|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-521 |
1.22e-91 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 290.04 E-value: 1.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQFAtGQTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ--PTLTPETTL- 87
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRiGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPqePPLDDDLTVl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 88 -ATLLGYASVFAALSRLEQGQG--------------LADDFDLLDGhWDLTDRLS-----LAFREADLppfsaDRPAFSL 147
Cdd:COG0488 80 dTVLDGDAELRALEAELEELEAklaepdedlerlaeLQEEFEALGG-WEAEARAEeilsgLGFPEEDL-----DRPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 148 SGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGN 226
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVaTRILELDRGKLTLYPGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 227 YDEYQRQRmAEQQAARAAlehavtDRRRTRARMQKEHDAAQRRSAQtlrtvdtlniASfervKYKgAAKERPGALRRqhr 306
Cdd:COG0488 234 YSAYLEQR-AERLEQEAA------AYAKQQKKIAKEEEFIRRFRAK----------AR----KAK-QAQSRIKALEK--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 307 eqnssLNAAVQQARERveeetPVMFTLPGSEvAAGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGC 378
Cdd:COG0488 289 -----LEREEPPRRDK-----TVEIRFPPPE-RLGKKVLELEGLSksygdktlLDD-----LSLRIDRGDRIGLIGPNGA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 379 gkttllktllgLEQAASGDVRL--SVSAAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSA 456
Cdd:COG0488 353 gkstllkllagELEPDSGTVKLgeTVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGV 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 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 |
3.06e-45 |
|
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: 167.42 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAW--VAQQPTLTPETTL--ATLLGYASVFAALSRL----------- 103
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVgyLPQEPQLDPTKTVreNVEEGVAEIKDALDRFneisakyaepd 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 --------EQGQgLADDFDLLDGhWDLTDRLSLAFREADLPPFsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:TIGR03719 115 adfdklaaEQAE-LQEIIDAADA-WDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 176 HLDRQGREWLYHQLESWQGGALIASHDRELLTRMPR-IIELTPTALRSYGGNYDEYqrqrmAEQQAARAALEhAVTDRRR 254
Cdd:TIGR03719 191 HLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGwILELDRGRGIPWEGNYSSW-----LEQKQKRLEQE-EKEESAR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 255 TRArMQKEHDAAqRRSAQTLRTVDTLNIASFERVkykgaakerpgalrrqhreqnssLNAAVQQARERVEeetpvMFTLP 334
Cdd:TIGR03719 265 QKT-LKRELEWV-RQSPKGRQAKSKARLARYEEL-----------------------LSQEFQKRNETAE-----IYIPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 335 GSEVaaGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRL--SVSA 404
Cdd:TIGR03719 315 GPRL--GDKVIEAENLTkafgdkllIDD-----LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 405 AYLDQHLTQLDLSLSVMAHLSledtpldEGLLRTRLAQLQL------------GADKVTLpLSALSGGERLKAALACVLw 472
Cdd:TIGR03719 388 AYVDQSRDALDPNKTVWEEIS-------GGLDIIKLGKREIpsrayvgrfnfkGSDQQKK-VGQLSGGERNRVHLAKTL- 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 473 rREPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGLKlTHSLAWRETS 533
Cdd:TIGR03719 459 -KSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIA-THILAFEGDS 517
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-517 |
1.14e-43 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 164.35 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 40 LVGRNGVGKTRLLRLLAG---LDSpagGHI--ERAAAVAWVAQQPTLTPETT--------LATLLGYASVFAALSR---- 102
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGevlLDD---GRIiyEQDLIVARLQQDPPRNVEGTvydfvaegIEEQAEYLKRYHDISHlvet 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 103 ------LEQGQGLADDFDLLDGhWDLTDRLSLAFREADLPPfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:PRK11147 111 dpseknLNELAKLQEQLDHHNL-WQLENRINEVLAQLGLDP---DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 177 LDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTALRSYGGNYDEYQrqrMAEQQAARA-ALEHAVTDRRR 254
Cdd:PRK11147 187 LDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMAtRIVDLDRGKLVSYPGNYDQYL---LEKEEALRVeELQNAEFDRKL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 255 TrarmQKEhdAAQRRSAQTLRTVDtlniasfE-RVKykgAAKerpgALRRQHREQNSSLNAAVQQarerVEEETpvmftl 333
Cdd:PRK11147 264 A----QEE--VWIRQGIKARRTRN-------EgRVR---ALK----ALRRERSERREVMGTAKMQ----VEEAS------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 334 pgsevAAGKQVLVVESLqldhapaaplNWRIDGPM-------------RIALKGPNGCGKTTLLKTLLGLEQAASGDVR- 399
Cdd:PRK11147 314 -----RSGKIVFEMENV----------NYQIDGKQlvkdfsaqvqrgdKIALIGPNGCGKTTLLKLMLGQLQADSGRIHc 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 400 ---LSVsaAYLDQHLTQLDLSLSVMAHLSL-EDTPLDEGLLRTRLAQLQ--LGADKVTL-PLSALSGGERLKAALACVLW 472
Cdd:PRK11147 379 gtkLEV--AYFDQHRAELDPEKTVMDNLAEgKQEVMVNGRPRHVLGYLQdfLFHPKRAMtPVKALSGGERNRLLLARLFL 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1512845752 473 RrePAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAF 517
Cdd:PRK11147 457 K--PSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-519 |
1.87e-38 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 149.16 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHI---ERAAAVAWVAQQPTLTPETTLATLLG---YASVFAALSRL-EQGQGLAd 111
Cdd:PRK10636 31 GLVGKNGCGKSTLLALLKNEISADGGSYtfpGNWQLAWVNQETPALPQPALEYVIDGdreYRQLEAQLHDAnERNDGHA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 112 dFDLLDGHWDLTDRLSLAFREADLPP---FSAD---RPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWL 185
Cdd:PRK10636 110 -IATIHGKLDAIDAWTIRSRAASLLHglgFSNEqleRPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 186 YHQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGNYDEYQRQR---MAEQQA------ARAALEHAVTDRRRT 255
Cdd:PRK10636 189 EKWLKSYQGTLILISHDRDFLDPIvDKIIHIEQQSLFEYTGNYSSFEVQRatrLAQQQAmyesqqERVAHLQSYIDRFRA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 256 RARMQKEhdaAQRRsaqtlrtvdtlnIASFERVKYKGAAK-ERPgaLRRQHREQNSSLNaavqqarerveeetPVmftLP 334
Cdd:PRK10636 269 KATKAKQ---AQSR------------IKMLERMELIAPAHvDNP--FHFSFRAPESLPN--------------PL---LK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 335 GSEVAAG-KQVLVVESLQLDHAPAAplnwridgpmRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VSAAYLDQH- 410
Cdd:PRK10636 315 MEKVSAGyGDRIILDSIKLNLVPGS----------RIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgIKLGYFAQHq 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 411 LTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLD 490
Cdd:PRK10636 385 LEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQR--PNLLLLDEPTNHLD 462
|
490 500
....*....|....*....|....*....
gi 1512845752 491 LASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:PRK10636 463 LDMRQALTEALIDFEGALVVVSHDRHLLR 491
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-536 |
7.65e-38 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 146.42 E-value: 7.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHI-------------EraaavawvaqqPTLTPETTL--ATLLGYASVFAALSRL 103
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEArpapgikvgylpqE-----------PQLDPEKTVreNVEEGVAEVKAALDRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 -------------------EQGQgLADDFDLLDGhWDLTDRLSLAfreAD---LPPfsADRPAFSLSGGERMKALLCGAF 161
Cdd:PRK11819 106 neiyaayaepdadfdalaaEQGE-LQEIIDAADA-WDLDSQLEIA---MDalrCPP--WDAKVTKLSGGERRRVALCRLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 162 VSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMPR-IIELTPTALRSYGGNYDEYqrqrmAEQQA 240
Cdd:PRK11819 179 LEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGwILELDRGRGIPWEGNYSSW-----LEQKA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 241 ARAALEhAVTDRRRTRArMQKEHD-----AAQRRSAQTLRtvdtlnIASFErvkykgaakerpgalrrqhreqnsSLNAA 315
Cdd:PRK11819 254 KRLAQE-EKQEAARQKA-LKRELEwvrqsPKARQAKSKAR------LARYE------------------------ELLSE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 316 VQQARERVEEetpvMFTLPGSEVaaGKQVLVVESLQ--------LDHapaapLNWRIDGPMRIALKGPNGCGKTTLLKTL 387
Cdd:PRK11819 302 EYQKRNETNE----IFIPPGPRL--GDKVIEAENLSksfgdrllIDD-----LSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 388 LGLEQAASGDVRL--SVSAAYLDQHLTQLDLSLSVMAHLSledtpldEGLLRTRLAQLQL------------GAD---KV 450
Cdd:PRK11819 371 TGQEQPDSGTIKIgeTVKLAYVDQSRDALDPNKTVWEEIS-------GGLDIIKVGNREIpsrayvgrfnfkGGDqqkKV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 451 tlplSALSGGERLKAALACVLwrREPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQGLKlTHSLAWR 530
Cdd:PRK11819 444 ----GVLSGGERNRLHLAKTL--KQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIA-THILAFE 516
|
....*..
gi 1512845752 531 ETS-WHF 536
Cdd:PRK11819 517 GDSqVEW 523
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-520 |
1.27e-34 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 138.45 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLA---------------------GLDSPA-----GGHIERAA--AVAWVAQQPTLTPETTLATL 90
Cdd:PLN03073 207 GLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvGDDTTAlqcvlNTDIERTQllEEEAQLVAQQRELEFETETG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LGYASVFAALSRLEQGQGLADDFDLLDghwdLTDRLSLAFREADLPP---FSAD---RPAFSLSGGERMKALLCGAFVSG 164
Cdd:PLN03073 287 KGKGANKDGVDKDAVSQRLEEIYKRLE----LIDAYTAEARAASILAglsFTPEmqvKATKTFSGGWRMRIALARALFIE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 165 ADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELL-TRMPRIIELTPTALRSYGGNYDEYQR---QRMAEQQA 240
Cdd:PLN03073 363 PDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLnTVVTDILHLHGQKLVTYKGDYDTFERtreEQLKNQQK 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 241 ARAALEhavtdrrRTRARMQKEHDAAqRRSAQTLRTVDTlNIASFERVKYKGAAKERPGalrrqhreqnsslnaavqqar 320
Cdd:PLN03073 443 AFESNE-------RSRSHMQAFIDKF-RYNAKRASLVQS-RIKALDRLGHVDAVVNDPD--------------------- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 321 erveeetpVMFTLPGSEVAAGKQVLVVESLQLDHaPAAP-----LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAAS 395
Cdd:PLN03073 493 --------YKFEFPTPDDRPGPPIISFSDASFGY-PGGPllfknLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSS 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 396 GDVRLSVS---AAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLW 472
Cdd:PLN03073 564 GTVFRSAKvrmAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1512845752 473 RRepAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQG 520
Cdd:PLN03073 644 KK--PHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISG 689
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-217 |
8.82e-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: 116.78 E-value: 8.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAaavawvaqqPTLTpettlatlLGYasvfaal 100
Cdd:cd03221 12 GKLLLKDISLTINPgDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------STVK--------IGY------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 srLEQgqgladdfdlldghwdltdrlslafreadlppfsadrpafsLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:cd03221 68 --FEQ-----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190
....*....|....*....|....*....|....*...
gi 1512845752 181 GREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTP 217
Cdd:cd03221 105 SIEALEEALKEYPGTVILVSHDRYFLDQVAtKIIELED 142
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
39-233 |
7.89e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.78 E-value: 7.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAaavawvaqqPTLTpettlatlLGYasvfaalsrleqgqgLADDFDLLDG 118
Cdd:COG0488 345 GLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETVK--------IGY---------------FDQHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 HWDLTDRLSLAFREAD------------LPPFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLY 186
Cdd:COG0488 393 DKTVLDELRDGAPGGTeqevrgylgrflFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1512845752 187 HQLESWQGGALIASHDRELLTRM-PRIIELTPTALRSYGGNYDEYQRQ 233
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVaTRILEFEDGGVREYPGGYDDYLEK 520
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-219 |
1.87e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 109.49 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQptlTPETT 86
Cdd:COG4133 1 MMLEAENLSCRRG-ERLLFSGLSFTLAAgEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE---DYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 87 LATLLGYASVFAALSRLEQGQGLADdfdlLDGHWDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGAD 166
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAA----LYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 167 YLLLDEPTNHLDRQGREWLYHQLESW--QGGA-LIASHDRELLTRMpRIIELTPTA 219
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHlaRGGAvLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-521 |
5.96e-26 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 111.52 E-value: 5.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqpTLTPETTLATLlgyasvfaalsrlEQGQGLADDFDLLD- 117
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNV-------------SLDPNERLGKL-------------RQDQFAFEEFTVLDt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 118 ---GHWDL------TDR-----------------LSLAFREAD----------------LP------PFSADRPAFSLsg 149
Cdd:PRK15064 85 vimGHTELwevkqeRDRiyalpemseedgmkvadLEVKFAEMDgytaearagelllgvgIPeeqhygLMSEVAPGWKL-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 150 germKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELL----TRMPriiELTPTALRSYGG 225
Cdd:PRK15064 163 ----RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLnsvcTHMA---DLDYGELRVYPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 226 NYDEYqrqrMaeqQAARAALEHAVTDRRRTRARMQKEHDAAQRRSAQT---------LRTVDTLNIasfERVKykgaAKE 296
Cdd:PRK15064 236 NYDEY----M---TAATQARERLLADNAKKKAQIAELQSFVSRFSANAskakqatsrAKQIDKIKL---EEVK----PSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 297 RpgalrrqhreQNSSLnaavqqareRVEEETPvMFtlpgsevaagKQVLVVESLQ--LDHAPA-APLNWRIDGPMRIALK 373
Cdd:PRK15064 302 R----------QNPFI---------RFEQDKK-LH----------RNALEVENLTkgFDNGPLfKNLNLLLEAGERLAII 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 374 GPNGCGKTTLLKTLLGLEQAASGDVRLSVSAA--YLDQ-HLTQLDLSLSVMAHLSLEDTPL-DEGLLRTRLAQLQLGADK 449
Cdd:PRK15064 352 GENGVGKTTLLRTLVGELEPDSGTVKWSENANigYYAQdHAYDFENDLTLFDWMSQWRQEGdDEQAVRGTLGRLLFSQDD 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 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 |
9.41e-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: 97.13 E-value: 9.41e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 454 LSALSGGERLKAALACVLWrrEPAQLLLLDEPTNHLDLASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLL--ENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLD 131
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-190 |
9.52e-20 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 88.95 E-value: 9.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 9 AFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqpTL------ 81
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPgEVTALLGPNGSGKSTLLRALAGLLKPSSGEV-------------LLdgrdla 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 82 -TPETTLATLLGYasvfaalsrLEQGQGLADDFDLLD-------------GHWDLTDRL--SLAFREADLPPFsADRPAF 145
Cdd:COG1120 67 sLSRRELARRIAY---------VPQEPPAPFGLTVRElvalgryphlglfGRPSAEDREavEEALERTGLEHL-ADRPVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1512845752 146 SLSGGERMKALLCGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLD------LAHQLE 175
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-220 |
2.30e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.41 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 10 FVLHQVTCQFaTGQTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaaVAWVAQQPTLTPETtLA 88
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECvAITGPSGSGKSTLLRALADLDPPTSGEI-----YLDGKPLSAMPPPE-WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 89 TLLGYasVFAALSRLEQ--GQGLADDFDLLDGHWDlTDRLSLAFREADLPPFSADRPAFSLSGGERMKALLCGAFVSGAD 166
Cdd:COG4619 74 RQVAY--VPQEPALWGGtvRDNLPFPFQLRERKFD-RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 167 YLLLDEPTNHLDRQGR----EWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTAL 220
Cdd:COG4619 151 VLLLDEPTSALDPENTrrveELLREYLAEEGRAVLWVSHDPEQIERVAdRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-175 |
3.03e-19 |
|
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: 84.62 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 26 FGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ-------------PTLTPETTLATLL 91
Cdd:pfam00005 1 LKNVSLTLNPgEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkslrkeigyvfqdPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 92 GYASVFAALSRLEQGQGLADDFDLLDGhWDLTDRLslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGL-GDLADRP-------------VGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 1512845752 172 EPTN 175
Cdd:pfam00005 147 EPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-202 |
9.47e-19 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 84.02 E-value: 9.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLATLLGYasVFAAL 100
Cdd:cd03214 11 GRTVLDDLSLSIEAgEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL------LDGKDLASLSPKELARKIAY--VPQAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 SRLEqgqglADDFdlldghwdltdrlslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDrq 180
Cdd:cd03214 83 ELLG-----LAHL--------------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD-- 129
|
170 180 190
....*....|....*....|....*....|..
