNKFLIENNMEPPKLLNFVNKlEKKGIDVPKVTSIEELASEI 296
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-225 |
8.54e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKS-TLLKVMGGIDddFTGdithpnqyriRYSSQKQDLDGNlsvfEAVLSSETSTLQII 98
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLID--YPG----------RVMAEKLEFNGQ----DLQRISEKERRNLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 99 KHYEQAVQQ---------YTVeqtdrNFQAMmaaqEAMDRHE----AWDYNAEIKtILSKLGIHDTTKQVN----SLSGG 161
Cdd:PRK11022 88 GAEVAMIFQdpmtslnpcYTV-----GFQIM----EAIKVHQggnkKTRRQRAID-LLNQVGIPDPASRLDvyphQLSGG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 162 QQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIV 225
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-232 |
9.44e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.92 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKV-IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIryssqkqdldgnlsV 83
Cdd:PRK13644 3 RLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--------LRPQKGKV--------------L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEAVLSSETSTLQIIKH-----YEQAVQQY---TVEQtDRNFQAMMAAQEAMDRHEAWDYN-AEIKtiLSKLGiHDTTKq 154
Cdd:PRK13644 61 VSGIDTGDFSKLQGIRKlvgivFQNPETQFvgrTVEE-DLAFGPENLCLPPIEIRKRVDRAlAEIG--LEKYR-HRSPK- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 155 vnSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY---PYTVLFVTHDRYFLnEVSTRIVELDRGK 231
Cdd:PRK13644 136 --TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhekGKTIVYITHNLEEL-HDADRIIVMDRGK 212
|
.
gi 488422749 232 L 232
Cdd:PRK13644 213 I 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-213 |
9.70e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 34 LVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyrIRYSSQKQDLDGNLsvfeavlssetstlqiIKHYEQAvqqytvEQT 113
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKIS------ILGQPTRQALQKNL----------------VAYVPQS------EEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 114 DRNFQAMMAAQEAMDR--HEAWDYNAE------IKTILSKLGIHDTT-KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEP 184
Cdd:PRK15056 90 DWSFPVLVEDVVMMGRygHMGWLRRAKkrdrqiVTAALARVDMVEFRhRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190
....*....|....*....|....*....|..
gi 488422749 185 TNHLDFES---INWLINYVKQYPYTVLFVTHD 213
Cdd:PRK15056 170 FTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-227 |
9.99e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.43 E-value: 9.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDD------DFTG-DITHPNQYRIR-------------YSSqkqdLDG 79
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEptsgeiLFDGqDITGLSGRELRplrrrmqmvfqdpYAS----LNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 NLSVFEAVlsSETSTLQIIKhyeqavqqyTVEQTDRNFQAMMAA----QEAMDR--HEawdynaeiktilsklgihdttk 153
Cdd:COG4608 111 RMTVGDII--AEPLRIHGLA---------SKAERRERVAELLELvglrPEHADRypHE---------------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 154 qvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFeSI-----NWLINYVKQYPYTVLFVTHD----RYFLNEVST-- 222
Cdd:COG4608 158 ----FSGGQRQRIGIARALALNPKLIVCDEPVSALDV-SIqaqvlNLLEDLQDELGLTYLFISHDlsvvRHISDRVAVmy 232
|
....*..
gi 488422749 223 --RIVEL 227
Cdd:COG4608 233 lgKIVEI 239
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
320-496 |
1.08e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 56.63 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK-------VAYfkQTEE 391
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEgpgaergVVF--QNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 TLN-RDI--------RMIDYLREESEVAKEKDGTTVSITQLLERFlfpssthgkkIYKLSGGEQKRLYLLRLLVHQPNVL 462
Cdd:PRK11248 81 LLPwRNVqdnvafglQLAGVEKMQRLEIAHQMLKKVGLEGAEKRY----------IWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 488422749 463 LLDEPTNDLDTET----LTILEDYIASFGGSVITVSHD 496
Cdd:PRK11248 151 LLDEPFGALDAFTreqmQTLLLKLWQETGKQVLLITHD 188
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
328-515 |
1.08e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 328 INGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTvKVAYFKQTE-ETLNRDIRMI------ 400
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH-DITRLKNREvPFLRRQIGMIfqdhhl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 401 ---------------------DYLREESEVAKEKDGttvsitqLLERFL-FPssthgkkiYKLSGGEQKRLYLLRLLVHQ 458
Cdd:PRK10908 91 lmdrtvydnvaipliiagasgDDIRRRVSAALDKVG-------LLDKAKnFP--------IQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 459 PNVLLLDEPTNDLD---TETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMM 515
Cdd:PRK10908 156 PAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
133-213 |
1.09e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 133 WDynaEIKTILSKLGIhdttkqvnSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQyPYTVLF 209
Cdd:PRK14243 138 WD---EVKDKLKQSGL--------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIStlrIEELMHELKE-QYTIII 205
|
....
gi 488422749 210 VTHD 213
Cdd:PRK14243 206 VTHN 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-233 |
1.12e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.87 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 7 EHLNKSY-ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGnlsvfe 85
Cdd:COG1132 343 ENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL---------------IDG------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 avlssetstlqiikhyeQAVQQYTVEQTDRNFqAMmAAQE------------AMDRHEAWDynAEIKTILSKLGIH---- 149
Cdd:COG1132 402 -----------------VDIRDLTLESLRRQI-GV-VPQDtflfsgtireniRYGRPDATD--EEVEEAAKAAQAHefie 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 150 ------DTtkQV----NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----INWLINYVKQypYTVLFVTHdRy 215
Cdd:COG1132 461 alpdgyDT--VVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLMKG--RTTIVIAH-R- 534
|
250 260
....*....|....*....|...
gi 488422749 216 flneVST-----RIVELDRGKLT 233
Cdd:COG1132 535 ----LSTirnadRILVLDDGRIV 553
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
331-475 |
1.16e-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: 55.33 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG--EDQQFEGTLKIGQtvkvayfKQTEETLNRDI---RMIDYLRE 405
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING-------RPLDKNFQRSTgyvEQQDVHSP 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 406 ESEVakekdgttvsitqlLERFLFPSSTHGkkiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:cd03232 93 NLTV--------------REALRFSALLRG-----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-226 |
1.36e-08 |
|
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: 57.77 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTL-LKVMGGIdddftgdithPNQYRIRYssQKQDLDGnLS-------------VFE 85
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI----------PSEGEIRF--DGQDLDG-LSrralrplrrrmqvVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 ---AVLSSETSTLQIIK-----HYEQAvqqyTVEQTDRNFQAMMAA----QEAMDR--HEawdynaeiktilsklgihdt 151
Cdd:COG4172 370 dpfGSLSPRMTVGQIIAeglrvHGPGL----SAAERRARVAEALEEvgldPAARHRypHE-------------------- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 152 tkqvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHD----RYFLNEV--- 220
Cdd:COG4172 426 ------FSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILDLLRDLQREHGLAYLFISHDlavvRALAHRVmvm 499
|
....*..
gi 488422749 221 -STRIVE 226
Cdd:COG4172 500 kDGKVVE 506
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
324-521 |
1.48e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 55.73 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 324 LTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQ--------QFEG--TLKI---------------- 377
Cdd:TIGR01978 6 LHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyevtsgtiLFKGqdLLELepderaraglflafqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 378 -----GQTVK----VAYFKQTEETLNRDIRMIDYLREESEVAK--EKDGttvsitQLLERFLFpssthgkkiYKLSGGEQ 446
Cdd:TIGR01978 86 peeipGVSNLeflrSALNARRSARGEEPLDLLDFEKLLKEKLAllDMDE------EFLNRSVN---------EGFSGGEK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 447 KRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLNKVAQEYWFI-HDGmmeRIVGS 521
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDYVHVlLDG---RIVKS 226
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-498 |
1.51e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAyfkqtEETlnrdiRMIDYLREESevAKEKDGTTvs 419
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRG-----DRS-----RFMAYLGHLP--GLKADLST-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 420 itqlLERFLFPSSTHGKK---------------------IYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTI 478
Cdd:PRK13543 100 ----LENLHFLCGLHGRRakqmpgsalaivglagyedtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180
....*....|....*....|...
gi 488422749 479 LEDYIASF---GGSVITVSHDRY 498
Cdd:PRK13543 176 VNRMISAHlrgGGAALVTTHGAY 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
341-515 |
1.53e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEdQQFEGTLKIGQTVKVAYfkqteeTLNRDIRMIDYLREESEVAkekdgTTVSI 420
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAW------SAAELARHRAYLSQQQTPP-----FAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 421 TQLLERFLfPSSTH---------------------GKKIYKLSGGEQKRLYL--LRLLVH---QPN--VLLLDEPTNDLD 472
Cdd:PRK03695 87 FQYLTLHQ-PDKTRteavasalnevaealglddklGRSVNQLSGGEWQRVRLaaVVLQVWpdiNPAgqLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488422749 473 TETLTILEDYIASF---GGSVITVSHDryfLNKV---AQEYWFIHDGMM 515
Cdd:PRK03695 166 VAQQAALDRLLSELcqqGIAVVMSSHD---LNHTlrhADRVWLLKQGKL 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
143-232 |
1.59e-08 |
|
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: 56.11 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 143 LSKLGIHD-TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDryfL 217
Cdd:cd03294 145 LELVGLEGwEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD---L 221
|
90
....*....|....*...
gi 488422749 218 NE---VSTRIVELDRGKL 232
Cdd:cd03294 222 DEalrLGDRIAIMKDGRL 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
309-519 |
1.72e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.85 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 309 LAYSRLGKQvYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQ 388
Cdd:PRK10419 4 LNVSGLSHH-YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 389 TEETLNRDIRMI---------------DYLREE-------SEVAKEkdgttVSITQLLERFLFPSSTHGKKIYKLSGGEQ 446
Cdd:PRK10419 83 QRKAFRRDIQMVfqdsisavnprktvrEIIREPlrhllslDKAERL-----ARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 447 KRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIV 519
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG---QIV 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
322-496 |
1.79e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.76 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 322 DSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILS-------------GED-QQF---EGTLKIG---QTV 381
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahghvwldGEHiQHYaskEVARRIGllaQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 382 KVAYFKQTEETLNRDIR----MIDYLREESEVAKEKDGTTVSITQLLerflfpssthGKKIYKLSGGEQKRLYLLRLLVH 457
Cdd:PRK10253 91 TTPGDITVQELVARGRYphqpLFTRWRKEDEEAVTKAMQATGITHLA----------DQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488422749 458 QPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:PRK10253 161 ETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
345-521 |
2.26e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.58 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 345 QRIGIVGPNGAGKTTMLN-------------ILSGEDQQFEGTLKIGQTVKVAYFKQTEE----TLNRDIRM--IDYLRE 405
Cdd:PRK13652 31 SRIAVIGPNGAGKSTLFRhfngilkptsgsvLIRGEPITKENIREVRKFVGLVFQNPDDQifspTVEQDIAFgpINLGLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 406 ESEVAKEKDGT--TVSITQLLERFlfPssthgkkiYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTIL 479
Cdd:PRK13652 111 EETVAHRVSSAlhMLGLEELRDRV--P--------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488422749 480 EDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIVGS 521
Cdd:PRK13652 181 NDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG---RIVAY 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
10-212 |
2.38e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.90 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 10 NKSYADKVIFDdLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQyriryssqkqdldGNLSVFEAVLS 89
Cdd:PRK13643 14 NSPFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGL--------LQPTE-------------GKVTVGDIVVS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 90 SeTSTLQIIKHYEQAV-------QQYTVEQTDRNFQAMMAAQEAMDRHEAWDYNAEiKTILSKLGIHDTTKQVNSLSGGQ 162
Cdd:PRK13643 72 S-TSKQKEIKPVRKKVgvvfqfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAE-KLEMVGLADEFWEKSPFELSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQYPYTVLFVTH 212
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-232 |
2.39e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 3 AYKIEHLNKSYAD--KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGI---DDDFTGDIThpnqyriryssqkqdL 77
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKIT---------------V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 78 DGnLSVFEAVLSSETSTLQIIkhYEQAVQQYtVEQTDRNFQAMMAAQEAMDRHEAWDYnaeIKTILSKLGIHDTTK-QVN 156
Cdd:PRK13640 70 DG-ITLTAKTVWDIREKVGIV--FQNPDNQF-VGATVGDDVAFGLENRAVPRPEMIKI---VRDVLADVGMLDYIDsEPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQYP----YTVLFVTHDryfLNEVS--TRIVELDRG 230
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkknnLTVISITHD---IDEANmaDQVLVLDDG 219
|
..
