|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-521 |
3.01e-102 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 317.39 E-value: 3.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFAtGQTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPADGHIERA--ASIAWVAQQPNVTPEMTL- 87
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRiGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkgLRIGYLPQEPPLDDDLTVl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 88 -AALLGYAPIFDALSRLEQGQVLAAD--------------FDLLDGhWDLPDRLS-----LAFREADLppfsaDRPVFSL 147
Cdd:COG0488 80 dTVLDGDAELRALEAELEELEAKLAEpdedlerlaelqeeFEALGG-WEAEARAEeilsgLGFPEEDL-----DRPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 148 SGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGN 226
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVaTRILELDRGKLTLYPGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 227 YDEYQRQRmAEQQAARAAlehavtERRRTRARMQKEHDAAQRRSAQtlrtvdtlniASfervKYKgAAKERPGALRRqhr 306
Cdd:COG0488 234 YSAYLEQR-AERLEQEAA------AYAKQQKKIAKEEEFIRRFRAK----------AR----KAK-QAQSRIKALEK--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 307 eqnssLNAAVQQARERveeetPVMFTLPGSEvAAGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGC 378
Cdd:COG0488 289 -----LEREEPPRRDK-----TVEIRFPPPE-RLGKKVLELEGLSksygdktlLDD-----LSLRIDRGDRIGLIGPNGA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 379 gkttllktllgLEQAASGDVRL--SVSAAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSA 456
Cdd:COG0488 353 gkstllkllagELEPDSGTVKLgeTVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGV 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694069477 457 LSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGL 521
Cdd:COG0488 433 LSGGEKARLALAKLLLS--PPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRV 495
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
39-533 |
1.07e-51 |
|
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: 185.14 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERA--ASIAWVAQQPNVTPEMTL--AALLGYAPIFDALSRLEQgqVLA---- 110
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgIKVGYLPQEPQLDPTKTVreNVEEGVAEIKDALDRFNE--ISAkyae 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 111 --ADFDLL--------------DGhWDLPDRLSLAFREADLPPFsaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:TIGR03719 113 pdADFDKLaaeqaelqeiidaaDA-WDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 175 NHLDRQGREWLYHQLESWQGGALIASHDRELLTRMPR-IIELTPTALRSYGGNYDEYqrqrmAEQQAARAALEhAVTERR 253
Cdd:TIGR03719 190 NHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGwILELDRGRGIPWEGNYSSW-----LEQKQKRLEQE-EKEESA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 254 RTRArMQKEHDAAqRRSAQTLRTVDTLNIASFERVkykgaakerpgalrrqhreqnssLNAAVQQARERVEeetpvMFTL 333
Cdd:TIGR03719 264 RQKT-LKRELEWV-RQSPKGRQAKSKARLARYEEL-----------------------LSQEFQKRNETAE-----IYIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 334 PGSEVaaGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRL--SVS 403
Cdd:TIGR03719 314 PGPRL--GDKVIEAENLTkafgdkllIDD-----LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 404 AAYLDQHLTQLDLSLSVMAHLSledtpldEGLLRTRLAQLQL------------GADKVTLpLSALSGGERLKAALACVL 471
Cdd:TIGR03719 387 LAYVDQSRDALDPNKTVWEEIS-------GGLDIIKLGKREIpsrayvgrfnfkGSDQQKK-VGQLSGGERNRVHLAKTL 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694069477 472 wrREPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGLKlTHSLAWRETS 533
Cdd:TIGR03719 459 --KSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIA-THILAFEGDS 517
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-517 |
1.26e-46 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 172.44 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAG---LDspaDGHI--ERAASIAWVAQQPNVTPEMT--------LAALLGYAPIFDALSR---- 102
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGevlLD---DGRIiyEQDLIVARLQQDPPRNVEGTvydfvaegIEEQAEYLKRYHDISHlvet 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 103 ------LEQGQVLAADFDLLDGhWDLPDRLSLAFREADLPPfsaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:PRK11147 111 dpseknLNELAKLQEQLDHHNL-WQLENRINEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 177 LDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTALRSYGGNYDEY-----QRQRMAEQQAA---RAALEH 247
Cdd:PRK11147 187 LDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMAtRIVDLDRGKLVSYPGNYDQYllekeEALRVEELQNAefdRKLAQE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 248 AVTERRRTRARmqkehdaaqrrsaqtlRTVDtlniasfE-RVKykgAAKerpgALRRQHREQNSSLNAAVQQarerVEEE 326
Cdd:PRK11147 267 EVWIRQGIKAR----------------RTRN-------EgRVR---ALK----ALRRERSERREVMGTAKMQ----VEEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 327 TpvmftlpgsevAAGKQVLVVESLqldhapaaplNWRIDGPM-------------RIALKGPNGCGKTTLLKTLLGLEQA 393
Cdd:PRK11147 313 S-----------RSGKIVFEMENV----------NYQIDGKQlvkdfsaqvqrgdKIALIGPNGCGKTTLLKLMLGQLQA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 394 ASGDVR----LSVsaAYLDQHLTQLDLSLSVMAHLSL-EDTPLDEGLLRTRLAQLQ--LGADKVTL-PLSALSGGERLKA 465
Cdd:PRK11147 372 DSGRIHcgtkLEV--AYFDQHRAELDPEKTVMDNLAEgKQEVMVNGRPRHVLGYLQdfLFHPKRAMtPVKALSGGERNRL 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 694069477 466 ALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAF 517
Cdd:PRK11147 450 LLARLFLK--PSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-536 |
5.53e-44 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 163.75 E-value: 5.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERA--ASIAWVAQQPNVTPEMTL--AALLGYAPIFDALSRL----------- 103
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARPApgIKVGYLPQEPQLDPEKTVreNVEEGVAEVKAALDRFneiyaayaepd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 104 --------EQGQvLAADFDLLDGhWDLPDRLSLAfreAD---LPPfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDE 172
Cdd:PRK11819 117 adfdalaaEQGE-LQEIIDAADA-WDLDSQLEIA---MDalrCPP--WDAKVTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 173 PTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMPR-IIELTPTALRSYGGNYDEYqrqrmAEQQAARAALEhAVTE 251
Cdd:PRK11819 190 PTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGwILELDRGRGIPWEGNYSSW-----LEQKAKRLAQE-EKQE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 252 RRRTRArMQKEHD-----AAQRRSAQTLRtvdtlnIASFErvkykgaakerpgalrrqhreqnsSLNAAVQQARERVEEe 326
Cdd:PRK11819 264 AARQKA-LKRELEwvrqsPKARQAKSKAR------LARYE------------------------ELLSEEYQKRNETNE- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 327 tpvMFTLPGSEVaaGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDV 398
Cdd:PRK11819 312 ---IFIPPGPRL--GDKVIEAENLSksfgdrllIDD-----LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 399 RL--SVSAAYLDQHLTQLDLSLSVMAHLSledtpldEGLLRTRLAQLQL------------GAD---KVtlplSALSGGE 461
Cdd:PRK11819 382 KIgeTVKLAYVDQSRDALDPNKTVWEEIS-------GGLDIIKVGNREIpsrayvgrfnfkGGDqqkKV----GVLSGGE 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 462 RLKAALACVLwrREPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGLKlTHSLAWRETS-WHF 536
Cdd:PRK11819 451 RNRLHLAKTL--KQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIA-THILAFEGDSqVEW 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-519 |
1.98e-43 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 163.42 E-value: 1.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERAA--SIAWVAQQpnvTPEMTLAALlGYAPIFDALSRLEQGQVLAADfDLL 116
Cdd:PRK10636 31 GLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQE---TPALPQPAL-EYVIDGDREYRQLEAQLHDAN-ERN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 117 DGH--------------WDLPDRLS-----LAFREADLppfsaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHL 177
Cdd:PRK10636 106 DGHaiatihgkldaidaWTIRSRAAsllhgLGFSNEQL-----ERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 178 DRQGREWLYHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGNYDEYQRQR---MAEQQA------ARAALEH 247
Cdd:PRK10636 181 DLDAVIWLEKWLKSYQGTLILISHDRDFLDPIvDKIIHIEQQSLFEYTGNYSSFEVQRatrLAQQQAmyesqqERVAHLQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 248 AVTERRRTRARMQKEhdaAQRRsaqtlrtvdtlnIASFERVKYKGAAK-ERPgaLRRQHREQNSSLNaavqqarerveee 326
Cdd:PRK10636 261 SYIDRFRAKATKAKQ---AQSR------------IKMLERMELIAPAHvDNP--FHFSFRAPESLPN------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 327 tPVmftLPGSEVAAG-KQVLVVESLQLDHAPAAplnwridgpmRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VS 403
Cdd:PRK10636 311 -PL---LKMEKVSAGyGDRIILDSIKLNLVPGS----------RIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgIK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 404 AAYLDQH-LTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLWRRepAQLLLL 482
Cdd:PRK10636 377 LGYFAQHqLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQR--PNLLLL 454
|
490 500 510
....*....|....*....|....*....|....*..
gi 694069477 483 DEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLR 491
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-520 |
3.62e-36 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 143.08 E-value: 3.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLA---------------------GLDSPA-----DGHIERA----ASIAWVAQQPNVTPEMTLA 88
Cdd:PLN03073 207 GLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvGDDTTAlqcvlNTDIERTqlleEEAQLVAQQRELEFETETG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 89 AllGYAPIFDALSRLEQGQVLAADFDLLDghwdLPDRLSLAFREADLPP---FSAD---RPVFSLSGGERMKALLCGAFV 162
Cdd:PLN03073 287 K--GKGANKDGVDKDAVSQRLEEIYKRLE----LIDAYTAEARAASILAglsFTPEmqvKATKTFSGGWRMRIALARALF 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 163 SGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELL-TRMPRIIELTPTALRSYGGNYDEYQRQRMAEQQAA 241
Cdd:PLN03073 361 IEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLnTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQ 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 242 RAALEhavtERRRTRARMQKEHDAAqRRSAQTLRTVDTlNIASFERVKYKGAAKERPGalrrqhreqnsslnaavqqare 321
Cdd:PLN03073 441 QKAFE----SNERSRSHMQAFIDKF-RYNAKRASLVQS-RIKALDRLGHVDAVVNDPD---------------------- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 322 rveeetpVMFTLPGSEVAAGKQVLVVESLQLDHaPAAP-----LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASG 396
Cdd:PLN03073 493 -------YKFEFPTPDDRPGPPIISFSDASFGY-PGGPllfknLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 397 DVRLSVS---AAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLWR 473
Cdd:PLN03073 565 TVFRSAKvrmAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK 644
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 694069477 474 RepAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQG 520
Cdd:PLN03073 645 K--PHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG 689
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-233 |
2.35e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 133.27 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERAA--SIAWVAQ-QPNVTPEMTLaallgyapiF 97
Cdd:COG0488 327 DKTLLDDLSLRIDRgDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvKIGYFDQhQEELDPDKTV---------L 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 98 DALSRLEQG-------QVLAadfDLLdghwdlpdrlslaFREADlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLL 170
Cdd:COG0488 398 DELRDGAPGgteqevrGYLG---RFL-------------FSGDD-----AFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694069477 171 DEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGNYDEYQRQ 233
Cdd:COG0488 457 DEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVaTRILEFEDGGVREYPGGYDDYLEK 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-217 |
1.16e-31 |
|
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: 119.09 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIawvaqqpnvtpemtlaaLLGYapifdal 100
Cdd:cd03221 12 GKLLLKDISLTINPgDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------------KIGY------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 101 srLEQgqvlaadfdlldghwdlpdrlslafreadlppfsadrpvfsLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:cd03221 68 --FEQ-----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190
....*....|....*....|....*....|....*...
gi 694069477 181 GREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTP 217
Cdd:cd03221 105 SIEALEEALKEYPGTVILVSHDRYFLDQVAtKIIELED 142
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-219 |
5.71e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 116.42 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIeraasiaWVAQQPNVTPEMT 86
Cdd:COG4133 1 MMLEAENLSCRRG-ERLLFSGLSFTLAAgEALALTGPNGSGKTTLLRILAGLLPPSAGEV-------LWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 87 LAALLGYAP----IFDALSRLEQGQVLAAdfdlLDGHWDLPDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFV 162
Cdd:COG4133 73 YRRRLAYLGhadgLKPELTVRENLRFWAA----LYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 163 SGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGA-LIASHDRELLTRMpRIIELTPTA 219
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHlaRGGAvLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-190 |
7.97e-27 |
|
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: 108.98 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 9 AFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAW 74
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPgEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaslsrrELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 75 VAQQPNVTPEMTLA--ALLGYAPIFDALSRLEqgqvlAADFDLLDGhwdlpdrlslAFREADLPPFsADRPVFSLSGGER 152
Cdd:COG1120 80 VPQEPPAPFGLTVRelVALGRYPHLGLFGRPS-----AEDREAVEE----------ALERTGLEHL-ADRPVDELSGGER 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 694069477 153 MKALLCGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLD------LAHQLE 175
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
150-521 |
4.79e-25 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 108.83 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 150 GERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELL----TRMPriiELTPTALRSYGG 225
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLnsvcTHMA---DLDYGELRVYPG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 226 NYDEYqrqrMaeqQAARAALEHAVTERRRTRARMQKEHDAAQRRSAQT---------LRTVDTLNIasfERVKykgaAKE 296
Cdd:PRK15064 236 NYDEY----M---TAATQARERLLADNAKKKAQIAELQSFVSRFSANAskakqatsrAKQIDKIKL---EEVK----PSS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 297 RpgalrrqhreQNSSLnaavqqareRVEEETPvMFtlpgsevaagKQVLVVESLQ--LDHAPA-APLNWRIDGPMRIALK 373
Cdd:PRK15064 302 R----------QNPFI---------RFEQDKK-LH----------RNALEVENLTkgFDNGPLfKNLNLLLEAGERLAII 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 374 GPNGCGKTTLLKTLLGLEQAASGDVRLSVSAA--YLDQ-HLTQLDLSLSVMAHLSLEDTPL-DEGLLRTRLAQLQLGADK 449
Cdd:PRK15064 352 GENGVGKTTLLRTLVGELEPDSGTVKWSENANigYYAQdHAYDFENDLTLFDWMSQWRQEGdDEQAVRGTLGRLLFSQDD 431
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 450 VTLPLSALSGGE--RLkaalacvLWRR---EPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGL 521
Cdd:PRK15064 432 IKKSVKVLSGGEkgRM-------LFGKlmmQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSL 501
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
454-519 |
6.42e-24 |
|
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: 97.52 E-value: 6.42e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 454 LSALSGGERLKAALACVLWrrEPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLL--ENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLD 131
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-215 |
1.14e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.78 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE--------RAASIAWVAQQ 78
Cdd:COG1121 5 PAIELENLTVSYG-GRPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkpprrARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 79 PNVTP-------EMTLAALLGYAPIFDALSRLEQGQVLAAdfdlldghwdLpDRLSLAfreaDLppfsADRPVFSLSGGE 151
Cdd:COG1121 84 AEVDWdfpitvrDVVLMGRYGRRGLFRRPSRADREAVDEA----------L-ERVGLE----DL----ADRPIGELSGGQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694069477 152 RMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGALIA-SHDRELLTRM-PRIIEL 215
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGKTILVvTHDLGAVREYfDRVLLL 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-220 |
1.14e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.04 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 10 FVLHQVTCQFaTGQTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPADGHI-----ERAAS--------IAWV 75
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECvAITGPSGSGKSTLLRALADLDPPTSGEIyldgkPLSAMpppewrrqVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 76 AQQPnVTPEMTLAAllgyapifdalsrleqgqVLAADFDLLDGHWDlPDRLSLAFREADLPPFSADRPVFSLSGGERMKA 155
Cdd:COG4619 80 PQEP-ALWGGTVRD------------------NLPFPFQLRERKFD-RERALELLERLGLPPDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLDRQGR----EWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTAL 220
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTrrveELLREYLAEEGRAVLWVSHDPEQIERVAdRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-175 |
1.80e-22 |
|
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: 93.48 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 26 FGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE-------------RAASIAWVAQQPNVTPEMTLAALL 91
Cdd:pfam00005 1 LKNVSLTLNPgEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 92 GYAPIFDALSRLEQGQVLAADFDLLDGhWDLPDRLslafreadlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGL-GDLADRP-------------VGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 694069477 172 EPTN 175
Cdd:pfam00005 147 EPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-215 |
2.36e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 95.29 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGqtlfgplsvslepSLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERA--------ASIAWVAQQPNVT 82
Cdd:cd03235 14 VLEDVSFEVKPG-------------EFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkplekerKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 83 P-------EMTLAALLGYAPIFDALSRLEQGQVLAAdfdlldghwdLpDRLSLAfreaDLppfsADRPVFSLSGGERMKA 155
Cdd:cd03235 81 RdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEA----------L-ERVGLS----EL----ADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTR-MPRIIEL 215
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEyFDRVLLL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-202 |
6.70e-22 |
|
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: 92.88 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIeraasiaWVAQQP-NVTPEMTLAALLGYAPifda 99
Cdd:cd03214 11 GRTVLDDLSLSIEAgEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------LLDGKDlASLSPKELARKIAYVP---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 100 lsrleqgQVLAAdFDLldghwdlpdrlslafreADLppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDr 179
Cdd:cd03214 80 -------QALEL-LGL-----------------AHL----ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD- 129
|
170 180 190
....*....|....*....|....*....|...
