|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-492 |
5.94e-130 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 389.81 E-value: 5.94e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 15 AFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP--------------- 77
Cdd:COG0488 7 SFGgrPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPldddltvldtvldgd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 78 ---------------------ETLHTQSLLQAVLAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLL 136
Cdd:COG0488 87 aelraleaeleeleaklaepdEDLERLAELQEEFEALGGWEAEAR---AEEILSGLGFPEEDLDRPVSELSGGWRRRVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 137 ARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFalPC--------S 208
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLY--PGnysayleqR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 209 AARQALQEQDESAALRHKAEQKE-IDRVSASARRlatwgrvydnedlARKAKQMEKQVARLKDEQTELSVGPPwRLVLQG 287
Cdd:COG0488 242 AERLEQEAAAYAKQQKKIAKEEEfIRRFRAKARK-------------AKQAQSRIKALEKLEREEPPRRDKTV-EIRFPP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 288 DALPADRLLEMDtlHVSPAPGQPSLFtTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPG 365
Cdd:COG0488 308 PERLGKKVLELE--GLSKSYGDKTLL-DDLsLRIDRGDRIGLIGPNGAGKSTLLKLL---AGELEPDSGtVKLGETVKIG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 366 YYDQTLAQLPDEASLLEALTPFAPSADTRK-RALIAA-GFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTN 443
Cdd:COG0488 382 YFDQHQEELDPDKTVLDELRDGAPGGTEQEvRGYLGRfLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1439757928 444 HLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEW 492
Cdd:COG0488 462 HLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-484 |
1.04e-58 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 206.94 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP---------------ETLHTQ 83
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPalpqpaleyvidgdrEYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 SLLQA--------VLAPLPADAREAQRWL----AERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK10636 96 AQLHDanerndghAIATIHGKLDAIDAWTirsrAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 152 PGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFALPCS----------AARQALQE--QDE 219
Cdd:PRK10636 176 PTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSsfevqratrlAQQQAMYEsqQER 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 220 SAALrhkaeQKEIDRVSASarrlatwgrvydnedlARKAKQMEKQVARLkdEQTEL----SVGPPWRLVL-QGDALPaDR 294
Cdd:PRK10636 256 VAHL-----QSYIDRFRAK----------------ATKAKQAQSRIKML--ERMELiapaHVDNPFHFSFrAPESLP-NP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 295 LLEMDtlHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRLHPRLhpGYYDQ-TLAQ 373
Cdd:PRK10636 312 LLKME--KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL--GYFAQhQLEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 374 LPDEASLLEALTPFAPSADTRKRALIAAGFGWarHSQKVST----LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEG 449
Cdd:PRK10636 388 LRADESPLQHLARLAPQELEQKLRDYLGGFGF--QGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
490 500 510
....*....|....*....|....*....|....*
gi 1439757928 450 KAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLI 484
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLV 500
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-506 |
5.35e-56 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 197.04 E-value: 5.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 16 FG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA--------------------------GQC 67
Cdd:PRK15064 11 FGakPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlgklrqdqfafeeftvldtvimGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 68 LMARVEQH------LPETLHTQSL----LQAVLAPL---PADAReaqrwlAERLLAQMGFTpavMEQQTATLSG---GQH 131
Cdd:PRK15064 91 ELWEVKQErdriyaLPEMSEEDGMkvadLEVKFAEMdgyTAEAR------AGELLLGVGIP---EEQHYGLMSEvapGWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 132 TRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAV-TNSSWI----LR------DQTL 200
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVcTHMADLdygeLRvypgnyDEYM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 201 hsfalpcSAARQAlQEQDESAALRHKAEQKE----IDRVSASAR--RLATwgrvydnedlaRKAKQMEKqvarLK-DEQT 273
Cdd:PRK15064 242 -------TAATQA-RERLLADNAKKKAQIAElqsfVSRFSANASkaKQAT-----------SRAKQIDK----IKlEEVK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 274 ELSVGPPWRLVLQGDALpaDRL-LEMDTLhvSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASP 352
Cdd:PRK15064 299 PSSRQNPFIRFEQDKKL--HRNaLEVENL--TKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL---VGELEP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 353 LPG-LRLHPRLHPGYYDQ-TLAQLPDEASLLEALTPFAPSAD-------TRKRALiaagFGWARHSQKVSTLSGGERSRL 423
Cdd:PRK15064 372 DSGtVKWSENANIGYYAQdHAYDFENDLTLFDWMSQWRQEGDdeqavrgTLGRLL----FSQDDIKKSVKVLSGGEKGRM 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 424 LFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQ 503
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
...