gi 1512845752 181 grewLYHQLE----------SWQGGALIASHD 202
Cdd:cd03214 130 ----IAHQIEllellrrlarERGKTVVMVLHD 157
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-237 |
1.75e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 88.41 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAwvaqqptltpettlatlLGYasvFAal 100
Cdd:PRK15064 331 NGPLFKNLNLLLEAgERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN-----------------IGY---YA-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 srleqgQGLADDFDlldGHWDLTDRLSLAFREAD------------LppFSAD---RPAFSLSGGERMKALLCGAFVSGA 165
Cdd:PRK15064 389 ------QDHAYDFE---NDLTLFDWMSQWRQEGDdeqavrgtlgrlL--FSQDdikKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 166 DYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTALRSYGGNYDEYQRQRMAE 237
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLAtRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-209 |
2.35e-18 |
|
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: 84.52 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQFATGQTLfGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHI---------ERAAAVAWVAQQPTL 81
Cdd:COG4555 4 VENLSKKYGKVPAL-KDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrkEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 82 TPETTLATLLGYASVFAALSRLeQGQGLADDFDlldghwDLTDRLslafreaDLPPFsADRPAFSLSGGERMKALLCGAF 161
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGL-FDEELKKRIE------ELIELL-------GLEEF-LDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 162 VSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGA-LIASHDRELLTRM 209
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGKTvLFSSHIMQEVEAL 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-215 |
2.64e-18 |
|
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: 83.74 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGqtlfgplsvslepSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAvawvaqqptltPETTLATL 90
Cdd:cd03235 14 VLEDVSFEVKPG-------------EFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----------PLEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LGYASVFAALSRleqgqgladDFDL---------LDGHWDLTDRLSLAFREA-----------DLppfsADRPAFSLSGG 150
Cdd:cd03235 70 IGYVPQRRSIDR---------DFPIsvrdvvlmgLYGHKGLFRRLSKADKAKvdealervglsEL----ADRQIGELSGG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 151 ERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTR-MPRIIEL 215
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEyFDRVLLL 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-215 |
4.85e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.60 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAavawvaqqptlTPETT 86
Cdd:COG1121 5 PAIELENLTVSYG-GRPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----------KPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 87 LATLLGYasvfaalsrLEQGQGLADDF-----DL----LDGHWDLTDRLSLAFREA--------DLPPFsADRPAFSLSG 149
Cdd:COG1121 73 ARRRIGY---------VPQRAEVDWDFpitvrDVvlmgRYGRRGLFRRPSRADREAvdealervGLEDL-ADRPIGELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 150 GERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGALIA-SHDRELLTRM-PRIIEL 215
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGKTILVvTHDLGAVREYfDRVLLL 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
29-215 |
5.74e-17 |
|
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: 78.59 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERaaavawvaqqptltpettlatllgyasvfaalsrleqgq 107
Cdd:cd03230 19 ISLTVEKgEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--------------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 glaDDFDLLDGHWDLTDRLSLAFREADLPP-FSAdRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLY 186
Cdd:cd03230 60 ---LGKDIKKEPEEVKRRIGYLPEEPSLYEnLTV-RENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|...
gi 1512845752 187 HQLESW--QGGA-LIASHD-RELLTRMPRIIEL 215
Cdd:cd03230 136 ELLRELkkEGKTiLLSSHIlEEAERLCDRVAIL 168
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-201 |
3.79e-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: 77.01 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQfATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavAWVAQQPTLTPETTLATL 90
Cdd:TIGR01189 3 ARNLACS-RGERMLFEGLSFTLNAgEALQVTGPNGIGKTTLLRILAGLLRPDSGEVR-----WNGTPLAEQRDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 -LGYAS-VFAALSRLEQGQGLADDFDLLDGH-WDLTDRLSLAFREadlppfsaDRPAFSLSGGERMKALLCGAFVSGADY 167
Cdd:TIGR01189 77 yLGHLPgLKPELSALENLHFWAAIHGGAQRTiEDALAAVGLTGFE--------DLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1512845752 168 LLLDEPTNHLDRQGREWLYHQLESW---QGGALIASH 201
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-215 |
5.82e-16 |
|
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: 75.36 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptltpettlatl 90
Cdd:cd00267 2 IENLSFRYG-GRTALDNVSLTLKAgEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 lgyasvfaalsrleqgqgladdfdlLDGHwDLTDRLSLAFReadlppfsaDRPA--FSLSGGERMKALLCGAFVSGADYL 168
Cdd:cd00267 58 -------------------------IDGK-DIAKLPLEELR---------RRIGyvPQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 169 LLDEPTNHLDRQGREWLYHQLESW-QGGA--LIASHDRELLTRMP-RIIEL 215
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRtvIIVTHDPELAELAAdRVIVL 153
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-215 |
1.03e-15 |
|
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: 76.60 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 10 FVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLA 88
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL------VDGKDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 89 TLLGY-----------ASVFA--ALSrLEQgQGLADDfdlldghwDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKA 155
Cdd:COG1122 75 RKVGLvfqnpddqlfaPTVEEdvAFG-PEN-LGLPRE--------EIRERVEEALELVGLEHL-ADRPPHELSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 156 LLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW--QGGALI-ASHDRELLTRM-PRIIEL 215
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGKTVIiVTHDLDLVAELaDRVIVL 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
29-202 |
1.61e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 75.87 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RAAAVAWVAQ------QPTLTPETTLATLLGYas 95
Cdd:COG1131 19 VSLTVEPgEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEVRRRigyvpqEPALYPDLTVRENLRF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 96 vFAALSRLEQGQGLADDFDLLDgHWDLTDRlslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:COG1131 97 -FARLYGLPRKEARERIDELLE-LFGLTDA--------------ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190
....*....|....*....|....*....|
gi 1512845752 176 HLDRQGREWLYHQLESW--QGGA-LIASHD 202
Cdd:COG1131 161 GLDPEARRELWELLRELaaEGKTvLLSTHY 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-206 |
2.88e-15 |
|
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: 74.81 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGQT-LFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLT------ 82
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 83 ---PETTLATLlgyaSVFA--ALSrLEQgQGLADDfdlldghwDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALL 157
Cdd:cd03225 81 fqnPDDQFFGP----TVEEevAFG-LEN-LGLPEE--------EIEERVEEALELVGLEGL-RDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 158 CGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELL 206
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLL 197
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
419-519 |
1.82e-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: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 419 SVMAHL----SLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALACVLwRREPaQLLLLDEPTNHLDLAST 494
Cdd:COG4619 89 TVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRAL-LLQP-DVLLLDEPTSALDPENT 166
|
90 100
....*....|....*....|....*....
gi 1512845752 495 QAIESALAAFP----GAMLVVSHDEAFLQ 519
Cdd:COG4619 167 RRVEELLREYLaeegRAVLWVSHDPEQIE 195
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-215 |
3.73e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.03 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGqtlfgplsvslepSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQqPTLT--PETTLA 88
Cdd:NF040873 7 VLHGVDLTIPAG-------------SLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYV-PQRSevPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 89 TLLGYASVFAALSRLEQGQGLADDFDLLDghwDLTDRLSLAfreaDLppfsADRPAFSLSGGERMKALLCGAFVSGADYL 168
Cdd:NF040873 73 TVRDLVAMGRWARRGLWRRLTRDDRAAVD---DALERVGLA----DL----AGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1512845752 169 LLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTRMPRIIEL 215
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
39-213 |
4.43e-13 |
|
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: 68.39 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptLTPETTLATL--------LGY----ASVFAALSR--LE 104
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPTSGSV--------------LLDGTDIRQLdpadlrrnIGYvpqdVTLFYGTLRdnIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 105 QGQGLADDFDLLDghwdltdrlslAFREADLPPFSADRPA----------FSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:cd03245 100 LGAPLADDERILR-----------AAELAGVTDFVNKHPNgldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1512845752 175 NHLDRQGREWLYHQLESWQGG--ALIASHDRELLTRMPRII 213
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRII 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-235 |
5.90e-13 |
|
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: 71.12 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 25 LFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptlTPETT-LA-------TLLGYAS 95
Cdd:TIGR03719 337 LIDDLSFKLPPgGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE--------------IGETVkLAyvdqsrdALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 96 VFAALSrleqgqglaDDFDLLD-GHWDLTDRLSLA---FREADlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:TIGR03719 403 VWEEIS---------GGLDIIKlGKREIPSRAYVGrfnFKGSD-----QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 172 EPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMP-RIIELTPTA-LRSYGGNYDEYQRQRM 235
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIAtHILAFEGDShVEWFEGNFSEYEEDKK 534
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
39-208 |
7.85e-13 |
|
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: 67.67 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIE---RAAAVAWVAQQPTLTPETTlATLLGYASVFAAL--------SRLEQGQ 107
Cdd:cd03226 30 ALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKERRKSIGYVMQDV-DYQLFTDSVREELllglkeldAGNEQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 GLADDFDLldghWDLtdrlslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW--- 184
Cdd:cd03226 109 TVLKDLDL----YAL-----------------KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERvge 167
|
170 180
....*....|....*....|....*
gi 1512845752 185 LYHQLESwQGGA-LIASHDRELLTR 208
Cdd:cd03226 168 LIRELAA-QGKAvIVITHDYEFLAK 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-215 |
1.56e-12 |
|
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: 69.79 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 5 AHIPAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavAWVAQQPTLTP 83
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPgERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL-----INGVDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 84 ETtLATLLGYAS----VFAAlsrleqgqGLADDfdLLDGHWDLTD-RLSLAFREADLPPFSADRP----------AFSLS 148
Cdd:COG4988 407 AS-WRRQIAWVPqnpyLFAG--------TIREN--LRLGRPDASDeELEAALEAAGLDEFVAALPdgldtplgegGRGLS 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 149 GGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRtvILITHRLALLAQADRILVL 544
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
29-215 |
1.76e-12 |
|
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: 66.99 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQqptltpETTLATL----LGYasVFaalsrl 103
Cdd:TIGR02211 24 VSLSIGKGeIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLS------SNERAKLrnkkLGF--IY------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 eQGQGLADDFD--------LLDGHWDLTDRLSLAF---READLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDE 172
Cdd:TIGR02211 90 -QFHHLLPDFTalenvampLLIGKKSVKEAKERAYemlEKVGLEHRINHRPS-ELSGGERQRVAIARALVNQPSLVLADE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1512845752 173 PTNHLDRQGREWLYH---QLESWQGGA-LIASHDRELLTRMPRIIEL 215
Cdd:TIGR02211 168 PTGNLDNNNAKIIFDlmlELNRELNTSfLVVTHDLELAKKLDRVLEM 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-201 |
1.87e-12 |
|
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: 66.47 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGQtlfgplsvslepsLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTltpeTTLATL 90
Cdd:cd03268 15 VLDDISLHVKKGE-------------IYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----RRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LGYASVFAALSRLEQGQGLADDFDLLDGHWD-LTDRLSLAFReadlppfsADRPAFSLSGGerMKALLC--GAFVSGADY 167
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDeVLDVVGLKDS--------AKKKVKGFSLG--MKQRLGiaLALLGNPDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1512845752 168 LLLDEPTNHLDRQGREWLYHQLESWQ---GGALIASH 201
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRdqgITVLISSH 184
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-215 |
4.11e-12 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 68.47 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 5 AHIPAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI-------------ERAA 70
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRRPALRPVSFTVPPgERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadadSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 71 AVAWVAQQPTLTPETTLATLlgyasvfaALSRLEqgqglADDfdlldghwdltDRLSLAFREADLPPFSADRPAF----- 145
Cdd:TIGR02857 397 QIAWVPQHPFLFAGTIAENI--------RLARPD-----ASD-----------AEIREALERAGLDEFVAALPQGldtpi 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 146 -----SLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:TIGR02857 453 geggaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRtvLLVTHRLALAALADRIVVL 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
34-208 |
9.68e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 34 EPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpetTLATLLGYASVFAALSRL----EQGQGL 109
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-------------------LVAGDDVEALSARAASRRvasvPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 110 ADDFDLLD-------------GHWDLTDRLSL--AFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK09536 89 SFEFDVRQvvemgrtphrsrfDTWTETDRAAVerAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1512845752 175 NHLDrqgrewLYHQ---LESWQ-----GGALIAS-HDRELLTR 208
Cdd:PRK09536 168 ASLD------INHQvrtLELVRrlvddGKTAVAAiHDLDLAAR 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-204 |
1.16e-11 |
|
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: 64.08 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ-----------PTLTPETTLAT 89
Cdd:cd03259 12 SVRALDDLSLTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPerrnigmvfqdYALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 90 LLGYASVFAALSRLEQgqgladdfdlldghwdlTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:cd03259 92 NIAFGLKLRGVPKAEI-----------------RARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1512845752 170 LDEPTNHLDRQGREWLYHQLESWQGG----ALIASHDRE 204
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRElgitTIYVTHDQE 192
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-224 |
2.30e-11 |
|
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: 63.47 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTP--ETTLATLLGYASVFAALS---RL 103
Cdd:cd03297 17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqQRKIGLVFQQYALFPHLNvreNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 EQGQGLADDFDLLDGHWDLTDRLSLAFREadlppfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGRE 183
Cdd:cd03297 97 AFGLKRKRNREDRISVDELLDLLGLDHLL--------NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1512845752 184 WLYHQLES----WQGGALIASHDRELLTRM-PRIIELTPTALRSYG 224
Cdd:cd03297 169 QLLPELKQikknLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-261 |
4.52e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 40 LVGRNGVGKTRLLRLLAGLDSPAGGHIE-------------RAAavawvaqqptLTPETTLATLLGyasvfaalsrleqg 106
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHcgtklevayfdqhRAE----------LDPEKTVMDNLA-------------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 107 qgladdfdllDGHWDLT----DRLSLAFREADL-PPFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG 181
Cdd:PRK11147 406 ----------EGKQEVMvngrPRHVLGYLQDFLfHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 182 REWLYHQLESWQGGALIASHDRELltrmpriIELTPT---------ALRSYGGNYDEYQRQR---MAEQQAARAALEHAV 249
Cdd:PRK11147 476 LELLEELLDSYQGTVLLVSHDRQF-------VDNTVTecwifegngKIGRYVGGYHDARQQQaqyLALKQPAVKKKEEAA 548
|
250
....*....|..