gi 488422749 231 KL 232
Cdd:PRK13640 220 KL 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-496 |
3.00e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGNLSVFEAVLSSETSTLQIIk 99
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---------------IDGQEMRFASTTAALAAGVAII- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 100 HYE-QAVQQYTVEQTdrnfqaMMAAQ-----EAMDRHEAwdyNAEIKTILSKLGIH-DTTKQVNSLSGGQQKRVVLAKTL 172
Cdd:PRK11288 85 YQElHLVPEMTVAEN------LYLGQlphkgGIVNRRLL---NYEAREQLEHLGVDiDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 173 IEQPDLLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHdryflnevstRIVELDR--GKLTTYpgnyedyiamra 247
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLfrvIRELRAEGRVILYVSH----------RMEEIFAlcDAITVF------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 248 ekevieqkqndkqralykqelawmRAGAKARSTKQQARIHRfndlEANVKQQQTQDKGELNLAYSR-LGKQVYELDSLTk 326
Cdd:PRK11288 214 ------------------------KDGRYVATFDDMAQVDR----DQLVQAMVGREIGDIYGYRPRpLGEVRLRLDGLK- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 327 tinGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQT---------------- 389
Cdd:PRK11288 265 ---GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPRDAiragimlcpedrkaeg 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 -------EETLNRDIR--------MIDYlREESEVAKEKdgttvsITQLleRFLFPSstHGKKIYKLSGGEQKRLYLLRL 454
Cdd:PRK11288 342 iipvhsvADNINISARrhhlragcLINN-RWEAENADRF------IRSL--NIKTPS--REQLIMNLSGGNQQKAILGRW 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 488422749 455 LVHQPNVLLLDEPTNDLD----TETLTILEDyIASFGGSVITVSHD 496
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDvgakHEIYNVIYE-LAAQGVAVLFVSSD 455
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
334-377 |
3.17e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.70 E-value: 3.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488422749 334 FQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI 377
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
320-400 |
3.69e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayFKQTEETLNRDIR 398
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMR---FASTTAALAAGVA 82
|
..
gi 488422749 399 MI 400
Cdd:PRK11288 83 II 84
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
321-472 |
3.82e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.81 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 321 LDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGqtvkvayfkqtEETLN------ 394
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG-----------EKRMNdvppae 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMI--DY---------------LR----EESEVAK--EKDGTTVSITQLLERflfpssthgkKIYKLSGGEQKRLYL 451
Cdd:PRK11000 75 RGVGMVfqSYalyphlsvaenmsfgLKlagaKKEEINQrvNQVAEVLQLAHLLDR----------KPKALSGGQRQRVAI 144
|
170 180
....*....|....*....|.
gi 488422749 452 LRLLVHQPNVLLLDEPTNDLD 472
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLD 165
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
296-475 |
4.48e-08 |
|
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: 56.26 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 296 VKQQQTQDKGELNLAYSRlGKQVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNIL------SGEDQ 369
Cdd:TIGR02203 311 LDSPPEKDTGTRAIERAR-GDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepDSGQI 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 370 QFEG------TLK--------IGQTVKVayFkqtEETLNRDI---RMIDYLREESEVAKEKDGTTVSITQLLERFLFPSS 432
Cdd:TIGR02203 390 LLDGhdladyTLAslrrqvalVSQDVVL--F---NDTIANNIaygRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488422749 433 THGKKiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:TIGR02203 465 ENGVL---LSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-232 |
5.10e-08 |
|
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: 55.96 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-----------DITHP--------NQYrIRYSSQKQDLDGN 80
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvDMTKPgpdgrgraKRY-IGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 LSVFEAVlsSETSTLQIIKHYEQAVQQYTVEQTdrnfqammaaqeAMDRHEAwdynaeiKTILSKLgihdttkqVNSLSG 160
Cdd:TIGR03269 380 RTVLDNL--TEAIGLELPDELARMKAVITLKMV------------GFDEEKA-------EEILDKY--------PDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
5.12e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.46 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 1 MEAYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGgidddftgdithpnqyRIRYSSQKQDLDGN 80
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFN----------------RLLELNEEARVEGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 LSVF-EAVLSSETSTLQIIKHYEQAVQQ---------YTVEQTDRNFQAMMAAQEAMDRHEAWdynaeiktILSKLGIHD 150
Cdd:PRK14267 66 VRLFgRNIYSPDVDPIEVRREVGMVFQYpnpfphltiYDNVAIGVKLNGLVKSKKELDERVEW--------ALKKAALWD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 151 TTKQ-----VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLINYVKQyPYTVLFVTHDRYFLNEVST 222
Cdd:PRK14267 138 EVKDrlndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSD 216
|
250
....*....|
gi 488422749 223 RIVELDRGKL 232
Cdd:PRK14267 217 YVAFLYLGKL 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-189 |
6.63e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSY-ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGidddftgdithpnqYrirYSSQKQD--LDGNls 82
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG--------------Y---YPLTEGEirLDGR-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 vfeavlssETSTL--QIIKHYEQAVQQYTVEQTDrNFQAMMAAQEAMDRHEAWDYNAEIKtiLSKL------GIHDTT-K 153
Cdd:PRK10790 404 --------PLSSLshSVLRQGVAMVQQDPVVLAD-TFLANVTLGRDISEEQVWQALETVQ--LAELarslpdGLYTPLgE 472
|
170 180 190
....*....|....*....|....*....|....*.
gi 488422749 154 QVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-513 |
6.68e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 53.24 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 333 LFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTvkVAYFKQTEETLNRDIRmiDYLREESEVAKE 412
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEPWIQNGTIR--ENILFGKPFDEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 413 KDGTTVSITQLLERF-LFPSS--TH-GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET-LTILEDYIASF- 486
Cdd:cd03250 96 RYEKVIKACALEPDLeILPDGdlTEiGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLl 175
|
170 180
....*....|....*....|....*....
gi 488422749 487 --GGSVITVSHDRYFLNKVAQEYwFIHDG 513
Cdd:cd03250 176 lnNKTRILVTHQLQLLPHADQIV-VLDNG 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
330-475 |
6.88e-08 |
|
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: 53.77 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 330 GRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSgedqQF----EGTLKI-GQTV----------KVAYFKQTEETLN 394
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP----RFydvdSGRILIdGHDVrdytlaslrrQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRM-IDY-LREESEVAKEKDGTTVSITQLLERFlfPSSTH---GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTN 469
Cdd:cd03251 90 DTVAEnIAYgRPGATREEVEEAARAANAHEFIMEL--PEGYDtviGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
....*.
gi 488422749 470 DLDTET 475
Cdd:cd03251 168 ALDTES 173
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-213 |
8.02e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.78 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRYSSQkqdlDGNLSVF 84
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSAR--------LAPDAGEVHYRMR----DGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EAVLSSETSTLQiikHYEQA-VQQYTVEQTDRNFQA-------MMAAQEamdRH------EAWDYNAEIKTILSKLGIHD 150
Cdd:PRK11701 76 YALSEAERRRLL---RTEWGfVHQHPRDGLRMQVSAggnigerLMAVGA---RHygdiraTAGDWLERVEIDAARIDDLP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 151 TTkqvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFeSI-----NWLINYVKQYPYTVLFVTHD 213
Cdd:PRK11701 150 TT-----FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVqarllDLLRGLVRELGLAVVIVTHD 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-231 |
8.02e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.28 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYA-----DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdithpnqyrIRYSSQKQDLDG 79
Cdd:PRK13637 4 KIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL---------------LKPTSGKIIIDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 nlsvfeAVLSSETSTLQIIKHYEQAVQQYTVEQTdrnFQammaaqEAMDRHEAW----------DYNAEIKTILSKLGI- 148
Cdd:PRK13637 69 ------VDITDKKVKLSDIRKKVGLVFQYPEYQL---FE------ETIEKDIAFgpinlglseeEIENRVKRAMNIVGLd 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 149 HDTTKQVN--SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVK----QYPYTVLFVTHDRYFLNEVST 222
Cdd:PRK13637 134 YEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKelhkEYNMTIILVSHSMEDVAKLAD 213
|
....*....
gi 488422749 223 RIVELDRGK 231
Cdd:PRK13637 214 RIIVMNKGK 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-232 |
8.33e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.94 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 10 NKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG----------IDDDFTGDITHPNQYRIRYSSQKQDLDG 79
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAllipsegkvyVDGLDTSDEENLWDIRNKAGMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 nlsvfeavlssetstlQIIKhyeqavqqyTVEQTDRNFQAMMAAQEAMDRHEAWDYNaeiktiLSKLGIHDTTKQV-NSL 158
Cdd:PRK13633 97 ----------------QIVA---------TIVEEDVAFGPENLGIPPEEIRERVDES------LKKVGMYEYRRHApHLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHdryFLNEV--STRIVELDRGKL 232
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGKV 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-240 |
8.56e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.24 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIF-----DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDiTHPNQYRIryssqkqdlDGN 80
Cdd:PRK13645 9 LDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAI---------PAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 81 LSVFEAVLSSETSTLQIIKHYEQAVQQYTVEQtDRNFQAMMAAQeamDRHEAWDYNAEIKTILSkLGIHDTTKQVNSLSG 160
Cdd:PRK13645 79 LKKIKEVKRLRKEIGLVFQFPEYQLFQETIEK-DIAFGPVNLGE---NKQEAYKKVPELLKLVQ-LPEDYVKRSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----INWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTTYP 236
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
....