gi 694069477 180 qgrewLYHQLE----------SWQGGALIASHD 202
Cdd:cd03214 130 -----IAHQIEllellrrlarERGKTVVMVLHD 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-209 |
6.79e-22 |
|
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: 94.92 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFATGQTLfGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHIeraasiaWVAQQPNVTPEMTLAAL 90
Cdd:COG4555 4 VENLSKKYGKVPAL-KDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-------LIDGEDVRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 91 LGYAP----IFDALSRLEQGQVLAADFDLLDGhwDLPDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGAD 166
Cdd:COG4555 76 IGVLPdergLYDRLTVRENIRYFAELYGLFDE--ELKKRIEELIELLGLEEF-LDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 694069477 167 YLLLDEPTNHLDRQGREWLYHQLESW--QGGA-LIASHDRELLTRM 209
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALkkEGKTvLFSSHIMQEVEAL 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-237 |
3.21e-21 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 96.88 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGhieraaSIAWvaqqpnvtpemTLAALLGYAPifdal 100
Cdd:PRK15064 331 NGPLFKNLNLLLEAgERLAIIGENGVGKTTLLRTLVGELEPDSG------TVKW-----------SENANIGYYA----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 101 srleqgQVLAADFD----LLD--GHWDLPDRLSLAFReADLPP--FSAD---RPVFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:PRK15064 389 ------QDHAYDFEndltLFDwmSQWRQEGDDEQAVR-GTLGRllFSQDdikKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 170 LDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTALRSYGGNYDEYQRQRMAE 237
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLAtRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
29-202 |
1.75e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 90.51 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE----------RAA--SIAWVAQQPNVTPEMTLAALLGYap 95
Cdd:COG1131 19 VSLTVEPgEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpAEVrrRIGYVPQEPALYPDLTVRENLRF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 96 iFDALSRLEQGQVLAADFDLLDgHWDLPDRlslafreadlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:COG1131 97 -FARLYGLPRKEARERIDELLE-LFGLTDA--------------ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190
....*....|....*....|....*....|
gi 694069477 176 HLDRQGREWLYHQLESW--QGGA-LIASHD 202
Cdd:COG1131 161 GLDPEARRELWELLRELaaEGKTvLLSTHY 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
29-215 |
1.41e-18 |
|
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: 83.22 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIEraasiawVAQQPNVTPEMTLAALLGYAPifdalsrleqgq 107
Cdd:cd03230 19 ISLTVEKgEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-------VLGKDIKKEPEEVKRRIGYLP------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 108 vlaadfdlldGHWDLPDRLSLafREadlppfsadrpVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYH 187
Cdd:cd03230 80 ----------EEPSLYENLTV--RE-----------NLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|..
gi 694069477 188 QLESW--QGGA-LIASHD-RELLTRMPRIIEL 215
Cdd:cd03230 137 LLRELkkEGKTiLLSSHIlEEAERLCDRVAIL 168
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-206 |
1.04e-17 |
|
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: 81.74 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQT-LFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWV 75
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 76 AQQPN---VTPemTLAALLGYAPIFDALSRLEQGQvlaadfdlldghwdlpdRLSLAFREADLPPFsADRPVFSLSGGER 152
Cdd:cd03225 81 FQNPDdqfFGP--TVEEEVAFGLENLGLPEEEIEE-----------------RVEEALELVGLEGL-RDRSPFTLSGGQK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 153 MKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELL 206
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLL 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-215 |
5.08e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGqtlfgplsvslepSLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERA--ASIAWVAQQPNVTPEMTL- 87
Cdd:NF040873 7 VLHGVDLTIPAG-------------SLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAggARVAYVPQRSEVPDSLPLt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 88 ---AALLGYAPIFDALSRLEQGQVLAADFDLldghwdlpDRLSLAfreaDLppfsADRPVFSLSGGERMKALLCGAFVSG 164
Cdd:NF040873 74 vrdLVAMGRWARRGLWRRLTRDDRAAVDDAL--------ERVGLA----DL----AGRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 694069477 165 ADYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTRMPRIIEL 215
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-215 |
8.93e-17 |
|
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: 77.67 E-value: 8.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIEraasiawvaqqpnvtpemtlaal 90
Cdd:cd00267 2 IENLSFRYG-GRTALDNVSLTLKAgEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 91 lgyapifdalsrleqgqvlaadfdlLDGHWDLPDRLSLAFREADLppfsadrpVFSLSGGERMKALLCGAFVSGADYLLL 170
Cdd:cd00267 58 -------------------------IDGKDIAKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694069477 171 DEPTNHLDRQGREWLYHQLESW-QGGA--LIASHDRELLTRMP-RIIEL 215
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELaEEGRtvIIVTHDPELAELAAdRVIVL 153
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-215 |
1.14e-16 |
|
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: 79.30 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 10 FVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE------RAASIAWVAQQ---- 78
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkdiTKKNLRELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 79 ----------PNVTPEMTLAAL-LGYAPIfDALSRLEQgqvLAADFDLldghwdlpdrlslafreADLppfsADRPVFSL 147
Cdd:COG1122 81 fqnpddqlfaPTVEEDVAFGPEnLGLPRE-EIRERVEE---ALELVGL-----------------EHL----ADRPPHEL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694069477 148 SGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGALI-ASHDRELLTRM-PRIIEL 215
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGKTVIiVTHDLDLVAELaDRVIVL 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
39-208 |
1.44e-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: 78.45 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHI----------ERAASIAWVAQQPN-------VTPEMTLAALLGYAPIFDAls 101
Cdd:cd03226 30 ALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikakERRKSIGYVMQDVDyqlftdsVREELLLGLKELDAGNEQA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 102 rleqGQVLAaDFDLldghWDLPDRLslafreadlppfsadrPvFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG 181
Cdd:cd03226 108 ----ETVLK-DLDL----YALKERH----------------P-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190
....*....|....*....|....*....|.
gi 694069477 182 REW---LYHQLESwQGGA-LIASHDRELLTR 208
Cdd:cd03226 162 MERvgeLIRELAA-QGKAvIVITHDYEFLAK 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-201 |
1.54e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.17 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQfATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIeRAASIAWVAQQPNVTPEMtlaAL 90
Cdd:TIGR01189 3 ARNLACS-RGERMLFEGLSFTLNAgEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-RWNGTPLAEQRDEPHENI---LY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 91 LGYAP-IFDALSRLEQGQVLAADFDLLDGH-WDLPDRLSLAFREadlppfsaDRPVFSLSGGERMKALLCGAFVSGADYL 168
Cdd:TIGR01189 78 LGHLPgLKPELSALENLHFWAAIHGGAQRTiEDALAAVGLTGFE--------DLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 694069477 169 LLDEPTNHLDRQGREWLYHQLESW---QGGALIASH 201
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-215 |
6.22e-16 |
|
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: 80.57 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 5 AHIPAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAA 70
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPgERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldpaSWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 71 SIAWVAQQPnVTPEMTLAA-LLGYAPifDA-LSRLEQ--GQVLAADFdlLDGhwdLPDRLslafreadlppfsaDRPV-- 144
Cdd:COG4988 412 QIAWVPQNP-YLFAGTIREnLRLGRP--DAsDEELEAalEAAGLDEF--VAA---LPDGL--------------DTPLge 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694069477 145 --FSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRtvILITHRLALLAQADRILVL 544
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-204 |
1.08e-15 |
|
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: 76.02 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE-----------RAASIAWVAQQPNVTPEMTLAA 89
Cdd:cd03259 12 SVRALDDLSLTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtgvppERRNIGMVFQDYALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 90 LLGYApifdalsrLEQGQVLAAdfdlldghwDLPDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:cd03259 92 NIAFG--------LKLRGVPKA---------EIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 694069477 170 LDEPTNHLDRQGREWLYHQLESWQGG----ALIASHDRE 204
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRElgitTIYVTHDQE 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-235 |
1.39e-15 |
|
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: 79.59 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 25 LFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERAAS--IAWVAQqpnvtpemTLAALLGYAPIFDALS 101
Cdd:TIGR03719 337 LIDDLSFKLPPgGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvkLAYVDQ--------SRDALDPNKTVWEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 102 rleQGQvlaadfDLLD-GHWDLPDRLSLA---FREADlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHL 177
Cdd:TIGR03719 409 ---GGL------DIIKlGKREIPSRAYVGrfnFKGSD-----QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 178 DRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTA-LRSYGGNYDEYQRQRM 235
Cdd:TIGR03719 475 DVETLRALEEALLNFAGCAVVISHDRWFLDRIAtHILAFEGDShVEWFEGNFSEYEEDKK 534
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-215 |
2.30e-15 |
|
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: 75.22 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 10 FVLHQVTCQFATGQTLFgplsvslepslcgLVGRNGVGKTRLLRLLAGLDSPADGHIE-----------------RAASI 72
Cdd:cd03255 18 QALKGVSLSIEKGEFVA-------------IVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisklsekelaafRRRHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 73 AWVAQQPNVTPEMT------LAALLGYAPIFDALSRLEQgqvlaadfdLLDgHWDLPDRLslafreadlppfsaDRPVFS 146
Cdd:cd03255 85 GFVFQSFNLLPDLTalenveLPLLLAGVPKKERRERAEE---------LLE-RVGLGDRL--------------NHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694069477 147 LSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESWQGGALI-ASHDRELLTRMPRIIEL 215
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEvmeLLRELNKEAGTTIVvVTHDPELAEYADRIIEL 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-215 |
3.06e-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: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 5 AHIPAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADG----------HIERAA--- 70
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRRPALRPVSFTVPPgERVALVGPSGAGKSTLLNLLLGFVDPTEGsiavngvplaDADADSwrd 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 71 SIAWVAQQPNVTPEmTLAALLgyapifdALSRLEQGqvlaadfdlldghwdlPDRLSLAFREADLPPFSADRPVF----- 145
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENI-------RLARPDAS----------------DAEIREALERAGLDEFVAALPQGldtpi 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 146 -----SLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:TIGR02857 453 geggaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRtvLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
39-213 |
3.76e-15 |
|
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: 74.55 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWVAQQP---------NVTpemtlaalLGYAPI 96
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqldpaDLRRNIGYVPQDVtlfygtlrdNIT--------LGAPLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 97 FDAlsRLEQGQVLAADFDLLDGHwdlPDRLSLAFREADlppfsadrpvFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:cd03245 106 DDE--RILRAAELAGVTDFVNKH---PNGLDLQIGERG----------RGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 694069477 177 LDRQGREWLYHQLESWQGG--ALIASHDRELLTRMPRII 213
Cdd:cd03245 171 MDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRII 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-201 |
6.01e-15 |
|
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: 73.79 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQtlfgplsvslepsLCGLVGRNGVGKTRLLRLLAGLDSPADGHIEraasIAWVAQQPNVTPEMTLAAL 90
Cdd:cd03268 15 VLDDISLHVKKGE-------------IYGFLGPNGAGKTTTMKIILGLIKPDSGEIT----FDGKSYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 91 LGYAPIFDALSRLEQGQVLAADFDLLDGHWD-LPDRLSLAFReadlppfsADRPVFSLSGGerMKALLC--GAFVSGADY 167
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDeVLDVVGLKDS--------AKKKVKGFSLG--MKQRLGiaLALLGNPDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 694069477 168 LLLDEPTNHLDRQGREWLYHQLESWQ---GGALIASH 201
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRdqgITVLISSH 184
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-224 |
8.33e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 73.48 E-value: 8.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPSLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE-----------------RAASIAWVAQQPNVTPEMTLAALL 91
Cdd:cd03297 17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinlppQQRKIGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 92 GYApifdaLSRLEQGQVLaadfdlldghwDLPDRLSLAFREADLppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:cd03297 97 AFG-----LKRKRNREDR-----------ISVDELLDLLGLDHL----LNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 694069477 172 EPTNHLDRQGREWLYHQLES----WQGGALIASHDRELLTRM-PRIIELTPTALRSYG 224
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQikknLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
36-205 |
1.31e-13 |
|
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: 71.00 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 36 SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWVAQQPNVTPEMTLAALLgyapifdALSR 102
Cdd:TIGR03873 28 SLTGLLGPNGSGKSTLLRLLAGALRPDAGTVdlagvdlhglsrrARARRVALVEQDSDTAVPLTVRDVV-------ALGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 103 LEQGQVLAADFDLLDGhwdLPDRLSLAFREADLppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD---R 179
Cdd:TIGR03873 101 IPHRSLWAGDSPHDAA---VVDRALARTELSHL----ADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvraQ 173
|
170 180
....*....|....*....|....*.
gi 694069477 180 QGREWLYHQLESWQGGALIASHDREL 205
Cdd:TIGR03873 174 LETLALVRELAATGVTVVAALHDLNL 199
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
419-519 |
1.77e-13 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 69.46 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 419 SVMAHL----SLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLwRREPaQLLLLDEPTNHLDLAST 494
Cdd:COG4619 89 TVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL-LLQP-DVLLLDEPTSALDPENT 166
|
90 100
....*....|....*....|....*....
gi 694069477 495 QAIESALAAFP----GAMLVVSHDEAFLQ 519
Cdd:COG4619 167 RRVEELLREYLaeegRAVLWVSHDPEQIE 195
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
29-202 |
2.02e-13 |
|
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: 69.46 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPADGHIeraasiaWVAQQpNVTPEMTLA-ALLGYAP----IFDALSR 102
Cdd:cd03263 21 LSLNVYKGEIfGLLGHNGAGKTTTLKMLTGELRPTSGTA-------YINGY-SIRTDRKAArQSLGYCPqfdaLFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 103 LEQGQVLAadfdLLDGH--WDLPDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:cd03263 93 REHLRFYA----RLKGLpkSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180
....*....|....*....|....
gi 694069477 181 GREWLYHQLESWQGGA--LIASHD 202
Cdd:cd03263 168 SRRAIWDLILEVRKGRsiILTTHS 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-178 |
3.16e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 68.76 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFATGQTLfGPLSVSLEPSLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERA------------ASIAWVAQQP 79
Cdd:cd03264 3 LENLTKRYGKKRAL-DGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkqpqklrRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 80 NVTPEMTLAALLGYAPifdALSRLEQGQVLAADFDLLDgHWDLPDRlslafreadlppfsADRPVFSLSGGERMKALLCG 159
Cdd:cd03264 82 GVYPNFTVREFLDYIA---WLKGIPSKEVKARVDEVLE-LVNLGDR--------------AKKKIGSLSGGMRRRVGIAQ 143
|
170
....*....|....*....
gi 694069477 160 AFVSGADYLLLDEPTNHLD 178
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLD 162
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-261 |
4.27e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLDSPADGHIERAA--SIAWVAQ-QPNVTPEMTlaallgyapIFDALSRLEQ-----GQvlaa 111
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHCGTklEVAYFDQhRAELDPEKT---------VMDNLAEGKQevmvnGR---- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 112 dfdlldghwdlpDRLSLAFREADL-PPFSADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLE 190
Cdd:PRK11147 417 ------------PRHVLGYLQDFLfHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 191 SWQGGALIASHDRELltrmpriIELTPT---------ALRSYGGNYDEYQRQR---MAEQQAARAALEHAVTERRRTRAR 258
Cdd:PRK11147 485 SYQGTVLLVSHDRQF-------VDNTVTecwifegngKIGRYVGGYHDARQQQaqyLALKQPAVKKKEEAAAPKAETVKR 557
|
...
gi 694069477 259 MQK 261
Cdd:PRK11147 558 SSK 560
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
29-215 |
4.39e-13 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 68.53 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHIEraasiaWVAQQPNVTPEMTLAAL----LGYapIFdalsrl 103
Cdd:TIGR02211 24 VSLSIGKGeIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVL------FNGQSLSKLSSNERAKLrnkkLGF--IY------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 104 eQGQVLAADFD--------LLDGHWDLPDRLSLAF---READLPPFSADRPVfSLSGGERMKALLCGAFVSGADYLLLDE 172
Cdd:TIGR02211 90 -QFHHLLPDFTalenvampLLIGKKSVKEAKERAYemlEKVGLEHRINHRPS-ELSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 694069477 173 PTNHLDRQGREWLYH---QLESWQGGA-LIASHDRELLTRMPRIIEL 215
Cdd:TIGR02211 168 PTGNLDNNNAKIIFDlmlELNRELNTSfLVVTHDLELAKKLDRVLEM 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
34-208 |
6.54e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.64 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 34 EPSLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE------RAASIAWVAQQPNVTPEMTLAALlgyapIFDALSRLEQGQ 107
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvEALSARAASRRVASVPQDTSLSF-----EFDVRQVVEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 108 V-LAADFDlldgHWDLPDRLSL--AFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDrqgrew 184
Cdd:PRK09536 103 TpHRSRFD----TWTETDRAAVerAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD------ 171
|
170 180 190
....*....|....*....|....*....|...