gi 1439757928 504 AVA 506
Cdd:PRK15064 528 GIE 530
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-488 |
5.04e-54 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 193.63 E-value: 5.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 15 AFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ------------------ 74
Cdd:PRK11147 12 SFSdaPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvydfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 75 -HLPETL---HTQSLLQAV---------LAPLPADAREAQRWLAE----RLLAQMGFTPavmEQQTATLSGGQHTRLLLA 137
Cdd:PRK11147 92 eEQAEYLkryHDISHLVETdpseknlneLAKLQEQLDHHNLWQLEnrinEVLAQLGLDP---DAALSSLSGGWLRKAALG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 138 RALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTL----------LDAVTNSSWILRDQTLhsfalpc 207
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFirnmatrivdLDRGKLVSYPGNYDQY------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 208 saarqaLQEQDEsaALRHKAEQK-EIDRVSAS----------ARRLATWGRVYdnedlARKAkqmekqvarLKDEQTEls 276
Cdd:PRK11147 242 ------LLEKEE--ALRVEELQNaEFDRKLAQeevwirqgikARRTRNEGRVR-----ALKA---------LRRERSE-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 277 vgppwRLVLQGDAL----PADR----LLEMDTLHVSpAPGQPSL--FTTGVARlrsGDRVAIMGRNGGGKSSLLRLLWQQ 346
Cdd:PRK11147 298 -----RREVMGTAKmqveEASRsgkiVFEMENVNYQ-IDGKQLVkdFSAQVQR---GDKIALIGPNGCGKTTLLKLMLGQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 347 MNNASPlpglRLH--PRLHPGYYDQTLAQLPDEASLLEALtpfapsADTRKRALIAagfGWARH----------SQK--- 411
Cdd:PRK11147 369 LQADSG----RIHcgTKLEVAYFDQHRAELDPEKTVMDNL------AEGKQEVMVN---GRPRHvlgylqdflfHPKram 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 412 --VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAG 488
Cdd:PRK11147 436 tpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNG 514
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-471 |
1.05e-52 |
|
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: 188.61 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 22 SLSFTlkKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA----------------GQCLMARVEQHLPETLHTQSL 85
Cdd:TIGR03719 25 SLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvgylpqepqldpTKTVRENVEEGVAEIKDALDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 86 LQAVLAPL--PADAREA----QRWLAERLLAQMGFT--------------PAvMEQQTATLSGGQHTRLLLARALIRQPD 145
Cdd:TIGR03719 103 FNEISAKYaePDADFDKlaaeQAELQEIIDAADAWDldsqleiamdalrcPP-WDADVTKLSGGERRRVALCRLLLSKPD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 146 LLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNssWIL---RDQTL-----HSFALPCSAARQALQEQ 217
Cdd:TIGR03719 182 MLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILeldRGRGIpwegnYSSWLEQKQKRLEQEEK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 218 DESAalRHKAEQKEID--RVSASARRLATWGRVYDNEDLARKAKQMekqvarlKDEQTELSVGPPWRLvlqgdalpADRL 295
Cdd:TIGR03719 260 EESA--RQKTLKRELEwvRQSPKGRQAKSKARLARYEELLSQEFQK-------RNETAEIYIPPGPRL--------GDKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 296 LEMDtlHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPGYYDQTLAQL 374
Cdd:TIGR03719 323 IEAE--NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI---TGQEQPDSGtIEIGETVKLAYVDQSRDAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 375 PDEASLLEALTPFAP-----SADTRKRALIAA-GFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDME 448
Cdd:TIGR03719 398 DPNKTVWEEISGGLDiiklgKREIPSRAYVGRfNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
490 500
....*....|....*....|...