gi 488422749 237 GNYE 240
Cdd:PRK13645 234 SPFE 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-221 |
1.05e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 3 AYKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDD-----------DFTGDITHP---NQYRI 68
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevrvegrvEFFNQNIYErrvNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 69 RYSSQKQDLDGNL---SVFEAVlsseTSTLQIIKHYEQavqqytVEQTDRNFQAMMAAqeamdrhEAWDynaEIKtilsk 145
Cdd:PRK14258 87 RRQVSMVHPKPNLfpmSVYDNV----AYGVKIVGWRPK------LEIDDIVESALKDA-------DLWD---EIK----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 146 lgiHDTTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLI-NYVKQYPYTVLFVTHDRYFLNEVS 221
Cdd:PRK14258 142 ---HKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLIqSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
341-496 |
1.11e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSG-----------EDQQFEG--TLKIG--------QTVK------------VAYFK 387
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGfykptggtillRGQHIEGlpGHQIArmgvvrtfQHVRlfremtvienllVAQHQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QTEETLNRD-IRMIDYLREESEvAKEKDGT---TVSITQLLERflfPSSThgkkiykLSGGEQKRLYLLRLLVHQPNVLL 463
Cdd:PRK11300 108 QLKTGLFSGlLKTPAFRRAESE-ALDRAATwleRVGLLEHANR---QAGN-------LAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 488422749 464 LDEPT---NDLDTETLTILEDYI-ASFGGSVITVSHD 496
Cdd:PRK11300 177 LDEPAaglNPKETKELDELIAELrNEHNVTVLLIEHD 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-191 |
1.16e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYAD--KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKV----MGGIDDDFTGDIthpnqyriryssQKQDLDG 79
Cdd:COG2401 31 LEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLlagaLKGTPVAGCVDV------------PDNQFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 80 NLSVFEAVLSSETSTlqiikhyeQAVQqytveqtdrnfqammaaqeamdrheawdynaeiktILSKLGIHDTT---KQVN 156
Cdd:COG2401 99 EASLIDAIGRKGDFK--------DAVE-----------------------------------LLNAVGLSDAVlwlRRFK 135
|
170 180 190
....*....|....*....|....*....|....*
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE 191
Cdd:COG2401 136 ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-213 |
1.23e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 4 YKIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIRYSS-----QKQDLD 78
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 79 GNLSVFEAVLSSEtstLQIIKHY--EQAVQQYTVEQTDRnfqammaAQEAMDRheawdynAEIKTILSKLgihdttkqVN 156
Cdd:PRK10575 92 QQLPAAEGMTVRE---LVAIGRYpwHGALGRFGAADREK-------VEEAISL-------VGLKPLAHRL--------VD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHD 213
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQERGLTVIAVLHD 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
322-496 |
1.36e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.01 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 322 DSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTL----KIGQTVKVAYFKQTEEtlnrdi 397
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYALSEAER------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RMIdyLREESEVAKE--KDG--TTVSI-----------------------TQLLERFLFPSSthgkKIYKL----SGGEQ 446
Cdd:PRK11701 84 RRL--LRTEWGFVHQhpRDGlrMQVSAggnigerlmavgarhygdirataGDWLERVEIDAA----RIDDLpttfSGGMQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488422749 447 KRLYLLRLLVHQPNVLLLDEPTNDLDTET----LTILEDYIASFGGSVITVSHD 496
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHD 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
327-497 |
1.47e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 327 TINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLN----ILSGEDQ-QFEG------TLkigQTVKVAY--FKQTEETL 393
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSallrLLSTEGEiQIDGvswnsvTL---QTWRKAFgvIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRDIRM-ID----YLREESEVAKEKDGTTVSITQLLERFLFPSSTHGkkiYKLSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:TIGR01271 1305 SGTFRKnLDpyeqWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG---YVLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190
....*....|....*....|....*....|
gi 488422749 469 NDLDTETLTILEDYIA-SFGGSVITVSHDR 497
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTLKqSFSNCTVILSEHR 1411
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
330-495 |
1.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 330 GRTLFqDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAYFKQT-------------------- 389
Cdd:PRK13649 20 GRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirkkvglvfqfpesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 390 -EETLNRDI----RMIDYLREESE-VAKEKDgTTVSITQLLerflfpsstHGKKIYKLSGGEQKRLYLLRLLVHQPNVLL 463
Cdd:PRK13649 99 fEETVLKDVafgpQNFGVSQEEAEaLAREKL-ALVGISESL---------FEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 488422749 464 LDEPTNDLD----TETLTILEDYIASfGGSVITVSH 495
Cdd:PRK13649 169 LDEPTAGLDpkgrKELMTLFKKLHQS-GMTIVLVTH 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-232 |
1.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 19 FDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGNLSVFEAVLSSETSTLQII 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVK---------------IDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 99 KHYEQAVQQYTVEQTdrnfQAMMAAQEAMDRHEAWDYNAEIKTILSKLGIhdTTKQVNSLSGGQQKRVVLAKTLIEQPDL 178
Cdd:PRK13642 88 QNPDNQFVGATVEDD----VAFGMENQGIPREEMIKRVDEALLAVNMLDF--KTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 179 LLLDEPTNHLD---FESINWLINYVK-QYPYTVLFVTHDryfLNEV--STRIVELDRGKL 232
Cdd:PRK13642 162 IILDESTSMLDptgRQEIMRVIHEIKeKYQLTVLSITHD---LDEAasSDRILVMKAGEI 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-233 |
1.67e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 22 LSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---------THPNQYRIRYSSQKQDLdgnlSVFEAVLSSEt 92
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkpvtaEQPEDYRKLFSAVFTDF----HLFDQLLGPE- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 93 stlqiikhyeqavqqytveqtdrNFQAMMAAQEAmdrheaWdynAEIKTILSKLGIHDTTKQVNSLSGGQQKRVVLAKTL 172
Cdd:PRK10522 417 -----------------------GKPANPALVEK------W---LERLKMAHKLELEDGRISNLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 173 IEQPDLLLLDEPTNHLD--FESINW--LINYVKQYPYTVLFVTH-DRYFlnEVSTRIVELDRGKLT 233
Cdd:PRK10522 465 AEERDILLLDEWAADQDphFRREFYqvLLPLLQEMGKTIFAISHdDHYF--IHADRLLEMRNGQLS 528
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-240 |
2.43e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRYSSQKQDLDGNLSVFEAVLSSETSTLQIIK 99
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAL--------LLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 100 HYEQA---------VQQY--------TVEQtDRNFQAM---MAAQEAMDRheawdynaeIKTILSKLGIHDTTKQVN--S 157
Cdd:PRK13651 96 KIKKIkeirrrvgvVFQFaeyqlfeqTIEK-DIIFGPVsmgVSKEEAKKR---------AAKYIELVGLDESYLQRSpfE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLTT 234
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
....*.
gi 488422749 235 YPGNYE 240
Cdd:PRK13651 246 DGDTYD 251
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-224 |
2.68e-07 |
|
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: 52.37 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 32 IGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYR--IRY--SSQKQDLdgnlsvFEAVLSSETSTlqIIKhyeqavQQ 107
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeiLDEfrGSELQNY------FTKLLEGDVKV--IVK------PQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 108 YtVEQTDRNFQAmmaaqEAMDRHEAWDYNAEIKTILSKLGI-HDTTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTN 186
Cdd:cd03236 95 Y-VDLIPKAVKG-----KVGELLKKKDERGKLDELVDQLELrHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488422749 187 HLDFE---SINWLINYVKQYPYTVLFVTHDRYFLNEVSTRI 224
Cdd:cd03236 169 YLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-480 |
2.91e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.22 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 349 IVGPNGAGKTTMLNILSG-----EDQQFEGTLKI-GQTVkvayFKQTEETLNRDIRMIDYLREE---------------- 406
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLdGQDI----FKMDVIELRRRVQMVFQIPNPipnlsifenvalglkl 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 407 SEVAKEKDGTTVSITQLLERFLFPSSTH---GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILE 480
Cdd:PRK14247 110 NRLVKSKKELQERVRWALEKAQLWDEVKdrlDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIE 186
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-192 |
3.11e-07 |
|
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: 51.77 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 18 IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---------HPNQYR--IRYSSQKQDL-DGnlSVFE 85
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdirdlNLRWLRsqIGLVSQEPVLfDG--TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 AVLSSETSTlqiikhyeqavqqyTVEQTDRnfqammAAQEAmdrheawdyNAEiKTILSKLGIHDTtkQV----NSLSGG 161
Cdd:cd03249 96 NIRYGKPDA--------------TDEEVEE------AAKKA---------NIH-DFIMSLPDGYDT--LVgergSQLSGG 143
|
170 180 190
....*....|....*....|....*....|.
gi 488422749 162 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFES 192
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-513 |
3.44e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 348 GIVGPNGAGKTTMLNILSG--EDQQFE-------------GTLKIGQTVKVAYFKQTEETLNRDIRM-IDY-LRE----E 406
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGllRPQKGAvlwqgkpldyskrGLLALRQQVATVFQDPEQQIFYTDIDSdIAFsLRNlgvpE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 407 SEVAKEKDGTTVSITQllERFlfpsstHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDy 482
Cdd:PRK13638 111 AEITRRVDEALTLVDA--QHF------RHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrTQMIAIIRR- 181
|
170 180 190
....*....|....*....|....*....|.
gi 488422749 483 IASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:PRK13638 182 IVAQGNHVIISSHDIDLIYEISDAVYVLRQG 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-192 |
3.66e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 15 DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQY------------RIRYSSQKQDLDGNlS 82
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrsKIGVVSQDPLLFSN-S 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETSTLQIIKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDR-------------HEAWDYN----AEIKTILSK 145
Cdd:PTZ00265 476 IKNNIKYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLndmsnttdsneliEMRKNYQtikdSEVVDVSKK 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 146 LGIHD------------TTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES 192
Cdd:PTZ00265 556 VLIHDfvsalpdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
336-496 |
3.74e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 336 DITQIIQSGQRIGIVGPNGAGKTTMLnilsgedQQFEGTLKIGQ-TVKVAYFKQTEETLNRDIRMI------------DY 402
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLM-------QHFNALLKPSSgTITIAGYHITPETGNKNLKKLrkkvslvfqfpeAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 403 LREES----------------EVAKEKdgttvsITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:PRK13641 98 LFENTvlkdvefgpknfgfseDEAKEK------ALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190
....*....|....*....|....*....|....
gi 488422749 467 PTNDLD----TETLTILEDYIASfGGSVITVSHD 496
Cdd:PRK13641 172 PAAGLDpegrKEMMQLFKDYQKA-GHTVILVTHN 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
329-496 |
4.58e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.77 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 329 NGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNIL-------SGE--------DQQFEGTLKIGQTVKVAyFKQTEETL 393
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLngilkpsSGRilfdgkpiDYSRKGLMKLRESVGMV-FQDPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 -----NRDIRM--IDYLREESEVAKEKDgttvsitQLLERFLFPSSTHgKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:PRK13636 96 fsasvYQDVSFgaVNLKLPEDEVRKRVD-------NALKRTGIEHLKD-KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190
....*....|....*....|....*....|....
gi 488422749 467 PTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:PRK13636 168 PTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
157-235 |
4.67e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDryfLNEV---STRIVELDR 229
Cdd:PRK11144 128 SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSHS---LDEIlrlADRVVVLEQ 204
|
....*.
gi 488422749 230 GKLTTY 235
Cdd:PRK11144 205 GKVKAF 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
341-468 |
4.82e-07 |
|
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: 51.14 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGT----------LKIGQTVK--VAY-------FKQ--TEETLnrdiRM 399
Cdd:COG0410 26 VEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSirfdgeditgLPPHRIARlgIGYvpegrriFPSltVEENL----LL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 IDYLREESEVAKEKdgttvsitqlLERF--LFP---------SSThgkkiykLSGGEQKRLYLLRLLVHQPNVLLLDEPT 468
Cdd:COG0410 102 GAYARRDRAEVRAD----------LERVyeLFPrlkerrrqrAGT-------LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-189 |
5.04e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.74 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 30 EKIGLVGINGTGKSTLLKVMGGidddftgdithpnqyRIRyssqkQDLDGNLSVfeaVLSSETSTLQIIKHYEQAVQQ-- 107
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAF---------------RSP-----KGVKGSGSV---LLNGMPIDAKEMRAISAYVQQdd 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 108 -----YTVEQtDRNFQAMMAaqeaMDRHEAWDYNAE-IKTILSKLGIHD-------TTKQVNSLSGGQQKRVVLAKTLIE 174
Cdd:TIGR00955 109 lfiptLTVRE-HLMFQAHLR----MPRRVTKKEKRErVDEVLQALGLRKcantrigVPGRVKGLSGGERKRLAFASELLT 183
|
170
....*....|....*
gi 488422749 175 QPDLLLLDEPTNHLD 189
Cdd:TIGR00955 184 DPPLLFCDEPTSGLD 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
341-493 |
5.44e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIG-QTVKVAYFKQ-----TEETLNRDIRMI-----DYLREESEV 409
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRLSFEQlqklvSDEWQRNNTDMLspgedDTGRTTAEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 410 AKE--KD-------GTTVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILE 480
Cdd:PRK10938 106 IQDevKDparceqlAQQFGITALLDR----------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170
....*....|...
gi 488422749 481 DYIASFGGSVITV 493
Cdd:PRK10938 176 ELLASLHQSGITL 188
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
158-193 |
5.94e-07 |
|
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: 50.12 E-value: 5.94e-07
10 20 30
....*....|....*....|....*....|....*.
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESI 193
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-232 |
6.14e-07 |
|
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: 52.41 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 14 ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVM-------GG---IDDDFTGDITHPNQYR-IRYSSQKQDLdGNLS 82
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdSGqilLDGHDLADYTLASLRRqVALVSQDVVL-FNDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETstlqiikhyeqavQQYTVEQTDRNFQAMMAaQEAMDRheawdynaeiktilSKLGIHDTTKQVNS-LSGG 161
Cdd:TIGR02203 422 IANNIAYGRT-------------EQADRAEIERALAAAYA-QDFVDK--------------LPLGLDTPIGENGVlLSGG 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488422749 162 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQyPYTVLFVTHdRYFLNEVSTRIVELDRGKL 232
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESerlVQAALERLMQ-GRTTLVIAH-RLSTIEKADRIVVMDDGRI 545
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-496 |
6.94e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTV----KVAYFKQ----------------TEET-- 392
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrRKEFARRigvvfgqrsqlwwdlpAIDSfr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 393 LNRDI---------RMIDYLREESEvakekdgttvsitqlLERFLfpssthGKKIYKLSGGEQKRLYLLRLLVHQPNVLL 463
Cdd:COG4586 119 LLKAIyripdaeykKRLDELVELLD---------------LGELL------DTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 488422749 464 LDEPTNDLDTET-LTI---LEDYIASFGGSVITVSHD 496
Cdd:COG4586 178 LDEPTIGLDVVSkEAIrefLKEYNRERGTTILLTSHD 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
330-475 |
7.10e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 52.43 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 330 GRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTV-----------KVAYFKQTE-------- 390
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYLPQEPyifsgsil 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 391 ETL---NRDIRMIDYLREESEVAKEKDgttvSITQLLERFLFPSSTHGKKIyklSGGEQKRLYLLRLLVHQPNVLLLDEP 467
Cdd:TIGR01193 566 ENLllgAKENVSQDEIWAACEIAEIKD----DIENMPLGYQTELSEEGSSI---SGGQKQRIALARALLTDSKVLILDES 638
|
....*...