gi 694069477 185 LYHQ---LESWQ-----GGALIAS-HDRELLTR 208
Cdd:PRK09536 172 INHQvrtLELVRrlvddGKTAVAAiHDLDLAAR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-218 |
8.81e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFATGQTLFGPLSVSLEPslcG----LVGRNGVGKTRLLRLLAGLDSPADGHIER--AASIAWVAQQPNV 81
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKP---GerllITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 82 tPEMTLAALLGYAPIFDALSRLEQGQVLAAdFDLldGHwdLPDRLSlafREADLppfsaDRpvfSLSGGERMKALLCGAF 161
Cdd:COG4178 438 -PLGTLREALLYPATAEAFSDAELREALEA-VGL--GH--LAERLD---EEADW-----DQ---VLSLGEQQRLAFARLL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 162 VSGADYLLLDEPTNHLDRQGREWLYHQL-ESWQGGALIA-SHDRELLTRMPRIIELTPT 218
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLrEELPGTTVISvGHRSTLAAFHDRVLELTGD 559
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-217 |
9.20e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 25 LFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHI------------ERAASIAWVAQQPNVTPEMT-LAAL 90
Cdd:PRK13538 16 LFSGLSFTLNAGeLVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdEYHQDLLYLGHQPGIKTELTaLENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 91 LGYAPIFDALSRLEQGQVLAadfdlldghwdlpdRLSLAFREadlppfsaDRPVFSLSGGERMKALLCGAFVSGADYLLL 170
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEALA--------------QVGLAGFE--------DVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 694069477 171 DEPTNHLDRQGREWLYHQLESW--QGG-ALIASH-DRELLTRMPRIIELTP 217
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQHaeQGGmVILTTHqDLPVASDKVRKLRLGQ 204
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-190 |
1.57e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 10 FVLHQVTCQFAtGQTLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWV 75
Cdd:PRK10575 12 FALRNVSFRVP-GRTLLHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsskAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 76 AQQPNVTPEMTLAAL--LGYAPIFDALSRLEqgqvlAADfdlldghwdlPDRLSLAFREADLPPFsADRPVFSLSGGERM 153
Cdd:PRK10575 91 PQQLPAAEGMTVRELvaIGRYPWHGALGRFG-----AAD----------REKVEEAISLVGLKPL-AHRLVDSLSGGERQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 694069477 154 KALLCGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALD------IAHQVD 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-256 |
1.99e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 24 TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE--RAASIAWVAQQ-PNVTPEMTlaallgyapIFDA 99
Cdd:PRK11819 338 LLIDDLSFSLPPgGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKigETVKLAYVDQSrDALDPNKT---------VWEE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 100 LSrleQGQvlaadfDLLD-GHWDLPDRLSLA---FREADlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:PRK11819 409 IS---GGL------DIIKvGNREIPSRAYVGrfnFKGGD-----QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTN 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 176 HLDRQGREWLYHQLESWQGGALIASHDRELLTRMPRIIeltpTALRS------YGGNYDEYQ---RQRMAEQqaarAALE 246
Cdd:PRK11819 475 DLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI----LAFEGdsqvewFEGNFQEYEedkKRRLGAD----AARP 546
|
250
....*....|
gi 694069477 247 HAVTERRRTR 256
Cdd:PRK11819 547 HRIKYKKLTR 556
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-215 |
2.68e-12 |
|
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: 69.02 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQF-ATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASI 72
Cdd:COG4987 332 PSLELEDVSFRYpGAGRPVLDGLSLTLPPgERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdldedDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 73 AWVAQQP---------NVT---PEMTLAALLgyapifDALSRLEQGQVLAAdfdlldghwdLPDRLslafreaDLPPFSA 140
Cdd:COG4987 412 AVVPQRPhlfdttlreNLRlarPDATDEELW------AALERVGLGDWLAA----------LPDGL-------DTWLGEG 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 141 DRPvfsLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:COG4987 469 GRR---LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRtvLLITHRLAGLERMDRILVL 542
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
39-200 |
3.15e-12 |
|
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: 65.85 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIErAASIAwVAQQPnvtpemtLAAL--LGYAP----IFDALSRLEQGQVLAaD 112
Cdd:cd03266 35 GLLGPNGAGKTTTLRMLAGLLEPDAGFAT-VDGFD-VVKEP-------AEARrrLGFVSdstgLYDRLTARENLEYFA-G 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 113 FDLLDGHwDLPDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD----RQGREWLYHQ 188
Cdd:cd03266 105 LYGLKGD-ELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvmatRALREFIRQL 182
|
170
....*....|..
gi 694069477 189 LEswQGGALIAS 200
Cdd:cd03266 183 RA--LGKCILFS 192
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
39-178 |
3.64e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 66.20 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIAWvAQQPNVTPEMTLaaLLGyapifdalsrleQGQVLAadfdlldg 118
Cdd:cd03267 51 GFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW-KRRKKFLRRIGV--VFG------------QKTQLW-------- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 119 hWDLPDRLSLAFREA--DLPPFSA-----------------DRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03267 108 -WDLPVIDSFYLLAAiyDLPPARFkkrldelselldleellDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
36-275 |
5.26e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.27 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 36 SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERAASI--AWVAQQpnvtpemTLAALLGYAPIFDALSRLEQGQVLAADF 113
Cdd:PRK10636 339 SRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklGYFAQH-------QLEFLRADESPLQHLARLAPQELEQKLR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 114 DLLDGHWDLPDRLSlafreadlppfsadRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQ 193
Cdd:PRK10636 412 DYLGGFGFQGDKVT--------------EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 194 GGALIASHDRELLTRMPRIIELTPTA-LRSYGGNYDEYQrQRMAEQQAARAALEHAVTERRRTRARM---QKEHDAAQRR 269
Cdd:PRK10636 478 GALVVVSHDRHLLRSTTDDLYLVHDGkVEPFDGDLEDYQ-QWLSDVQKQENQTDEAPKENNANSAQArkdQKRREAELRT 556
|
....*.
gi 694069477 270 SAQTLR 275
Cdd:PRK10636 557 QTQPLR 562
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-216 |
5.62e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.82 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIeRAASIAWVAQQPNVTPEMtlaALLGYAP-IFDA 99
Cdd:cd03231 12 GRALFSGLSFTLAAgEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-LLNGGPLDFQRDSIARGL---LYLGHAPgIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 100 LSRLEQGQVLAADFDlLDGHWDLPDRLSLAFREadlppfsaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR 179
Cdd:cd03231 88 LSVLENLRFWHADHS-DEQVEEALARVGLNGFE--------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 694069477 180 QGREWLYHQLESW--QGGALIAS--HDRELLTRMPRIIELT 216
Cdd:cd03231 159 AGVARFAEAMAGHcaRGGMVVLTthQDLGLSEAGARELDLG 199
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-214 |
1.99e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 64.34 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFATGQ---TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI--------ERAASIAWV 75
Cdd:COG1116 6 PALELRGVSKRFPTGGggvTALDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkpvtGPGPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 76 AQQPNVTPEMTLAALLGYAPIFDALSRLEQGQVLAadfDLLdghwdlpDRLSLAFREADLPpfsadrpvFSLSGGERMKA 155
Cdd:COG1116 86 FQEPALLPWLTVLDNVALGLELRGVPKAERRERAR---ELL-------ELVGLAGFEDAYP--------HQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLES-WQGG---ALIASHDRE----------LLTRMP-RIIE 214
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETgktVLFVTHDVDeavfladrvvVLSARPgRIVE 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-215 |
2.60e-11 |
|
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: 62.23 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHIeraasiawvaqqpnvtpemtlaaLLGYAPIFDALSRLEQGQ 107
Cdd:cd03246 21 VSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRV-----------------------RLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 108 V--LAADFDLLDGhwdlpdrlSLAfrEAdlppfsadrpvfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWL 185
Cdd:cd03246 78 VgyLPQDDELFSG--------SIA--EN------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|...
gi 694069477 186 YHQLESWQGG---ALIASHDRELLTRMPRIIEL 215
Cdd:cd03246 136 NQAIAALKAAgatRIVIAHRPETLASADRILVL 168
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-207 |
2.78e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.83 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 23 QTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPADGHI--------ERA----ASIAWVAQQPNVTPEMTLAA 89
Cdd:PRK13537 20 KLVVDGLSFHVQRGECfGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepvpSRArharQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 90 LLgyaPIFDALSRLEQGQVLAAdfdlldghwdLPDRLSLAFREAdlppfSADRPVFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:PRK13537 100 NL---LVFGRYFGLSAAAARAL----------VPPLLEFAKLEN-----KADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 694069477 170 LDEPTNHLDRQGREWLYHQLESwqggaLIASHDRELLT 207
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRS-----LLARGKTILLT 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-202 |
3.42e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.58 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERA-ASIAWVAQQPNVTPEMTLAALLgyapifdalsrleqgqvlaadFDLLD 117
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIElDTVSYKPQYIKADYEGTVRDLL---------------------SSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 118 GHWDLPdrlslAFREADLPPFS----ADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGR----EWLYHQL 189
Cdd:cd03237 88 DFYTHP-----YFKTEIAKPLQieqiLDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFA 162
|
170
....*....|...
gi 694069477 190 ESWQGGALIASHD 202
Cdd:cd03237 163 ENNEKTAFVVEHD 175
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
28-178 |
4.15e-11 |
|
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: 62.91 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 28 PLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE----------------RAASIAWVAQQP--NVTPEMTLA 88
Cdd:cd03257 23 DVSFSIKKgETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllklsrrlrkiRRKEIQMVFQDPmsSLNPRMTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 89 ALlgyapIFDALSRLEQgqvlaadfdlLDGHWDLPDRLSLAFREADLPPFSADRPVFSLSGGERMKALLCGAFVSGADYL 168
Cdd:cd03257 103 EQ-----IAEPLRIHGK----------LSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLL 167
|
170
....*....|
gi 694069477 169 LLDEPTNHLD 178
Cdd:cd03257 168 IADEPTSALD 177
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
39-209 |
4.42e-11 |
|
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: 62.94 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIAW-----VAQQPNVTPEMT---LAALLGyapifdaLSRLEQGQVLA 110
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSllglgGGFNPELTGRENiylNGRLLG-------LSRKEIDEKID 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 111 --ADFdlldghwdlpdrlslafreADLPPFsADRPVFSLSGGerMKALLcgAF-VSGA---DYLLLDEPTNHLDRQGREW 184
Cdd:cd03220 125 eiIEF-------------------SELGDF-IDLPVKTYSSG--MKARL--AFaIATAlepDILLIDEVLAVGDAAFQEK 180
|
170 180
....*....|....*....|....*...
gi 694069477 185 LYHQLESW--QGGALI-ASHDRELLTRM 209
Cdd:cd03220 181 CQRRLRELlkQGKTVIlVSHDPSSIKRL 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-202 |
4.59e-11 |
|
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: 62.49 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFATGQ---TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI--------ERAASIAWVAQQP 79
Cdd:cd03293 3 VRNVSKTYGGGGgavTALEDISLSVEEgEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvtGPGPDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 80 NVTPEMTLA--ALLGyapifdalsrLEQGQVLAAdfdlldghwDLPDRLSLAFREADLPPFSADRPvFSLSGGERMKALL 157
Cdd:cd03293 83 ALLPWLTVLdnVALG----------LELQGVPKA---------EARERAEELLELVGLSGFENAYP-HQLSGGMRQRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694069477 158 CGAFVSGADYLLLDEPTNHLDRQGR----EWLYHQLESWQGGALIASHD 202
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTReqlqEELLDIWRETGKTVLLVTHD 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-215 |
4.83e-11 |
|
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: 61.63 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPADGHIeraasiawvaqqpnvtpemtl 87
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKV-------------AIVGPSGSGKSTLLKLLLRLYDPTSGEI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 88 aaLLGYAPIfdalsrleqgqvlaADFDLldghWDLPDRLSLAFREADLppfsadrpvFS-------LSGGERMKALLCGA 160
Cdd:cd03228 60 --LIDGVDL--------------RDLDL----ESLRKNIAYVPQDPFL---------FSgtireniLSGGQRQRIAIARA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 161 FVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGG--ALIASHDRELLTRMPRIIEL 215
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTIRDADRIIVL 167
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-182 |
1.20e-10 |
|
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: 63.77 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPADGHI----------------ERAASIAW 74
Cdd:COG1123 280 AVDDVSLTLRRGETL-------------GLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrslrELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 75 VAQQPNVT--PEMTLAALLGYAP-IFDALSRLEQGQVLAadfDLLDghwdlpdrlslafrEADLPPFSADRPVFSLSGGE 151
Cdd:COG1123 347 VFQDPYSSlnPRMTVGDIIAEPLrLHGLLSRAERRERVA---ELLE--------------RVGLPPDLADRYPHELSGGQ 409
|
170 180 190
....*....|....*....|....*....|.
gi 694069477 152 RMKALLCGAFVSGADYLLLDEPTNHLDRQGR 182
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQ 440
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-207 |
1.45e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.73 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLE-PSLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERAAS--IAWVAQQPNVTPEMTLAALLGYAPIFD 98
Cdd:PLN03073 521 GPLLFKNLNFGIDlDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrMAVFSQHHVDGLDLSSNPLLYMMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 99 ALSRleqgQVLAADFdlldGHWDLPDRLSLafreadlppfsadRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:PLN03073 601 GVPE----QKLRAHL----GSFGVTGNLAL-------------QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180
....*....|....*....|....*....
gi 694069477 179 RQGREWLYHQLESWQGGALIASHDRELLT 207
Cdd:PLN03073 660 LDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
457-519 |
1.59e-10 |
|
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: 59.57 E-value: 1.59e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHDEAFLQ 519
Cdd:cd00267 81 LSGGQRQRVALARALLLN--PDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAE 144
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-190 |
2.01e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWVAQQPnVTPE-MTLAALLGY 93
Cdd:PRK11231 21 LSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpismlssrQLARRLALLPQHH-LTPEgITVRELVAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 94 --APIFDALSRLEQgqvlaADFDLLDghWDLPDRLSLAFreadlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:PRK11231 100 grSPWLSLWGRLSA-----EDNARVN--QAMEQTRINHL---------ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170
....*....|....*....
gi 694069477 172 EPTNHLDrqgrewLYHQLE 190
Cdd:PRK11231 164 EPTTYLD------INHQVE 176
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
370-519 |
2.06e-10 |
|
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: 60.35 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLSV----------SAAYLDQHLT-QLdLSLSVMAHL--SLEDTPLDEGLL 436
Cdd:cd03226 29 IALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDyQL-FTDSVREELllGLKELDAGNEQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 437 RTRLAQLQLGADKVTLPLSaLSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESA---LAAFPGAMLVVSH 513
Cdd:cd03226 108 ETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKD--LLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITH 184
|
....*.
gi 694069477 514 DEAFLQ 519
Cdd:cd03226 185 DYEFLA 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-178 |
2.38e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIAWVAQQPNVTPEMTLAALLGyapifdalsrleqgqvlAADFDLLDG 118
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEFLR-----------------SANTDDFGS 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694069477 119 HW---DLPDRLSLafrEADLppfsaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:COG1245 433 SYyktEIIKPLGL---EKLL-----DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
39-235 |
2.73e-10 |
|
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: 62.93 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWVAQQP---------NVT---PEMTLAALLgy 93
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaSLRRQIGVVLQDVflfsgtireNITlgdPDATDEEII-- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 94 apifDALsrleqgQVLAADFDLLDghwdLPDRLslafreadlppfsaDRPV----FSLSGGERMKALLCGAFVSGADYLL 169
Cdd:COG2274 583 ----EAA------RLAGLHDFIEA----LPMGY--------------DTVVgeggSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 170 LDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL---------TPTALRSYGGNYDEYQRQRM 235
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKGRtvIIIAHRLSTIRLADRIIVLdkgrivedgTHEELLARKGLYAELVQQQL 711
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-219 |
2.95e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI----------ERAASIAWVAQQPNVTPEMTLAA- 89
Cdd:PRK13539 14 GRVLFSGLSFTLAAgEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkldggdiddpDVAEACHYLGHRNAMKPALTVAEn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 90 LLGYAPIFDAlsrlEQGQVLAA--DFDLldghwdlpdrlslafreADLppfsADRPVFSLSGGERMKALLCGAFVSGADY 167
Cdd:PRK13539 94 LEFWAAFLGG----EELDIAAAleAVGL-----------------APL----AHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 168 LLLDEPTNHLDRQGREWL-----YHqLEswQGGALIASHDRELLTRMPRIIELTPTA 219
Cdd:PRK13539 149 WILDEPTAALDAAAVALFaelirAH-LA--QGGIVIAATHIPLGLPGARELDLGPFA 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
39-186 |
6.20e-10 |
|
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: 59.31 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGH------------IERAASIAWVAQQPNVTPEMT-------LAALLGYaPIFDA 99
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepREVRRRIGIVFQDLSVDDELTgwenlyiHARLYGV-PGAER 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 100 LSRLEQgqVLAAdFDLLDghwdlpdrlslafreadlppfSADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR 179
Cdd:cd03265 109 RERIDE--LLDF-VGLLE---------------------AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
....*....