gi 1439757928 449 GKAALAQTLRDYPGGVLLVSHDR 471
Cdd:TIGR03719 478 TLRALEEALLNFAGCAVVISHDR 500
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-203 |
6.84e-51 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 182.96 E-value: 6.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLpETLH-TQSLLQ 87
Cdd:COG0488 320 GLSKSYGdkTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDpDKTVLD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 aVLAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESF 167
Cdd:COG0488 399 -ELRDGAPGGTEQE---VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
170 180 190
....*....|....*....|....*....|....*.
gi 1439757928 168 LQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSF 203
Cdd:COG0488 475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-199 |
2.96e-48 |
|
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: 164.54 E-value: 2.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQhlpetlhtqs 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 llqavlaplpadareaqrwlaerllaqmgftpavmeqqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 1439757928 165 ESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQT 199
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-502 |
1.86e-47 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 176.59 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQ-----VLDGTlaPTS-----------GSVSLAGQCLM-ARVE--QHLPET 79
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGI--PKNcqilhveqevvGDDTTALQCVLnTDIErtQLLEEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 LH------------------------------TQSLLQAV--LAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLS 127
Cdd:PLN03073 270 AQlvaqqrelefetetgkgkgankdgvdkdavSQRLEEIYkrLELIDAYTAEAR---AASILAGLSFTPEMQVKATKTFS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 128 GGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSFALPC 207
Cdd:PLN03073 347 GGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDY 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 208 SAARQALQEQDESAALRHKAEQKE-------IDRVSASARRLATwgrvydnedLARKAKQMEK-----QVARLKDEQTEL 275
Cdd:PLN03073 427 DTFERTREEQLKNQQKAFESNERSrshmqafIDKFRYNAKRASL---------VQSRIKALDRlghvdAVVNDPDYKFEF 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 276 SVgppwrlvlqgdalPADRlLEMDTLHVSPA----PGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNnas 351
Cdd:PLN03073 498 PT-------------PDDR-PGPPIISFSDAsfgyPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQ--- 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 352 PLPGLRLH-PRLHPGYYDQTLAQLPDEAS--LLEALTPFAPSADTRKRA-LIAAGFGWARHSQKVSTLSGGERSRLLFVG 427
Cdd:PLN03073 561 PSSGTVFRsAKVRMAVFSQHHVDGLDLSSnpLLYMMRCFPGVPEQKLRAhLGSFGVTGNLALQPMYTLSGGQKSRVAFAK 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 428 LSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARL 502
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKT 715
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-471 |
3.09e-46 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 170.68 E-value: 3.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 22 SLSFTlkKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA-GqclmARV-----EQHLPETlhtQSLLQAVLAPLpA 95
Cdd:PRK11819 27 SLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApG----IKVgylpqEPQLDPE---KTVRENVEEGV-A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 DAREAQR---WLAERLLAQMGFTPAVMEQQT----------------------------------ATLSGGQHTRLLLAR 138
Cdd:PRK11819 97 EVKAALDrfnEIYAAYAEPDADFDALAAEQGelqeiidaadawdldsqleiamdalrcppwdakvTKLSGGERRRVALCR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 139 ALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNssWIL---RDQTL-----HSFALPCSAA 210