gi 488422749 468 TNDLDTET 475
Cdd:TIGR01193 639 TSNLDTIT 646
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
292-577 |
7.17e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 292 LEANVKQQQTQdkgELNLAYSRLGKQVYELDSLTKTI---NG---------RTLFQDITQIIQSGQRIGIVGPNGAGKTT 359
Cdd:PLN03232 582 VNANVSLQRIE---ELLLSEERILAQNPPLQPGAPAIsikNGyfswdsktsKPTLSDINLEIPVGSLVAIVGGTGEGKTS 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 360 MLNILSGEDQQFEgTLKIGQTVKVAYFKQTEETLNRDIRmiDYLREESEVAKEKDGTTVSITQLLERF-LFPS---STHG 435
Cdd:PLN03232 659 LISAMLGELSHAE-TSSVVIRGSVAYVPQVSWIFNATVR--ENILFGSDFESERYWRAIDVTALQHDLdLLPGrdlTEIG 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 436 KKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLNKVaQEYWFIHD 512
Cdd:PLN03232 736 ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDelkGKTRVLVTNQLHFLPLM-DRIILVSE 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 513 GMMERiVGSFEDY----ETYKK------EKDKQLAIEKQATNTSKTQIK-----ERKKTGlSYKEKREYESLMSRIEETE 577
Cdd:PLN03232 815 GMIKE-EGTFAELsksgSLFKKlmenagKMDATQEVNTNDENILKLGPTvtidvSERNLG-STKQGKRGRSVLVKQEERE 892
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-238 |
7.44e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.63 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQKQDLDGNLS---VFE---AVLSSETS 93
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK-DLLGMKDDEWRAVRSDiqmIFQdplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 94 TLQIIKhyeqavqqytveQTDRNFQAMMAAQEAMDRheawdynaeIKTILSKLGIhdTTKQVN----SLSGGQQKRVVLA 169
Cdd:PRK15079 117 IGEIIA------------EPLRTYHPKLSRQEVKDR---------VKAMMLKVGL--LPNLINryphEFSGGQCQRIGIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488422749 170 KTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIveldrgkLTTYPGN 238
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV-------LVMYLGH 239
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-213 |
8.56e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.85 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQKQDL---DGNLS 82
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVEGPGAERGVvfqNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETSTLQIikhyeQAVQQYTVEQTDRNFQAMMAAQEAmDRHEAWdynaeiktilsklgihdttkqvnSLSGGQ 162
Cdd:PRK11248 83 PWRNVQDNVAFGLQL-----AGVEKMQRLEIAHQMLKKVGLEGA-EKRYIW-----------------------QLSGGQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTNHLD-F--ESINWLINYV-----KQypytVLFVTHD 213
Cdd:PRK11248 134 RQRVGIARALAANPQLLLLDEPFGALDaFtrEQMQTLLLKLwqetgKQ----VLLITHD 188
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-505 |
9.16e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.78 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTlkigqtVKVAYFKQTEETLnRDIRmidylREESEVAKEKD 414
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT------ITVGGMVLSEETV-WDVR-----RQVGMVFQNPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 415 ----GTTV-------------SITQLLER------------FLFPSSTHgkkiykLSGGEQKRLYLLRLLVHQPNVLLLD 465
Cdd:PRK13635 92 nqfvGATVqddvafglenigvPREEMVERvdqalrqvgmedFLNREPHR------LSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488422749 466 EPTNDLD----TETLTILEDYIASFGGSVITVSHDryfLNKVAQ 505
Cdd:PRK13635 166 EATSMLDprgrREVLETVRQLKEQKGITVLSITHD---LDEAAQ 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
331-496 |
9.40e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV-------------KVAYFKQTeETLNRD 396
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIpamsrsrlytvrkRMSMLFQS-GALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 397 IRMIDY----LREESEVAKEKDGTTVSITqlLERF-------LFPSsthgkkiyKLSGGEQKRLYLLRLLVHQPNVLLLD 465
Cdd:PRK11831 99 MNVFDNvaypLREHTQLPAPLLHSTVMMK--LEAVglrgaakLMPS--------ELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 488422749 466 EPTNDLDTETLTILEDYI----ASFGGSVITVSHD 496
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLIselnSALGVTCVVVSHD 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-185 |
9.53e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGI--DDDFTGDIThpnqyriryssqkqdLDGNLSVFEAVLSSETSTLQI 97
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEIL---------------FDGEVCRFKDIRDSEALGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 98 IkHYEQA-VQQYTV--------EQTDRNFqammaaqeaMDRHEAwdyNAEIKTILSKLGIHDT-TKQVNSLSGGQQKRVV 167
Cdd:NF040905 83 I-HQELAlIPYLSIaeniflgnERAKRGV---------IDWNET---NRRARELLAKVGLDESpDTLVTDIGVGKQQLVE 149
|
170
....*....|....*...
gi 488422749 168 LAKTLIEQPDLLLLDEPT 185
Cdd:NF040905 150 IAKALSKDVKLLILDEPT 167
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-232 |
1.04e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 49.80 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYAD--KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---------HPNQYRIRYSSQ 73
Cdd:cd03244 4 EFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiGLHDLRSRISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 74 KQD---LDG----NLSVFEavlssetstlqiiKHYEQAVQQytveqtdrnfqammaaqeAMDRHEAWDYnaeiktILSKL 146
Cdd:cd03244 84 PQDpvlFSGtirsNLDPFG-------------EYSDEELWQ------------------ALERVGLKEF------VESLP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 147 GIHDTTKQVN--SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLI-NYVKQypYTVLFVTHdRyfLNEV 220
Cdd:cd03244 127 GGLDTVVEEGgeNLSVGQRQLLCLARALLRKSKILVLDEATASVDPETdalIQKTIrEAFKD--CTVLTIAH-R--LDTI 201
|
250
....*....|....
gi 488422749 221 --STRIVELDRGKL 232
Cdd:cd03244 202 idSDRILVLDKGRV 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
439-495 |
1.11e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.42 E-value: 1.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 439 YKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD-TETLTIlEDYIASFGG--SVITVSH 495
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAKI-EELILELKKdyTIVIVTH 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-233 |
1.13e-06 |
|
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: 51.67 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 14 ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdiTHPNQYRIRyssqkqdLDGNlsvfeavlssets 93
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV--------WPPTAGSVR-------LDGA------------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 94 tlqIIKHYE------------QAVQQY--TVEQ-----TDRNFQAMMAAQEAMDRHEawdynaeikTILS-KLGiHDTtk 153
Cdd:COG4618 395 ---DLSQWDreelgrhigylpQDVELFdgTIAEniarfGDADPEKVVAAAKLAGVHE---------MILRlPDG-YDT-- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 154 QV----NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHDRYFLNEVStRIVE 226
Cdd:COG4618 460 RIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALaaaIRALKARGATVVVITHRPSLLAAVD-KLLV 538
|
....*..
gi 488422749 227 LDRGKLT 233
Cdd:COG4618 539 LRDGRVQ 545
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
320-495 |
1.15e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQTEE------- 391
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPRDAQAagiaiih 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 ---------------TLNRDIR---MIDY--LREESEVAKEKDGTTVSITQLLERflfpssthgkkiykLSGGEQKRLYL 451
Cdd:COG1129 86 qelnlvpnlsvaeniFLGREPRrggLIDWraMRRRARELLARLGLDIDPDTPVGD--------------LSVAQQQLVEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488422749 452 LRLLVHQPNVLLLDEPT---NDLDTETL-TILEDyIASFGGSVITVSH 495
Cdd:COG1129 152 ARALSRDARVLILDEPTaslTEREVERLfRIIRR-LKAQGVAIIYISH 198
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
330-517 |
1.23e-06 |
|
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: 51.29 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 330 GRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVkvayfkqteETLNRDI--RMIDYLREE 406
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdGADL---------SQWDREElgRHIGYLPQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 407 SEVAkekDGTtvsITQLLERFLFPSSThgkKIYK----------------------------LSGGEQKRLYLLRLLVHQ 458
Cdd:COG4618 415 VELF---DGT---IAENIARFGDADPE---KVVAaaklagvhemilrlpdgydtrigeggarLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 459 PNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLN---KVAqeywFIHDGMMER 517
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLLAavdKLL----VLRDGRVQA 546
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-189 |
1.23e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.42 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG--IDDDFTGDI-------THPNQYRIRYSSQKQ 75
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTIlannrkpTKQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DLDGNLSVFEAVLssetstlqiikhyeqavqqytveqtdrnFQAMMAAQEAMDRHEAwdyNAEIKTILSKLGIHDTTKQV 155
Cdd:PLN03211 150 ILYPHLTVRETLV----------------------------FCSLLRLPKSLTKQEK---ILVAESVISELGLTKCENTI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488422749 156 --NS----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:PLN03211 199 igNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
336-495 |
1.26e-06 |
|
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: 49.72 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 336 DITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGqtvkvayfkqteetlNRDIRMIDYLREESEVA-KEKD 414
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID---------------GIDISTIPLEDLRSSLTiIPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 415 GTTVS--ITQLLERFLFPSSthgKKIYK----------LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDY 482
Cdd:cd03369 91 PTLFSgtIRSNLDPFDEYSD---EEIYGalrvsegglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170
....*....|....*
gi 488422749 483 I-ASFGGS-VITVSH 495
Cdd:cd03369 168 IrEEFTNStILTIAH 182
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-235 |
1.33e-06 |
|
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: 49.33 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKV--IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNqyrIRYSSQK-QDLDGNL 81
Cdd:cd03369 8 EVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG---IDISTIPlEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 82 SVF--EAVLSSET--STLQIIKHYeqavqqytveqTDRnfqammaaqeamdrheawdynaEIKTILSklgihdTTKQVNS 157
Cdd:cd03369 85 TIIpqDPTLFSGTirSNLDPFDEY-----------SDE----------------------EIYGALR------VSEGGLN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESiNWLINYVKQYPY---TVLFVTHDryfLNEVS--TRIVELDRGKL 232
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DALIQKTIREEFtnsTILTIAHR---LRTIIdyDKILVMDAGEV 201
|
...
gi 488422749 233 TTY 235
Cdd:cd03369 202 KEY 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
319-496 |
1.35e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 319 YELDSLTKTINGrtlfqdITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVAyfkQTEETLNRDIR 398
Cdd:PRK13642 14 YEKESDVNQLNG------VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 399 MIDYLRE--------ESEVAKEKDGTTVSITQLLERF---LFPSST---HGKKIYKLSGGEQKRLYLLRLLVHQPNVLLL 464
Cdd:PRK13642 85 MVFQNPDnqfvgatvEDDVAFGMENQGIPREEMIKRVdeaLLAVNMldfKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 488422749 465 DEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:PRK13642 165 DESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-212 |
1.44e-06 |
|
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: 49.92 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 7 EHLNKSYAD-KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQK----------Q 75
Cdd:cd03253 4 ENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ-DIREVTLDslrraigvvpQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 DldgnlsvfeAVLSSETstlqiIKHyeqAVQQYTVEQTDrnfQAMMAAQEAMDRHEawdynaEIK-------TILSKLGI 148
Cdd:cd03253 83 D---------TVLFNDT-----IGY---NIRYGRPDATD---EEVIEAAKAAQIHD------KIMrfpdgydTIVGERGL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 149 HdttkqvnsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESINWLINyvkqyPYTVLFVTH 212
Cdd:cd03253 137 K--------LSGGEKQRVAIARAILKNPPILLLDEATSALDthtereiQAALRDVSK-----GRTTIVIAH 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
323-503 |
1.45e-06 |
|
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: 51.48 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 323 SLTKTINGrtlfqdITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTvkVAYFKQTEETLNrdirmiDY 402
Cdd:TIGR00957 649 DLPPTLNG------ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQAWIQN------DS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 403 LREE----SEVAKEKDGTTVSITQLLERF-LFPSSTH---GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTE 474
Cdd:TIGR00957 715 LRENilfgKALNEKYYQQVLEACALLPDLeILPSGDRteiGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190
....*....|....*....|....*....|....