gi 694069477 180 QGRE--WLY 186
Cdd:cd03265 165 QTRAhvWEY 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-215 |
9.43e-10 |
|
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: 58.98 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFATGQ---TLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHIE---------------- 67
Cdd:COG4181 7 PIIELRGLTKTVGTGAgelTILKGISLEVEAGeSVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlfaldedarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 68 -RAASIAWVAQQPNVTPEMT------LAALLGYAPifDALSRleqgqvlAADfdLLDghwdlpdRLSLAFREADLPPfsa 140
Cdd:COG4181 87 lRARHVGFVFQSFQLLPTLTalenvmLPLELAGRR--DARAR-------ARA--LLE-------RVGLGHRLDHYPA--- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 141 drpvfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESWQGGALI-ASHDRELLTRMPRIIEL 215
Cdd:COG4181 146 -----QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELNRERGTTLVlVTHDPALAARCDRVLRL 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-206 |
1.20e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.25 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPsLCGLVGRNGVGKTRLLRLLAGLDSPADGhieraaSIAWVAQQPNVTPEMTLAALLGYAPIFDALSRleqgQV 108
Cdd:PRK13638 22 LDFSLSP-VTGLVGANGCGKSTLFMNLSGLLRPQKG------AVLWQGKPLDYSKRGLLALRQQVATVFQDPEQ----QI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 109 LAADFD---------LLDGHWDLPDRLSLAFREADLPPFSaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR 179
Cdd:PRK13638 91 FYTDIDsdiafslrnLGVPEAEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190
....*....|....*....|....*....|
gi 694069477 180 QGREWLYHQLE--SWQGG-ALIASHDRELL 206
Cdd:PRK13638 170 AGRTQMIAIIRriVAQGNhVIISSHDIDLI 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-178 |
1.46e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIAWVAQQPNVTPEMTLAALLGYAPifdalsrleqgqvlaadfDLLDG 118
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPDYDGTVEDLLRSIT------------------DDLGS 430
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694069477 119 HW---DLPDRLSLafreADLppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:PRK13409 431 SYyksEIIKPLQL----ERL----LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-172 |
1.65e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIAWVAqqpNVT----PEMT 86
Cdd:COG1134 41 ALKDVSFEVERGESV-------------GIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL---ELGagfhPELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 87 -------LAALLGyapifdaLSRLEQGQVLA--ADFdlldghwdlpdrlslafreADLPPFsADRPVFSLSGGerMKALL 157
Cdd:COG1134 105 greniylNGRLLG-------LSRKEIDEKFDeiVEF-------------------AELGDF-IDQPVKTYSSG--MRARL 155
|
170
....*....|....*....
gi 694069477 158 cgAF-VSGA---DYLLLDE 172
Cdd:COG1134 156 --AFaVATAvdpDILLVDE 172
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
453-518 |
1.94e-09 |
|
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: 57.48 E-value: 1.94e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPGA---MLVVSHDEAFL 518
Cdd:cd03225 131 SPFTLSGGQKQRVAIAGVLAMD--PDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLL 197
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-215 |
2.87e-09 |
|
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: 57.42 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 14 QVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIEraasiawVAQQPnvtpemtLAALLG 92
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAgEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIR-------VNGQD-------VSDLRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 93 YAPifdALSRLEQGQVLAaDFDLL-----------------DGHWDLPDRLSLAFREADLPPFSADRPVfSLSGGERMKA 155
Cdd:cd03292 71 RAI---PYLRRKIGVVFQ-DFRLLpdrnvyenvafalevtgVPPREIRKRVPAALELVGLSHKHRALPA-ELSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW-QGGA--LIASHDRELLTRM-PRIIEL 215
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTtvVVATHAKELVDTTrHRVIAL 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
369-519 |
2.90e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 369 RIALKGPNGCGKT-------------------TLLKTLLGLEQ----AASGDVRLSVS------AAYLDQ-----HLTQL 414
Cdd:PRK11147 31 RVCLVGRNGAGKStlmkilngevllddgriiyEQDLIVARLQQdpprNVEGTVYDFVAegieeqAEYLKRyhdisHLVET 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 415 DLS---LSVMAHLSLEDTPLDEGLLRTR----LAQLQLGADKvtlPLSALSGGERLKAALACVLwRREPaQLLLLDEPTN 487
Cdd:PRK11147 111 DPSeknLNELAKLQEQLDHHNLWQLENRinevLAQLGLDPDA---ALSSLSGGWLRKAALGRAL-VSNP-DVLLLDEPTN 185
|
170 180 190
....*....|....*....|....*....|..
gi 694069477 488 HLDLASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:PRK11147 186 HLDIETIEWLEGFLKTFQGSIIFISHDRSFIR 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-178 |
3.15e-09 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 57.58 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQtlfgplsvslepsLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE--------------RAA--SIAW 74
Cdd:cd03256 16 ALKDVSLSINPGE-------------FVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkalRQLrrQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 75 VAQQPNVTPEMT-----LAALLGYAPIFDALSRLEQGQVLAADFDLLdghwDLPDRLSLAFREADlppfsadrpvfSLSG 149
Cdd:cd03256 83 IFQQFNLIERLSvlenvLSGRLGRRSTWRSLFGLFPKEEKQRALAAL----ERVGLLDKAYQRAD-----------QLSG 147
|
170 180
....*....|....*....|....*....
gi 694069477 150 GERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-183 |
3.37e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.58 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATgQTLFGPLSVSL-EPSLCGLVGRNGVGKTRLLRLLAGLDSPADGHI--------ERAAS---IAWVAQQ 78
Cdd:PRK11432 8 VLKNITKRFGS-NTVIDNLNLTIkQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvtHRSIQqrdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 79 PNVTPEMTLAALLGYAPIFDALSRLEQGQvlaadfdlldghwdlpdRLSLAFREADLPPFsADRPVFSLSGGERMKALLC 158
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQ-----------------RVKEALELVDLAGF-EDRYVDQISGGQQQRVALA 148
|
170 180
....*....|....*....|....*....
gi 694069477 159 GAFVSGADYLLLDEPTNHLD----RQGRE 183
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDanlrRSMRE 177
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-518 |
3.40e-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: 59.41 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERAASiaWvaqqpnvtpEMTLAALLGYApIFDALSRLEQGQVLAA------D 112
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYDEEPS--W---------DEVLKRFRGTE-LQDYFKKLANGEIKVAhkpqyvD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 113 F----------DLLD-----GHWD-LPDRLSLAFreadlppfSADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:COG1245 171 LipkvfkgtvrELLEkvderGKLDeLAEKLGLEN--------ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 177 LDrqgrewlyhqleswqggaliashdrelltrmpriIeltptalrsyggnydeyqRQRMAeqqAARAALEHAvterRRTR 256
Cdd:COG1245 243 LD----------------------------------I------------------YQRLN---VARLIRELA----EEGK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 257 ARMQKEHDAAqrrsaqTLRTV-DTLNIASFERVKY-----------------KGAAKE-----RPGALRRQHREQnssln 313
Cdd:COG1245 264 YVLVVEHDLA------ILDYLaDYVHILYGEPGVYgvvskpksvrvginqylDGYLPEenvriRDEPIEFEVHAP----- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 314 aavqqareRVEEETPVMFTLPGSEVAAGKQVLVVESlqldhapaaplnwridGPMR----IALKGPNGCGKTTLLKTLLG 389
Cdd:COG1245 333 --------RREKEEETLVEYPDLTKSYGGFSLEVEG----------------GEIRegevLGIVGPNGIGKTTFAKILAG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 390 LEQAASGDVRLSVSAAYLDQHLTQlDLSLSVMAHLSLEDTP-LDEGLLRTRLAQ-LQLGA--DKvtlPLSALSGGERLKA 465
Cdd:COG1245 389 VLKPDEGEVDEDLKISYKPQYISP-DYDGTVEEFLRSANTDdFGSSYYKTEIIKpLGLEKllDK---NVKDLSGGELQRV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 466 ALACVLWRrePAQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:COG1245 465 AIAACLSR--DADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-206 |
4.71e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFATGQTLfGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHIERAAS--IAWVAQQPNVTPE---- 84
Cdd:PRK09544 7 LENVSVSFGQRRVL-SDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDTTlplt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 85 ----MTLAALLGYAPIFDALSRLEQGQVLaadfdlldghwdlpdrlslafreadlppfsaDRPVFSLSGGERMKALLCGA 160
Cdd:PRK09544 86 vnrfLRLRPGTKKEDILPALKRVQAGHLI-------------------------------DAPMQKLSGGETQRVLLARA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 694069477 161 FVSGADYLLLDEPTNHLDRQGREWLY---HQLESWQG-GALIASHDRELL 206
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYdliDQLRRELDcAVLMVSHDLHLV 184
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-191 |
5.43e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.92 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPADGHIE----------RAA--SIAWVAQQPNVTPEMTLAA-LLGYA 94
Cdd:PRK13536 60 LSFTVASGECfGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLAraRIGVVPQFDNLDLEFTVREnLLVFG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 95 PIFdalsRLEQGQVLAAdfdlldghwdLPDRLSLAFREAdlppfSADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK13536 140 RYF----GMSTREIEAV----------IPSLLEFARLES-----KADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170
....*....|....*..
gi 694069477 175 NHLDRQGREWLYHQLES 191
Cdd:PRK13536 201 TGLDPHARHLIWERLRS 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-190 |
6.66e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWVAQ 77
Cdd:PRK13548 17 LLDDVSLTLRPGEVV-------------AILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladwspaELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 78 QPNVTPEMTLAAL--LGYAPifDALSRLEQGQVLAAdfdlldghwdlpdrlslAFREADLPPFsADRPVFSLSGGERMKA 155
Cdd:PRK13548 84 HSSLSFPFTVEEVvaMGRAP--HGLSRAEDDALVAA-----------------ALAQVDLAHL-AGRDYPQLSGGEQQRV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 694069477 156 LL------CGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:PRK13548 144 QLarvlaqLWEPDGPPRWLLLDEPTSALD------LAHQHH 178
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
39-209 |
9.28e-09 |
|
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: 54.89 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIEraasiawvaqqpnvtpemtlaallgyapiFDalsrleqGQVLAadfDLLDG 118
Cdd:cd03229 30 ALLGPSGSGKSTLLRCIAGLEEPDSGSIL-----------------------------ID-------GEDLT---DLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 119 HWDLPDRLSLAFREADLPP-FSA-DRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA 196
Cdd:cd03229 71 LPPLRRRIGMVFQDFALFPhLTVlENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQL 150
|
170
....*....|....*..
gi 694069477 197 ----LIASHDRELLTRM 209
Cdd:cd03229 151 gitvVLVTHDLDEAARL 167
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-201 |
1.11e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 25 LFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPADGHIEraasiawVAQQPNVTPEMT-LAALLGYAPIFDA-LS 101
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVqGDNGAGKTTLLRVLAGLLHVESGQIQ-------IDGKTATRGDRSrFMAYLGHLPGLKAdLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 102 RLEQGQVLAAdfdlldghwdlpdrlsLAFREADLPPFSA----------DRPVFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:PRK13543 99 TLENLHFLCG----------------LHGRRAKQMPGSAlaivglagyeDTLVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 694069477 172 EPTNHLDRQGREWLYHQLESW---QGGALIASH 201
Cdd:PRK13543 163 EPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
29-174 |
1.18e-08 |
|
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: 55.91 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERA-ASIAWVAQQPNVTPEMT------L 87
Cdd:cd03219 19 VSFSVRPgEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditglpphEIArLGIGRTFQIPRLFPELTvlenvmV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 88 AALLGYA-PIFDALSRLEQGQVLAADFDLLDghwdlpdRLSLAFReadlppfsADRPVFSLSGGERMKALLCGAFVSGAD 166
Cdd:cd03219 99 AAQARTGsGLLLARARREEREARERAEELLE-------RVGLADL--------ADRPAGELSYGQQRRLEIARALATDPK 163
|
....*...
gi 694069477 167 YLLLDEPT 174
Cdd:cd03219 164 LLLLDEPA 171
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
453-516 |
1.36e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.93 E-value: 1.36e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHDEA 516
Cdd:NF040873 116 QLGELSGGQRQRALLAQGLAQE--ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-178 |
1.46e-08 |
|
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: 55.26 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGL-----DSPADGHI---------------ERAA 70
Cdd:cd03260 15 ALKDISLDIPKGEIT-------------ALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVlldgkdiydldvdvlELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 71 SIAWVAQQPNVTPeMTLAALLGYAPifdalsRLeQGQVLAADFDlldghwdlpDRLSLAFREADLPPFSADRP-VFSLSG 149
Cdd:cd03260 82 RVGMVFQKPNPFP-GSIYDNVAYGL------RL-HGIKLKEELD---------ERVEEALRKAALWDEVKDRLhALGLSG 144
|
170 180
....*....|....*....|....*....
gi 694069477 150 GERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALD 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-174 |
1.49e-08 |
|
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: 55.13 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 23 QTLFGpLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAAS-IAWVAQQPNVTPEMT- 86
Cdd:cd03224 14 QILFG-VSLTVPEGEIvALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrditglpphERARAgIGYVPEGRRIFPELTv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 87 -----LAALlgyapifdALSRLEQGQVLAADFDLLDghwDLPDRLslafreadlppfsaDRPVFSLSGGER-MKALlCGA 160
Cdd:cd03224 93 eenllLGAY--------ARRRAKRKARLERVYELFP---RLKERR--------------KQLAGTLSGGEQqMLAI-ARA 146
|
170
....*....|....
gi 694069477 161 FVSGADYLLLDEPT 174
Cdd:cd03224 147 LMSRPKLLLLDEPS 160
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-274 |
1.65e-08 |
|
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: 57.22 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFATGQT-LFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLdSPADGHIE-----------------R 68
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETvALVGESGSGKSTLALALMGL-LPHGGRISgevlldgrdllelsealR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 69 AASIAWVAQQPnvtpemtLAALLGYAPIFDALSRLEQGQVLAADFDlldghwdlpDRLSLAFREADLPPFsADRPVFSLS 148
Cdd:COG1123 82 GRRIGMVFQDP-------MTQLNPVTVGDQIAEALENLGLSRAEAR---------ARVLELLEAVGLERR-LDRYPHQLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 149 GGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG----GALIASHDRELLTRMP-RIIELtptalrsy 223
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHDLGVVAEIAdRVVVM-------- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 694069477 224 ggnydeyQRQRMAEQQAARAALEHAVTERRRTRARMQKEHDAAQRRSAQTL 274
Cdd:COG1123 217 -------DDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
400-527 |
1.77e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 400 LSVSAAYLDQH---LTQLD----LSLSVMAHLSLEDtplDEGLLRTRLAQLQLGaDKVTLPLSALSGGERLKAALACVL- 471
Cdd:PRK03695 67 LARHRAYLSQQqtpPFAMPvfqyLTLHQPDKTRTEA---VASALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAAVVl 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694069477 472 --WRR-EP-AQLLLLDEPTNHLDLASTQAIESALAAFP---GAMLVVSHDeaflqglkLTHSL 527
Cdd:PRK03695 143 qvWPDiNPaGQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD--------LNHTL 197
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
358-527 |
2.14e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.23 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 358 APLNWRIDGPMRIALKGPNGCGkTTLLKTLLGLEQAASGDVRL------SVSAAYLDQH---LTQLDLSLSVMA---HLS 425
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAG-KSTLLARMAGLLPGQGEILLngrplsDWSAAELARHrayLSQQQSPPFAMPvfqYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 426 L-----EDTPLDEGLLRTRLAQLQLgADKVTLPLSALSGGERLKAALACVLWRREP-----AQLLLLDEPTNHLDLASTQ 495
Cdd:COG4138 92 LhqpagASSEAVEQLLAQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpeGQLLLLDEPMNSLDVAQQA 170
|
170 180 190
....*....|....*....|....*....|....*
gi 694069477 496 AIESALAAFP---GAMLVVSHDeaflqglkLTHSL 527
Cdd:COG4138 171 ALDRLLRELCqqgITVVMSSHD--------LNHTL 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
39-206 |
2.23e-08 |
|
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: 54.86 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERA-ASIAWVAQQPNVTPEMT----LAALLGYAPIFDA- 99
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmhKRArLGIGYLPQEASIFRKLTveenILAVLEIRGLSKKe 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 100 -LSRLEQgqvLAADFDLldghwdlpDRLslafreadlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03218 110 rEEKLEE---LLEEFHI--------THL-------------RKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190
....*....|....*....|....*....|..