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILeldRGRGIpwegnYSSWLEQKAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 211 RQALQEQDESAalRHKAEQKEIDRVSASARrlatwgrvydnedlARKAK---------QMEKQVARLKDEQTELSVGPPW 281
Cdd:PRK11819 255 RLAQEEKQEAA--RQKALKRELEWVRQSPK--------------ARQAKskarlaryeELLSEEYQKRNETNEIFIPPGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 282 RL---VLQGDALP---ADRLLeMDTLHVSPAPGqpslfttGVarlrsgdrVAIMGRNGGGKSSLLRLLWQQmnnASPLPG 355
Cdd:PRK11819 319 RLgdkVIEAENLSksfGDRLL-IDDLSFSLPPG-------GI--------VGIIGPNGAGKSTLFKMITGQ---EQPDSG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 356 -LRLHPRLHPGYYDQTLAQLPDEASLLEALtpfAPSADTRK--------RALIAA-GFGWARHSQKVSTLSGGERSRllf 425
Cdd:PRK11819 380 tIKIGETVKLAYVDQSRDALDPNKTVWEEI---SGGLDIIKvgnreipsRAYVGRfNFKGGDQQKKVGVLSGGERNR--- 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 426 vgLSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDR 471
Cdd:PRK11819 454 --LHLAKTlkqggNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDR 502
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
319-486 |
1.49e-37 |
|
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: 135.65 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPglRLHPRLHPGYYDQtlaqlpdeasllealtpfapsadtrkral 398
Cdd:cd03221 22 TINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--TWGSTVKIGYFEQ----------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 399 iaagfgwarhsqkvstLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESC 478
Cdd:cd03221 71 ----------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVA 134
|
....*...
gi 1439757928 479 NRFWLIDS 486
Cdd:cd03221 135 TKIIELED 142
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-197 |
6.64e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.54 E-value: 6.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA-------------- 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmpppewrrqvayvp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 71 --------RVEQHLPEtlhtqsllqavlaPLPADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIR 142
Cdd:COG4619 81 qepalwggTVRDNLPF-------------PFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 143 QPDLLLLDEPGNHLDLPTLLWLESFLQTW----QGSFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-181 |
8.77e-29 |
|
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: 114.76 E-value: 8.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MAR----V 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsrreLARriayV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 73 EQHLPETLHTqSLLQAVL----------APLPADAREAqrwlAERLLAQMGfTPAVMEQQTATLSGGQHTRLLLARALIR 142
Cdd:COG1120 81 PQEPPAPFGL-TVRELVAlgryphlglfGRPSAEDREA----VEEALERTG-LEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1439757928 143 QPDLLLLDEPGNHLDLP----TLLWLESFLQTWQGSFVLVSHD 181
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHD 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-276 |
1.11e-28 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 120.66 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPEtlhtqsLLQAVLAPLPADAR 98
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLE------FLRADESPLQHLAR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 99 EAQRWLAERL---LAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSF 175
Cdd:PRK10636 401 LAPQELEQKLrdyLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 176 VLVSHDNTLLDAVTNSSWILRDQTLHSFALPCSAARQALQEQDESAAlRHKAEQKEIDRVSASARR--------LATWGR 247
Cdd:PRK10636 481 VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQEN-QTDEAPKENNANSAQARKdqkrreaeLRTQTQ 559
|
250 260
....*....|....*....|....*....