gi 1512845752 250 TDRRRTRARMQK 261
Cdd:PRK11147 549 APKAETVKRSSK 560
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-216 |
8.07e-11 |
|
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: 61.74 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeRAAAVAWVAQQPTLTPEttLATLLGYASVFAAL 100
Cdd:cd03231 12 GRALFSGLSFTLAAgEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-LLNGGPLDFQRDSIARG--LLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 SRLEQGQGLADDFDlLDGHWDLTDRLSLAFREadlppfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:cd03231 89 SVLENLRFWHADHS-DEQVEEALARVGLNGFE--------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1512845752 181 GREWLYHQLESW--QGGALIAS--HDRELLTRMPRIIELT 216
Cdd:cd03231 160 GVARFAEAMAGHcaRGGMVVLTthQDLGLSEAGARELDLG 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
36-275 |
1.66e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.65 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 36 SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQptltpETTLATLLGYASVFAALSRL---EQGQGLADd 112
Cdd:PRK10636 339 SRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFA-----QHQLEFLRADESPLQHLARLapqELEQKLRD- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 113 fdLLDGHWDLTDRLSlafreadlppfsadRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW 192
Cdd:PRK10636 413 --YLGGFGFQGDKVT--------------EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 193 QGGALIASHDRELLTRMPRIIELTPTA-LRSYGGNYDEYQrQRMAEQQAARAALEHAVTDRRRTRARM---QKEHDAAQR 268
Cdd:PRK10636 477 EGALVVVSHDRHLLRSTTDDLYLVHDGkVEPFDGDLEDYQ-QWLSDVQKQENQTDEAPKENNANSAQArkdQKRREAELR 555
|
....*..
gi 1512845752 269 RSAQTLR 275
Cdd:PRK10636 556 TQTQPLR 562
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
457-519 |
1.80e-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: 1.80e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHDEAFLQ 519
Cdd:cd00267 81 LSGGQRQRVALARALLLN--PDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAE 144
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-215 |
2.05e-10 |
|
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: 59.54 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlatLLGYASVFA-ALSRLEQG 106
Cdd:cd03246 21 VSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRV-----------------------RLDGADISQwDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 107 QG-LADDFDLLDGhwDLTDRLslafreadlppfsadrpafsLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWL 185
Cdd:cd03246 78 VGyLPQDDELFSG--SIAENI--------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|...
gi 1512845752 186 YHQLESWQGG---ALIASHDRELLTRMPRIIEL 215
Cdd:cd03246 136 NQAIAALKAAgatRIVIAHRPETLASADRILVL 168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-219 |
2.29e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.27 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 22 GQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLATLLGYASVF-AA 99
Cdd:PRK13539 14 GRVLFSGLSFTLAAgEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK------LDGGDIDDPDVAEACHYLGHRNAMkPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 100 LSRLEQGQGLAddfDLLDGHwDLTDRLSLAFreADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR 179
Cdd:PRK13539 88 LTVAENLEFWA---AFLGGE-ELDIAAALEA--VGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1512845752 180 QGREWL-----YHqLEswQGGALIASHDRELLTRMPRIIELTPTA 219
Cdd:PRK13539 161 AAVALFaelirAH-LA--QGGIVIAATHIPLGLPGARELDLGPFA 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
39-200 |
2.40e-10 |
|
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: 60.46 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraAAVAWVAQQPtLTPETTLATLLGYASVFAALSRLEQGQGLADdFDLLDG 118
Cdd:cd03266 35 GLLGPNGAGKTTTLRMLAGLLEPDAGFAT--VDGFDVVKEP-AEARRRLGFVSDSTGLYDRLTARENLEYFAG-LYGLKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 HwDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD----RQGREWLYHQLEswQG 194
Cdd:cd03266 111 D-ELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvmatRALREFIRQLRA--LG 186
|
....*.
gi 1512845752 195 GALIAS 200
Cdd:cd03266 187 KCILFS 192
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
370-519 |
2.74e-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: 59.96 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLSV----------SAAYLDQHLT-QLdLSLSVMAHL--SLEDTPLDEGLL 436
Cdd:cd03226 29 IALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDyQL-FTDSVREELllGLKELDAGNEQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 437 RTRLAQLQLGADKVTLPLSaLSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESA---LAAFPGAMLVVSH 513
Cdd:cd03226 108 ETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKD--LLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITH 184
|
....*.
gi 1512845752 514 DEAFLQ 519
Cdd:cd03226 185 DYEFLA 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
29-202 |
3.58e-10 |
|
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: 59.83 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlaTLLGYaSVFAALSRLEQGQ 107
Cdd:cd03263 21 LSLNVYKGEIfGLLGHNGAGKTTTLKMLTGELRPTSGTA----------------------YINGY-SIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 GLADDFDLLDghWDLTDRLSLAF--------------------READLPPFsADRPAFSLSGGERMKALLCGAFVSGADY 167
Cdd:cd03263 78 GYCPQFDALF--DELTVREHLRFyarlkglpkseikeevelllRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1512845752 168 LLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHD 202
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRsiILTTHS 191
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-215 |
4.44e-10 |
|
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: 58.55 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettl 87
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKV-------------AIVGPSGSGKSTLLKLLLRLYDPTSGEI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 88 atLLGyasvfaalsrleqGQGLADdfdlLDGHWdLTDRLSLAFREADLppfsadrpaFS-------LSGGERMKALLCGA 160
Cdd:cd03228 60 --LID-------------GVDLRD----LDLES-LRKNIAYVPQDPFL---------FSgtireniLSGGQRQRIAIARA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 161 FVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGG--ALIASHDRELLTRMPRIIEL 215
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTIRDADRIIVL 167
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-217 |
4.92e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 25 LFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAqqptltPETTLATLL--GYAS-VFAAL 100
Cdd:PRK13538 16 LFSGLSFTLNAGeLVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ------RDEYHQDLLylGHQPgIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 101 SRLE------QGQGLADDFDLldghWDLTDRLSLAFREadlppfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK13538 90 TALEnlrfyqRLHGPGDDEAL----WEALAQVGLAGFE--------DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1512845752 175 NHLDRQGREWLYHQLESW--QGG-ALIASH-DRELLTRMPRIIELTP 217
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHaeQGGmVILTTHqDLPVASDKVRKLRLGQ 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-215 |
5.12e-10 |
|
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: 62.09 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQF-ATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPET 85
Cdd:COG4987 332 PSLELEDVSFRYpGAGRPVLDGLSLTLPPgERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT------LGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 86 TLATLLGYAS----VFAA-------LSRLEqgqglADDFDLLDghwdltdrlslAFREADLPPFSADRP----------A 144
Cdd:COG4987 406 DLRRRIAVVPqrphLFDTtlrenlrLARPD-----ATDEELWA-----------ALERVGLGDWLAALPdgldtwlgegG 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 145 FSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL 215
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRtvLLITHRLAGLERMDRILVL 542
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
36-205 |
8.09e-10 |
|
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: 59.44 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 36 SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RAAAVAWVAQQPTLTPETTLATLLGYASVFAALSRLEQGQGL 109
Cdd:TIGR03873 28 SLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlHGLSRRARARRVALVEQDSDTAVPLTVRDVVALGRIPHRSLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 110 ADDFDLLDGhwdLTDRLSLAFREADLppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD---RQGREWLY 186
Cdd:TIGR03873 108 AGDSPHDAA---VVDRALARTELSHL----ADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvraQLETLALV 180
|
170
....*....|....*....
gi 1512845752 187 HQLESWQGGALIASHDREL 205
Cdd:TIGR03873 181 RELAATGVTVVAALHDLNL 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
453-518 |
2.11e-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: 2.11e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPGA---MLVVSHDEAFL 518
Cdd:cd03225 131 SPFTLSGGQKQRVAIAGVLAMD--PDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLL 197
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-207 |
2.25e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 58.66 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 23 QTLFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlaTLLGyASVFAALS 101
Cdd:PRK13537 20 KLVVDGLSFHVQRGECfGLLGPNGAGKTTTLRMLLGLTHPDAGSI----------------------SLCG-EPVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 102 RLEQGQGLADDFDLLDGhwDLTDR-----------LSLAFREADLPPF--------SADRPAFSLSGGERMKALLCGAFV 162
Cdd:PRK13537 77 HARQRVGVVPQFDNLDP--DFTVRenllvfgryfgLSAAAARALVPPLlefaklenKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1512845752 163 SGADYLLLDEPTNHLDRQGREWLYHQLESwqggaLIASHDRELLT 207
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRS-----LLARGKTILLT 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-256 |
2.32e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 24 TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE-------------RAaavawvaqqpTLTPETTlat 89
Cdd:PRK11819 338 LLIDDLSFSLPPgGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKigetvklayvdqsRD----------ALDPNKT--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 90 llgyasVFAALSrleqgqglaDDFDLLD-GHWDLTDRLSLA---FREADlppfsADRPAFSLSGGERMKALLCGAFVSGA 165
Cdd:PRK11819 405 ------VWEEIS---------GGLDIIKvGNREIPSRAYVGrfnFKGGD-----QQKKVGVLSGGERNRLHLAKTLKQGG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 166 DYLLLDEPTNHLDRQGREWLYHQLESWQGGALIASHDRELLTRMPRIIeltpTALRS------YGGNYDEYQ---RQRMA 236
Cdd:PRK11819 465 NVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI----LAFEGdsqvewFEGNFQEYEedkKRRLG 540
|
250 260
....*....|....*....|
gi 1512845752 237 EQqaarAALEHAVTDRRRTR 256
Cdd:PRK11819 541 AD----AARPHRIKYKKLTR 556
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-218 |
2.75e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.44 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFATGQTLFGPLSVSLEPslcG----LVGRNGVGKTRLLRLLAGLDSPAGGHIERaaavawvaqqPTLT- 82
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKP---GerllITGPSGSGKSTLLRAIAGLWPYGSGRIAR----------PAGAr 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 83 ----------PETTLATLLGYAsvfaalsrleqgqGLADDFDlldghwdlTDRLSLAFREADLPPFsADRPAFS------ 146
Cdd:COG4178 428 vlflpqrpylPLGTLREALLYP-------------ATAEAFS--------DAELREALEAVGLGHL-AERLDEEadwdqv 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 147 LSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL-ESWQGGALIA-SHDRELLTRMPRIIELTPT 218
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPGTTVISvGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
369-519 |
2.82e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 369 RIALKGPNGCGKT-------------------TLLKTLLGLEQ----AASGDVRLSVS------AAYLDQ-----HLTQL 414
Cdd:PRK11147 31 RVCLVGRNGAGKStlmkilngevllddgriiyEQDLIVARLQQdpprNVEGTVYDFVAegieeqAEYLKRyhdisHLVET 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 415 DLS---LSVMAHLSLEDTPLDEGLLRTR----LAQLQLGADKvtlPLSALSGGERLKAALACVLwRREPaQLLLLDEPTN 487
Cdd:PRK11147 111 DPSeknLNELAKLQEQLDHHNLWQLENRinevLAQLGLDPDA---ALSSLSGGWLRKAALGRAL-VSNP-DVLLLDEPTN 185
|
170 180 190
....*....|....*....|....*....|..
gi 1512845752 488 HLDLASTQAIESALAAFPGAMLVVSHDEAFLQ 519
Cdd:PRK11147 186 HLDIETIEWLEGFLKTFQGSIIFISHDRSFIR 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-202 |
3.00e-09 |
|
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: 57.10 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQFATGQ---TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQqptltPETTL 87
Cdd:cd03293 3 VRNVSKTYGGGGgavTALEDISLSVEEgEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 88 ----ATLLGYASVF--AALSrLEQgQGLADDfdlldghwDLTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLCGAF 161
Cdd:cd03293 78 vfqqDALLPWLTVLdnVALG-LEL-QGVPKA--------EARERAEELLELVGLSGFENAYPH-QLSGGMRQRVALARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1512845752 162 VSGADYLLLDEPTNHLDRQGR----EWLYHQLESWQGGALIASHD 202
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTReqlqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
39-209 |
3.72e-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: 56.04 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIERAaavawvaqqptltpettlatllgyasvfaalsrleqGQGLADDFDLLDg 118
Cdd:cd03229 30 ALLGPSGSGKSTLLRCIAGLEEPDSGSILID------------------------------------GEDLTDLEDELP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 hwDLTDRLSLAFREADLPP-FSA-DRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQGGA 196
Cdd:cd03229 73 --PLRRRIGMVFQDFALFPhLTVlENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQL 150
|
170
....*....|....*..