gi 694069477 179 R---QGREWLYHQLESWQGGALIASHD-RELL 206
Cdd:cd03218 166 PiavQDIQKIIKILKDRGIGVLITDHNvRETL 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-518 |
2.93e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIAWVaqqpnvtpemtLAALLGYApIFDALSRLEQGQVLAA------D 112
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEV-----------LKRFRGTE-LQNYFKKLYNGEIKVVhkpqyvD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 113 F----------DLLD-----GHWD-LPDRLSLafrEADLppfsaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:PRK13409 171 LipkvfkgkvrELLKkvderGKLDeVVERLGL---ENIL-----DRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 177 LDrqgrewlyhqleswqggaliashdrelltrmpriIeltptalrsyggnydeyqRQRMAeqqAARAalehaVTERRRTR 256
Cdd:PRK13409 243 LD----------------------------------I------------------RQRLN---VARL-----IRELAEGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 257 ARMQKEHDAAqrrsaqTLRTV-DTLNIASFERVKY-----------------KGAAKE-----RPGALRRQHREqnssln 313
Cdd:PRK13409 263 YVLVVEHDLA------VLDYLaDNVHIAYGEPGAYgvvskpkgvrvgineylKGYLPEenmriRPEPIEFEERP------ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 314 aavqqarERVEEETPVMFTLPGSEVAAGKQVLVVESlqldhapaaplnwridGPMR----IALKGPNGCGKTTLLKTLLG 389
Cdd:PRK13409 331 -------PRDESERETLVEYPDLTKKLGDFSLEVEG----------------GEIYegevIGIVGPNGIGKTTFAKLLAG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 390 LEQAASGDVRLSVSAAYLDQHLTQlDLSLSVMAHLSLEDTPLDEGLLRTRLAQ-LQLGA--DKvtlPLSALSGGERLKAA 466
Cdd:PRK13409 388 VLKPDEGEVDPELKISYKPQYIKP-DYDGTVEDLLRSITDDLGSSYYKSEIIKpLQLERllDK---NVKDLSGGELQRVA 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 467 LACVLWRrePAQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:PRK13409 464 IAACLSR--DADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMI 517
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-202 |
3.94e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 27 GPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLdSPADGHI-------------ERAASIAWVAQQPNVTPEMtlaallg 92
Cdd:PRK03695 13 GPLSAEVRAGeILHLVGPNGAGKSTLLARMAGL-LPGSGSIqfagqpleawsaaELARHRAYLSQQQTPPFAM------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 93 yaPIFDALSR-LEQGQVLAADFDLLDghwDLPDRLSLAfreaDLPPfsadRPVFSLSGGERMKALLCGAFV-------SG 164
Cdd:PRK03695 85 --PVFQYLTLhQPDKTRTEAVASALN---EVAEALGLD----DKLG----RSVNQLSGGEWQRVRLAAVVLqvwpdinPA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 694069477 165 ADYLLLDEPTNHLDRQGREWLY---HQLESWQGGALIASHD 202
Cdd:PRK03695 152 GQLLLLDEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHD 192
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
38-191 |
4.59e-08 |
|
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: 55.12 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 38 CGLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIAWVAQQPNVTPEMTLAalLGY----APIFDALSRLEqgqvlaadf 113
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRR--IGYvfqeARLFPHLSVRG--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 114 DLLDGHW--DLPDRLSLAFREADLPPFS--ADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL 189
Cdd:TIGR02142 95 NLRYGMKraRPSERRISFERVIELLGIGhlLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
..
gi 694069477 190 ES 191
Cdd:TIGR02142 175 ER 176
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
453-514 |
5.24e-08 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 53.94 E-value: 5.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694069477 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHD 514
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQD--PDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-189 |
1.47e-07 |
|
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: 53.90 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIA 73
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPgERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldqdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 74 WVAQQPNVTPEMTLAALLGYAP------IFDALSRLEQGQVLAAdfdlldghwdLPDRLSLAFREADLppfsadrpvfSL 147
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRLARPdatdeeLWAALERVGLADWLRA----------LPDGLDTVLGEGGA----------RL 472
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 694069477 148 SGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL 189
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
457-516 |
1.78e-07 |
|
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: 53.83 E-value: 1.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694069477 457 LSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEA 516
Cdd:TIGR02857 459 LSGGQAQRLALARAFLR--DAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLA 518
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
142-219 |
1.81e-07 |
|
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: 51.84 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 142 RPVFSLSGGERMKA------LLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL-ESWQGGA----LIASHDRELLTRMP 210
Cdd:cd03240 111 DMRGRCSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDEENIEESLAEIiEERKSQKnfqlIVITHDEELVDAAD 190
|
....*....
gi 694069477 211 RIIELTPTA 219
Cdd:cd03240 191 HIYRVEKDG 199
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
370-514 |
2.14e-07 |
|
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: 52.35 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 370 IALKGPNGCG----------KTtllktllgleQAASGDVRL---SVSA----------AYLDQHlTQLDLSLSV------ 420
Cdd:COG1120 30 TALLGPNGSGkstllralagLL----------KPSSGEVLLdgrDLASlsrrelarriAYVPQE-PPAPFGLTVrelval 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 421 --MAHLSL--EDTPLDEGLLRTRLAQLQLG--ADKvtlPLSALSGGERLKAALACVLwrrepAQ---LLLLDEPTNHLDL 491
Cdd:COG1120 99 grYPHLGLfgRPSAEDREAVEEALERTGLEhlADR---PVDELSGGERQRVLIARAL-----AQeppLLLLDEPTSHLDL 170
|
170 180
....*....|....*....|....*..
gi 694069477 492 ASTQAIES---ALAAFPG-AMLVVSHD 514
Cdd:COG1120 171 AHQLEVLEllrRLARERGrTVVMVLHD 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-215 |
2.62e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGhieraaSIAWVAQQPNVTPEMTLAAL----LGYA-------PI 96
Cdd:PRK11629 28 VSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSG------DVIFNGQPMSKLSSAAKAELrnqkLGFIyqfhhllPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 97 FDALSRLEqgqvlaadFDLLDGH---WDLPDRLSLAFREADLPPFSADRPVfSLSGGERMKALLCGAFVSGADYLLLDEP 173
Cdd:PRK11629 102 FTALENVA--------MPLLIGKkkpAEINSRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 694069477 174 TNHLDRQGREWLYH---QLESWQGGA-LIASHDRELLTRMPRIIEL 215
Cdd:PRK11629 173 TGNLDARNADSIFQllgELNRLQGTAfLVVTHDLQLAKRMSRQLEM 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-204 |
2.93e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 52.41 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI----ERAASIAwvAQQPNVT 82
Cdd:COG3842 4 PALELENVSKRYG-DVTALDDVSLSIEPgEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLP--PEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 83 ---------PEMTLAALLGYAPIFDALSRLEQGQVLAADFDL--LDGHwdlpdrlslafreadlppfsADRPVFSLSGGE 151
Cdd:COG3842 81 mvfqdyalfPHLTVAENVAFGLRMRGVPKAEIRARVAELLELvgLEGL--------------------ADRYPHQLSGGQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 152 RMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQ---GG-ALIASHDRE 204
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQrelGItFIYVTHDQE 197
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-219 |
3.08e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 51.33 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSP---ADGHIeraasiaWVAQQPnVTPEMTLAALLGY---- 93
Cdd:COG4136 13 GRPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSPafsASGEV-------LLNGRR-LTALPAEQRRIGIlfqd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 94 APIFDALSrleQGQVLAadfdlldghWDLPDRLSLAFR---------EADLPPFsADRPVFSLSGGERMKALLCGAFVSG 164
Cdd:COG4136 85 DLLFPHLS---VGENLA---------FALPPTIGRAQRrarveqaleEAGLAGF-ADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 165 ADYLLLDEPTNHLDR----QGREWLYHQLESWQGGALIASHDRELLTRMPRIIELTPTA 219
Cdd:COG4136 152 PRALLLDEPFSKLDAalraQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQ 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
370-491 |
3.38e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.55 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 370 IALKGPNGCGKTTLLKTLLGLEQAASGDV-------------RLSVSAAYLDQ-HLTQLDLS------------LSVMAH 423
Cdd:PRK11231 31 TALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpismlssrQLARRLALLPQhHLTPEGITvrelvaygrspwLSLWGR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 424 LSLEDTPL-DEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDL 491
Cdd:PRK11231 111 LSAEDNARvNQAMEQTRINHL---ADR---RLTDLSGGQRQRAFLAMVLAQDTP--VVLLDEPTTYLDI 171
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
37-208 |
3.46e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 37 LCGLVGRNGVGKTRLLRLLAGLDSPADGHI---------ERAA---SIAWVAQQPNVTPEMTLAALLGYapifdalsrle 104
Cdd:PRK13540 29 LLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqsikkDLCTyqkQLCFVGHRSGINPYLTLRENCLY----------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 105 qgqvlaaDFDLLDGHWDLpDRLSLAFREADLppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW 184
Cdd:PRK13540 98 -------DIHFSPGAVGI-TELCRLFSLEHL----IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*..
gi 694069477 185 LYHQLESW--QGGA-LIASHDRELLTR 208
Cdd:PRK13540 166 IITKIQEHraKGGAvLLTSHQDLPLNK 192
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-178 |
4.44e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.01 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIEraasiawvaqqpnvtpemtlaaLLGYAPIfdalsrlEQGQ 107
Cdd:COG4586 41 ISFTIEPgEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR----------------------VLGYVPF-------KRRK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 108 VLAADFDLLDGH-----WDLP--DRLSL----------AFREA--------DLPPFsADRPVFSLSGGERMKALLCGAFV 162
Cdd:COG4586 92 EFARRIGVVFGQrsqlwWDLPaiDSFRLlkaiyripdaEYKKRldelvellDLGEL-LDTPVRQLSLGQRMRCELAAALL 170
|
170
....*....|....*.
gi 694069477 163 SGADYLLLDEPTNHLD 178
Cdd:COG4586 171 HRPKILFLDEPTIGLD 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
40-185 |
4.96e-07 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 51.24 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLDSPADG-HIE--------------RAaSIAWVaqqpnvTPEMTLAaLLGYAPIFDAlsrle 104
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgerrggedvwelRK-RIGLV------SPALQLR-FPRDETVLDV----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 105 qgqVLAADFDLLdGHWDLPD--------RLSLAFREADLppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:COG1119 101 ---VLSGFFDSI-GLYREPTdeqrerarELLELLGLAHL----ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
....*....
gi 694069477 177 LDRQGREWL 185
Cdd:COG1119 173 LDLGARELL 181
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
391-514 |
5.23e-07 |
|
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: 50.97 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 391 EQAASGDVRLSVSAAYLdqhltqldlsLSVMAHLSL--EDTPLDEGLLRTRLAQLQLgADKVTLPLSALSGGERLKAALA 468
Cdd:TIGR03873 81 EQDSDTAVPLTVRDVVA----------LGRIPHRSLwaGDSPHDAAVVDRALARTEL-SHLADRDMSTLSGGERQRVHVA 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 694069477 469 CVLwRREPaQLLLLDEPTNHLDLASTQAIESALA--AFPGAMLVVS-HD 514
Cdd:TIGR03873 150 RAL-AQEP-KLLLLDEPTNHLDVRAQLETLALVRelAATGVTVVAAlHD 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
40-221 |
5.96e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.55 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLDSPADGHIE-----------------RAASIAWVAQQPNVTPemTLAALLGYApiFDALSR 102
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmdeearaklRAKHVGFVFQSFMLIP--TLNALENVE--LPALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 103 LEqgqvlaADFDLLDGHWDLPDRLSLAFREADLPPfsadrpvfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGR 182
Cdd:PRK10584 117 GE------SSRQSRNGAKALLEQLGLGKRLDHLPA--------QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 694069477 183 EW---LYHQLESWQGGALI-ASHDRELLTRMPRIIELTPTALR 221
Cdd:PRK10584 183 DKiadLLFSLNREHGTTLIlVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
457-519 |
6.28e-07 |
|
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: 50.28 E-value: 6.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694069477 457 LSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFLQ 519
Cdd:cd03245 141 LSGGQRQAVALARALLNDPP--ILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-183 |
9.07e-07 |
|
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: 51.25 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLE---PSLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE-------------------RAasIAWVAQQPNVTPEMT 86
Cdd:COG4148 16 LDVDFTlpgRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflpphrRR--IGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 87 LAALLGYapifdALSRLEQGQVlAADFDlldghwDLPDRLSLafreADLppfsADRPVFSLSGGERM-----KALLcgaf 161
Cdd:COG4148 94 VRGNLLY-----GRKRAPRAER-RISFD------EVVELLGI----GHL----LDRRPATLSGGERQrvaigRALL---- 149
|
170 180
....*....|....*....|..
gi 694069477 162 vSGADYLLLDEPTNHLDRQGRE 183
Cdd:COG4148 150 -SSPRLLLMDEPLAALDLARKA 170
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
29-178 |
9.34e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.37 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSL-EPSLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWVAQQPNVTPEMTLAALLG-- 92
Cdd:PRK10253 26 LTVEIpDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaskEVARRIGLLAQNATTPGDITVQELVArg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 93 ---YAPIFDALSRLEQgqvlaadfdlldghwdlpDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:PRK10253 106 rypHQPLFTRWRKEDE------------------EAVTKAMQATGITHL-ADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
....*....
gi 694069477 170 LDEPTNHLD 178
Cdd:PRK10253 167 LDEPTTWLD 175
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-178 |
9.71e-07 |
|
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: 49.59 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFATGQTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI---------ERAASIAWVAQQPNV 81
Cdd:cd03269 3 VENVTKRFGRVTALDD-ISFSVEKgEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkpldiAARNRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 82 TPEMT-------LAALLGYaPIFDALSRLEqgqvlaadfdlldghwDLPDRLSLAFREadlppfsaDRPVFSLSGGERMK 154
Cdd:cd03269 82 YPKMKvidqlvyLAQLKGL-KKEEARRRID----------------EWLERLELSEYA--------NKRVEELSKGNQQK 136
|
170 180
....*....|....*....|....
gi 694069477 155 ALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLD 160
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
12-201 |
1.03e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVtcQFATGQTLFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPADGHIERAAS---------IAWVAQQPNV 81
Cdd:PRK13541 4 LHQL--QFNIEQKNLFDLSITFLPSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCninniakpyCTYIGHNLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 82 TPEMT-LAALLGYAPIFDALSRLEqgqvlAADfdlldgHWdlpdrlslaFREADLppfsADRPVFSLSGGERMKALLCGA 160
Cdd:PRK13541 82 KLEMTvFENLKFWSEIYNSAETLY-----AAI------HY---------FKLHDL----LDEKCYSLSSGMQKIVAIARL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 694069477 161 FVSGADYLLLDEPTNHLDRQGREWLYH--QLESWQGG-ALIASH 201
Cdd:PRK13541 138 IACQSDLWLLDEVETNLSKENRDLLNNliVMKANSGGiVLLSSH 181
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-219 |
1.11e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 48.69 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 10 FVLHQVTCQFATGQTLFGPLSVSLEPslcG----LVGRNGVGKTRLLRLLAGLDSPADGHIERAAS--IAWVAQQPNVtP 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKP---GdrllITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGedLLFLPQRPYL-P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 84 EMTLAALLGYaPIFDALSRLEQgQvlaadfdlldghwdlpdRLSLAfreadlppfsadrpvfslsggeRMkallcgaFVS 163
Cdd:cd03223 77 LGTLREQLIY-PWDDVLSGGEQ-Q-----------------RLAFA----------------------RL-------LLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 164 GADYLLLDEPTNHLDRQGREWLYHQLESwQGGALIA-SHDRELLTRMPRIIELTPTA 219
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKE-LGITVISvGHRPSLWKFHDRVLDLDGEG 164
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-219 |
1.13e-06 |
|
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: 49.74 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 10 FVLHQVTcqfatGQTL--FGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPADGHIE------------------- 67
Cdd:COG4778 14 FTLHLQG-----GKRLpvLDGVSFSVAAGECvALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdlaqaspreil 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 68 --RAASIAWVAQQPNVTPEMTlaAL-LGYAPIFDALSRLEQGQVLAADfdLLDgHWDLPDRLslafreADLPP--FSadr 142
Cdd:COG4778 89 alRRRTIGYVSQFLRVIPRVS--ALdVVAEPLLERGVDREEARARARE--LLA-RLNLPERL------WDLPPatFS--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 143 pvfslsGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESwQGGALIA-SHDRELLTRMP-RIIELTP 217
Cdd:COG4778 155 ------GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVvveLIEEAKA-RGTAIIGiFHDEEVREAVAdRVVDVTP 227
|
..
gi 694069477 218 TA 219
Cdd:COG4778 228 FS 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
29-174 |
1.16e-06 |
|
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: 50.04 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE---------RAASIAW--VA---QQPNVTPEMT------L 87
Cdd:COG0411 23 VSLEVERgEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglPPHRIARlgIArtfQNPRLFPELTvlenvlV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 88 AALLGY-APIFDALSRLeqGQVLAADFDLLDGHWDLPDRLSLAFReadlppfsADRPVFSLSGGERmKAL-LCGAFVSGA 165
Cdd:COG0411 103 AAHARLgRGLLAALLRL--PRARREEREARERAEELLERVGLADR--------ADEPAGNLSYGQQ-RRLeIARALATEP 171
|
....*....