gi 1439757928 248 VYDNEdLARKAKQMEKQVARLKDEQTELS 276
Cdd:PRK10636 560 PLRKE-IARLEKEMEKLNAQLAQAEEKLG 587
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-188 |
2.58e-28 |
|
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: 112.19 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVEtaFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ------- 74
Cdd:COG4133 2 MLEAENLSCR--RGerLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrrlay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 75 --HLPETLHTQSLLQAVLAPLPADAREAQRWLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG4133 80 lgHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1439757928 153 GNHLDLPTLLWLESFLQTW---QGSFVLVSHDNTLLDAV 188
Cdd:COG4133 159 FTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-189 |
3.33e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.88 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVetAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR------V 72
Cdd:COG1121 3 MMPAIELENLTV--SYGgrPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRArrrigyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 73 EQHLpetlhtqsllqAVLAPLPADARE------------------AQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRL 134
Cdd:COG1121 81 PQRA-----------EVDWDFPITVRDvvlmgrygrrglfrrpsrADREAVDEALERVGLE-DLADRPIGELSGGQQQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 135 LLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQG---SFVLVSHDntlLDAVT 189
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD---LGAVR 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-152 |
5.35e-28 |
|
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: 109.27 E-value: 5.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP---------------ETLHTQS 84
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkeigyvfqdpqlfprLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 85 LLQAVLAPLPADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-230 |
5.44e-28 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 118.51 E-value: 5.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL----PE---------------- 78
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRaeldPEktvmdnlaegkqevmv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 ---TLHTQSLLQAVLAPlPADAReaqrwlaerllaqmgfTPavmeqqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:PRK11147 414 ngrPRHVLGYLQDFLFH-PKRAM----------------TP------VKALSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 156 LDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWIL----------------RDQTLHSFALPCSAARQALQEQDE 219
Cdd:PRK11147 471 LDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFegngkigryvggyhdaRQQQAQYLALKQPAVKKKEEAAAP 550
|
250
....*....|.
gi 1439757928 220 SAALRHKAEQK 230
Cdd:PRK11147 551 KAETVKRSSKK 561
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-197 |
6.75e-28 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 111.02 E-value: 6.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------------------------MARVE 73
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslkelrrkvglvfqnpddqffGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 74 QHL---PETLHTQsllqavlaplPADAREAQRWLAERLLAQmgftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLD 150
Cdd:cd03225 95 EEVafgLENLGLP----------EEEIEERVEEALELVGLE-----GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1439757928 151 EPGNHLDLPTLLWLESFLQTWQG---SFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-181 |
1.67e-27 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 111.10 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG-----QCLMAR-------VEQHLPETLHTQSL 85
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkEPREARrqigvlpDERGLYDRLTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 86 LQ--AVLAPLPADAREAqrwLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLW 163
Cdd:COG4555 95 IRyfAELYGLFDEELKK---RIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRL 170
|
170 180
....*....|....*....|.
gi 1439757928 164 LESFLQTW--QGSFVLVS-HD 181
Cdd:COG4555 171 LREILRALkkEGKTVLFSsHI 191
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-181 |
6.01e-27 |
|
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: 108.96 E-value: 6.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL----------PET-LHTQSLL 86
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvglvfqnPDDqLFAPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 QAV---LAPLPADAREAQRwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLW 163
Cdd:COG1122 95 EDVafgPENLGLPREEIRE-RVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRE 172
|
170 180
....*....|....*....|.
gi 1439757928 164 LESFLQTWQG---SFVLVSHD 181
Cdd:COG1122 173 LLELLKRLNKegkTVIIVTHD 193
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-157 |
9.49e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.61 E-value: 9.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-------CLMARV-----EQHLPETLhT--QSL- 85
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaEVRRRIgyvpqEPALYPDL-TvrENLr 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 86 LQAVLAPLPADAREAQrwlAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG1131 96 FFARLYGLPRKEARER---IDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-181 |
1.11e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 106.75 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 6 TAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARveqhlpetlhtqsl 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 86 lqavlaplpaDAREAQRWLA--ERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLW 163
Cdd:cd03214 67 ----------SPKELARKIAyvPQALELLGLAHLA-DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180
....*....|....*....|..