gi 1512845752 197 ----LIASHDRELLTRM 209
Cdd:cd03229 151 gitvVLVTHDLDEAARL 167
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-215 |
5.90e-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: 56.26 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 14 QVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptlTPETTLATLLG 92
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAgEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIR--------------VNGQDVSDLRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 93 yasvfAALSRLEQGQGLA-DDFDLL-----------------DGHWDLTDRLSLAFREADLPPFSADRPAfSLSGGERMK 154
Cdd:cd03292 71 -----RAIPYLRRKIGVVfQDFRLLpdrnvyenvafalevtgVPPREIRKRVPAALELVGLSHKHRALPA-ELSGGEQQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 155 ALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW-QGGA--LIASHDRELLTRM-PRIIEL 215
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTtvVVATHAKELVDTTrHRVIAL 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-178 |
6.09e-09 |
|
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: 56.05 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQFATGQTLfGPLSVSLEPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ------------P 79
Cdd:cd03264 3 LENLTKRYGKKRAL-DGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQklrrrigylpqeF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 80 TLTPETTLATLLGYAsvfAALSRLEQGQGLADDFDLLDgHWDLTDRlslafreadlppfsADRPAFSLSGGERMKALLCG 159
Cdd:cd03264 82 GVYPNFTVREFLDYI---AWLKGIPSKEVKARVDEVLE-LVNLGDR--------------AKKKIGSLSGGMRRRVGIAQ 143
|
170
....*....|....*....
gi 1512845752 160 AFVSGADYLLLDEPTNHLD 178
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLD 162
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-215 |
6.62e-09 |
|
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: 56.34 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 10 FVLHQVTCQFATGQTLFgplsvslepslcgLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLAT 89
Cdd:cd03255 18 QALKGVSLSIEKGEFVA-------------IVGPSGSGKSTLLNILGGLDRPTSGEVR------VDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 90 L----LGYasVFaalsrleQGQGLADDFDLLD-----------GHWDLTDRLSLAFREADLPPFSADRPAfSLSGGERMK 154
Cdd:cd03255 79 FrrrhIGF--VF-------QSFNLLPDLTALEnvelplllagvPKKERRERAEELLERVGLGDRLNHYPS-ELSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 155 ALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESWQGGALI-ASHDRELLTRMPRIIEL 215
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEvmeLLRELNKEAGTTIVvVTHDPELAEYADRIIEL 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
453-516 |
1.57e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.55 E-value: 1.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHDEA 516
Cdd:NF040873 116 QLGELSGGQRQRALLAQGLAQE--ADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
400-527 |
1.78e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 400 LSVSAAYLDQH---LTQLD----LSLSVMAHLSLEDtplDEGLLRTRLAQLQLGaDKVTLPLSALSGGERLKAALACVL- 471
Cdd:PRK03695 67 LARHRAYLSQQqtpPFAMPvfqyLTLHQPDKTRTEA---VASALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAAVVl 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 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 |
1.87e-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: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 358 APLNWRIDGPMRIALKGPNGCGkTTLLKTLLGLEQAASGDVRL------SVSAAYLDQH---LTQLDLSLSVMA---HLS 425
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAG-KSTLLARMAGLLPGQGEILLngrplsDWSAAELARHrayLSQQQSPPFAMPvfqYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 426 L-----EDTPLDEGLLRTRLAQLQLgADKVTLPLSALSGGERLKAALACVLWRREP-----AQLLLLDEPTNHLDLASTQ 495
Cdd:COG4138 92 LhqpagASSEAVEQLLAQLAEALGL-EDKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpeGQLLLLDEPMNSLDVAQQA 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1512845752 496 AIESALAAFP---GAMLVVSHDeaflqglkLTHSL 527
Cdd:COG4138 171 ALDRLLRELCqqgITVVMSSHD--------LNHTL 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-182 |
1.91e-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: 56.84 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPettLATL 90
Cdd:COG1123 280 AVDDVSLTLRRGETL-------------GLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE---LRRR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LG------YASVFAALSRLEQ-GQGLaDDFDLLDGHwDLTDRLSLAFREADLPPFSADRPAFSLSGGERMKALLCGAFVS 163
Cdd:COG1123 344 VQmvfqdpYSSLNPRMTVGDIiAEPL-RLHGLLSRA-ERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALAL 421
|
170
....*....|....*....
gi 1512845752 164 GADYLLLDEPTNHLDRQGR 182
Cdd:COG1123 422 EPKLLILDEPTSALDVSVQ 440
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
39-178 |
3.05e-08 |
|
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: 54.65 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGhieraaavawvaqqptltpETTLATLLGYASVFAALSRLE----QGQGLAddfd 114
Cdd:cd03267 51 GFIGPNGAGKTTTLKILSGLLQPTSG-------------------EVRVAGLVPWKRRKKFLRRIGvvfgQKTQLW---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 115 lldghWDLTDRLSLAFREA--DLPPFSA-----------------DRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTN 175
Cdd:cd03267 108 -----WDLPVIDSFYLLAAiyDLPPARFkkrldelselldleellDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
...
gi 1512845752 176 HLD 178
Cdd:cd03267 183 GLD 185
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-214 |
3.16e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 54.71 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFATGQ---TLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVaqqptLTP 83
Cdd:COG1116 6 PALELRGVSKRFPTGGggvTALDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 84 ETTL----ATLLGYASVFA--ALSRLEQGQGLADDFDLLDghwDLTDRLSLAFREADLPpfsadrpaFSLSGGERMKALL 157
Cdd:COG1116 81 DRGVvfqePALLPWLTVLDnvALGLELRGVPKAERRERAR---ELLELVGLAGFEDAYP--------HQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 158 CGAFVSGADYLLLDEPTNHLDRQGREWLYHQLES-WQGG---ALIASHDRE----------LLTRMP-RIIE 214
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETgktVLFVTHDVDeavfladrvvVLSARPgRIVE 221
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-207 |
3.20e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 22 GQTLFGPLSVSLE-PSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLAT--LLGYASVFA 98
Cdd:PLN03073 521 GPLLFKNLNFGIDlDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSnpLLYMMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 99 ALSRLEQGQGLaddfdlldGHWDLTDRLSLafreadlppfsadRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:PLN03073 601 GVPEQKLRAHL--------GSFGVTGNLAL-------------QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180
....*....|....*....|....*....
gi 1512845752 179 RQGREWLYHQLESWQGGALIASHDRELLT 207
Cdd:PLN03073 660 LDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-206 |
3.26e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPsLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLATLLG-------YASVFAALS 101
Cdd:PRK13638 22 LDFSLSP-VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQdpeqqifYTDIDSDIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 102 RLEQGQGLADDfdlldghwDLTDRLSLAFREADLPPFSaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG 181
Cdd:PRK13638 101 FSLRNLGVPEA--------EITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180
....*....|....*....|....*...
gi 1512845752 182 REWLYHQLE--SWQGG-ALIASHDRELL 206
Cdd:PRK13638 172 RTQMIAIIRriVAQGNhVIISSHDIDLI 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
38-191 |
4.46e-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: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 38 CGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLAtlLGY----ASVFAALSRLEqgqgladdf 113
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRR--IGYvfqeARLFPHLSVRG--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 114 DLLDGHWDLTDRLSLAFREA-----DLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQ 188
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERviellGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
...
gi 1512845752 189 LES 191
Cdd:TIGR02142 174 LER 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-202 |
5.25e-08 |
|
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: 53.95 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvAQQPTLT--PETTLATLLGyaSVFAALSRLEQGQGLADDFDLl 116
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIE--------IELDTVSykPQYIKADYEG--TVRDLLSSITKDFYTHPYFKT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 117 dghwDLTDRLSLafrEADLppfsaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGR----EWLYHQLESW 192
Cdd:cd03237 98 ----EIAKPLQI---EQIL-----DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENN 165
|
170
....*....|
gi 1512845752 193 QGGALIASHD 202
Cdd:cd03237 166 EKTAFVVEHD 175
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
453-514 |
5.59e-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: 5.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG---AMLVVSHD 514
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQD--PDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-190 |
6.02e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 10 FVLHQVTCQFAtGQTLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptLTPETTLA 88
Cdd:PRK10575 12 FALRNVSFRVP-GRTLLHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI--------------LLDAQPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 89 TLLGYAsvFA-ALSRLEQGQGLADDFDLLD-------------GHWDLTDRLSL--AFREADLPPFsADRPAFSLSGGER 152
Cdd:PRK10575 77 SWSSKA--FArKVAYLPQQLPAAEGMTVRElvaigrypwhgalGRFGAADREKVeeAISLVGLKPL-AHRLVDSLSGGER 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1512845752 153 MKALLCGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALD------IAHQVD 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-274 |
6.09e-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: 55.29 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFATGQT-LFGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLdSPAGGHIEraAAVAWVAQQPTLTPET 85
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVpAVDGVSLTIAPGETvALVGESGSGKSTLALALMGL-LPHGGRIS--GEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 86 TLATLLGYasVF----AALSRLEQGQGLADDFDLLD-GHWDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGA 160
Cdd:COG1123 80 LRGRRIGM--VFqdpmTQLNPVTVGDQIAEALENLGlSRAEARARVLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 161 FVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG----GALIASHDRELLTRMP-RIIELtptalrsyggnydeyQRQRM 235
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHDLGVVAEIAdRVVVM---------------DDGRI 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 1512845752 236 AEQQAARAALEHAVTDRRRTRARMQKEHDAAQRRSAQTL 274
Cdd:COG1123 222 VEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
41-202 |
6.16e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 41 VGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptLTPETTLATLLGYASVFAALSRLEQGQGLADDFDL-LDGH 119
Cdd:PRK11247 44 VGRSGCGKSTLLRLLAGLETPSAGEL--------------LAGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLgLKGQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 120 WdlTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLES-WQG---G 195
Cdd:PRK11247 110 W--RDAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlWQQhgfT 186
|
....*..
gi 1512845752 196 ALIASHD 202
Cdd:PRK11247 187 VLLVTHD 193
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
39-235 |
6.47e-08 |
|
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: 55.23 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RaaavawvaqqpTLTPETtLATLLGY----ASVFA-------ALS 101
Cdd:COG2274 505 AIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlR-----------QIDPAS-LRRQIGVvlqdVFLFSgtireniTLG 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 102 RLEqgqglADDFDLLDghwdltdrlslAFREADLPPFSADRP----------AFSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:COG2274 573 DPD-----ATDEEIIE-----------AARLAGLHDFIEALPmgydtvvgegGSNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 172 EPTNHLDRQGREWLYHQLESWQGGA--LIASHDRELLTRMPRIIEL---------TPTALRSYGGNYDEYQRQRM 235
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLKGRtvIIIAHRLSTIRLADRIIVLdkgrivedgTHEELLARKGLYAELVQQQL 711
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
39-206 |
6.84e-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: 53.32 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLATL-LGY----ASVFAALSRLEQGQGLADDF 113
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIVGLVKPDSGKIL------LDGQDITKLPMHKRARLgIGYlpqeASIFRKLTVEENILAVLEIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 114 DLLDGHWdlTDRLSLAFREADLPPfSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR---QGREWLYHQLE 190
Cdd:cd03218 104 GLSKKER--EEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPiavQDIQKIIKILK 180
|
170
....*....|....*..
gi 1512845752 191 SWQGGALIASHD-RELL 206
Cdd:cd03218 181 DRGIGVLITDHNvRETL 197
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-215 |
7.68e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.21 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFATGQ---TLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVawvaqqptLTP 83
Cdd:COG4181 7 PIIELRGLTKTVGTGAgelTILKGISLEVEAGeSVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--------LFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 84 --ETTLATL----LGYasVF------AALSRLE------QGQGLADDFDLLDghwDLTDRLSLAFREADLPPfsadrpaf 145
Cdd:COG4181 79 ldEDARARLrarhVGF--VFqsfqllPTLTALEnvmlplELAGRRDARARAR---ALLERVGLGHRLDHYPA-------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 146 SLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESWQGGALI-ASHDRELLTRMPRIIEL 215
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELNRERGTTLVlVTHDPALAARCDRVLRL 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-189 |
8.73e-08 |
|
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: 54.67 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavAWVAQQPTLTPETT 86
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPgERVAILGPSGSGKSTLLATLAGLLDPLQGEV------TLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 87 LATLLGY----ASVFAALSR--LEQGQGLADDFDLLDghwdltdrlslAFREADLPPFSADRP----------AFSLSGG 150
Cdd:TIGR02868 407 VRRRVSVcaqdAHLFDTTVRenLRLARPDATDEELWA-----------ALERVGLADWLRALPdgldtvlgegGARLSGG 475
|
170 180 190
....*....|....*....|....*....|....*....
gi 1512845752 151 ERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL 189
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
374-518 |
1.48e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 374 GPNGCGKTTLLKTLLGLEQAASGDVRLSVSAAYLDQHLTQlDLSLSVMAHLSLEDTPLDEGLLRTRLAQ-LQLGA--DKv 450
Cdd:PRK13409 372 GPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKP-DYDGTVEDLLRSITDDLGSSYYKSEIIKpLQLERllDK- 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 451 tlPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:PRK13409 450 --NVKDLSGGELQRVAIAACLSR--DADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMI 517
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-215 |
1.62e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.51 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptLTPETTLATLLGYASvfAALSRLEQG- 106
Cdd:PRK11629 28 VSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV--------------IFNGQPMSKLSSAAK--AELRNQKLGf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 107 ----QGLADDFD--------LLDGH---WDLTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLD 171
Cdd:PRK11629 92 iyqfHHLLPDFTalenvampLLIGKkkpAEINSRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1512845752 172 EPTNHLDRQGREWLYH---QLESWQGGA-LIASHDRELLTRMPRIIEL 215
Cdd:PRK11629 171 EPTGNLDARNADSIFQllgELNRLQGTAfLVVTHDLQLAKRMSRQLEM 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
457-516 |
1.63e-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: 1.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 457 LSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEA 516
Cdd:TIGR02857 459 LSGGQAQRLALARAFLR--DAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLA 518
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
370-514 |
2.22e-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: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCG----------KTtllktllgleQAASGDVRL---SVSA----------AYLDQHlTQLDLSLSV------ 420
Cdd:COG1120 30 TALLGPNGSGkstllralagLL----------KPSSGEVLLdgrDLASlsrrelarriAYVPQE-PPAPFGLTVrelval 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 421 --MAHLSL--EDTPLDEGLLRTRLAQLQLG--ADKvtlPLSALSGGERLKAALACVLwrrepAQ---LLLLDEPTNHLDL 491
Cdd:COG1120 99 grYPHLGLfgRPSAEDREAVEEALERTGLEhlADR---PVDELSGGERQRVLIARAL-----AQeppLLLLDEPTSHLDL 170
|
170 180
....*....|....*....|....*..