gi 694069477 166 DYLLLDEPT 174
Cdd:COG0411 172 KLLLLDEPA 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
31-192 |
1.24e-06 |
|
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: 49.65 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 31 VSLE---PSLCGLVGRNGVGKTRLLRLLAGLDSPADGHI----ERAASIAwvAQQPNVTPEMTLAALLGYAPIFDALSrl 103
Cdd:cd03296 21 VSLDipsGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVP--VQERNVGFVFQHYALFRHMTVFDNVA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 104 eqgqvlaadFDLLDGH-WDLPDRLSLAFREADLPPFS-----ADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHL 177
Cdd:cd03296 97 ---------FGLRVKPrSERPPEAEIRAKVHELLKLVqldwlADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170
....*....|....*
gi 694069477 178 DRQGREwlyhQLESW 192
Cdd:cd03296 168 DAKVRK----ELRRW 178
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
41-191 |
1.41e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 41 VGRNGVGKTRLLRLLAGLDSPADG----HIERAASIAWVAQQPNVTPEM----TlaallgyapifDALSRLEQGQVLAAD 112
Cdd:PRK10938 35 VGANGSGKSALARALAGELPLLSGerqsQFSHITRLSFEQLQKLVSDEWqrnnT-----------DMLSPGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 113 FDLLDGHWD--LPDRLSLAFREADLppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLE 190
Cdd:PRK10938 104 EIIQDEVKDpaRCEQLAQQFGITAL----LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179
|
.
gi 694069477 191 S 191
Cdd:PRK10938 180 S 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
23-174 |
1.50e-06 |
|
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: 49.60 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 23 QTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE-RAASIAwvaqqpNVTPEMTLAALLGYAP----I 96
Cdd:COG0410 17 HVLHG-VSLEVEEgEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDIT------GLPPHRIARLGIGYVPegrrI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 97 FDALS---RLEQGQVLAADFDllDGHWDLPDRLSLaF-READLppfsADRPVFSLSGGER-MKALlcG-AFVSGADYLLL 170
Cdd:COG0410 90 FPSLTveeNLLLGAYARRDRA--EVRADLERVYEL-FpRLKER----RRQRAGTLSGGEQqMLAI--GrALMSRPKLLLL 160
|
....
gi 694069477 171 DEPT 174
Cdd:COG0410 161 DEPS 164
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
41-202 |
1.64e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.68 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 41 VGRNGVGKTRLLRLLAGLDSPADGHIerAASIAWVAQQPNVTPEM-TLAALLGYAPIFDALSrleqgqvLAadfdlLDGH 119
Cdd:PRK11247 44 VGRSGCGKSTLLRLLAGLETPSAGEL--LAGTAPLAEAREDTRLMfQDARLLPWKKVIDNVG-------LG-----LKGQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 120 WDlpDRLSLAFREADLPPFSADRPVfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLES-WQG---G 195
Cdd:PRK11247 110 WR--DAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlWQQhgfT 186
|
....*..
gi 694069477 196 ALIASHD 202
Cdd:PRK11247 187 VLLVTHD 193
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
370-514 |
1.66e-06 |
|
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: 48.59 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRL---SVSA----------AYLDQHLTQLDLslsvmAHLsledtpldegll 436
Cdd:cd03214 28 VGILGPNGAGKSTLLKTLAGLLKPSSGEILLdgkDLASlspkelarkiAYVPQALELLGL-----AHL------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 437 rtrlaqlqlgADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG----AMLVVS 512
Cdd:cd03214 91 ----------ADR---PFNELSGGERQRVLLARALAQE--PPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVL 155
|
..
gi 694069477 513 HD 514
Cdd:cd03214 156 HD 157
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-178 |
3.05e-06 |
|
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: 48.42 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAD---GHI-----ERAA-----SIAWVAQ 77
Cdd:cd03234 22 ILNDVSLHVESGQVM-------------AILGSSGSGKTTLLDAISGRVEGGGttsGQIlfngqPRKPdqfqkCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 78 QPNVTPEMTLAALLGYAPIF--DALSRLEQGQVLAADFDLLDghwdlpdrlsLAFREAdlppfsADRPVFSLSGGERMKA 155
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILrlPRKSSDAIRKKRVEDVLLRD----------LALTRI------GGNLVKGISGGERRRV 152
|
170 180
....*....|....*....|...
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLD 175
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-204 |
3.29e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 49.37 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPADGHI--------------ERaaSIAWVA 76
Cdd:COG1118 17 LLDDVSLEIASGELV-------------ALLGPSGSGKTTLLRIIAGLETPDSGRIvlngrdlftnlpprER--RVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 77 QQPNVTPEMTLAALLGYAPIFDALSRLE-QGQVLaadfDLLDghwdlpdrlslafrEADLPPFsADRPVFSLSGGERMKA 155
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEiRARVE----ELLE--------------LVQLEGL-ADRYPSQLSGGQRQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLD----RQGREWLYHQLESWQGGALIASHDRE 204
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQE 195
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-183 |
3.44e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 49.30 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 28 PLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERaaSIAWVAQQPNVTPEMTLAALLGY 93
Cdd:COG3839 21 DIDLDIEDgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrdvtdlppkDR--NIAMVFQSYALYPHMTVYENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 94 ApifdalsrLEQGQVLAADFDlldghwdlpDRLslafREA----DLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:COG3839 99 P--------LKLRKVPKAEID---------RRV----REAaellGLEDL-LDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170
....*....|....
gi 694069477 170 LDEPTNHLDRQGRE 183
Cdd:COG3839 157 LDEPLSNLDAKLRV 170
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
457-521 |
3.46e-06 |
|
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: 47.39 E-value: 3.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694069477 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIES---ALAAFPGAMLVVSHDEAFLQGL 521
Cdd:cd03230 96 LSGGMKQRLALAQALLHD--PELLILDEPTSGLDPESRREFWEllrELKKEGKTILLSSHILEEAERL 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
39-215 |
3.50e-06 |
|
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: 47.04 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIeraasiaWVAQQPnVTPEMTLAALlgyapifdalsrleqgqvlaadfdlldg 118
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPDSGEI-------LVDGKE-VSFASPRDAR---------------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 119 hwdlpdRLSLAFreadlppfsadrpVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGA 196
Cdd:cd03216 74 ------RAGIAM-------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGVA 134
|
170 180
....*....|....*....|
gi 694069477 197 LI-ASHdrelltRMPRIIEL 215
Cdd:cd03216 135 VIfISH------RLDEVFEI 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
453-518 |
3.53e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 3.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 453 PLSALSGGERLKAALACVLWRrEPaQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:PRK15064 152 LMSEVAPGWKLRVLLAQALFS-NP-DILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-190 |
3.63e-06 |
|
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: 48.39 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERaaSIAWVAQ 77
Cdd:cd03300 3 LENVSKFYG-GFVALDGVSLDIKEgEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgkditnlpphKR--PVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 78 QPNVTPEMTLAALLGYAPIFDALSRLEQGQVLAADFDL--LDGHwdlpdrlslafreadlppfsADRPVFSLSGGERMKA 155
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLvqLEGY--------------------ANRKPSQLSGGQQQRV 139
|
170 180 190
....*....|....*....|....*....|....*
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLDRQGREWLyhQLE 190
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDM--QLE 172
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
370-522 |
4.77e-06 |
|
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: 47.47 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 370 IALKGPNGCG----------KTtllktllgleQAASGDVRL------SVSAAYLDQ-----HLTQLDLSLSVMAHL---- 424
Cdd:COG4133 31 LALTGPNGSGkttllrilagLL----------PPSAGEVLWngepirDAREDYRRRlaylgHADGLKPELTVRENLrfwa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 425 SLEDTPLDEGLLRTRLAQLQLG--ADKvtlPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALA 502
Cdd:COG4133 101 ALYGLRADREAIDEALEAVGLAglADL---PVRQLSAGQKRRVALARLLLS--PAPLWLLDEPFTALDAAGVALLAELIA 175
|
170 180
....*....|....*....|...
gi 694069477 503 AFP---GAMLVVSHDEAFLQGLK 522
Cdd:COG4133 176 AHLargGAVLLTTHQPLELAAAR 198
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
39-173 |
5.24e-06 |
|
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: 48.04 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERA-ASIAWVAQQPNVTPEMTLAA-LLGYAPIFDALSRL 103
Cdd:TIGR04406 31 GLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmhERArLGIGYLPQEASIFRKLTVEEnIMAVLEIRKDLDRA 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 104 EQGQVLAAdfdlldghwdLPDRLSLAFreadlppfSADRPVFSLSGGERMKALLCGAFVSGADYLLLDEP 173
Cdd:TIGR04406 111 EREERLEA----------LLEEFQISH--------LRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
457-513 |
5.77e-06 |
|
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: 46.83 E-value: 5.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 457 LSGGERLKAALACVLWRRePAqLLLLDEPTNHLDLASTQAIESALAAFPGAM---LVVSH 513
Cdd:cd03246 97 LSGGQRQRLGLARALYGN-PR-ILVLDEPNSHLDVEGERALNQAIAALKAAGatrIVIAH 154
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
39-186 |
5.85e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.86 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIE--------------RAASIAWVAQQPNVTPEMTLAA--LLGYAP----IFD 98
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrsprdaQAAGIAIIHQELNLVPNLSVAEniFLGREPrrggLID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 99 ALSRLEQGQVLAADFDLldghwdlpdrlslafreaDLPPfsaDRPVFSLSGGER-----MKALlcgafVSGADYLLLDEP 173
Cdd:COG1129 114 WRAMRRRARELLARLGL------------------DIDP---DTPVGDLSVAQQqlveiARAL-----SRDARVLILDEP 167
|
170
....*....|...
gi 694069477 174 TNHLDRQGREWLY 186
Cdd:COG1129 168 TASLTEREVERLF 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
448-521 |
7.03e-06 |
|
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: 46.41 E-value: 7.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694069477 448 DKVTLPLSalsGGERLKAALACVLwRREPaQLLLLDEPTNHLDLASTQAIESAL----AAFPGAMLVVSHDEAFLQGL 521
Cdd:cd03229 95 ENIALGLS---GGQQQRVALARAL-AMDP-DVLLLDEPTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARL 167
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
455-518 |
7.51e-06 |
|
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: 48.60 E-value: 7.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFL 518
Cdd:COG4988 472 RGLSGGQAQRLALARALLR--DAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL 535
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
458-521 |
1.07e-05 |
|
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: 46.66 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 458 SGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQA----IESALAAfpG-AMLVVSHDEAFLQGL 521
Cdd:COG4778 154 SGGEQQRVNIARGFIADPP--LLLLDEPTASLDAANRAVvvelIEEAKAR--GtAIIGIFHDEEVREAV 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
39-215 |
1.10e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIE-----------RAASIAWVA---QQPNVTPEMTLAA--LLGYAP------- 95
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILidgqemrfastTAALAAGVAiiyQELHLVPEMTVAEnlYLGQLPhkggivn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 96 ----IFDALSRLEQgqvLAADFDlldghwdlpdrlslafreadlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:PRK11288 114 rrllNYEAREQLEH---LGVDID-------------------------PDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 694069477 172 EPTNHLDRQGREWLY---HQLESwQGGALI-ASHdrelltRMPRIIEL 215
Cdd:PRK11288 166 EPTSSLSAREIEQLFrviRELRA-EGRVILyVSH------RMEEIFAL 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
455-519 |
1.21e-05 |
|
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: 48.29 E-value: 1.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 455 SALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFLQ 519
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRN--PRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIR 674
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
38-193 |
1.47e-05 |
|
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: 46.56 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 38 CGLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERaaSIAWVAQQPNVTPEMTLAALLGYAPIFDALSRLE 104
Cdd:cd03299 28 FVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditnlppeKR--DISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 105 -QGQVLAADFDLLDGHWdlpdrlslafreadlppfsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGRE 183
Cdd:cd03299 106 iERKVLEIAEMLGIDHL-------------------LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170
....*....|
gi 694069477 184 WLYHQLESWQ 193
Cdd:cd03299 167 KLREELKKIR 176
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
369-487 |
1.53e-05 |
|
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: 44.95 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 369 RIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSA-------------AYLDQHlTQLDLSLSV-------MAHLSLED 428
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQD-PQLFPRLTVrenlrlgLLLKGLSK 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694069477 429 TPLDEGL--LRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTN 487
Cdd:pfam00005 92 REKDARAeeALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTK--PKLLLLDEPTA 150
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
410-492 |
1.73e-05 |
|
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: 45.95 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 410 HLT---QLDLSLSVMAHLsledTPLDEGLLRTRLAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEPT 486
Cdd:cd03298 84 HLTveqNVGLGLSPGLKL----TAEDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKP--VLLLDEPF 156
|
....*.
gi 694069477 487 NHLDLA 492
Cdd:cd03298 157 AALDPA 162
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
455-518 |
2.61e-05 |
|
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: 47.07 E-value: 2.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAI-ESALAAFPG-AMLVVSHDEAFL 518
Cdd:COG4987 470 RRLSGGERRRLALARALLR--DAPILLLDEPTEGLDAATEQALlADLLEALAGrTVLLITHRLAGL 533
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
39-174 |
2.73e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIE--------------RAASIAWVAQQPNVTPEMTLA--ALLGYAPIF----- 97
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvrirsprdaIALGIGMVHQHFMLVPNLTVAenIVLGLEPTKggrld 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 98 --DALSRLEQgqvLAADFDLldghwdlpdrlslafreaDLPPfsaDRPVFSLSGGER-----MKALLCgafvsGADYLLL 170
Cdd:COG3845 115 rkAARARIRE---LSERYGL------------------DVDP---DAKVEDLSVGEQqrveiLKALYR-----GARILIL 165
|
....
gi 694069477 171 DEPT 174
Cdd:COG3845 166 DEPT 169
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
40-180 |
2.74e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLdspadgHIERAASIAWVAQQPNVTPEmtlaallgyAPIFDALSRLeqGQVLAAdFDLLD-- 117
Cdd:COG2401 61 IVGASGSGKSTLLRLLAGA------LKGTPVAGCVDVPDNQFGRE---------ASLIDAIGRK--GDFKDA-VELLNav 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694069477 118 GHWDLPdrlslAFReadlppfsadRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:COG2401 123 GLSDAV-----LWL----------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-178 |
3.41e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.39 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsVSLEPSlcglvgrnGVGKTRLLRLLAGLDSPADGHIERAAS------------------- 71
Cdd:PRK11124 17 ALFDITLDCPQGETL-----VLLGPS--------GAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkairelrrn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 72 IAWVAQQPNVTPEMTLAALLGYAPIfdALSRLEQGQVLAADFDLLDghwdlpdRLSLAfreadlpPFsADRPVFSLSGGE 151
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNLIEAPC--RVLGLSKDQALARAEKLLE-------RLRLK-------PY-ADRFPLHLSGGQ 146
|
170 180
....*....|....*....|....*..
gi 694069477 152 RMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-208 |
3.55e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.45 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPADGHI----------ERAA------SIAW 74
Cdd:PRK10419 27 VLNNVSLSLKSGETV-------------ALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaklNRAQrkafrrDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 75 VAQQP--NVTPEMTLAALLGyAPIFDALSRLEQGQVlaadfdlldghwdlpDRLSLAFREADLPPFSADRPVFSLSGGER 152
Cdd:PRK10419 94 VFQDSisAVNPRKTVREIIR-EPLRHLLSLDKAERL---------------ARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 153 MKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQ---GGA-LIASHDRELLTR 208
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqqfGTAcLFITHDLRLVER 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-229 |
4.95e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.87 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 14 QVTCQFATGQTLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPADGHI---------ERAASIAWVAQQPNVTp 83
Cdd:PRK10908 6 HVSKAYLGGRQALQGVTFHMRPGeMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrLKNREVPFLRRQIGMI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 84 eMTLAALLGYAPIFD--ALSRLEQGQVLAadfdlldghwDLPDRLSLAFREADLPPFSADRPVfSLSGGERMKALLCGAF 161
Cdd:PRK10908 85 -FQDHHLLMDRTVYDnvAIPLIIAGASGD----------DIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694069477 162 VSGADYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTRMPRIIeLTPTALRSYGGNYDE 229
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRM-LTLSDGHLHGGVGGE 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-218 |
5.24e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.09 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 5 AHIPAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGH------------------ 65
Cdd:PRK14271 17 AAAPAMAAVNLTLGFA-GKTVLDQVSMGFPArAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvllggrsifnyrd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 66 -IERAASIAWVAQQPNVTPEMTLAALLGYAPIFDALSRLEQGQVLAADFDLLdGHWD-LPDRLSlafreadlppfsaDRP 143
Cdd:PRK14271 96 vLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV-GLWDaVKDRLS-------------DSP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 144 vFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG--GALIASH---------DRELLTRMPRI 212
Cdd:PRK14271 162 -FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHnlaqaarisDRAALFFDGRL 240
|
....*.
gi 694069477 213 IELTPT 218
Cdd:PRK14271 241 VEEGPT 246
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-178 |
5.32e-05 |
|
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: 44.80 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPADGHIeraasiaWVAQQPnvTPEMTLAAL 90
Cdd:cd03261 15 VLKGVDLDVRRGEIL-------------AIIGPSGSGKSTLLRLIVGLLRPDSGEV-------LIDGED--ISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 91 L------GY----APIFDALSRLEQGQVlaadfdLLDGHWDLPDRL-----SLAFREADLPPFsADRPVFSLSGGERMKA 155
Cdd:cd03261 73 YrlrrrmGMlfqsGALFDSLTVFENVAF------PLREHTRLSEEEireivLEKLEAVGLRGA-EDLYPAELSGGMKKRV 145
|
170 180
....*....|....*....|...