gi 1439757928 164 LESFLQTWQGSF----VLVSHD 181
Cdd:cd03214 136 LLELLRRLARERgktvVMVLHD 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-480 |
3.16e-25 |
|
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: 109.22 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPT---SGSVSLAGQCL------- 68
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 69 -----------------MARVEQHLPETLHTQSLlqavlaplpadAREAQRWLAERLLAQMGFtPAVMEQQTATLSGGQH 131
Cdd:COG1123 81 rgrrigmvfqdpmtqlnPVTVGDQIAEALENLGL-----------SRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 132 TRLLLARALIRQPDLLLLDEPGNHLDLPT---LLWLESFLQTWQG-SFVLVSHDntlLDAVtnsswilrdqtlhsfalpc 207
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHD---LGVV------------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 208 saarqaLQEQDESAALRH--KAEQKEIDRVSASARRLATWGRVYDNEDLARKAKQMEKQVARLKDeqteLSV-----GPP 280
Cdd:COG1123 207 ------AEIADRVVVMDDgrIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRN----LSKrypvrGKG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 281 WRLVLQGdalpadrllemdtlhVSpapgqpslFTtgvarLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHP 360
Cdd:COG1123 277 GVRAVDD---------------VS--------LT-----LRRGETLGLVGESGSGKSTLARLL------------LGLLR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 361 ------RLH----PGYYDQTLAQL----------PD---------EASLLEALT--PFAPSADTRKRAL-------IAAG 402
Cdd:COG1123 317 ptsgsiLFDgkdlTKLSRRSLRELrrrvqmvfqdPYsslnprmtvGDIIAEPLRlhGLLSRAERRERVAellervgLPPD 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 403 FGWARHSQkvstLSGGERSRllfvgLSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDY---PG-GVLLVSHDRQL 473
Cdd:COG1123 397 LADRYPHE----LSGGQRQR-----VAIARAlalepKLLILDEPTSALDVSVQAQILNLLRDLqreLGlTYLFISHDLAV 467
|
....*..
gi 1439757928 474 ISESCNR 480
Cdd:COG1123 468 VRYIADR 474
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-152 |
4.78e-25 |
|
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: 103.67 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------------MARVEQHl 76
Cdd:cd03219 5 GLTKRFGGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglppheiarlgIGRTFQI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 77 PETLHTQSLLQAVLAPLPADAREAQRWL------------AERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQP 144
Cdd:cd03219 84 PRLFPELTVLENVMVAAQARTGSGLLLArarreerearerAEELLERVGLAD-LADRPAGELSYGQQRRLEIARALATDP 162
|
....*...
gi 1439757928 145 DLLLLDEP 152
Cdd:cd03219 163 KLLLLDEP 170
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-152 |
7.20e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 103.97 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVetAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------- 68
Cdd:COG0411 1 SDPLLEVRGLTK--RFGGLvaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 69 --MARVEQH---LPE-----------TLHTQSLLQAVLAPLPADAREAQRWL--AERLLAQMGFTpAVMEQQTATLSGGQ 130
Cdd:COG0411 79 lgIARTFQNprlFPEltvlenvlvaaHARLGRGLLAALLRLPRARREEREARerAEELLERVGLA-DRADEPAGNLSYGQ 157
|
170 180
....*....|....*....|..
gi 1439757928 131 HTRLLLARALIRQPDLLLLDEP 152
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEP 179
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-197 |
7.52e-25 |
|
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: 100.78 E-value: 7.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 10 LHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmarveqhlpetlhtqsllqav 89
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK----------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 laplpadarEAQRWLAERLLAQMGFTPavmeqQtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQ 169
Cdd:cd00267 62 ---------DIAKLPLEELRRRIGYVP-----Q---LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|.
gi 1439757928 170 TWQG---SFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:cd00267 125 ELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-181 |
7.99e-25 |
|
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: 102.97 E-value: 7.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQHLPETLH-TQSL 85
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrrlrkirrkeIQMVFQDPMSSLNpRMTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 86 LQAVLAPL----PADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD---- 157
Cdd:cd03257 102 GEQIAEPLrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDvsvq 181
|
170 180
....*....|....*....|....*..