gi 1512845752 492 ASTQAIES---ALAAFPG-AMLVVSHD 514
Cdd:COG1120 171 AHQLEVLEllrRLARERGrTVVMVLHD 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-214 |
2.25e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHieraaavawvaqqptltpettlATLLGyASVFAALSRLEQGQ 107
Cdd:TIGR01257 1958 LCVGVRPGECfGLLGVNGAGKTTTFKMLTGDTTVTSGD----------------------ATVAG-KSILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 GLADDFDLLDGHWDLTDRLSLAFREADLPP-----------------FSADRPAFSLSGGERMKALLCGAFVSGADYLLL 170
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAeeiekvanwsiqslglsLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 171 DEPTNHLDRQGREWLYHQLESW--QGGALI-ASHDRE----LLTRMPRIIE 214
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIirEGRAVVlTSHSMEeceaLCTRLAIMVK 2145
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
28-178 |
3.04e-07 |
|
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: 51.35 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 28 PLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ----------------------PTLTPE 84
Cdd:cd03257 23 DVSFSIKKgETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkirrkeiqmvfqdpmsslnPRMTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 85 TTLATLLgyasvfaalsrLEQGQgladdfdlLDGHWDLTDRLSLAFREADLPPFSADRPAFSLSGGERMKALLCGAFVSG 164
Cdd:cd03257 103 EQIAEPL-----------RIHGK--------LSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170
....*....|....
gi 1512845752 165 ADYLLLDEPTNHLD 178
Cdd:cd03257 164 PKLLIADEPTSALD 177
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
142-219 |
3.06e-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: 51.07 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 142 RPAFSLSGGERMKA------LLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL-ESWQGGA----LIASHDRELLTRMP 210
Cdd:cd03240 111 DMRGRCSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDEENIEESLAEIiEERKSQKnfqlIVITHDEELVDAAD 190
|
....*....
gi 1512845752 211 RIIELTPTA 219
Cdd:cd03240 191 HIYRVEKDG 199
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
370-491 |
3.29e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.55 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDV-------------RLSVSAAYLDQ-HLTQLDLS------------LSVMAH 423
Cdd:PRK11231 31 TALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpismlssrQLARRLALLPQhHLTPEGITvrelvaygrspwLSLWGR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 424 LSLEDTPL-DEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDL 491
Cdd:PRK11231 111 LSAEDNARvNQAMEQTRINHL---ADR---RLTDLSGGQRQRAFLAMVLAQDTP--VVLLDEPTTYLDI 171
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-191 |
4.00e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.14 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlaTLLGyASVFAALSRLEQGQ 107
Cdd:PRK13536 60 LSFTVASGECfGLLGPNGAGKSTIARMILGMTSPDAGKI----------------------TVLG-VPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 GLADDFDLLDGHWDLTDRLSLAFR---------EADLPPF--------SADRPAFSLSGGERMKALLCGAFVSGADYLLL 170
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRyfgmstreiEAVIPSLlefarlesKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180
....*....|....*....|.
gi 1512845752 171 DEPTNHLDRQGREWLYHQLES 191
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRS 217
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
391-514 |
6.28e-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: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 391 EQAASGDVRLSVSAAYLdqhltqldlsLSVMAHLSL--EDTPLDEGLLRTRLAQLQLgADKVTLPLSALSGGERLKAALA 468
Cdd:TIGR03873 81 EQDSDTAVPLTVRDVVA----------LGRIPHRSLwaGDSPHDAAVVDRALARTEL-SHLADRDMSTLSGGERQRVHVA 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1512845752 469 CVLwRREPaQLLLLDEPTNHLDLASTQAIESALA--AFPGAMLVVS-HD 514
Cdd:TIGR03873 150 RAL-AQEP-KLLLLDEPTNHLDVRAQLETLALVRelAATGVTVVAAlHD 196
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
457-519 |
6.83e-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: 6.83e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 457 LSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFLQ 519
Cdd:cd03245 141 LSGGQRQAVALARALLNDPP--ILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-68 |
7.88e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.47 E-value: 7.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIER 68
Cdd:COG1134 41 ALKDVSFEVERGESV-------------GIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
41-191 |
1.06e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 41 VGRNGVGKTRLLRLLAGLDSPAGGHieraaavawvaqqptltpettlatllgYASVFAALSRL--EQGQGLADD------ 112
Cdd:PRK10938 35 VGANGSGKSALARALAGELPLLSGE---------------------------RQSQFSHITRLsfEQLQKLVSDewqrnn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 113 FDLL----------------DGHWD--LTDRLSLAFREADLppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK10938 88 TDMLspgeddtgrttaeiiqDEVKDpaRCEQLAQQFGITAL----LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170
....*....|....*..
gi 1512845752 175 NHLDRQGREWLYHQLES 191
Cdd:PRK10938 164 DGLDVASRQQLAELLAS 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-213 |
1.07e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.40 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 40 LVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAvawvaqqpTLTPETTLATLLGYASVFAALSRLEQGQGLADD--FDLLD 117
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM--------VLSEETVWDVRRQVGMVFQNPDNQFVGATVQDDvaFGLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 118 G---HWDLTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLY---HQLES 191
Cdd:PRK13635 110 IgvpREEMVERVDQALRQVGMEDFLNREPH-RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLetvRQLKE 188
|
170 180
....*....|....*....|...
gi 1512845752 192 WQGGALIA-SHDRELLTRMPRII 213
Cdd:PRK13635 189 QKGITVLSiTHDLDEAAQADRVI 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
374-518 |
1.13e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 374 GPNGCGKTTLLKTLLGLEQAASGDVRLSVSAAYLDQHLTQlDLSLSVMAHLSLEDTP-LDEGLLRTRLAQ-LQLGA--DK 449
Cdd:COG1245 373 GPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISP-DYDGTVEEFLRSANTDdFGSSYYKTEIIKpLGLEKllDK 451
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 450 vtlPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:COG1245 452 ---NVKDLSGGELQRVAIAACLSR--DADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
12-201 |
1.15e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVtcQFATGQTLFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLtpeTTLATL 90
Cdd:PRK13541 4 LHQL--QFNIEQKNLFDLSITFLPSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC---TYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LGYASVFAALSRLEQGQGLADDFDLLDG---HWDLTDRLslafreadlppfsaDRPAFSLSGGERMKALLCGAFVSGADY 167
Cdd:PRK13541 79 LGLKLEMTVFENLKFWSEIYNSAETLYAaihYFKLHDLL--------------DEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1512845752 168 LLLDEPTNHLDRQGREWLYH--QLESWQGG-ALIASH 201
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNliVMKANSGGiVLLSSH 181
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
39-68 |
1.37e-06 |
|
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: 49.45 E-value: 1.37e-06
10 20 30
....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIER 68
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGIYPPDSGTVTV 81
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
40-216 |
1.48e-06 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 49.39 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 40 LVGRNGVGKTRLLRLLAGLDSPAGGHI------------ERAAAVAWVAQQPTLTPETTLAtlLGYASVFAALSRLEQGQ 107
Cdd:TIGR01184 16 LIGHSGCGKSTLLNLISGLAQPTSGGVilegkqitepgpDRMVVFQNYSLLPWLTVRENIA--LAVDRVLPDLSKSERRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 108 gladdfdLLDGHWDLtdrlsLAFREAdlppfsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYH 187
Cdd:TIGR01184 94 -------IVEEHIAL-----VGLTEA------ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....
gi 1512845752 188 QL-ESWQGG---ALIASHD-RELLTRMPRIIELT 216
Cdd:TIGR01184 156 ELmQIWEEHrvtVLMVTHDvDEALLLSDRVVMLT 189
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-201 |
1.61e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 25 LFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptltPETTLATLLGYASVFAALSRL 103
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVqGDNGAGKTTLLRVLAGLLHVESGQIQ---------------IDGKTATRGDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 104 EqgqGLADDFDLLDghwDLTDRLSLAFREADLPPFSA----------DRPAFSLSGGERMKALLCGAFVSGADYLLLDEP 173
Cdd:PRK13543 91 P---GLKADLSTLE---NLHFLCGLHGRRAKQMPGSAlaivglagyeDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 1512845752 174 TNHLDRQGREWLYHQLESW---QGGALIASH 201
Cdd:PRK13543 165 YANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-190 |
1.66e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 49.38 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTpeTTLATL 90
Cdd:PRK13548 17 LLDDVSLTLRPGEVV-------------AILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA--RRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LGYASV-FA-------ALSRLEQGQGLADDFDLLDghwdltdrlsLAFREADLPPFsADRPAFSLSGGERMKALL----- 157
Cdd:PRK13548 82 PQHSSLsFPftveevvAMGRAPHGLSRAEDDALVA----------AALAQVDLAHL-AGRDYPQLSGGEQQRVQLarvla 150
|
170 180 190
....*....|....*....|....*....|....
gi 1512845752 158 -CGAFVSGADYLLLDEPTNHLDrqgrewLYHQLE 190
Cdd:PRK13548 151 qLWEPDGPPRWLLLDEPTSALD------LAHQHH 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
370-514 |
1.90e-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: 48.20 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRL---SVSA----------AYLDQHLTQLDLslsvmAHLsledtpldegll 436
Cdd:cd03214 28 VGILGPNGAGKSTLLKTLAGLLKPSSGEILLdgkDLASlspkelarkiAYVPQALELLGL-----AHL------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 437 rtrlaqlqlgADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG----AMLVVS 512
Cdd:cd03214 91 ----------ADR---PFNELSGGERQRVLLARALAQE--PPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVL 155
|
..
gi 1512845752 513 HD 514
Cdd:cd03214 156 HD 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-178 |
2.76e-06 |
|
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: 48.65 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavAWVAQQPTLTPETTLATL 90
Cdd:cd03261 15 VLKGVDLDVRRGEIL-------------AIIGPSGSGKSTLLRLIVGLLRPDSGEVL-----IDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LGYASVFaalsrleQGQGLADDFDLLD------------GHWDLTDRLSLAFREADLPPFSADRPAfSLSGGERMKALLC 158
Cdd:cd03261 77 RRMGMLF-------QSGALFDSLTVFEnvafplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPA-ELSGGMKKRVALA 148
|
170 180
....*....|....*....|
gi 1512845752 159 GAFVSGADYLLLDEPTNHLD 178
Cdd:cd03261 149 RALALDPELLLYDEPTAGLD 168
|
|
| 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 1512845752 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIES---ALAAFPGAMLVVSHDEAFLQGL 521
Cdd:cd03230 96 LSGGMKQRLALAQALLHD--PELLILDEPTSGLDPESRREFWEllrELKKEGKTILLSSHILEEAERL 161
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-190 |
4.01e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.47 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTL------------TPE-TTLATLLGYA 94
Cdd:PRK11231 21 LSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLarrlallpqhhlTPEgITVRELVAYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 95 -----SVFAALSRleqgqglaDDFDLLDGHWDLTDRLSLafreadlppfsADRPAFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:PRK11231 101 rspwlSLWGRLSA--------EDNARVNQAMEQTRINHL-----------ADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180
....*....|....*....|.
gi 1512845752 170 LDEPTNHLDrqgrewLYHQLE 190
Cdd:PRK11231 162 LDEPTTYLD------INHQVE 176
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-174 |
5.53e-06 |
|
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: 47.43 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 23 QTLFGpLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIERaaavaWVAQQPTLTPETTLATLLGYA----SVF 97
Cdd:cd03224 14 QILFG-VSLTVPEGEIvALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-----DGRDITGLPPHERARAGIGYVpegrRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 98 AALSRLE------QGQGLADDFDLLDGHWDLTDRLSlAFReadlppfsaDRPAFSLSGGER-MKAlLCGAFVSGADYLLL 170
Cdd:cd03224 88 PELTVEEnlllgaYARRRAKRKARLERVYELFPRLK-ERR---------KQLAGTLSGGEQqMLA-IARALMSRPKLLLL 156
|
....
gi 1512845752 171 DEPT 174
Cdd:cd03224 157 DEPS 160
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
457-513 |
5.83e-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: 5.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 457 LSGGERLKAALACVLWRRePAqLLLLDEPTNHLDLASTQAIESALAAFPGAM---LVVSH 513
Cdd:cd03246 97 LSGGQRQRLGLARALYGN-PR-ILVLDEPNSHLDVEGERALNQAIAALKAAGatrIVIAH 154
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
370-522 |
6.24e-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: 47.09 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCG----------KTtllktllgleQAASGDVRL------SVSAAYLDQ-----HLTQLDLSLSVMAHL---- 424
Cdd:COG4133 31 LALTGPNGSGkttllrilagLL----------PPSAGEVLWngepirDAREDYRRRlaylgHADGLKPELTVRENLrfwa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 425 SLEDTPLDEGLLRTRLAQLQLG--ADkvtLPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALA 502
Cdd:COG4133 101 ALYGLRADREAIDEALEAVGLAglAD---LPVRQLSAGQKRRVALARLLLS--PAPLWLLDEPFTALDAAGVALLAELIA 175
|
170 180
....*....|....*....|...