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLD 168
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
370-514 |
5.86e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 44.71 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLSV-SAAYLDQHLtQLDLSLSVMAHL-SLEDTPLDEGLLRTRLAQ-LQLg 446
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYI-KADYEGTVRDLLsSITKDFYTHPYFKTEIAKpLQI- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694069477 447 ADKVTLPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLD----LASTQAIES-ALAAFPGAMlVVSHD 514
Cdd:cd03237 106 EQILDREVPELSGGELQRVAIAACLSK--DADIYLLDEPSAYLDveqrLMASKVIRRfAENNEKTAF-VVEHD 175
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
448-514 |
6.93e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.65 E-value: 6.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 448 DKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHD 514
Cdd:PRK14246 145 DRLNSPASQLSGGQQQRLTIARALALK--PKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
36-191 |
6.95e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 44.72 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 36 SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIeRAASI--AWVAQQPNVTP-----------------EMTLAALLGYAPI 96
Cdd:PRK13643 33 SYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-TVGDIvvSSTSKQKEIKPvrkkvgvvfqfpesqlfEETVLKDVAFGPQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 97 FDALSRLEQGQVLAADFDLLDghwdlpdrLSLAFREadlppfsadRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:PRK13643 112 NFGIPKEKAEKIAAEKLEMVG--------LADEFWE---------KSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170
....*....|....*
gi 694069477 177 LDRQGREWLYHQLES 191
Cdd:PRK13643 175 LDPKARIEMMQLFES 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
40-178 |
7.06e-05 |
|
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: 44.02 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIawVAQQPNVTPEMTLAA--LLGYAPIFDaLSRLE 104
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtaappaDRPVSM--LFQENNLFAHLTVEQnvGLGLSPGLK-LTAED 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694069477 105 QGQVLAAdfdlldghwdlPDRLSLAFREADLPPfsadrpvfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03298 106 RQAIEVA-----------LARVGLAGLEKRLPG--------ELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-234 |
7.54e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.32 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 20 ATGQTLFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWVAQQPnvtpem 85
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTLlfegedistlkpeIYRQQVSYCAQTP------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 86 tlaALLGYApIFDALSRLEQGQVLAADfdlldghwdlPDRLSLAFREADLPPFSADRPVFSLSGGERMKALLCGAFVSGA 165
Cdd:PRK10247 91 ---TLFGDT-VYDNLIFPWQIRNQQPD----------PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694069477 166 DYLLLDEPTNHLDRQGR----EWLYHQLESWQGGALIASHDRELLTRMPRIIELTPtalrsYGGNYDEYQRQR 234
Cdd:PRK10247 157 KVLLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQP-----HAGEMQEARYEL 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
417-521 |
8.28e-05 |
|
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: 45.20 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 417 SLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALA-CVLWRrepAQLLLLDEPTNHLDLASTQ 495
Cdd:TIGR02633 364 VLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAkMLLTN---PRVLILDEPTRGVDVGAKY 440
|
90 100
....*....|....*....|....*....
gi 694069477 496 AIE---SALAAFPGAMLVVSHDEAFLQGL 521
Cdd:TIGR02633 441 EIYkliNQLAQEGVAIIVVSSELAEVLGL 469
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
29-205 |
8.64e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 44.34 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE------RAASIAWVAQQPNVT---PEMTLAAllgyAPIFD 98
Cdd:PRK13647 24 LSLSIPEgSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevNAENEKWVRSKVGLVfqdPDDQVFS----STVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 99 ALSRLEQGQVLAADfdlldghwDLPDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:PRK13647 100 DVAFGPVNMGLDKD--------EVERRVEEALKAVRMWDF-RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190
....*....|....*....|....*....|
gi 694069477 179 RQGREWLYHQLE--SWQGGALI-ASHDREL 205
Cdd:PRK13647 171 PRGQETLMEILDrlHNQGKTVIvATHDVDL 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
40-178 |
8.73e-05 |
|
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: 43.78 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERaaSIAWVAQQPNVTPEMTlaallgyapIFDALSrleqg 106
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdlppkDR--DIAMVFQNYALYPHMT---------VYDNIA----- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694069477 107 qvlaadFDLLDGHWDlPDRLSLAFRE-ADLPPFSA--DRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03301 95 ------FGLKLRKVP-KDEIDERVREvAELLQIEHllDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
360-513 |
8.84e-05 |
|
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: 43.14 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSvsaaylDQHLTQLDLSlSVMAHLSL--EDTPLDEGLLR 437
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID------GVDLRDLDLE-SLRKNIAYvpQDPFLFSGTIR 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694069477 438 TRLaqlqlgadkvtlplsaLSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:cd03228 94 ENI----------------LSGGQRQRIAIARALLRD--PPILILDEATSALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-213 |
9.11e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 44.24 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLDSPADGHIERA-------------ASIAWVAQQP-NVTPEMTLAALLGYApifdalsrLEQ 105
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlseetvwdvrRQVGMVFQNPdNQFVGATVQDDVAFG--------LEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 106 GQVlaadfdlldGHWDLPDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWL 185
Cdd:PRK13635 110 IGV---------PREEMVERVDQALRQVGMEDF-LNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190
....*....|....*....|....*....|..
gi 694069477 186 Y---HQLESWQGGALIA-SHDRELLTRMPRII 213
Cdd:PRK13635 180 LetvRQLKEQKGITVLSiTHDLDEAAQADRVI 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-174 |
9.15e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 31 VSLE-PS--LCGLVGRNGVGKTRLLRLLAGLDSPADGHIE-----------RAAS---IAWVAQQ--PNVTPEMTL---- 87
Cdd:NF033858 20 VSLDiPAgcMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadarhRRAVcprIAYMPQGlgKNLYPTLSVfenl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 88 ---AALLGyapifdaLSRLEQGQVLAadfDLLdghwdlpdrlslafREADLPPFsADRPVFSLSGGERMKALLCGAFVSG 164
Cdd:NF033858 100 dffGRLFG-------QDAAERRRRID---ELL--------------RATGLAPF-ADRPAGKLSGGMKQKLGLCCALIHD 154
|
170
....*....|
gi 694069477 165 ADYLLLDEPT 174
Cdd:NF033858 155 PDLLILDEPT 164
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
360-514 |
9.75e-05 |
|
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: 43.68 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRL--------SVSAAYLDQH--------LTQLDL-SLSVMA 422
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekeRKRIGYVPQRrsidrdfpISVRDVvLMGLYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 423 HLSLEDTP-------LDEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQ 495
Cdd:cd03235 98 HKGLFRRLskadkakVDEALERVGLSEL---ADR---QIGELSGGQQQRVLLARALVQD--PDLLLLDEPFAGVDPKTQE 169
|
170 180
....*....|....*....|..
gi 694069477 496 AIESALAAFPG---AMLVVSHD 514
Cdd:cd03235 170 DIYELLRELRRegmTILVVTHD 191
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
457-501 |
1.17e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.01 E-value: 1.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 694069477 457 LSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESAL 501
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSP--ILILDEATSALDTESERAIQAAL 523
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
422-514 |
1.21e-04 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 43.59 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 422 AHLSLED------------TPLDEGLLRTRLAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEP---- 485
Cdd:COG3840 84 PHLTVAQniglglrpglklTAEQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRP--ILLLDEPfsal 160
|
90 100 110
....*....|....*....|....*....|....
gi 694069477 486 -----TNHLDLASTQAIESALaafpgAMLVVSHD 514
Cdd:COG3840 161 dpalrQEMLDLVDELCRERGL-----TVLMVTHD 189
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
369-518 |
1.44e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 369 RIALKGPNGCGKTTLLKTLLG--------------LEQAASGD---------------VRLSVSAAYLDQHLTQLDLSLS 419
Cdd:PLN03073 205 HYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhVEQEVVGDdttalqcvlntdierTQLLEEEAQLVAQQRELEFETE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 420 VMAHLSLEDTPLDEGLLRTRLAQ-----------------------LQLGADKVTLPLSALSGGERLKAALACVLWrREP 476
Cdd:PLN03073 285 TGKGKGANKDGVDKDAVSQRLEEiykrlelidaytaearaasilagLSFTPEMQVKATKTFSGGWRMRIALARALF-IEP 363
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 694069477 477 aQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:PLN03073 364 -DLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFL 404
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
455-518 |
1.45e-04 |
|
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: 44.41 E-value: 1.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694069477 455 SALSGGERLKAALACVLWrREPaQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:TIGR03269 426 DELSEGERHRVALAQVLI-KEP-RIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFV 491
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
122-209 |
1.50e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.84 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 122 LPDRLSLAfreaDLPPFSADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGRE---WLYHQLESWQGGALI 198
Cdd:PRK13645 130 VPELLKLV----QLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRII 205
|
90
....*....|..
gi 694069477 199 -ASHDRELLTRM 209
Cdd:PRK13645 206 mVTHNMDQVLRI 217
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
142-222 |
1.81e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 142 RPVFSLSGGERMKALLCGAF-----VSGA-----DYLLLDEPTNHLDRQGREWLYHQLESWQGG---ALIASHDRELLTR 208
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALalsevLQNRggarlEALFIDEGFGTLDPEALEAVATALELIRTEnrmVGVISHVEELKER 198
|
90
....*....|....
gi 694069477 209 MPRIIELTPTALRS 222
Cdd:cd03279 199 IPQRLEVIKTPGGS 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
40-213 |
1.96e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.78 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLDSPADGHI----ERAASIAwvAQQPNVT---------PEMTLAALLGYApifdalsrLEQG 106
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAGFETPDSGRImldgQDITHVP--AENRHVNtvfqsyalfPHMTVFENVAFG--------LRMQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 107 QVLAADFDlldghwdlpDRLSLAFREADLPPFsADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLY 186
Cdd:PRK09452 115 KTPAAEIT---------PRVMEALRMVQLEEF-AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQ 184
|
170 180 190
....*....|....*....|....*....|..
gi 694069477 187 HQLESWQ---GGALI-ASHDR-ELLTRMPRII 213
Cdd:PRK09452 185 NELKALQrklGITFVfVTHDQeEALTMSDRIV 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
370-514 |
2.15e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 43.22 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRL------SVSAAYLDQHL------TQLDLSLSV----------MAHLSLE 427
Cdd:PRK13548 31 VAILGPNGAGKSTLLRALSGELSPDSGEVRLngrplaDWSPAELARRRavlpqhSSLSFPFTVeevvamgrapHGLSRAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 428 DTPL-DEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVL---WRREPAQ-LLLLDEPTNHLDLASTQAIESALA 502
Cdd:PRK13548 111 DDALvAAALAQVDLAHL---AGR---DYPQLSGGEQQRVQLARVLaqlWEPDGPPrWLLLDEPTSALDLAHQHHVLRLAR 184
|
170
....*....|....*.
gi 694069477 503 AF----PGAMLVVSHD 514
Cdd:PRK13548 185 QLaherGLAVIVVLHD 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
391-518 |
2.23e-04 |
|
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: 43.12 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 391 EQAASGDVRLSVSAAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLqlgadkVTLPLSALSGGERLKAALACV 470
Cdd:cd03236 80 TKLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHV------LDRNIDQLSGGELQRVAIAAA 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 694069477 471 LWRRepAQLLLLDEPTNHLD----LASTQAIESaLAAFPGAMLVVSHDEAFL 518
Cdd:cd03236 154 LARD--ADFYFFDEPSSYLDikqrLNAARLIRE-LAEDDNYVLVVEHDLAVL 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
440-515 |
2.49e-04 |
|
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: 42.48 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 440 LAQLQLGADKVTLPlSALSGGERLKAALAcvlwrR----EPaQLLLLDEPTNHLDLASTQAIESALAAFPG----AMLVV 511
Cdd:cd03255 125 LERVGLGDRLNHYP-SELSGGQQQRVAIA-----RalanDP-KIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVV 197
|
....
gi 694069477 512 SHDE 515
Cdd:cd03255 198 THDP 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
454-501 |
2.58e-04 |
|
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: 42.15 E-value: 2.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 694069477 454 LSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESAL 501
Cdd:cd03213 109 LRGLSGGERKRVSIALELVSNPS--LLFLDEPTSGLDSSSALQVMSLL 154
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
315-515 |
2.64e-04 |
|
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: 43.50 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 315 AVQQARERVEEETPVMFTLPGSEVAA------GKQVLVVESLQLDHAPAAPLNWRIDGPM----RIALKGPNGCGKTTLL 384
Cdd:TIGR02868 299 RVRAAAERIVEVLDAAGPVAEGSAPAagavglGKPTLELRDLSAGYPGAPPVLDGVSLDLppgeRVAILGPSGSGKSTLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 385 KTLLGLEQAASGDVRLS-VSAAYLDQHLTQLDLSLSVM-AHLSleDTPLDEGLLRTR-----------LAQLQLGADKVT 451
Cdd:TIGR02868 379 ATLAGLLDPLQGEVTLDgVPVSSLDQDEVRRRVSVCAQdAHLF--DTTVRENLRLARpdatdeelwaaLERVGLADWLRA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 452 LPL----------SALSGGERLKAALACVLWrrEPAQLLLLDEPTNHLDL-ASTQAIESALAAFPG-AMLVVSHDE 515
Cdd:TIGR02868 457 LPDgldtvlgeggARLSGGERQRLALARALL--ADAPILLLDEPTEHLDAeTADELLEDLLAALSGrTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
455-513 |
3.14e-04 |
|
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: 42.46 E-value: 3.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694069477 455 SALSGGERLKAALACVLWRrEPaQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:cd03248 149 SQLSGGQKQRVAIARALIR-NP-QVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
140-213 |
4.10e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 42.34 E-value: 4.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 140 ADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL----ESWQGGALIASHDRELLTRMP-RII 213
Cdd:PRK13637 138 KDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLAdRII 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
370-497 |
4.92e-04 |
|
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: 41.93 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VSAAYLDQHL----------TQLDLSLSVMAHLSL--EDTPLDEGL 435
Cdd:cd03267 50 VGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglVPWKRRKKFLrrigvvfgqkTQLWWDLPVIDSFYLlaAIYDLPPAR 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 436 LRTRLAQ----LQLGaDKVTLPLSALSGGERLKAALACVLWrREPaQLLLLDEPTNHLDLASTQAI 497
Cdd:cd03267 130 FKKRLDElselLDLE-ELLDTPVRQLSLGQRMRAEIAAALL-HEP-EILFLDEPTIGLDVVAQENI 192
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
369-492 |
5.51e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.49 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 369 RIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSaaylDQHLT---QLDLSL-----SVMAHLSLEDT---PLDEGLlr 437
Cdd:PRK10771 27 RVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ----DHTTTppsRRPVSMlfqenNLFSHLTVAQNiglGLNPGL-- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 438 tRL-----AQLQLGADKVT-------LPlSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLA 492
Cdd:PRK10771 101 -KLnaaqrEKLHAIARQMGiedllarLP-GQLSGGQRQRVALARCLVREQP--ILLLDEPFSALDPA 163
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-67 |
6.20e-04 |
|
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: 41.50 E-value: 6.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPADGHIE 67
Cdd:COG1127 20 VLDGVSLDVPRGEIL-------------AIIGGSGSGKSVLLKLIIGLLRPDSGEIL 63
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-180 |
6.28e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 42.52 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLdSPADGH-----IERAAS--------IAWVAQQPNVtPEMTL 87
Cdd:PRK11174 362 GKTLAGPLNFTLPAgQRIALVGPSGAGKTSLLNALLGF-LPYQGSlkingIELRELdpeswrkhLSWVGQNPQL-PHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 88 AA--LLGYAPIFDA--LSRLEQGQVLaadfDLLDghwDLPDRLSLAFREADLppfsadrpvfSLSGGERMKALLCGAFVS 163
Cdd:PRK11174 440 RDnvLLGNPDASDEqlQQALENAWVS----EFLP---LLPQGLDTPIGDQAA----------GLSVGQAQRLALARALLQ 502
|
170
....*....|....*..
gi 694069477 164 GADYLLLDEPTNHLDRQ 180
Cdd:PRK11174 503 PCQLLLLDEPTASLDAH 519
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
39-213 |
6.34e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHIEraasiaWVAQQPNVTPEMtlaallgyapifdalsrleqgqvlaadfdlldg 118
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDE------WDGITPVYKPQY--------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 119 hwdlpdrlslafreadlppfsadrpvFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGR----EWLYHQLESWQG 194
Cdd:cd03222 70 --------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKK 123
|
170
....*....|....*....