gi 488422749 475 TLT-ILEDYIASFG----GSVITVSHDRYFLNKV 503
Cdd:TIGR00957 795 VGKhIFEHVIGPEGvlknKTRILVTHGISYLPQV 828
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
348-496 |
1.65e-06 |
|
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: 50.48 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 348 GIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTV---------------KVAYFKQT---------EETLN---RDIRMI 400
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQEarlfphlsvRGNLLygrKRAPRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 401 DYLREESEVAkekdgTTVSITQLLERFlfPSsthgkkiyKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDT----ETL 476
Cdd:COG4148 109 ERRISFDEVV-----ELLGIGHLLDRR--PA--------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaEIL 173
|
170 180
....*....|....*....|
gi 488422749 477 TILEDYIASFGGSVITVSHD 496
Cdd:COG4148 174 PYLERLRDELDIPILYVSHS 193
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-189 |
1.90e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.20 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 23 SLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDI---------THPNQYRIRYSSQKQDLDGNLsvfeavlssets 93
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhttTPPSRRPVSMLFQENNLFSHL------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 94 tlqiikhyeqavqqyTVEQtdrNFqammaaqeAMDRHEAWDYNAE----IKTILSKLGIHDTTKQVNS-LSGGQQKRVVL 168
Cdd:PRK10771 87 ---------------TVAQ---NI--------GLGLNPGLKLNAAqrekLHAIARQMGIEDLLARLPGqLSGGQRQRVAL 140
|
170 180
....*....|....*....|.
gi 488422749 169 AKTLIEQPDLLLLDEPTNHLD 189
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALD 161
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
157-231 |
2.36e-06 |
|
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: 48.62 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYV--------KqypyTVLFVTHDRYFLNEVStRIVELD 228
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCilglllnnK----TRILVTHQLQLLPHAD-QIVVLD 201
|
...
gi 488422749 229 RGK 231
Cdd:cd03250 202 NGR 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-233 |
2.49e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT---------HPNQ---YRIRYSSQKQDLDG---NLSVF 84
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldghevvtrSPQDglaNGIVYISEDRKRDGlvlGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 E----AVLSSETSTLQIIKHYEQavqQYTVEQTDRNFQammaaqeamdrheawdynaeIKTilsklgiHDTTKQVNSLSG 160
Cdd:PRK10762 349 EnmslTALRYFSRAGGSLKHADE---QQAVSDFIRLFN--------------------IKT-------PSMEQAIGLLSG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 161 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESINWLINYVKQYPYTVLFVTHDryfLNEV---STRIVELDRGKLT 233
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVgakKEIYQLINQFKAEGLSIILVSSE---MPEVlgmSDRILVMHEGRIS 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
318-495 |
2.82e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 318 VYELDSLTKTINGRT--LFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV---------KVAY 385
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisdvhqNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 386 ---FKQTEETLNRDIRMIDYLREESEVAKEKDGTTVSITQLLERFLFPSSTHGKkiykLSGGEQKRLYLLRLLVHQPNVL 462
Cdd:TIGR01257 2017 cpqFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190
....*....|....*....|....*....|....*.
gi 488422749 463 LLDEPTNDLDTETLTILEDYIASF---GGSVITVSH 495
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIireGRAVVLTSH 2128
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
154-189 |
3.02e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 3.02e-06
10 20 30
....*....|....*....|....*....|....*.
gi 488422749 154 QVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-220 |
3.06e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDD-DFT-GDITHPNQYRIRYSSQKQDLDGnlsV 83
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyEVTgGTVEFKGKDLLELSPEDRAGEG---I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 84 FEAVlssetstlqiikhyeqavqQYTVE----------QTDRNFQAMMAAQEAMDRHEAWDYnAEIKTILSKLGIHDTTK 153
Cdd:PRK09580 81 FMAF-------------------QYPVEipgvsnqfflQTALNAVRSYRGQEPLDRFDFQDL-MEEKIALLKMPEDLLTR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 154 QVN-SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHDRYFLNEV 220
Cdd:PRK09580 141 SVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVadgVNSLRDGKRSFIIVTHYQRILDYI 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-192 |
3.25e-06 |
|
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: 48.76 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKV-IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDGN--L 81
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL---------------IDGIdiR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 82 SVFEAVLSSETStlqiikhyeqavqqyTVEQTDRNFQAMMAAQEAMDRHEAWDynAEIKTILSKLGIHDTTKQV------ 155
Cdd:cd03254 69 DISRKSLRSMIG---------------VVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKEAGAHDFIMKLpngydt 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488422749 156 ------NSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES 192
Cdd:cd03254 132 vlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-246 |
3.38e-06 |
|
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: 50.33 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 17 VIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHP--NQYRIRYssqkQDLDGNLSVF--EAVLSSET 92
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDglNIAKIGL----HDLRFKITIIpqDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 93 STLQIikhyeQAVQQYTVEQtdrnfqaMMAAQEAmdrheawdynAEIKTILSKLGI---HDTTKQVNSLSGGQQKRVVLA 169
Cdd:TIGR00957 1376 LRMNL-----DPFSQYSDEE-------VWWALEL----------AHLKTFVSALPDkldHECAEGGENLSVGQRQLVCLA 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 170 KTLIEQPDLLLLDEPTNHLDFESINWLINYVK-QYP-YTVLFVTHDryfLNEVS--TRIVELDRGKLTTYpGNYEDYIAM 245
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLIQSTIRtQFEdCTVLTIAHR---LNTIMdyTRVIVLDKGEVAEF-GAPSNLLQQ 1509
|
.
gi 488422749 246 R 246
Cdd:TIGR00957 1510 R 1510
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
134-233 |
3.74e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 134 DYNAEIKTI---LSKLGIHDTTKQ--VNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FEsINWLINYVKQYP 204
Cdd:PRK13549 377 DDAAELKTIlesIQRLKVKTASPElaIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYE-IYKLINQLVQQG 455
|
90 100 110
....*....|....*....|....*....|..
gi 488422749 205 YTVLFVTHDryfLNEV---STRIVELDRGKLT 233
Cdd:PRK13549 456 VAIIVISSE---LPEVlglSDRVLVMHEGKLK 484
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
158-232 |
3.93e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.31 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SInwL-----INyvKQYPYTVLFVTHD----RyflnEVSTRIV 225
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrSI--LdllkdIN--RELGLTIVLITHEmdvvR----RICDRVA 212
|
....*..
gi 488422749 226 ELDRGKL 232
Cdd:COG1135 213 VLENGRI 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-224 |
3.94e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDD---FTGDithpnqyRIRYSS---------QKQDLDG-NLS-VFE 85
Cdd:PRK15093 24 DRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrVTAD-------RMRFDDidllrlsprERRKLVGhNVSmIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 86 AVLS----SETSTLQIIkhyeQAVQQYTVEqtDRNFQAMmaaqeamdrheAWDYNAEIKtILSKLGIHDTTKQVNS---- 157
Cdd:PRK15093 97 EPQScldpSERVGRQLM----QNIPGWTYK--GRWWQRF-----------GWRKRRAIE-LLHRVGIKDHKDAMRSfpye 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQ-YPYTVLFVTHDRYFLNEVSTRI 224
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqaqIFRLLTRLNQnNNTTILLISHDLQMLSQWADKI 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-233 |
4.20e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 21 DLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQKQDLD------GNLSVF-EAVLSSETs 93
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDT-LITSTSKNKDIKqirkkvGLVFQFpESQLFEET- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 94 tlqIIKHYEQAVQQYTVEQTDrnfqammaaQEAMDRHEawdynaeiktiLSKLGIHDTTKQVN--SLSGGQQKRVVLAKT 171
Cdd:PRK13649 103 ---VLKDVAFGPQNFGVSQEE---------AEALAREK-----------LALVGISESLFEKNpfELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 172 LIEQPDLLLLDEPTNHLDFESINWLINYVK---QYPYTVLFVTHDRYFLNEVSTRIVELDRGKLT 233
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKklhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-472 |
4.36e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 48.70 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVK-------VAYFKqteETLNRDIRMIDY---- 402
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdGVPVTgpgadrgVVFQK---DALLPWLNVLDNvafg 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 403 LR-------EESEVAKEKdgttvsiTQL--LERFlfpsstHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD 472
Cdd:COG4525 101 LRlrgvpkaERRARAEEL-------LALvgLADF------ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-495 |
4.40e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.10 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 349 IVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVayfkQTEETLN--RDIRMIDYLREESE--------------VAKE 412
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF----DAEKGIClpPEKRRIGYVFQDARlfphykvrgnlrygMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 413 KDGTTVSITQLL--ERFL--FPSSthgkkiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDT----ETLTILEDYIA 484
Cdd:PRK11144 105 MVAQFDKIVALLgiEPLLdrYPGS--------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAR 176
|
170
....*....|.
gi 488422749 485 SFGGSVITVSH 495
Cdd:PRK11144 177 EINIPILYVSH 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
341-577 |
4.71e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTvKVAYFKQTEETLNRDIRmiDYLREESEVAKEKDGTTVSI 420
Cdd:PLN03130 640 VPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG-TVAYVPQVSWIFNATVR--DNILFGSPFDPERYERAIDV 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 421 TQL---LErfLFPSSTH---GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETL-----TILEDYIAsfGGS 489
Cdd:PLN03130 717 TALqhdLD--LLPGGDLteiGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGrqvfdKCIKDELR--GKT 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 490 VITVSHDRYFLNKVaQEYWFIHDGM--------------------MERiVGSFEDYETYKKEKDKQLAIEKQATNtskTQ 549
Cdd:PLN03130 793 RVLVTNQLHFLSQV-DRIILVHEGMikeegtyeelsnngplfqklMEN-AGKMEEYVEENGEEEDDQTSSKPVAN---GN 867
|
250 260
....*....|....*....|....*...
gi 488422749 550 IKERKKTGLSYKEKREYESLMSRIEETE 577
Cdd:PLN03130 868 ANNLKKDSSSKKKSKEGKSVLIKQEERE 895
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
336-505 |
4.77e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.62 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 336 DITQIIQSGQRIGIVGPNGAGKTTMLnilsgedQQFEGTLK-IGQTVKVAYFKQTEETLNRDIRMI-------------- 400
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLI-------QNINALLKpTTGTVTVDDITITHKTKDKYIRPVrkrigmvfqfpesq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 401 ---DYLREESEVAKEKDGTTVSIT-----QLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD 472
Cdd:PRK13646 98 lfeDTVEREIIFGPKNFKMNLDEVknyahRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 488422749 473 TET----LTILEDYIASFGGSVITVSHDryfLNKVAQ 505
Cdd:PRK13646 178 PQSkrqvMRLLKSLQTDENKTIILVSHD---MNEVAR 211
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
321-495 |
4.94e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 321 LDSLTKTINGRTLFQDITQIIQSGQRIgIVGPNGAGKTTMLNILSGEDQQFEGTL--KIGQTVKVAYFKQT----EETLN 394
Cdd:PRK13541 4 LHQLQFNIEQKNLFDLSITFLPSAITY-IKGANGCGKSSLLRMIAGIMQPSSGNIyyKNCNINNIAKPYCTyighNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMIDYLREESEVAKEKDGTTVSITQL-LERFLfpssthGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDT 473
Cdd:PRK13541 83 LEMTVFENLKFWSEIYNSAETLYAAIHYFkLHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180
....*....|....*....|....*
gi 488422749 474 ETLTILEDYI---ASFGGSVITVSH 495
Cdd:PRK13541 157 ENRDLLNNLIvmkANSGGIVLLSSH 181
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-235 |
5.90e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.85 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 19 FDDLSLAISNHEKIgLVGINGTGKSTLLKVMGGIdddftgdITHPNQYRIRYS--SQKQDLDGNLSVFEAVLSSETSTL- 95
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLL-------LGPSSSRKFDEEdfYLGDDPDLPEIEIELTFGSLLSRLl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 96 ------QIIKHYEQAVQQYTvEQTDRNFQAMMAAQEAMDRHEAWDYNAEIK-------TILSKLGIH---DTTKQVNSLS 159
Cdd:COG3593 86 rlllkeEDKEELEEALEELN-EELKEALKALNELLSEYLKELLDGLDLELElsldeleDLLKSLSLRiedGKELPLDRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 160 GGQQKRVVLA--KTLIE-----QPDLLLLDEPTNHLDFESINWLINYVKQY---PYTVLFVTHDRYFLNEV---STRIVE 226
Cdd:COG3593 165 SGFQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELsekPNQVIITTHSPHLLSEVpleNIRRLR 244
|
....*....
gi 488422749 227 LDRGKLTTY 235
Cdd:COG3593 245 RDSGGTTST 253
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
333-479 |
5.90e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 333 LFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQ--QFEGTLKIGQTVKV--------AYFKQT-----EETLNRDI 397
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKqetfarisGYCEQNdihspQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 RMIDYLREESEVAKEKDGTTV-SITQLLERFLFPSSTHG-KKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:PLN03140 975 IYSAFLRLPKEVSKEEKMMFVdEVMELVELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
....