gi 1512845752 503 AFP---GAMLVVSHDEAFLQGLK 522
Cdd:COG4133 176 AHLargGAVLLTTHQPLELAAAR 198
|
|
| 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 1512845752 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFL 518
Cdd:COG4988 472 RGLSGGQAQRLALARALLR--DAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL 535
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
448-521 |
8.49e-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: 8.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752 448 DKVTLPLSalsGGERLKAALACVLwRREPaQLLLLDEPTNHLDLASTQAIESAL----AAFPGAMLVVSHDEAFLQGL 521
Cdd:cd03229 95 ENIALGLS---GGQQQRVALARAL-AMDP-DVLLLDEPTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARL 167
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-219 |
9.46e-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: 47.04 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 10 FVLHQVTcqfatGQTL--FGPLSVSLEPSLC-GLVGRNGVGKTRLLRLLAGLDSPAGGHIeRAAAVAWVAQQPTLTPETT 86
Cdd:COG4778 14 FTLHLQG-----GKRLpvLDGVSFSVAAGECvALTGPSGAGKSTLLKCIYGNYLPDSGSI-LVRHDGGWVDLAQASPREI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 87 LA---TLLGYASVF-------AAL-----SRLEQGQGLADDFD----LLDghwdltdRLSLAFREADLPP--FSadrpaf 145
Cdd:COG4778 88 LAlrrRTIGYVSQFlrviprvSALdvvaePLLERGVDREEARArareLLA-------RLNLPERLWDLPPatFS------ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 146 slsGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREW---LYHQLESwQGGALIA-SHDRELLTRMP-RIIELTPTA 219
Cdd:COG4778 155 ---GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVvveLIEEAKA-RGTAIIGiFHDEEVREAVAdRVVDVTPFS 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
458-521 |
1.08e-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: 1.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 458 SGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQA----IESALAAfpG-AMLVVSHDEAFLQGL 521
Cdd:COG4778 154 SGGEQQRVNIARGFIADPP--LLLLDEPTASLDAANRAVvvelIEEAKAR--GtAIIGIFHDEEVREAV 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-178 |
1.11e-05 |
|
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: 46.50 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQFATGQTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPT---------L 81
Cdd:cd03269 3 VENVTKRFGRVTALDD-ISFSVEKgEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpeergL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 82 TPETTLATLLGYasvFAALSRLEQGQGLADDFDLLDgHWDLTDRlslafreadlppfsADRPAFSLSGGERMKALLCGAF 161
Cdd:cd03269 82 YPKMKVIDQLVY---LAQLKGLKKEEARRRIDEWLE-RLELSEY--------------ANKRVEELSKGNQQKVQFIAAV 143
|
170
....*....|....*..
gi 1512845752 162 VSGADYLLLDEPTNHLD 178
Cdd:cd03269 144 IHDPELLILDEPFSGLD 160
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
455-519 |
1.17e-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: 1.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 455 SALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHDEAFLQ 519
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRN--PRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIR 674
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
39-173 |
1.20e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.95 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqpTLTPE--TTL-----ATL-LGY----ASVFAALS----- 101
Cdd:COG1137 33 GLLGPNGAGKTTTFYMIVGLVKPDSGRI-------------FLDGEdiTHLpmhkrARLgIGYlpqeASIFRKLTvedni 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 102 ----------------RLEQgqgLADDFDLldghwdltDRLslafreadlppfsADRPAFSLSGGERMKALLCGAFVSGA 165
Cdd:COG1137 100 lavlelrklskkereeRLEE---LLEEFGI--------THL-------------RKSKAYSLSGGERRRVEIARALATNP 155
|
....*...
gi 1512845752 166 DYLLLDEP 173
Cdd:COG1137 156 KFILLDEP 163
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-206 |
1.34e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.65 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQFATGQTLfGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLATL 90
Cdd:PRK09544 7 LENVSVSFGQRRVL-SDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LGY----------ASVFAALSRLEQGQGLaddfdlldghwdltdrlslafreadlppfsaDRPAFSLSGGERMKALLCGA 160
Cdd:PRK09544 86 VNRflrlrpgtkkEDILPALKRVQAGHLI-------------------------------DAPMQKLSGGETQRVLLARA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1512845752 161 FVSGADYLLLDEPTNHLDRQGREWLY---HQLESWQG-GALIASHDRELL 206
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYdliDQLRRELDcAVLMVSHDLHLV 184
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-66 |
1.47e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 47.40 E-value: 1.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 8 PAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI 66
Cdd:COG3842 4 PALELENVSKRYG-DVTALDDVSLSIEPgEFVALLGPSGCGKTTLLRMIAGFETPDSGRI 62
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
369-487 |
1.64e-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: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 369 RIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSA-------------AYLDQHlTQLDLSLSV-------MAHLSLED 428
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQD-PQLFPRLTVrenlrlgLLLKGLSK 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 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 |
1.75e-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: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 410 HLT---QLDLSLSVMAHLsledTPLDEGLLRTRLAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEPT 486
Cdd:cd03298 84 HLTveqNVGLGLSPGLKL----TAEDRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKP--VLLLDEPF 156
|
....*.
gi 1512845752 487 NHLDLA 492
Cdd:cd03298 157 AALDPA 162
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
129-219 |
1.76e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 45.94 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 129 AFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR----QGREWLYHQLESWQGGALIASHDRE 204
Cdd:COG4136 117 ALEEAGLAGFADRDPA-TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAalraQFREFVFEQIRQRGIPALLVTHDEE 195
|
90
....*....|....*
gi 1512845752 205 LLTRMPRIIELTPTA 219
Cdd:COG4136 196 DAPAAGRVLDLGNWQ 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-178 |
2.23e-05 |
|
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: 45.63 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGL-----DSPAGGHIERAAAVAWVAQQPTLTPET 85
Cdd:cd03260 15 ALKDISLDIPKGEIT-------------ALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 86 TLATLLGYASVFAAlsrleqgqGLADDFDL---LDGHWD---LTDRLSLAFREADLPPFSADRP-AFSLSGGERMKALLC 158
Cdd:cd03260 82 RVGMVFQKPNPFPG--------SIYDNVAYglrLHGIKLkeeLDERVEEALRKAALWDEVKDRLhALGLSGGQQQRLCLA 153
|
170 180
....*....|....*....|
gi 1512845752 159 GAFVSGADYLLLDEPTNHLD 178
Cdd:cd03260 154 RALANEPEVLLLDEPTSALD 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-178 |
2.24e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqPTLTpettlatlLGYasvfaalsrleQGQGLADDFD---- 114
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEGEVD-----------EDLK--------ISY-----------KPQYISPDYDgtve 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 115 -LLDGHwdLTDRLSLAFREADL-PPFSA----DRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:COG1245 420 eFLRSA--NTDDFGSSYYKTEIiKPLGLekllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
39-173 |
2.53e-05 |
|
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: 45.73 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavaWVAQQPTLTPETTLATL-LGY----ASVFAALSrleqgqgLADDF 113
Cdd:TIGR04406 31 GLLGPNGAGKTTSFYMIVGLVRPDAGKIL------IDGQDITHLPMHERARLgIGYlpqeASIFRKLT-------VEENI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512845752 114 D-LLDGHWDLTDRLSLAFREADLPPFS----ADRPAFSLSGGERMKALLCGAFVSGADYLLLDEP 173
Cdd:TIGR04406 98 MaVLEIRKDLDRAEREERLEALLEEFQishlRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-178 |
2.54e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 46.23 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptltpettlatLLGY-------------A 94
Cdd:COG4586 41 ISFTIEPgEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR----------------------VLGYvpfkrrkefarriG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 95 SVFaalsrleqGQ--------GLADDFDLLDGHWDLTDRlslAFREA--------DLPPFsADRPAFSLSGGERMKALLC 158
Cdd:COG4586 99 VVF--------GQrsqlwwdlPAIDSFRLLKAIYRIPDA---EYKKRldelvellDLGEL-LDTPVRQLSLGQRMRCELA 166
|
170 180
....*....|....*....|
gi 1512845752 159 GAFVSGADYLLLDEPTNHLD 178
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLD 186
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
455-518 |
2.59e-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: 2.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAI-ESALAAFPG-AMLVVSHDEAFL 518
Cdd:COG4987 470 RRLSGGERRRLALARALLR--DAPILLLDEPTEGLDAATEQALlADLLEALAGrTVLLITHRLAGL 533
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
140-185 |
4.79e-05 |
|
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: 45.08 E-value: 4.79e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1512845752 140 ADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWL 185
Cdd:COG1119 136 ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELL 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
370-514 |
5.76e-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: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLSV-SAAYLDQHLtQLDLSLSVMAHL-SLEDTPLDEGLLRTRLAQ-LQLg 446
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYI-KADYEGTVRDLLsSITKDFYTHPYFKTEIAKpLQI- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 447 ADKVTLPLSALSGGERLKAALACVLWRrePAQLLLLDEPTNHLD----LASTQAIES-ALAAFPGAMlVVSHD 514
Cdd:cd03237 106 EQILDREVPELSGGELQRVAIAACLSK--DADIYLLDEPSAYLDveqrLMASKVIRRfAENNEKTAF-VVEHD 175
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-229 |
6.23e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.48 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 14 QVTCQFATGQTLFGPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLDSPAGGHI---ERAAAVAWVAQQPTLTPETTLA- 88
Cdd:PRK10908 6 HVSKAYLGGRQALQGVTFHMRPGeMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsGHDITRLKNREVPFLRRQIGMIf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 89 ---TLLGYASVFAALSRLEQGQGLADDfdlldghwDLTDRLSLAFREADLPPFSADRPaFSLSGGERMKALLCGAFVSGA 165
Cdd:PRK10908 86 qdhHLLMDRTVYDNVAIPLIIAGASGD--------DIRRRVSAALDKVGLLDKAKNFP-IQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 166 DYLLLDEPTNHLDRQGREWLYHQLESWQG---GALIASHDRELLTRMPRIIeLTPTALRSYGGNYDE 229
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRM-LTLSDGHLHGGVGGE 222
|
|
| 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 1512845752 448 DKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSHD 514
Cdd:PRK14246 145 DRLNSPASQLSGGQQQRLTIARALALK--PKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
23-174 |
7.53e-05 |
|
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: 44.20 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 23 QTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE-------RaaavawvaqqptLTPETTLATLLGYA 94
Cdd:COG0410 17 HVLHG-VSLEVEEgEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditG------------LPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 95 ----SVFAALS---RLEQGQGLADDFDllDGHWDLTDRLSLaF-READLppfsADRPAFSLSGGER-MKALlcG-AFVSG 164
Cdd:COG0410 84 pegrRIFPSLTveeNLLLGAYARRDRA--EVRADLERVYEL-FpRLKER----RRQRAGTLSGGEQqMLAI--GrALMSR 154
|
170
....*....|
gi 1512845752 165 ADYLLLDEPT 174
Cdd:COG0410 155 PKLLLLDEPS 164
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
36-202 |
8.35e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 44.45 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 36 SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQPTLTPETTLATL-------LGYASVFAALSRLEQGQG 108
Cdd:PRK13636 33 EVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVfqdpdnqLFSASVYQDVSFGAVNLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 109 LADDfdlldghwDLTDRLSLAFREADLPPFSaDRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQ 188
Cdd:PRK13636 113 LPED--------EVRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL 183
|
170
....*....|....*...
gi 1512845752 189 LESWQGGA----LIASHD 202
Cdd:PRK13636 184 LVEMQKELgltiIIATHD 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
417-521 |
8.36e-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: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 417 SLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALA-CVLWRrepAQLLLLDEPTNHLDLASTQ 495
Cdd:TIGR02633 364 VLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAkMLLTN---PRVLILDEPTRGVDVGAKY 440
|
90 100
....*....|....*....|....*....
gi 1512845752 496 AIE---SALAAFPGAMLVVSHDEAFLQGL 521
Cdd:TIGR02633 441 EIYkliNQLAQEGVAIIVVSSELAEVLGL 469
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
360-513 |
9.09e-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: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSvsaaylDQHLTQLDLSlSVMAHLSL--EDTPLDEGLLR 437
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID------GVDLRDLDLE-SLRKNIAYvpQDPFLFSGTIR 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752 438 TRLaqlqlgadkvtlplsaLSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:cd03228 94 ENI----------------LSGGQRQRIAIARALLRD--PPILILDEATSALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-202 |
9.43e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 27 GPLSVSLEPS-LCGLVGRNGVGKTRLLRLLAGLdSPAGGHIeraaavaWVAQQPTLT-PETTLATLLGYAS--------- 95
Cdd:PRK03695 13 GPLSAEVRAGeILHLVGPNGAGKSTLLARMAGL-LPGSGSI-------QFAGQPLEAwSAAELARHRAYLSqqqtppfam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 96 -VFAALSR-LEQGQGLADDFDLLDghwDLTDRLSLafreADLPPfsadRPAFSLSGGERMKALLCGAFV-------SGAD 166
Cdd:PRK03695 85 pVFQYLTLhQPDKTRTEAVASALN---EVAEALGL----DDKLG----RSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQ 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1512845752 167 YLLLDEPTNHLDRQGREWLY---HQLESWQGGALIASHD 202
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHD 192
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
360-514 |
1.02e-04 |
|
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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRL--------SVSAAYLDQH--------LTQLDL-SLSVMA 422
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekeRKRIGYVPQRrsidrdfpISVRDVvLMGLYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 423 HLSLEDTP-------LDEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQ 495
Cdd:cd03235 98 HKGLFRRLskadkakVDEALERVGLSEL---ADR---QIGELSGGQQQRVLLARALVQD--PDLLLLDEPFAGVDPKTQE 169
|
170 180
....*....|....*....|..
gi 1512845752 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 1512845752 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 1512845752 422 AHLSLED------------TPLDEGLLRTRLAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEP---- 485
Cdd:COG3840 84 PHLTVAQniglglrpglklTAEQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRP--ILLLDEPfsal 160
|
90 100 110
....*....|....*....|....*....|....
gi 1512845752 486 -----TNHLDLASTQAIESALaafpgAMLVVSHD 514
Cdd:COG3840 161 dpalrQEMLDLVDELCRERGL-----TVLMVTHD 189
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
453-518 |
1.24e-04 |
|
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: 44.78 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLD----LASTQAIESaLAAFPGAMLVVSHDEAFL 518
Cdd:COG1245 209 DISELSGGELQRVAIAAALLRD--ADFYFFDEPSSYLDiyqrLNVARLIRE-LAEEGKYVLVVEHDLAIL 275
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
40-180 |
1.25e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.41 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 40 LVGRNGVGKTRLLRLLAG--LDSPAGGHIEraaavawvAQQPTLTPETTLATLLGYASVFAALSRLEQGQGLADDFDLLd 117
Cdd:COG2401 61 IVGASGSGKSTLLRLLAGalKGTPVAGCVD--------VPDNQFGREASLIDAIGRKGDFKDAVELLNAVGLSDAVLWL- 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 118 ghwdltdrlslafreadlppfsadRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:COG2401 132 ------------------------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
39-215 |
1.36e-04 |
|
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: 42.42 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlatllgyasvfaalsrleqgqgladdfdLLDG 118
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPDSGEI------------------------------------------------LVDG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 HwdltdrlSLAFREadlpPFSADR----PAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESW-- 192
Cdd:cd03216 62 K-------EVSFAS----PRDARRagiaMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLra 130
|
170 180
....*....|....*....|....