gi 694069477 195 GALIASHDRELLTRMPRII 213
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRI 142
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
457-515 |
8.29e-04 |
|
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: 40.42 E-value: 8.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694069477 457 LSGGERLKAALACVL--WRREPAQLLLLDEPTNHLDLASTQAIESALAAF--PGA-MLVVSHDE 515
Cdd:cd03227 78 LSGGEKELSALALILalASLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAqVIVITHLP 141
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
454-515 |
8.59e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 41.13 E-value: 8.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 454 LSALSGGERLKAALACVL--WRREPAQLLLLDEPTNHLDLASTQAIESAL-AAFPGA-MLVVSHDE 515
Cdd:cd03273 164 LTELSGGQRSLVALSLILalLLFKPAPMYILDEVDAALDLSHTQNIGRMIkTHFKGSqFIVVSLKE 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
371-514 |
9.20e-04 |
|
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: 41.01 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 371 ALKGPNGCG-----KTTLLKTLLGLEQAASGDVRLSVSAAYLD---------------QHLTQLDLS------LSVMAHL 424
Cdd:cd03260 30 ALIGPSGCGkstllRLLNRLNDLIPGAPDEGEVLLDGKDIYDLdvdvlelrrrvgmvfQKPNPFPGSiydnvaYGLRLHG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 425 SLEDTPLDEgLLRTRLAQLQLGaDKVTLPLSA--LSGGERLKAALACVlWRREPAqLLLLDEPTNHLDLASTQAIESALA 502
Cdd:cd03260 110 IKLKEELDE-RVEEALRKAALW-DEVKDRLHAlgLSGGQQQRLCLARA-LANEPE-VLLLDEPTSALDPISTAKIEELIA 185
|
170
....*....|....
gi 694069477 503 AF--PGAMLVVSHD 514
Cdd:cd03260 186 ELkkEYTIVIVTHN 199
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
36-202 |
9.45e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.37 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 36 SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERAA---------------SIAWVAQQPNVTpemtlaalLGYAPIFDAL 100
Cdd:PRK13636 33 EVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklreSVGMVFQDPDNQ--------LFSASVYQDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 101 SRLEQGQVLAADfdlldghwDLPDRLSLAFREADLPPFSaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:PRK13636 105 SFGAVNLKLPED--------EVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180
....*....|....*....|....*.
gi 694069477 181 GREWLYHQLESWQGGA----LIASHD 202
Cdd:PRK13636 176 GVSEIMKLLVEMQKELgltiIIATHD 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
429-513 |
9.47e-04 |
|
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: 41.22 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 429 TPLDEGLLRTRLAQLQLG--ADKvtlPLSALSGGERLKAALAcvlwR---REPaQLLLLDEPTNHLDLAST----QAIEs 499
Cdd:COG1119 116 TDEQRERARELLELLGLAhlADR---PFGTLSQGEQRRVLIA----RalvKDP-ELLILDEPTAGLDLGARelllALLD- 186
|
90
....*....|....*
gi 694069477 500 ALAAFPG-AMLVVSH 513
Cdd:COG1119 187 KLAAEGApTLVLVTH 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
417-512 |
1.03e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 417 SLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALA-CVLwrREPaQLLLLDEPTNHLDLASTQ 495
Cdd:PRK13549 366 ALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAkCLL--LNP-KILILDEPTRGIDVGAKY 442
|
90 100
....*....|....*....|
gi 694069477 496 AIE---SALAAFPGAMLVVS 512
Cdd:PRK13549 443 EIYkliNQLVQQGVAIIVIS 462
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
114-219 |
1.07e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 114 DLLDGhwdLPDRLSLAFrEADLPPFSADRPVFSLSGGERMKALLC---GAFVSGADYlLLDEPTNHLDRQGREWLYHQLE 190
Cdd:PRK00635 448 EVLQG---LKSRLSILI-DLGLPYLTPERALATLSGGEQERTALAkhlGAELIGITY-ILDEPSIGLHPQDTHKLINVIK 522
|
90 100 110
....*....|....*....|....*....|..
gi 694069477 191 SW--QGGA-LIASHDRELLTRMPRIIELTPTA 219
Cdd:PRK00635 523 KLrdQGNTvLLVEHDEQMISLADRIIDIGPGA 554
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
36-229 |
1.33e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.89 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 36 SLCGLVGRNGVGKTRLLRLLAGLDSPA-DGHIERAASIAWVAQQP---NVTPEMTLaaLLGYAPIFDALSRLEQGQVLAA 111
Cdd:PLN03232 644 SLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSwifNATVRENI--LFGSDFESERYWRAIDVTALQH 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 112 DFDLLDGHwdlpDRLSLAFREADLppfsadrpvfslSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQgrewLYHQL-- 189
Cdd:PLN03232 722 DLDLLPGR----DLTEIGERGVNI------------SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH----VAHQVfd 781
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 694069477 190 ----ESWQGGA-LIASHDRELLTRMPRIIELTPTALRSYgGNYDE 229
Cdd:PLN03232 782 scmkDELKGKTrVLVTNQLHFLPLMDRIILVSEGMIKEE-GTFAE 825
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-208 |
1.71e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.58 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAG--LDSPADGHIERAASIAWVAQQPNVTPEMTLAALLGYAPifdalSRLEQ 105
Cdd:PRK13547 20 LSLRIEPGrVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLP-----QAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 106 GQVLAADFDLLDGHWDLPDR-----------LSLAFREADLPPFSAdRPVFSLSGGE-------RMKALL--CGAFVSGA 165
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARRagalthrdgeiAWQALALAGATALVG-RDVTTLSGGElarvqfaRVLAQLwpPHDAAQPP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694069477 166 DYLLLDEPTNHLDrqgrewLYHQ---LES-------WQGGALIASHDRELLTR 208
Cdd:PRK13547 174 RYLLLDEPTAALD------LAHQhrlLDTvrrlardWNLGVLAIVHDPNLAAR 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
36-215 |
2.09e-03 |
|
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: 39.76 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 36 SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIERAASIAWVAQQP---------NVtpemtlaaLLGYapIFDAlSRLEqg 106
Cdd:cd03250 32 ELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPwiqngtireNI--------LFGK--PFDE-ERYE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 107 QVLAA-----DFDLLDGHwdlpdrlslafreadlppfsaDRPV-----FSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:cd03250 99 KVIKAcalepDLEILPDG---------------------DLTEigekgINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 694069477 177 LDRQGREWLYHQ--LESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:cd03250 158 VDAHVGRHIFENciLGLLLNNKtrILVTHQLQLLPHADQIVVL 200
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-178 |
2.11e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 40.09 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFATGQTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHIEraasiaWVAQQPNVT-------- 82
Cdd:COG4152 4 LKGLTKRFGDKTAVDD-VSFTVPKgEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL------WDGEPLDPEdrrrigyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 83 PE-------MT-------LAALLGYAPIfDALSRLEqgqvlaadfDLLDGHwDLPDRlslafreadlppfsADRPVFSLS 148
Cdd:COG4152 77 PEerglypkMKvgeqlvyLARLKGLSKA-EAKRRAD---------EWLERL-GLGDR--------------ANKKVEELS 131
|
170 180 190
....*....|....*....|....*....|
gi 694069477 149 GGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
457-513 |
2.34e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 40.53 E-value: 2.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 694069477 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:COG1132 477 LSGGQRQRIAIARALLKD--PPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
455-514 |
2.37e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 39.80 E-value: 2.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694069477 455 SALSGGERLKAALACVLwRREPAqLLLLDEPTNHLDLASTQAIESALAAFP----GAMLVVSHD 514
Cdd:PRK11629 144 SELSGGERQRVAIARAL-VNNPR-LVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHD 205
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
455-519 |
2.45e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 40.60 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESAL--AAFPGAMLVVSHDEAFLQ 519
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQ--PCQLLLLDEPTASLDAHSEQLVMQALnaASRRQTTLMVTHQLEDLA 548
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-178 |
2.74e-03 |
|
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: 39.49 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 12 LHQVTCQFATGQTLFGPLS-VSLE---PSLCGLVGRNGVGKTRLLRLLAGLDSPADGHIE--------------RAAS-- 71
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKdVSLSvpkGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKARrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 72 IAWVAQQPNVTPEMTLAALLGYAPIFDALSRLEQGQVLAADFDLLdghwDLPDRlslafreadlppfsADRPVFSLSGGE 151
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELV----GLEDK--------------ADAYPAQLSGGQ 145
|
170 180
....*....|....*....|....*..
gi 694069477 152 RMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALD 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
440-495 |
2.86e-03 |
|
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: 40.19 E-value: 2.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 694069477 440 LAQLQLGADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQ 495
Cdd:TIGR02633 125 LRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ--ARLLILDEPSSSLTEKETE 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
374-516 |
3.19e-03 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 39.28 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 374 GPNGCG-----------KttllktllgleQAASGDVRL--------SVSA----AYLDQHLTqLDLSLSVMAHLSL--ED 428
Cdd:COG1131 33 GPNGAGktttirmllglL-----------RPTSGEVRVlgedvardPAEVrrriGYVPQEPA-LYPDLTVRENLRFfaRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 429 TPLDEGLLRTRLAQL--QLG-ADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIES---ALA 502
Cdd:COG1131 101 YGLPRKEARERIDELleLFGlTDAADRKVGTLSGGMKQRLGLALALLHD--PELLILDEPTSGLDPEARRELWEllrELA 178
|
170
....*....|....*.
gi 694069477 503 AFPGAMLVVSH--DEA 516
Cdd:COG1131 179 AEGKTVLLSTHylEEA 194
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-183 |
3.33e-03 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 39.46 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPADGHI------------ERA------ASIAWVAQQPNVTPEMTLAA 89
Cdd:COG4525 26 VSLTIESgEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvpvtgpgaDRGvvfqkdALLPWLNVLDNVAFGLRLRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 90 LlgyapifDALSRLEQGQVLAADFDLLDghwdlpdrlslafreadlppfSADRPVFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:COG4525 106 V-------PKAERRARAEELLALVGLAD---------------------FARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170
....*....|....
gi 694069477 170 LDEPTNHLDRQGRE 183
Cdd:COG4525 158 MDEPFGALDALTRE 171
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
220-257 |
3.51e-03 |
|
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: 36.78 E-value: 3.51e-03
10 20 30
....*....|....*....|....*....|....*...
gi 694069477 220 LRSYGGNYDEYQRQRMAEQQAARAALEHAVTERRRTRA 257
Cdd:pfam12848 8 LTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEE 45
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
39-173 |
3.64e-03 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 38.97 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 39 GLVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIawVAQQPNVTPEMTLAA--LLGYAPIFDaLSRL 103
Cdd:COG3840 29 AILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltalppaERPVSM--LFQENNLFPHLTVAQniGLGLRPGLK-LTAE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 104 EQGQVLAAdfdlldghwdlPDRLSLAFREADLPPfsadrpvfSLSGGERMKALLCGAFVSGADYLLLDEP 173
Cdd:COG3840 106 QRAQVEQA-----------LERVGLAGLLDRLPG--------QLSGGQRQRVALARCLVRKRPILLLDEP 156
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
453-497 |
3.73e-03 |
|
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: 38.89 E-value: 3.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 694069477 453 PLSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAI 497
Cdd:cd03266 133 RVGGFSTGMRQKVAIARALVHDPP--VLLLDEPTTGLDVMATRAL 175
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-178 |
3.95e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 39.13 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 18 QFATGQTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGL-----------DSPADGH-------IERAASIAWVAQQ 78
Cdd:PRK14247 12 SFGQVEVLDG-VNLEIPDnTITALMGPSGSGKSTLLRVFNRLielypearvsgEVYLDGQdifkmdvIELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 79 PNVTPEMTLAALLGYAPifdALSRLEQGQVlaadfdlldghwDLPDRLSLAFREADLPPFSADR---PVFSLSGGERMKA 155
Cdd:PRK14247 91 PNPIPNLSIFENVALGL---KLNRLVKSKK------------ELQERVRWALEKAQLWDEVKDRldaPAGKLSGGQQQRL 155
|
170 180
....*....|....*....|...
gi 694069477 156 LLCGAFVSGADYLLLDEPTNHLD 178
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLD 178
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
37-215 |
4.12e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 40.09 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 37 LCGLVGRNGVGKTRLLRLLAGLDSPADGHIE-----------------RAASIAWVAQQPNVTPEMTLAALLGYAPIFDA 99
Cdd:PRK10535 36 MVAIVGASGSGKSTLMNILGCLDKPTSGTYRvagqdvatldadalaqlRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 100 LSRLEQgqvLAADFDLLDghwdlpdRLSLAFReADLPPFSadrpvfsLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR 179
Cdd:PRK10535 116 LERKQR---LLRAQELLQ-------RLGLEDR-VEYQPSQ-------LSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 694069477 180 QGRE---WLYHQLESWQGGALIASHDRELLTRMPRIIEL 215
Cdd:PRK10535 178 HSGEevmAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
134-202 |
4.14e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 39.30 E-value: 4.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694069477 134 DLPPFSADRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG-REWL--YHQLESWQGGALIASHD 202
Cdd:PRK13651 153 GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGvKEILeiFDNLNKQGKTIILVTHD 224
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
453-515 |
4.27e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694069477 453 PLSALSGGER----LKAALACVLWRREPAQLLLLDEPTNHLD------LasTQAIESALAAFPgAMLVVSHDE 515
Cdd:PRK03918 785 PLTFLSGGERialgLAFRLALSLYLAGNIPLLILDEPTPFLDeerrrkL--VDIMERYLRKIP-QVIIVSHDE 854
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
457-529 |
5.88e-03 |
|
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: 38.47 E-value: 5.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694069477 457 LSGGERLKAALACVLwRREPaQLLLLDEPTNHLDLASTQAIESalaafpgaMLVVSHDEAFLQGLKLTHSL--AW 529
Cdd:cd03299 130 LSGGEQQRVAIARAL-VVNP-KILLLDEPFSALDVRTKEKLRE--------ELKKIRKEFGVTVLHVTHDFeeAW 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
360-514 |
7.45e-03 |
|
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: 38.16 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSA---------AYLDQHL------TQLDLSLSVMAH- 423
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgraiPYLRRKIgvvfqdFRLLPDRNVYENv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 424 -LSLEDTPLDEGLLRTR----LAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIE 498
Cdd:cd03292 100 aFALEVTGVPPREIRKRvpaaLELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIM 176
|
170
....*....|....*....
gi 694069477 499 SALAAF--PGAMLVVS-HD 514
Cdd:cd03292 177 NLLKKInkAGTTVVVAtHA 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-209 |
8.01e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 38.10 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 36 SLCGLVGRNGVGKTRLLRLLAGL----DSP--ADGH-------------IERAASIAWVAQQPNVTPEMTLAALLGYAPI 96
Cdd:PRK14246 37 SIFGIMGPSGSGKSTLLKVLNRLieiyDSKikVDGKvlyfgkdifqidaIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 97 FDALSRLEQGQVLAADFDLLDGHW-DLPDRLslafreadlppfsaDRPVFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:PRK14246 117 SHGIKEKREIKKIVEECLRKVGLWkEVYDRL--------------NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 694069477 176 HLD---RQGREWLYHQLESwQGGALIASHDRELLTRM 209
Cdd:PRK14246 183 MIDivnSQAIEKLITELKN-EIAIVIVSHNPQQVARV 218
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
444-489 |
8.88e-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: 37.98 E-value: 8.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 694069477 444 QLGADKVTL--PLSALSGGE--RLKaaLACVLWRREPAQ-LLLLDEPTNHL 489
Cdd:cd03271 155 DVGLGYIKLgqPATTLSGGEaqRIK--LAKELSKRSTGKtLYILDEPTTGL 203
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
40-214 |
9.60e-03 |
|
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: 38.54 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 40 LVGRNGVGKTRLLRLLAGLDSPADGHI-------------ERAASIAWVAQQPNVTPEmTLAALLGYAPIFDALS-RLEQ 105
Cdd:TIGR02203 363 LVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdladytlaSLRRQVALVSQDVVLFND-TIANNIAYGRTEQADRaEIER 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 106 GQVLAADFDLLDGhwdLPDRLslafreadlppfsaDRPVFS----LSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG 181
Cdd:TIGR02203 442 ALAAAYAQDFVDK---LPLGL--------------DTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 694069477 182 REWLYHQLESWQGG--ALIASH--------DRELLTRMPRIIE 214
Cdd:TIGR02203 505 ERLVQAALERLMQGrtTLVIAHrlstiekaDRIVVMDDGRIVE 547
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
371-514 |
9.71e-03 |
|
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: 37.91 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 371 ALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VSAAYLDQHLTQ---------LDLSLSVMAHL----SLEDTPLDEGL 435
Cdd:COG4555 31 GLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgeDVRKEPREARRQigvlpdergLYDRLTVRENIryfaELYGLFDEELK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 436 LRT----RLAQLQLGADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAF---PGAM 508
Cdd:COG4555 111 KRIeeliELLGLEEFLDR---RVGELSTGMKKKVALARALVHD--PKVLLLDEPTNGLDVMARRLLREILRALkkeGKTV 185
|
....*.
gi 694069477 509 LVVSHD 514
Cdd:COG4555 186 LFSSHI 191
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
371-490 |
9.95e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 38.28 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694069477 371 ALKGPNGCGKTTLLKTLLGLEQAASGDVRLS-VSAAYLDQHLTQLDL---SLSVMAHLSLEDTpLDEGLLRTRLAQLQLg 446
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQRPINMmfqSYALFPHMTVEQN-IAFGLKQDKLPKAEI- 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 694069477 447 ADKVTLPLS-------------ALSGGERLKAALACVLWRRepAQLLLLDEPTNHLD 490
Cdd:PRK11607 127 ASRVNEMLGlvhmqefakrkphQLSGGQRQRVALARSLAKR--PKLLLLDEPMGALD 181
|
|
| |