gi 488422749 476 LTIL 479
Cdd:PLN03140 1055 AAIV 1058
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-191 |
6.48e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.19 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 7 EHLNKSYADKV-IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRySSQKQDLDGNLS-VF 84
Cdd:PRK13657 338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT-DIR-TVTRASLRRNIAvVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 -EAVLSSET--STLQIIKhyeqavqqytveqTDRNFQAMMAAQEamdRHEAWDYnaeiktILSKLGIHDTT--KQVNSLS 159
Cdd:PRK13657 416 qDAGLFNRSieDNIRVGR-------------PDATDEEMRAAAE---RAQAHDF------IERKPDGYDTVvgERGRQLS 473
|
170 180 190
....*....|....*....|....*....|..
gi 488422749 160 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE 191
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
336-495 |
6.49e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 47.49 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 336 DITQIIQSGQRIGIVGPNGAGKTTMLNIL-------SGE---DQQ-----------------------FEGTLK-----I 377
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALfrlvelsSGSiliDGVdiskiglhdlrsrisiipqdpvlFSGTIRsnldpF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 378 GQtvkvayfkQTEETLNRDIRMIdYLREESEVAKEKDGTTVsitqllerflfpssTHGKKIykLSGGEQKRLYLLRLLVH 457
Cdd:cd03244 102 GE--------YSDEELWQALERV-GLKEFVESLPGGLDTVV--------------EEGGEN--LSVGQRQLLCLARALLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488422749 458 QPNVLLLDEPTNDLDTETLTILEDYIASF--GGSVITVSH 495
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-233 |
8.20e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 19 FDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNQyRIRYSSQKQDLDGNLsVF------------EA 86
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK-EINALSTAQRLARGL-VYlpedrqssglylDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 87 VLSSETSTLQiikHYEQAVQQYTveqtdrnfqammaAQEA--MDRHEAwdynaeiktilsKLGI--HDTTKQVNSLSGGQ 162
Cdd:PRK15439 357 PLAWNVCALT---HNRRGFWIKP-------------ARENavLERYRR------------ALNIkfNHAEQAARTLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 163 QKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQYPYTVLFVTHDryfLNEV---STRIVELDRGKLT 233
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSArndIYQLIRSIAAQNVAVLFISSD---LEEIeqmADRVLVMHQGEIS 482
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-184 |
8.77e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.84 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 6 IEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG-IDDD-----FTGDiTHPNQYRIR-YSSQKQ--- 75
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDhgeilFDGE-NIPAMSRSRlYTVRKRmsm 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 76 -----DLDGNLSVFEAV---LSSETstlqiikHYEQAVQQYTVeqtdrnfqaMMAaqeamdrheawdynaeiktiLSKLG 147
Cdd:PRK11831 89 lfqsgALFTDMNVFDNVaypLREHT-------QLPAPLLHSTV---------MMK--------------------LEAVG 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 488422749 148 IHDTTKQVNS-LSGGQQKRVVLAKTLIEQPDLLLLDEP 184
Cdd:PRK11831 133 LRGAAKLMPSeLSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-192 |
1.13e-05 |
|
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: 47.23 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 18 IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHpNQYRIRYSSQkQDLDGNLSVF--EAVLSSETSTL 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGHDVRDYTL-ASLRRQIGLVsqDVFLFNDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 96 QIIKHYEQAvqqyTVEQTDRNFQAMMAAQEAMDRHEAWDynaeikTILSKLGIhdttkqvnSLSGGQQKRVVLAKTLIEQ 175
Cdd:cd03251 95 NIAYGRPGA----TREEVEEAARAANAHEFIMELPEGYD------TVIGERGV--------KLSGGQRQRIAIARALLKD 156
|
170
....*....|....*..
gi 488422749 176 PDLLLLDEPTNHLDFES 192
Cdd:cd03251 157 PPILILDEATSALDTES 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-265 |
1.36e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.72 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 21 DLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDG-NLSVFEAVLSSETSTLQIIK 99
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL---------------IDGvDIAKISDAELREVRRKKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 100 HYEQ-AVQQYTVEQTDRNFQAMMAAQEAMDRHEawdynaEIKTILSKLGIHDTTKQV-NSLSGGQQKRVVLAKTLIEQPD 177
Cdd:PRK10070 111 VFQSfALMPHMTVLDNTAFGMELAGINAEERRE------KALDALRQVGLENYAHSYpDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 178 LLLLDEPTNHLD----FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKLttypgnyedyIAMRAEKEVIE 253
Cdd:PRK10070 185 ILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV----------VQVGTPDEILN 254
|
250
....*....|..
gi 488422749 254 QKQNDKQRALYK 265
Cdd:PRK10070 255 NPANDYVRTFFR 266
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
315-496 |
1.41e-05 |
|
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: 45.89 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 315 GKQVYELDSLTktinGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayFKQTEETL 393
Cdd:cd03215 1 GEPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVT---RRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 394 NRDIRMI--DYLRE----ESEVAKekdgtTVSITQLLerflfpssthgkkiyklSGGEQKRLYLLRLLVHQPNVLLLDEP 467
Cdd:cd03215 74 RAGIAYVpeDRKREglvlDLSVAE-----NIALSSLL-----------------SGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190
....*....|....*....|....*....|....
gi 488422749 468 TNDLDTET-----LTILEdyIASFGGSVITVSHD 496
Cdd:cd03215 132 TRGVDVGAkaeiyRLIRE--LADAGKAVLLISSE 163
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
159-213 |
1.48e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 1.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFeSI-----NWLINYVKQYPYTVLFVTHD 213
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVqaqvlNLMMDLQQELGLSYVFISHD 214
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-225 |
1.56e-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: 45.64 E-value: 1.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 154 QVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE-------SINWLINYVKQypyTVLFVTHDRYFLNEVSTRIV 225
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnaarAIRRLSEEGKK---TALVVEHDLAVLDYLSDRIH 143
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
336-472 |
1.62e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.56 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 336 DITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTL---------------KIGQTVKVAYFKQTEETLNRDIRmi 400
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatRSRNRYSVAYAAQKPWLLNATVE-- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 401 DYLREESEVAKEKDGTTVSITQL---LERFLFPSSTH-GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD 472
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLqpdIDLLPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
331-475 |
1.76e-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: 47.89 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 331 RTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGedqqF----EGTLKI-GQTVKvayfKQTEETLNRDIRM------ 399
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR----FydvtSGRILIdGQDIR----DVTQASLRAAIGIvpqdtv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 ---------IDYLR-----EESEVAKE-----------KDG--TTVSitqllERFLfpssthgkkiyKLSGGEQKRLYLL 452
Cdd:COG5265 443 lfndtiaynIAYGRpdaseEEVEAAARaaqihdfieslPDGydTRVG-----ERGL-----------KLSGGEKQRVAIA 506
|
170 180
....*....|....*....|...
gi 488422749 453 RLLVHQPNVLLLDEPTNDLDTET 475
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRT 529
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
156-227 |
1.92e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 1.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 156 NSLSGGQQKRVVLAKTLIEQPD--LLLLDEPTNHLDFESINWLINYVK---QYPYTVLFVTHDRYFLNEvSTRIVEL 227
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
325-513 |
1.95e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.65 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 325 TKTINGRTLFqditqiIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV----------KVAYFKQTEE-- 391
Cdd:PRK13647 18 TKALKGLSLS------IPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVnaenekwvrsKVGLVFQDPDdq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 392 ----TLNRDI----RMIDYLREESEVAKEKDGTTVSITQLLErflfpssthgKKIYKLSGGEQKRLYLLRLLVHQPNVLL 463
Cdd:PRK13647 92 vfssTVWDDVafgpVNMGLDKDEVERRVEEALKAVRMWDFRD----------KPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488422749 464 LDEPTNDLD---TETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:PRK13647 162 LDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
343-500 |
2.04e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 343 SGQRIGIVGPNGAGKTTMLNILSGedqqfegtlkigqtvkvayfkqteetlnrdirmidYLREESEVAKEKDGTTVSITQ 422
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR-----------------------------------ELGPPGGGVIYIDGEDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 423 LLERFLFPSsthGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET---------LTILEDYIASFGGSVITV 493
Cdd:smart00382 46 LDQLLLIIV---GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILT 122
|
....*..
gi 488422749 494 SHDRYFL 500
Cdd:smart00382 123 TNDEKDL 129
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
320-496 |
2.08e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 46.26 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQ------QFEGT------------LKIG--- 378
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRpdsgsvLFGGTdltgldeheiarLGIGrkf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 379 QTVKVaYFKQT-----EETLNRDIRMIDYLReesevAKEKDGTTVSITQLLER-FLfpssthGKKIYKLSG----GEQKR 448
Cdd:COG4674 92 QKPTV-FEELTvfenlELALKGDRGVFASLF-----ARLTAEERDRIEEVLETiGL------TDKADRLAGllshGQKQW 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488422749 449 LYLLRLLVHQPNVLLLDEPT---NDLDTE-TLTILEDyIASfGGSVITVSHD 496
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVagmTDAETErTAELLKS-LAG-KHSVVVVEHD 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
289-475 |
2.76e-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: 47.60 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 289 FNDLEANVKQQQTQDK---GELNLAYSRLgkqvyeldsltkTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILS 365
Cdd:TIGR01271 406 IGELFEKIKQNNKARKqpnGDDGLFFSNF------------SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 366 GEDQQFEGtlKIGQTVKVAYFKQTEETLNRDIR-------MIDYLREESevakekdgtTVSITQLLERF-LFPSSTH--- 434
Cdd:TIGR01271 474 GELEPSEG--KIKHSGRISFSPQTSWIMPGTIKdniifglSYDEYRYTS---------VIKACQLEEDIaLFPEKDKtvl 542
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488422749 435 GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:TIGR01271 543 GEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
158-212 |
3.06e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.17 E-value: 3.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----------FESINwlinyvKQYPYTVLFVTH 212
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemmemFYKLH------KEKGLTTVLVTH 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
326-528 |
3.13e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 326 KTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTV---KVAYFKQTEETLNRDIRMIDY 402
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYigdKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 403 LRE---------ESEVAK---EKDGT--TVSITQ-----------LLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVH 457
Cdd:PRK13631 114 LRRrvsmvfqfpEYQLFKdtiEKDIMfgPVALGVkkseakklakfYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 458 QPNVLLLDEPTNDLD----TETLTILEDYIASfGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIVGSFEDYETY 528
Cdd:PRK13631 194 QPEILIFDEPTAGLDpkgeHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKG---KILKTGTPYEIF 264
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
336-516 |
3.21e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.19 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 336 DITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI------GQTVKVAYFKQT-------------EETLNRD 396
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgvditDKKVKLSDIRKKvglvfqypeyqlfEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 397 IRM--IDYLREESEVaKEKDGTTVSITQL-LERFLfpssthGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD- 472
Cdd:PRK13637 105 IAFgpINLGLSEEEI-ENRVKRAMNIVGLdYEDYK------DKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDp 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488422749 473 ---TETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDGMME 516
Cdd:PRK13637 178 kgrDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
320-504 |
3.31e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG--EDQQFEGTLKI-GQTVKVAYFKQTEET---- 392
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFeGEELQASNIRDTERAgiai 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 393 ------------------LNRDIR---MIDYLREESEVAKekdgttvsitqLLERFLFPSSTHgKKIYKLSGGEQKRLYL 451
Cdd:PRK13549 87 ihqelalvkelsvlenifLGNEITpggIMDYDAMYLRAQK-----------LLAQLKLDINPA-TPVGNLGLGQQQLVEI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 452 LRLLVHQPNVLLLDEPTNDL---DTETL-TILEDyIASFGGSVITVSHDryfLNKVA 504
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLtesETAVLlDIIRD-LKAHGIACIYISHK---LNEVK 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
157-192 |
4.02e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 4.02e-05
10 20 30
....*....|....*....|....*....|....*.