gi 1512845752 193 QGGALI-ASHdrelltRMPRIIEL 215
Cdd:cd03216 131 QGVAVIfISH------RLDEVFEI 148
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-183 |
1.37e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 44.33 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATgQTLFGPLSVSL-EPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI--------ERAAAVA---WVAQQ 78
Cdd:PRK11432 8 VLKNITKRFGS-NTVIDNLNLTIkQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvtHRSIQQRdicMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 79 PTLTPETTLATLLGYASVFAALSRLEQGQgladdfdlldghwdltdRLSLAFREADLPPFsADRPAFSLSGGERMKALLC 158
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQ-----------------RVKEALELVDLAGF-EDRYVDQISGGQQQRVALA 148
|
170 180
....*....|....*....|....*....
gi 1512845752 159 GAFVSGADYLLLDEPTNHLD----RQGRE 183
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDanlrRSMRE 177
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
135-209 |
1.43e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.84 E-value: 1.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 135 LPPFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGRE---WLYHQLESWQGGALI-ASHDRELLTRM 209
Cdd:PRK13645 139 LPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIImVTHNMDQVLRI 217
|
|
| 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 1512845752 369 RIALKGPNGCGKTTLLKTLLG--------------LEQAASGD---------------VRLSVSAAYLDQHLTQLDLSLS 419
Cdd:PLN03073 205 HYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhVEQEVVGDdttalqcvlntdierTQLLEEEAQLVAQQRELEFETE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 420 VMAHLSLEDTPLDEGLLRTRLAQ-----------------------LQLGADKVTLPLSALSGGERLKAALACVLWrREP 476
Cdd:PLN03073 285 TGKGKGANKDGVDKDAVSQRLEEiykrlelidaytaearaasilagLSFTPEMQVKATKTFSGGWRMRIALARALF-IEP 363
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1512845752 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 1512845752 455 SALSGGERLKAALACVLWrREPaQLLLLDEPTNHLD----LASTQAIESALAAFPGAMLVVSHDEAFL 518
Cdd:TIGR03269 426 DELSEGERHRVALAQVLI-KEP-RIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFV 491
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
40-178 |
1.83e-04 |
|
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: 42.87 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 40 LVGRNGVGKTRLLRLLAGLDSPAGGHIErAAAVAWVAQQPTLTPettLATLLGYASVFAALSrLEQGQGLADDFDLldgH 119
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQSGRVL-INGVDVTAAPPADRP---VSMLFQENNLFAHLT-VEQNVGLGLSPGL---K 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 120 WDLTDR--LSLAFREADLPPFSADRPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03298 101 LTAEDRqaIEVALARVGLAGLEKRLPG-ELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
370-514 |
1.84e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 43.22 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRL------SVSAAYLDQHL------TQLDLSLSV----------MAHLSLE 427
Cdd:PRK13548 31 VAILGPNGAGKSTLLRALSGELSPDSGEVRLngrplaDWSPAELARRRavlpqhSSLSFPFTVeevvamgrapHGLSRAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 428 DTPL-DEGLLRTRLAQLqlgADKvtlPLSALSGGERLKAALACVL---WRREPAQ-LLLLDEPTNHLDLASTQAIESALA 502
Cdd:PRK13548 111 DDALvAAALAQVDLAHL---AGR---DYPQLSGGEQQRVQLARVLaqlWEPDGPPrWLLLDEPTSALDLAHQHHVLRLAR 184
|
170
....*....|....*.
gi 1512845752 503 AF----PGAMLVVSHD 514
Cdd:PRK13548 185 QLaherGLAVIVVLHD 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-174 |
1.93e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 31 VSLE-PS--LCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE------RAAAVAWVAQQ--------------PTLTPETTL 87
Cdd:NF033858 20 VSLDiPAgcMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmADARHRRAVCPriaympqglgknlyPTLSVFENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 88 ---ATLLGyasvfaaLSRLEQGQGLADdfdlldghwdLTDRLSLAfreadlpPFsADRPAFSLSGGERMKALLCGAFVSG 164
Cdd:NF033858 100 dffGRLFG-------QDAAERRRRIDE----------LLRATGLA-------PF-ADRPAGKLSGGMKQKLGLCCALIHD 154
|
170
....*....|
gi 1512845752 165 ADYLLLDEPT 174
Cdd:NF033858 155 PDLLILDEPT 164
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
29-174 |
1.95e-04 |
|
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: 43.19 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeRAAAVAWVAQQPTLTPETTLA------TLLGYASVF---- 97
Cdd:cd03219 19 VSFSVRPgEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGEDITGLPPHEIARLGIGrtfqipRLFPELTVLenvm 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512845752 98 -AALSRLEQGQGLADDFDLLDGHWDLTDRLsLAFreADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:cd03219 98 vAAQARTGSGLLLARARREEREARERAEEL-LER--VGLADL-ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-178 |
2.22e-04 |
|
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: 42.94 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGQtlfgplsvslepsLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWVAQQ------------ 78
Cdd:cd03256 16 ALKDVSLSINPGE-------------FVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqlrrqigm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 79 ----PTLTPETT-----LATLLGYASVFAALSRLEQGQGLADDFDLLdghwDLTDRLSLAFREADlppfsadrpafSLSG 149
Cdd:cd03256 83 ifqqFNLIERLSvlenvLSGRLGRRSTWRSLFGLFPKEEKQRALAAL----ERVGLLDKAYQRAD-----------QLSG 147
|
170 180
....*....|....*....|....*....
gi 1512845752 150 GERMKALLCGAFVSGADYLLLDEPTNHLD 178
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| 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 1512845752 391 EQAASGDVRLSVSAAYLDQHLTQLDLSLSVMAHLSLEDTPLDEGLLRTRLAQLqlgadkVTLPLSALSGGERLKAALACV 470
Cdd:cd03236 80 TKLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHV------LDRNIDQLSGGELQRVAIAAA 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 471 LWRRepAQLLLLDEPTNHLD----LASTQAIESaLAAFPGAMLVVSHDEAFL 518
Cdd:cd03236 154 LARD--ADFYFFDEPSSYLDikqrLNAARLIRE-LAEDDNYVLVVEHDLAVL 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
140-213 |
2.53e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.11 E-value: 2.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 140 ADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQL----ESWQGGALIASHDRELLTRMP-RII 213
Cdd:PRK13637 138 KDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLAdRII 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
315-515 |
2.55e-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: 43.89 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 315 AVQQARERVEEETPVMFTLPGSEVAA------GKQVLVVESLQLDHAPAAPLNWRIDGPM----RIALKGPNGCGKTTLL 384
Cdd:TIGR02868 299 RVRAAAERIVEVLDAAGPVAEGSAPAagavglGKPTLELRDLSAGYPGAPPVLDGVSLDLppgeRVAILGPSGSGKSTLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 385 KTLLGLEQAASGDVRLS-VSAAYLDQHLTQLDLSLSVM-AHLSleDTPLDEGLLRTR-----------LAQLQLGADKVT 451
Cdd:TIGR02868 379 ATLAGLLDPLQGEVTLDgVPVSSLDQDEVRRRVSVCAQdAHLF--DTTVRENLRLARpdatdeelwaaLERVGLADWLRA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 452 LPL----------SALSGGERLKAALACVLWrrEPAQLLLLDEPTNHLDL-ASTQAIESALAAFPG-AMLVVSHDE 515
Cdd:TIGR02868 457 LPDgldtvlgeggARLSGGERQRLALARALL--ADAPILLLDEPTEHLDAeTADELLEDLLAALSGrTVVLITHHL 530
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
141-193 |
2.73e-04 |
|
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: 42.71 E-value: 2.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1512845752 141 DRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQ 193
Cdd:cd03299 124 NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
440-515 |
2.81e-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: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 440 LAQLQLGADKVTLPlSALSGGERLKAALAcvlwrR----EPaQLLLLDEPTNHLDLASTQAIESALAAFPG----AMLVV 511
Cdd:cd03255 125 LERVGLGDRLNHYP-SELSGGQQQRVAIA-----RalanDP-KIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVV 197
|
....
gi 1512845752 512 SHDE 515
Cdd:cd03255 198 THDP 201
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-216 |
2.98e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 12 LHQVTCQFATGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAvawvaqqptltpETTLATL 90
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPINLTIKRgELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK------------PVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 91 LGYASVFAAL-------SRLEQGQGLADDFDLLDG---HWDLTDRLSLA-FREADLppfsadrpafSLSGGERMKALLCG 159
Cdd:PRK10522 393 EDYRKLFSAVftdfhlfDQLLGPEGKPANPALVEKwleRLKMAHKLELEdGRISNL----------KLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 160 AFVSGADYLLLDEPTNHLDRQGREWLYHQLESW---QGGALIA-SH--------DRELLTRMPRIIELT 216
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLlqeMGKTIFAiSHddhyfihaDRLLEMRNGQLSELT 531
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
454-501 |
3.05e-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: 3.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1512845752 454 LSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIESAL 501
Cdd:cd03213 109 LRGLSGGERKRVSIALELVSNPS--LLFLDEPTSGLDSSSALQVMSLL 154
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
455-513 |
3.29e-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: 3.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512845752 455 SALSGGERLKAALACVLWRrEPaQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:cd03248 149 SQLSGGQKQRVAIARALIR-NP-QVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-198 |
3.66e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.46 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 34 EPSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIeraaavawvaqqptltpettlatLLGYASVFAALSRLEQGQGLADDF 113
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV-----------------------LVGGKDIETNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 114 DLLDGHWDLTDRLSL-------AFREADLP----------PFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNH 176
Cdd:TIGR01257 1012 NILFHHLTVAEHILFyaqlkgrSWEEAQLEmeamledtglHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180
....*....|....*....|..
gi 1512845752 177 LDRQGREWLYHQLESWQGGALI 198
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTI 1113
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
40-221 |
3.86e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.07 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 40 LVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAwvaqqpTLTPETTLATL----LGYasVFAA------LSRLEQGQGL 109
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL------HQMDEEARAKLrakhVGF--VFQSfmliptLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 110 AddfdLLDGHWD---------LTDRLSLAFREADLPPfsadrpafSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQ 180
Cdd:PRK10584 113 A----LLRGESSrqsrngakaLLEQLGLGKRLDHLPA--------QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1512845752 181 GREW---LYHQLESWQGGALI-ASHDRELLTRMPRIIELTPTALR 221
Cdd:PRK10584 181 TGDKiadLLFSLNREHGTTLIlVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-67 |
3.88e-04 |
|
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: 42.78 E-value: 3.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1512845752 29 LSVSLE---PSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE 67
Cdd:COG4148 16 LDVDFTlpgRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIR 57
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
142-222 |
4.13e-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: 41.87 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 142 RPAFSLSGGERMKALLCGAF-----VSGA-----DYLLLDEPTNHLDRQGREWLYHQLESWQGG---ALIASHDRELLTR 208
Cdd:cd03279 119 RPVSTLSGGETFLASLSLALalsevLQNRggarlEALFIDEGFGTLDPEALEAVATALELIRTEnrmVGVISHVEELKER 198
|
90
....*....|....
gi 1512845752 209 MPRIIELTPTALRS 222
Cdd:cd03279 199 IPQRLEVIKTPGGS 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-219 |
4.28e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 40.99 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 10 FVLHQVTCQFATGQTLFGPLSVSLEPslcG----LVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVAWV--AQQPTLtP 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKP---GdrllITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLflPQRPYL-P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 84 ETTLATLLGYAsvfaalsrleqgqgladdfdlldghWDLTdrlslafreadlppfsadrpafsLSGGERMKALLCGAFVS 163
Cdd:cd03223 77 LGTLREQLIYP-------------------------WDDV-----------------------LSGGEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 164 GADYLLLDEPTNHLDRQGREWLYHQLESwQGGALIA-SHDRELLTRMPRIIELTPTA 219
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKE-LGITVISvGHRPSLWKFHDRVLDLDGEG 164
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
369-492 |
5.66e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.49 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 369 RIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSaaylDQHLT---QLDLSL-----SVMAHLSLEDT---PLDEGLlr 437
Cdd:PRK10771 27 RVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ----DHTTTppsRRPVSMlfqenNLFSHLTVAQNiglGLNPGL-- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 438 tRL-----AQLQLGADKVT-------LPlSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLA 492
Cdd:PRK10771 101 -KLnaaqrEKLHAIARQMGiedllarLP-GQLSGGQRQRVALARCLVREQP--ILLLDEPFSALDPA 163
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
370-497 |
5.69e-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: 41.55 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 370 IALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VSAAYLDQHL----------TQLDLSLSVMAHLSL--EDTPLDEGL 435
Cdd:cd03267 50 VGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglVPWKRRKKFLrrigvvfgqkTQLWWDLPVIDSFYLlaAIYDLPPAR 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 436 LRTRLAQ----LQLGaDKVTLPLSALSGGERLKAALACVLWrREPaQLLLLDEPTNHLDLASTQAI 497
Cdd:cd03267 130 FKKRLDElselLDLE-ELLDTPVRQLSLGQRMRAEIAAALL-HEP-EILFLDEPTIGLDVVAQENI 192
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-67 |
6.61e-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: 6.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIE 67
Cdd:COG1127 20 VLDGVSLDVPRGEIL-------------AIIGGSGSGKSVLLKLIIGLLRPDSGEIL 63
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
453-518 |
7.09e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 7.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 453 PLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLasTQAIESALA----AFPGAMLVVSHDEAFL 518
Cdd:PRK13409 209 DISELSGGELQRVAIAAALLRD--ADFYFFDEPTSYLDI--RQRLNVARLirelAEGKYVLVVEHDLAVL 274
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-66 |
7.81e-04 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 41.98 E-value: 7.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1512845752 28 PLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI 66
Cdd:COG3839 21 DIDLDIEDgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI 60
|
|
| 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 1512845752 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 1512845752 371 ALKGPNGCG-----KTTLLKTLLGLEQAASGDVRLSVSAAYLD---------------QHLTQLDLS------LSVMAHL 424
Cdd:cd03260 30 ALIGPSGCGkstllRLLNRLNDLIPGAPDEGEVLLDGKDIYDLdvdvlelrrrvgmvfQKPNPFPGSiydnvaYGLRLHG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 425 SLEDTPLDEgLLRTRLAQLQLGaDKVTLPLSA--LSGGERLKAALACVlWRREPAqLLLLDEPTNHLDLASTQAIESALA 502
Cdd:cd03260 110 IKLKEELDE-RVEEALRKAALW-DEVKDRLHAlgLSGGQQQRLCLARA-LANEPE-VLLLDEPTSALDPISTAKIEELIA 185
|
170
....*....|....