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES 192
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-232 |
4.15e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.84 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 12 SYAD-KVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIdddftgdithpnqyrIRYSSQKQDLDGnlsvfEAVLSS 90
Cdd:PRK13639 10 SYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI---------------LKPTSGEVLIKG-----EPIKYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 91 ETSTLQIIKHYEQAVQQY-------TVEQtDRNFQAM---MAAQEAMDRheawdynaeIKTILSKLGIHDTTKQV-NSLS 159
Cdd:PRK13639 70 KKSLLEVRKTVGIVFQNPddqlfapTVEE-DVAFGPLnlgLSKEEVEKR---------VKEALKAVGMEGFENKPpHHLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 160 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:PRK13639 140 GGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-213 |
4.57e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKS-TLLKVMGGIDDDftGDIThpnqyrirySSQKqdLDGNlsvfeavlssetstlQII 98
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAN--GRIG---------GSAT--FNGR---------------EIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 99 KHYEQAVQQYTVEQTDRNFQAMMAA-----------------QEAMDRHEAWDynaEIKTILSKLGIHDTTKQVN----S 157
Cdd:PRK09473 85 NLPEKELNKLRAEQISMIFQDPMTSlnpymrvgeqlmevlmlHKGMSKAEAFE---ESVRMLDAVKMPEARKRMKmyphE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESINWLINYVK-QYPYTVLFVTHD 213
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqAQIMTLLNELKrEFNTAIIMITHD 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
433-500 |
4.91e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 4.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488422749 433 THGKKIYKLSGGEQKRLYLLR-LLVHQPNVL-LLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFL 500
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLASeLFSEPPGTLfILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVL 152
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
422-513 |
5.07e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 422 QLLERFLFPSSThGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRY 498
Cdd:NF000106 127 ELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrdGATVLLTTQYME 205
|
90
....*....|....*
gi 488422749 499 FLNKVAQEYWFIHDG 513
Cdd:NF000106 206 EAEQLAHELTVIDRG 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-202 |
5.48e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.56 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 18 IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDF---TGDITHPNQyriryssqkqDLDGNLSVF--EAVLSSET 92
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGI----------PYKEFAEKYpgEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 93 STlqiikHyeqaVQQYTVEQTdrnfqammaaqeamdrheawdynaeIKTILSKLGiHDTtkqVNSLSGGQQKRVVLAKTL 172
Cdd:cd03233 92 DV-----H----FPTLTVRET-------------------------LDFALRCKG-NEF---VRGISGGERKRVSIAEAL 133
|
170 180 190
....*....|....*....|....*....|
gi 488422749 173 IEQPDLLLLDEPTNHLDFESINWLINYVKQ 202
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRT 163
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
441-495 |
5.75e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 5.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 441 LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGG----SVITVSH 495
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1417
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
341-496 |
5.97e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYfKQTEETLNRDIRMI---------------DYLR 404
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKAD-PEAQKLLRQKIQIVfqnpygslnprkkvgQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 405 EESEV-----AKEKdgtTVSITQLLERFLFPSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TET 475
Cdd:PRK11308 117 EPLLIntslsAAER---REKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvsvqAQV 193
|
170 180
....*....|....*....|.
gi 488422749 476 LTILEDYIASFGGSVITVSHD 496
Cdd:PRK11308 194 LNLMMDLQQELGLSYVFISHD 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
403-495 |
6.15e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 403 LREESEVAKEKDGTTVSITQLLERFL--FPSSTH---GKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLT 477
Cdd:PTZ00265 537 MRKNYQTIKDSEVVDVSKKVLIHDFVsaLPDKYEtlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
90 100
....*....|....*....|..
gi 488422749 478 ILEDYIASFGGS----VITVSH 495
Cdd:PTZ00265 617 LVQKTINNLKGNenriTIIIAH 638
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-244 |
6.34e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.17 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 14 ADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdLDG-NLSVFEavLSSET 92
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL---------------LDGhDLRDYT--LASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 93 STLQIIkhyEQAV----------------QQYTVEQTDRnfQAMMAaqEAMDRHEAWDYNaeIKTILSKLGIhdttkqvn 156
Cdd:PRK11176 417 NQVALV---SQNVhlfndtianniayartEQYSREQIEE--AARMA--YAMDFINKMDNG--LDTVIGENGV-------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVkQYPYTVLFVTHdRYFLNEVSTRIVELDRGKLT 233
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESeraIQAALDEL-QKNRTSLVIAH-RLSTIEKADEILVVEDGEIV 557
|
250
....*....|.
gi 488422749 234 TYpGNYEDYIA 244
Cdd:PRK11176 558 ER-GTHAELLA 567
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-189 |
8.01e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.06 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 18 IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNqyRIRYSSQ---------KQDLDGNLSVFEAVL 88
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQtswimpgtiKDNIIFGLSYDEYRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 89 SSETSTLQIikhyEQAVqqytveqtdrnfqAMMAAQEamdrheawdynaeiKTILSKLGIhdttkqvnSLSGGQQKRVVL 168
Cdd:TIGR01271 519 TSVIKACQL----EEDI-------------ALFPEKD--------------KTVLGEGGI--------TLSGGQRARISL 559
|
170 180
....*....|....*....|.
gi 488422749 169 AKTLIEQPDLLLLDEPTNHLD 189
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLD 580
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
341-530 |
9.89e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 44.68 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTM---LN----------ILSGEDQQFE--GTLKIGQTVKVAYFKQTEE----TLNRDIRM-- 399
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLflhFNgilkptsgevLIKGEPIKYDkkSLLEVRKTVGIVFQNPDDQlfapTVEEDVAFgp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 400 IDYLREESEVAKEkdgttvsITQLLERFLFpSSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TET 475
Cdd:PRK13639 105 LNLGLSKEEVEKR-------VKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgaSQI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 476 LTILEDyIASFGGSVITVSHDRYFLNKVAQEYWFIHDGmmeRIVGS------FEDYETYKK 530
Cdd:PRK13639 177 MKLLYD-LNKEGITIIISTHDVDLVPVYADKVYVMSDG---KIIKEgtpkevFSDIETIRK 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
441-529 |
9.96e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.38 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 441 LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD-------TETLTIL-EDYiasfggSVITVSH---------DR--YFLN 501
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDpisagkiEETLLGLkDDY------TMLLVTRsmqqasrisDRtgFFLD 222
|
90 100
....*....|....*....|....*...
gi 488422749 502 KVAQEYWFIHDGMMERIVGSFEDYETYK 529
Cdd:PRK14239 223 GDLIEYNDTKQMFMNPKHKETEDYISGK 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
436-496 |
1.00e-04 |
|
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: 44.56 E-value: 1.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488422749 436 KKIYKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-233 |
1.09e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLN-KSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTG-------DITH--PNQYR---IRYS 71
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGsirldgeDITGlsPRERRrlgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 72 S---QKQDLDGNLSVFE-AVLSSetstlqiikHYEQAVQQYTVeqtdRNFQAMMA-AQEAMDRHEawdynaeIKTIlskl 146
Cdd:COG3845 339 PedrLGRGLVPDMSVAEnLILGR---------YRRPPFSRGGF----LDRKAIRAfAEELIEEFD-------VRTP---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 147 GIHDTTKqvnSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINW----LINYVKQyPYTVLFVTHDryfLNEV-- 220
Cdd:COG3845 395 GPDTPAR---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFihqrLLELRDA-GAAVLLISED---LDEIla 467
|
250
....*....|....
gi 488422749 221 -STRIVELDRGKLT 233
Cdd:COG3845 468 lSDRIAVMYEGRIV 481
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
158-232 |
1.56e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.41 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SINWL---INyvKQYPYTVLFVTHDRYFLNEVSTRIVELDRGK 231
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSILELlkdIN--RELGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
.
gi 488422749 232 L 232
Cdd:PRK11153 219 L 219
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
341-504 |
1.59e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLkigqtvkvayfkqteetlnrdirmidylreesevakEKDGTTVSI 420
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND------------------------------------EWDGITPVY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 421 TQllerflfpssthgKKIyKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTE----TLTILEDYIASFGGSVITVSHD 496
Cdd:cd03222 66 KP-------------QYI-DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHD 131
|
....*...
gi 488422749 497 RYFLNKVA 504
Cdd:cd03222 132 LAVLDYLS 139
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-185 |
1.65e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 43.71 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 5 KIEHLNKSYADKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIThpnqyriryssqkqdldgnlsvF 84
Cdd:PRK11614 7 SFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV----------------------F 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 85 EAVLSSETSTLQIIKhyeQAVQqyTVEQTDRNFQAMMAAQE-AM-----DRHEAWDYNAEIKTILSKLgIHDTTKQVNSL 158
Cdd:PRK11614 65 DGKDITDWQTAKIMR---EAVA--IVPEGRRVFSRMTVEENlAMggffaERDQFQERIKWVYELFPRL-HERRIQRAGTM 138
|
170 180
....*....|....*....|....*..
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPT 185
Cdd:PRK11614 139 SGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
441-496 |
1.78e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.62 E-value: 1.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 441 LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGG--SVITVSHD 496
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-195 |
1.88e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.83 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 19 FDDLSLAISNHEKIG-LVGINGTGKSTLLKVMGGIDDDFTGDITHPNQYRIR---------------YSSQKQDLDGNLS 82
Cdd:COG3950 14 FEDLEIDFDNPPRLTvLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLirngefgdsaklilyYGTSRLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 83 VFEAVLSSETSTLQI-----------------IKHYEQAVQQYTVEQTDRNFQAMMAAQEAMDRHeawDYNAEIKTILSK 145
Cdd:COG3950 94 KLERLKEEYFSRLDGydslldedsnlreflewLREYLEDLENKLSDELDEKLEAVREALNKLLPD---FKDIRIDRDPGR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 146 LGIHDTTKQ---VNSLSGGQQKRVVLA--------------KTLIEQPDLLLLDEPTNHLdfeSINW 195
Cdd:COG3950 171 LVILDKNGEelpLNQLSDGERSLLALVgdlarrlaelnpalENPLEGEGIVLIDEIDLHL---HPKW 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-237 |
2.20e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 42.62 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 15 DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGG--IDDDFTGDIThpnqyriryssqkqdLDGnlsvfeavlSSET 92
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEIL---------------ING---------RPLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 93 STLQIIKHYeqavqqytVEQTDRNFqAMMAAQEAMdRHEAWdynaeiktilsklgihdttkqVNSLSGGQQKRVVLAKTL 172
Cdd:cd03232 75 KNFQRSTGY--------VEQQDVHS-PNLTVREAL-RFSAL---------------------LRGLSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 173 IEQPDLLLLDEPTNHLDFESINWLINYVKQY-------------PYTVLFVTHDRYFLnevstriveLDRGKLTTYPG 237
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLadsgqailctihqPSASIFEKFDRLLL---------LKRGGKTVYFG 192
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
341-499 |
2.32e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 341 IQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTV---KVAYFKQTEETLNRDIRMIDYLRE-ESEVAKEKDg 415
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVtaeQPEDYRKLFSAVFTDFHLFDQLLGpEGKPANPAL- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 416 ttvsITQLLERFLFPSSTH--GKKI--YKLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFG 487
Cdd:PRK10522 425 ----VEKWLERLKMAHKLEleDGRIsnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrREFYQVLLPLLQEMG 500
|
170
....*....|...
gi 488422749 488 GSVITVSH-DRYF 499
Cdd:PRK10522 501 KTIFAISHdDHYF 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-513 |
2.80e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTL------------KIGQTVKVAYFK 387
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhKLAAQLGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QTEETLNR------------------DIRMIDY--LREESEVAKEKDGTTVSITQllerflfpssthgkKIYKLSGGEQK 447
Cdd:PRK09700 87 QELSVIDEltvlenlyigrhltkkvcGVNIIDWreMRVRAAMMLLRVGLKVDLDE--------------KVANLSISHKQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488422749 448 RLYLLRLLVHQPNVLLLDEPTNDL---DTETLTILEDYIASFGGSVITVSHDRYFLNKVAQEYWFIHDG 513
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
159-232 |
2.96e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 2.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 159 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQYPYTVLFVTHDRYFLNEVSTRIVELDRGKL 232
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
316-539 |
3.38e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.71 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 316 KQVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGE--------DQQFEGTlKIGQtvkvayfK 387
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaykilegDILFKGE-SILD-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 388 QTEETLNRDIRM-------------IDYLR------------------EESEVAKEKdgttVSITQLLERFLFPSSTHGk 436
Cdd:CHL00131 77 EPEERAHLGIFLafqypieipgvsnADFLRlaynskrkfqglpeldplEFLEIINEK----LKLVGMDPSFLSRNVNEG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 437 kiykLSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLNKVAQEYwfIHDG 513
Cdd:CHL00131 152 ----FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLLDYIKPDY--VHVM 225
|
250 260
....*....|....*....|....*.
gi 488422749 514 MMERIVgsfedyetykKEKDKQLAIE 539
Cdd:CHL00131 226 QNGKII----------KTGDAELAKE 241
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-61 |
3.83e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 3.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488422749 20 DDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDIT 61
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
441-531 |
3.84e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.52 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 441 LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGG--SVITVSHDRYFLNKVAQEYWFIHDGMMERI 518
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
90
....*....|...
gi 488422749 519 VGSFEDYETYKKE 531
Cdd:PRK14267 230 GPTRKVFENPEHE 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-189 |
4.51e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.54 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 18 IFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHPNqyRIRYSSQ---------KQDLDGNLSVFEAvl 88
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQfswimpgtiKENIIFGVSYDEY-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 89 ssetstlqiikHYEQAVQQYTVEQTDRNFqammAAQEamdrheawdynaeiKTILSKLGIhdttkqvnSLSGGQQKRVVL 168
Cdd:cd03291 128 -----------RYKSVVKACQLEEDITKF----PEKD--------------NTVLGEGGI--------TLSGGQRARISL 170
|
170 180
....*....|....*....|.
gi 488422749 169 AKTLIEQPDLLLLDEPTNHLD 189
Cdd:cd03291 171 ARAVYKDADLYLLDSPFGYLD 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-202 |
4.79e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 4.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488422749 145 KLGIHDTTkqvnsLSGGQQKRVVLAKTLIEQ---PDLLLLDEPTNHLDFESINWLINYVKQ 202
Cdd:TIGR00630 822 RLGQPATT-----LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQR 877
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-221 |
5.73e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.07 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 15 DKVIFDDLSLAISNHEKIGLVGINGTGKSTLLKVMGGIDDDFTGDITHpNQYRIRYSSQKQDLDGNLSVFEAVLSSETST 94
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-DDITITHKTKDKYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 95 LqiikhYEQAVQQyTVEQTDRNFQamMAAQEAMDRheAWDynaeiktILSKLGIHDTTKQVN--SLSGGQQKRVVLAKTL 172
Cdd:PRK13646 98 L-----FEDTVER-EIIFGPKNFK--MNLDEVKNY--AHR-------LLMDLGFSRDVMSQSpfQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488422749 173 IEQPDLLLLDEPTNHLDFESINWLINYVKQYPY----TVLFVTHDryfLNEVS 221
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdenkTIILVSHD---MNEVA 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
320-480 |
5.80e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 42.37 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGR----TLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKvayfKQTEETLN 394
Cdd:COG1135 3 ELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVdGVDLT----ALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 ---RDIRMI---DYLREESEVA-----------KEKDGTTVSITQLLE-------RFLFPSsthgkkiyKLSGGEQKRLY 450
Cdd:COG1135 79 aarRKIGMIfqhFNLLSSRTVAenvalpleiagVPKAEIRKRVAELLElvglsdkADAYPS--------QLSGGQKQRVG 150
|
170 180 190
....*....|....*....|....*....|.
gi 488422749 451 LLRLLVHQPNVLLLDEPTNDLDTE-TLTILE 480
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPEtTRSILD 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
315-472 |
6.31e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 315 GKQVYELDSltktingRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVkvAYFKQTEETLN 394
Cdd:PTZ00243 664 TDDFFELEP-------KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSI--AYVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIR-MIDYLREESEvAKEKDGTTVS-----ITQL---LErflfpsSTHGKKIYKLSGGEQKRLYLLRLLVHQPNVLLLD 465
Cdd:PTZ00243 735 ATVRgNILFFDEEDA-ARLADAVRVSqleadLAQLgggLE------TEIGEKGVNLSGGQKARVSLARAVYANRDVYLLD 807
|
....*..
gi 488422749 466 EPTNDLD 472
Cdd:PTZ00243 808 DPLSALD 814
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
158-233 |
6.85e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESINWLINYVKQyPYTVLFVTHDryfLNEV---STRIVELDRG 230
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgakhEIYNVIYELAAQ-GVAVLFVSSD---LPEVlgvADRIVVMREG 472
|
...
gi 488422749 231 KLT 233
Cdd:PRK11288 473 RIA 475
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-496 |
7.11e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 41.90 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 335 QDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKI-GQTVKVAYFKQTEE----------------TLNRDI 397
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKkigiifqnpdnqfigaTVEDDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 398 ------RMIDylREE-----SEVAKEkdgttVSITQLLERflfpssthgkKIYKLSGGEQKRLYLLRLLVHQPNVLLLDE 466
Cdd:PRK13632 106 afglenKKVP--PKKmkdiiDDLAKK-----VGMEDYLDK----------EPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190
....*....|....*....|....*....|....
gi 488422749 467 PTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:PRK13632 169 STSMLDpkgkREIKKIMVDLRKTRKKTLISITHD 202
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
320-521 |
8.45e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG-----------------------EDQQFEGTLK 376
Cdd:PRK09580 3 SIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredyevtggtvefkgkdllelspEDRAGEGIFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 377 IGQ------TVKVAYFKQTEETLNRDIRMIDYLR--EESEVAKEKdgttVSITQLLERFLFPSSTHGkkiykLSGGEQKR 448
Cdd:PRK09580 83 AFQypveipGVSNQFFLQTALNAVRSYRGQEPLDrfDFQDLMEEK----IALLKMPEDLLTRSVNVG-----FSGGEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 449 LYLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASFGG---SVITVSHDRYFLNKVAQEywFIHDGMMERIVGS 521
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgkrSFIIVTHYQRILDYIKPD--YVHVLYQGRIVKS 227
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
157-218 |
8.79e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 8.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488422749 157 SLSGGQQK------RVVLAKTLIEQPDLLLLDEPTNHLDFESINW----LINYVK-QYPYTVLFVTHDRYFLN 218
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeIIEERKsQKNFQLIVITHDEELVD 187
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
134-232 |
9.81e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 134 DYNAEIKTILSKLGIHDTT-KQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWLINYVKQY---PYTVLF 209
Cdd:NF000106 120 DARARADELLERFSLTEAAgRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrdGATVLL 199
|
90 100
....*....|....*....|...
gi 488422749 210 VTHDRYFLNEVSTRIVELDRGKL 232
Cdd:NF000106 200 TTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
126-198 |
1.14e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.06 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 126 AMDRHEAWDYNAEIKTILSKLgihDTTKQVN-----------SLSGGQQKRVVLAKTLIEQ---PDLLLLDEPTNHLDFE 191
Cdd:cd03271 130 DMTVEEALEFFENIPKIARKL---QTLCDVGlgyiklgqpatTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFH 206
|
....*..
gi 488422749 192 SINWLIN 198
Cdd:cd03271 207 DVKKLLE 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
153-244 |
1.99e-03 |
|
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: 41.47 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 153 KQVNsLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESINWLINYVKQypYTVLFVTHDRYFLNEVSTRIV 225
Cdd:TIGR00957 757 KGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYLPQVDVIIV 833
|
90
....*....|....*....
gi 488422749 226 eLDRGKLTTYpGNYEDYIA 244
Cdd:TIGR00957 834 -MSGGKISEM-GSYQELLQ 850
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
137-241 |
2.12e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.92 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 137 AEIKTILSKLGIHDTTKQVNSLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---INWLINYVKQYPYTVLFVTHD 213
Cdd:PRK09700 389 AENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVSSE 468
|
90 100
....*....|....*....|....*...
gi 488422749 214 RYFLNEVSTRIVELDRGKLTTYPGNYED 241
Cdd:PRK09700 469 LPEIITVCDRIAVFCEGRLTQILTNRDD 496
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
315-476 |
2.15e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 315 GKQVYELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGQTVKVA---------- 384
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpakahqlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 385 -YFKQTEETL--NRDIRM-IDYLREESEVAKEKdgttvsITQLLERF---LFPSSTHGkkiyKLSGGEQKRLYLLRLLVH 457
Cdd:PRK15439 88 iYLVPQEPLLfpNLSVKEnILFGLPKRQASMQK------MKQLLAALgcqLDLDSSAG----SLEVADRQIVEILRGLMR 157
|
170 180
....*....|....*....|..
gi 488422749 458 QPNVLLLDEPTNDL---DTETL 476
Cdd:PRK15439 158 DSRILILDEPTASLtpaETERL 179
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
317-496 |
2.23e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.48 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 317 QVYELDSLTKTINGR-TLFQDITQIIQSGQRIGIVGPNGAGKT----TMLNILS-----GEDQQFEG----TLKIGQTVK 382
Cdd:PRK09473 14 DVKDLRVTFSTPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriGGSATFNGreilNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 383 V------AYFKQTEETLNRDIRMIDYLREESEVAKEKDGTTV---SItQLLERFLFPSSTHGKKIY--KLSGGEQKRLYL 451
Cdd:PRK09473 94 LraeqisMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAfeeSV-RMLDAVKMPEARKRMKMYphEFSGGMRQRVMI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488422749 452 LRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD 496
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
158-213 |
3.50e-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: 38.49 E-value: 3.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488422749 158 LSGGQQKRVVLAKTLIEQP----DLLLLDEPTNHLDFESINWLINYVKQY---PYTVLFVTHD 213
Cdd:cd03227 78 LSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHL 140
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
158-189 |
3.70e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 40.19 E-value: 3.70e-03
10 20 30
....*....|....*....|....*....|..
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
136-230 |
3.83e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 136 NAEIKTILSKLGIHDTTKQVNSLSGGQQKRVVLAKTLIEQ--PDLLLLDEPTNHLD---------FESINWLINYVKQYP 204
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKlkPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKN 116
|
90 100 110
....*....|....*....|....*....|.
gi 488422749 205 YTVLFVTHDRYFLNE-----VSTRIVELDRG 230
Cdd:smart00382 117 LTVILTTNDEKDLGPallrrRFDRRIVLLLI 147
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
157-217 |
3.94e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 39.24 E-value: 3.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 157 SLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESINWL-----INYVKQYPYTVLFVTHDRYFL 217
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmqegiLKFLQDDKRTLVLVTHKLQYL 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
441-504 |
4.43e-03 |
|
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: 39.65 E-value: 4.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488422749 441 LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLD----TETLTILEDYIASFGGSVITVSHD----RYFLNKVA 504
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHDlgvvAEIADRVA 222
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
338-367 |
4.88e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 39.76 E-value: 4.88e-03
10 20 30
....*....|....*....|....*....|
gi 488422749 338 TQIIQSGQRIGIVGPNGAGKTTMLNILSGE 367
Cdd:COG4962 176 RAAVRARLNILVSGGTGSGKTTLLNALSGF 205
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
435-504 |
4.97e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 4.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488422749 435 GKKIYKLSGGEQKRL---YLLRLLVHQPNVLLLDEPTNDLDTETLTILEDYIASF---GGSVITVSHDRYFLnKVA 504
Cdd:PRK00635 804 GRPLSSLSGGEIQRLklaYELLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLthqGHTVVIIEHNMHVV-KVA 878
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
320-366 |
6.90e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 6.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488422749 320 ELDSLTKTINGRTLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSG 366
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
157-218 |
7.36e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 7.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488422749 157 SLSGGQQK---RVVLAKTLIEQPDLLLLDEPTNHLDFESINWL---INYVKQYPYTVLFVTHDRYFLN 218
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLlelLKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
441-475 |
7.64e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 39.23 E-value: 7.64e-03
10 20 30
....*....|....*....|....*....|....*
gi 488422749 441 LSGGEQKRLYLLRLLVHQPNVLLLDEPTNDLDTET 475
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
320-480 |
8.07e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.01 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 320 ELDSLTKTINGR----TLFQDITQIIQSGQRIGIVGPNGAGKTTMLNILSGEDQQFEGTLKIGqTVKVAYFKQTEETL-N 394
Cdd:PRK11153 3 ELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD-GQDLTALSEKELRKaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488422749 395 RDIRMID---YLREESEVA-----------KEKDGTTVSITQLLERFlfpSSTHGKKIY--KLSGGEQKRLYLLRLLVHQ 458
Cdd:PRK11153 82 RQIGMIFqhfNLLSSRTVFdnvalplelagTPKAEIKARVTELLELV---GLSDKADRYpaQLSGGQKQRVAIARALASN 158
|
170 180
....*....|....*....|...
gi 488422749 459 PNVLLLDEPTNDLDTETL-TILE 480
Cdd:PRK11153 159 PKVLLCDEATSALDPATTrSILE 181
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
158-189 |
8.39e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 38.67 E-value: 8.39e-03
10 20 30
....*....|....*....|....*....|..
gi 488422749 158 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 189
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-227 |
8.94e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 8.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488422749 157 SLSGGQQKRVVLAKTLI---EQPDLLLLDEPTNHLDFESINWLINYVKQYPY---TVLFVTHDRYFLnEVSTRIVEL 227
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHqghTVVIIEHNMHVV-KVADYVLEL 884
|
|
| |