gi 1512845752 503 AF--PGAMLVVSHD 514
Cdd:cd03260 186 ELkkEYTIVIVTHN 199
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-234 |
9.56e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.85 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 20 ATGQTLFGPLSVSLEPSLCGLV-GRNGVGKTRLLRLLAGLDSPAGGHIeraaaVAWVAQQPTLTPET---------TLAT 89
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTL-----LFEGEDISTLKPEIyrqqvsycaQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 90 LLGyASVFAALSRLEQGQGLADDFDLLdghwdltdRLSLAFREadLPPFSADRPAFSLSGGERMKALLCGAFVSGADYLL 169
Cdd:PRK10247 92 LFG-DTVYDNLIFPWQIRNQQPDPAIF--------LDDLERFA--LPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 170 LDEPTNHLDRQGR----EWLYHQLESWQGGALIASHDRELLTRMPRIIELTPtalrsYGGNYDEYQRQR 234
Cdd:PRK10247 161 LDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQP-----HAGEMQEARYEL 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
457-515 |
9.73e-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: 40.04 E-value: 9.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 457 LSGGERLKAALACVL--WRREPAQLLLLDEPTNHLDLASTQAIESALAAF--PGA-MLVVSHDE 515
Cdd:cd03227 78 LSGGEKELSALALILalASLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAqVIVITHLP 141
|
|
| 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 1512845752 417 SLSVMAHLSLEDTPLDEGLLRTRLAQLQLGADKVTLPLSALSGGERLKAALA-CVLwrREPaQLLLLDEPTNHLDLASTQ 495
Cdd:PRK13549 366 ALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAkCLL--LNP-KILILDEPTRGIDVGAKY 442
|
90 100
....*....|....*....|
gi 1512845752 496 AIE---SALAAFPGAMLVVS 512
Cdd:PRK13549 443 EIYkliNQLVQQGVAIIVIS 462
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
39-186 |
1.08e-03 |
|
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: 40.82 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGH------------IERAAAVAWVAQQPTLTPETT-------LATLLGYASVFAA 99
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepREVRRRIGIVFQDLSVDDELTgwenlyiHARLYGVPGAERR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 100 lSRLEQgqgLADDFDLLDghwdltdrlslafreadlppfSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDR 179
Cdd:cd03265 110 -ERIDE---LLDFVGLLE---------------------AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
....*....
gi 1512845752 180 QGRE--WLY 186
Cdd:cd03265 165 QTRAhvWEY 173
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
429-513 |
1.11e-03 |
|
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: 40.84 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 429 TPLDEGLLRTRLAQLQLG--ADKvtlPLSALSGGERLKAALAcvlwR---REPaQLLLLDEPTNHLDLAST----QAIEs 499
Cdd:COG1119 116 TDEQRERARELLELLGLAhlADR---PFGTLSQGEQRRVLIA----RalvKDP-ELLILDEPTAGLDLGARelllALLD- 186
|
90
....*....|....*
gi 1512845752 500 ALAAFPG-AMLVVSH 513
Cdd:COG1119 187 KLAAEGApTLVLVTH 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
31-66 |
1.16e-03 |
|
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: 40.79 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1512845752 31 VSLE---PSLCGLVGRNGVGKTRLLRLLAGLDSPAGGHI 66
Cdd:cd03296 21 VSLDipsGELVALLGPSGSGKTTLLRLIAGLERPDSGTI 59
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-66 |
1.28e-03 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 41.29 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHI 66
Cdd:COG1118 17 LLDDVSLEIASGELV-------------ALLGPSGSGKTTLLRIIAGLETPDSGRI 59
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
29-205 |
2.16e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 40.10 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 29 LSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAAVawvaqqptLTPETT--LATLLGY-----------A 94
Cdd:PRK13647 24 LSLSIPEgSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE--------VNAENEkwVRSKVGLvfqdpddqvfsS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 95 SVFAALSRLEQGQGLADDfdlldghwDLTDRLSLAFREADLPPFsADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPT 174
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKD--------EVERRVEEALKAVRMWDF-RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190
....*....|....*....|....*....|....
gi 1512845752 175 NHLDRQGREWLYHQLE--SWQGGALI-ASHDREL 205
Cdd:PRK13647 167 AYLDPRGQETLMEILDrlHNQGKTVIvATHDVDL 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-254 |
2.17e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.08 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 5 AHIPAFVLHQVTCQFAtGQTLFGPLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGH------------------ 65
Cdd:PRK14271 17 AAAPAMAAVNLTLGFA-GKTVLDQVSMGFPArAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvllggrsifnyrd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 66 -IERAAAVAWVAQQPTLTPETTLATLLGYASVFAALSRlEQGQGLADDFDLLDGHWD-LTDRLSlafreadlppfsaDRP 143
Cdd:PRK14271 96 vLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPR-KEFRGVAQARLTEVGLWDaVKDRLS-------------DSP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 144 aFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQG--GALIASH---------DRELLTRMPRI 212
Cdd:PRK14271 162 -FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHnlaqaarisDRAALFFDGRL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1512845752 213 IELTPTAlrsyggnyDEYQRQRMAEQQAARAALEHAVTDRRR 254
Cdd:PRK14271 241 VEEGPTE--------QLFSSPKHAETARYVAGLSGDVKDAKR 274
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
457-513 |
2.30e-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: 2.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1512845752 457 LSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAFPG--AMLVVSH 513
Cdd:COG1132 477 LSGGQRQRIAIARALLKD--PPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
455-519 |
2.41e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 40.60 E-value: 2.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 455 SALSGGERLKAALACVLWRrePAQLLLLDEPTNHLDLASTQAIESAL--AAFPGAMLVVSHDEAFLQ 519
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQ--PCQLLLLDEPTASLDAHSEQLVMQALnaASRRQTTLMVTHQLEDLA 548
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-208 |
2.45e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 40.06 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 11 VLHQVTCQFATGQTLfgplsvslepslcGLVGRNGVGKTRLLRLLAGLDSPAGGHIERAAavawvaqqptlTPETTLAT- 89
Cdd:PRK10419 27 VLNNVSLSLKSGETV-------------ALLGRSGCGKSTLARLLVGLESPSQGNVSWRG-----------EPLAKLNRa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 90 ----------LLGYASVFAALSRLEQGQGLADDFDLLDGhWDLTDRLSLA---FREADLPPFSADRPAFSLSGGERMKAL 156
Cdd:PRK10419 83 qrkafrrdiqMVFQDSISAVNPRKTVREIIREPLRHLLS-LDKAERLARAsemLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1512845752 157 LCGAFVSGADYLLLDEPTNHLDRQGREWLYHQLESWQ---GGA-LIASHDRELLTR 208
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqqfGTAcLFITHDLRLVER 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
134-202 |
2.54e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.07 E-value: 2.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512845752 134 DLPPFSADRPAFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQG-REWL--YHQLESWQGGALIASHD 202
Cdd:PRK13651 153 GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGvKEILeiFDNLNKQGKTIILVTHD 224
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
39-213 |
2.55e-03 |
|
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: 39.09 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 39 GLVGRNGVGKTRLLRLLAGLDSPAGGHIEraaavawvaqqptltpettlatllgyasvfaalsrleqgqgladdfdlldg 118
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDE--------------------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 119 hWDltdRLSLAFReadlPPFsadrpaFSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGR----EWLYHQLESWQG 194
Cdd:cd03222 58 -WD---GITPVYK----PQY------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKK 123
|
170
....*....|....*....
gi 1512845752 195 GALIASHDRELLTRMPRII 213
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRI 142
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
455-514 |
2.71e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 39.41 E-value: 2.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512845752 455 SALSGGERLKAALACVLwRREPAqLLLLDEPTNHLDLASTQAIESALAAFP----GAMLVVSHD 514
Cdd:PRK11629 144 SELSGGERQRVAIARAL-VNNPR-LVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHD 205
|
|
| 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 1512845752 440 LAQLQLGADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQ 495
Cdd:TIGR02633 125 LRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ--ARLLILDEPSSSLTEKETE 178
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
114-219 |
3.06e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 114 DLLDGhwdLTDRLSLAFrEADLPPFSADRPAFSLSGGERMKALLC---GAFVSGADYlLLDEPTNHLDRQGREWLYHQLE 190
Cdd:PRK00635 448 EVLQG---LKSRLSILI-DLGLPYLTPERALATLSGGEQERTALAkhlGAELIGITY-ILDEPSIGLHPQDTHKLINVIK 522
|
90 100 110
....*....|....*....|....*....|..
gi 1512845752 191 SW--QGGA-LIASHDRELLTRMPRIIELTPTA 219
Cdd:PRK00635 523 KLrdQGNTvLLVEHDEQMISLADRIIDIGPGA 554
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
220-269 |
3.54e-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: 3.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 220 LRSYGGNYDEYQRQRMAE----------QQAARAALEHAVtDRRRTRARMQKehdAAQRR 269
Cdd:pfam12848 8 LTTYKGNYSTFLEQKEERleqqekayekQQKEIKKLEEFI-DRFRAKASKAK---QAQSR 63
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
374-516 |
4.11e-03 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 38.89 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 374 GPNGCG-----------KttllktllgleQAASGDVRL--------SVSA----AYLDQHLTqLDLSLSVMAHLSL--ED 428
Cdd:COG1131 33 GPNGAGktttirmllglL-----------RPTSGEVRVlgedvardPAEVrrriGYVPQEPA-LYPDLTVRENLRFfaRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 429 TPLDEGLLRTRLAQL--QLG-ADKVTLPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIES---ALA 502
Cdd:COG1131 101 YGLPRKEARERIDELleLFGlTDAADRKVGTLSGGMKQRLGLALALLHD--PELLILDEPTSGLDPEARRELWEllrELA 178
|
170
....*....|....*.
gi 1512845752 503 AFPGAMLVVSH--DEA 516
Cdd:COG1131 179 AEGKTVLLSTHylEEA 194
|
|
| 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 1512845752 453 PLSALSGGER----LKAALACVLWRREPAQLLLLDEPTNHLD------LasTQAIESALAAFPgAMLVVSHDE 515
Cdd:PRK03918 785 PLTFLSGGERialgLAFRLALSLYLAGNIPLLILDEPTPFLDeerrrkL--VDIMERYLRKIP-QVIIVSHDE 854
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
453-497 |
4.52e-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: 4.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1512845752 453 PLSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAI 497
Cdd:cd03266 133 RVGGFSTGMRQKVAIARALVHDPP--VLLLDEPTTGLDVMATRAL 175
|
|
| 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 1512845752 457 LSGGERLKAALACVLwRREPaQLLLLDEPTNHLDLASTQAIESalaafpgaMLVVSHDEAFLQGLKLTHSL--AW 529
Cdd:cd03299 130 LSGGEQQRVAIARAL-VVNP-KILLLDEPFSALDVRTKEKLRE--------ELKKIRKEFGVTVLHVTHDFeeAW 194
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
142-215 |
6.23e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 39.32 E-value: 6.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 142 RPAfSLSGGERMKALLCGAFVSGADYLLLDEPTNHLDRQGRE---WLYHQLESWQGGALIASHDRELLTRMPRIIEL 215
Cdd:PRK10535 141 QPS-QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
360-514 |
7.05e-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: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 360 LNWRIDGPMRIALKGPNGCGKTTLLKTLLGLEQAASGDVRLSVSA---------AYLDQHL------TQLDLSLSVMAH- 423
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgraiPYLRRKIgvvfqdFRLLPDRNVYENv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 424 -LSLEDTPLDEGLLRTR----LAQLQLGADKVTLPlSALSGGERLKAALACVLWRREPaqLLLLDEPTNHLDLASTQAIE 498
Cdd:cd03292 100 aFALEVTGVPPREIRKRvpaaLELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIM 176
|
170
....*....|....*....
gi 1512845752 499 SALAAF--PGAMLVVS-HD 514
Cdd:cd03292 177 NLLKKInkAGTTVVVAtHA 195
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-67 |
8.55e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 38.17 E-value: 8.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 12 LHQVTCQFATGQTLFGpLSVSLEP-SLCGLVGRNGVGKTRLLRLLAGLDSPAGGHIE 67
Cdd:COG4152 4 LKGLTKRFGDKTAVDD-VSFTVPKgEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL 59
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
371-490 |
8.73e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 38.66 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 371 ALKGPNGCGKTTLLKTLLGLEQAASGDVRLS-VSAAYLDQHLTQLDL---SLSVMAHLSLEDTpLDEGLLRTRLAQLQLg 446
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLSHVPPYQRPINMmfqSYALFPHMTVEQN-IAFGLKQDKLPKAEI- 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1512845752 447 ADKVTLPLS-------------ALSGGERLKAALACVLWRRepAQLLLLDEPTNHLD 490
Cdd:PRK11607 127 ASRVNEMLGlvhmqefakrkphQLSGGQRQRVALARSLAKR--PKLLLLDEPMGALD 181
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
371-514 |
9.62e-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: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 371 ALKGPNGCGKTTLLKTLLGLEQAASGDVRLS--VSAAYLDQHLTQ---------LDLSLSVMAHL----SLEDTPLDEGL 435
Cdd:COG4555 31 GLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgeDVRKEPREARRQigvlpdergLYDRLTVRENIryfaELYGLFDEELK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512845752 436 LRT----RLAQLQLGADKvtlPLSALSGGERLKAALACVLWRRepAQLLLLDEPTNHLDLASTQAIESALAAF---PGAM 508
Cdd:COG4555 111 KRIeeliELLGLEEFLDR---RVGELSTGMKKKVALARALVHD--PKVLLLDEPTNGLDVMARRLLREILRALkkeGKTV 185
|
....*.
gi 1512845752 509 LVVSHD 514
Cdd:COG4555 186 LFSSHI 191
|
|
|