gi 1439757928 158 ---LPTLLWLESFLQTwqgSFVLVSHD 181
Cdd:cd03257 182 aqiLDLLKKLQEELGL---TLLFITHD 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-203 |
9.02e-25 |
|
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: 102.23 E-value: 9.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--HLPETLHTQ-----SLLQAVL----- 90
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVPQRRSIDrdfpiSVRDVVLmglyg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 91 -APLPADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQ 169
Cdd:cd03235 98 hKGLFRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1439757928 170 TWQG---SFVLVSHD-NTLLDAVTNSswILRDQTLHSF 203
Cdd:cd03235 177 ELRRegmTILVVTHDlGLVLEYFDRV--LLLNRTVVAS 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-197 |
9.27e-25 |
|
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: 100.94 E-value: 9.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmarveqhlpetlhtqsllqavlaPLPADAREA 100
Cdd:cd03230 17 DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK-------------------------DIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 101 QRWLAerLLAQmgfTPAVMEQQTA----TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTW---QG 173
Cdd:cd03230 72 KRRIG--YLPE---EPSLYENLTVrenlKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGK 146
|
170 180
....*....|....*....|....
gi 1439757928 174 SFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:cd03230 147 TILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-181 |
2.18e-24 |
|
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: 101.22 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLK-----KGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM-ARVEQHLPETLHTQSLL--QAVLAP--- 92
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdSRKKINLPPQQRKIGLVfqQYALFPhln 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 93 --------LPADAREAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03297 92 vrenlafgLKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|.
gi 1439757928 165 ESFLQTWQGSF----VLVSHD 181
Cdd:cd03297 171 LPELKQIKKNLnipvIFVTHD 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-181 |
2.25e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 102.19 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVetAFG------PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR------ 71
Cdd:COG1124 1 MLEVRNLSV--SYGqggrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRrrkafr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 72 -----VEQHLPETLH-TQSLLQAVLAPLPA---DAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIR 142
Cdd:COG1124 79 rrvqmVFQDPYASLHpRHTVDRILAEPLRIhglPDREER---IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1439757928 143 QPDLLLLDEPGNHLDLPT----LLWLESFLQTWQGSFVLVSHD 181
Cdd:COG1124 156 EPELLLLDEPTSALDVSVqaeiLNLLKDLREERGLTYLFVSHD 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-203 |
8.88e-24 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 105.71 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 17 GP-LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSllqavlAPLPA 95
Cdd:PLN03073 521 GPlLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSS------NPLLY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 DAREAQRWLAERL---LAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQ 172
Cdd:PLN03073 595 MMRCFPGVPEQKLrahLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ 674
|
170 180 190
....*....|....*....|....*....|.
gi 1439757928 173 GSFVLVSHDNTLLDAVTNSSWILRDQTLHSF 203
Cdd:PLN03073 675 GGVLMVSHDEHLISGSVDELWVVSEGKVTPF 705
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-180 |
1.46e-23 |
|
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: 99.77 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSG-SVSLAGQCL----MARVEQHL----PETLH----TQS 84
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRggedVWELRKRIglvsPALQLrfprDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQAVL------APLPADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDL 158
Cdd:COG1119 97 VLDVVLsgffdsIGLYREPTDEQRERARELLELLGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
170 180
....*....|....*....|....*.
gi 1439757928 159 PTLLWLESFLQTW--QG--SFVLVSH 180
Cdd:COG1119 176 GARELLLALLDKLaaEGapTLVLVTH 201
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-197 |
6.56e-23 |
|
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: 96.94 E-value: 6.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR--------VEQHLPETLHTQSLLQAVL 90
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKerrksigyVMQDVDYQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 91 APLPADAREAQRwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL-ESFLQ 169
Cdd:cd03226 95 LGLKELDAGNEQ--AETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVgELIRE 171
|
170 180 190
....*....|....*....|....*....|
gi 1439757928 170 -TWQGSFVLV-SHDNTLLDAVTNSSWILRD 197
Cdd:cd03226 172 lAAQGKAVIViTHDYEFLAKVCDRVLLLAN 201
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
23-181 |
1.28e-22 |
|
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: 96.39 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPET-LHTQ--------SLLQAVLAPL 93
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE----PVTGPGPDRgYVFQqdallpwlTVLDNVALGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 94 ---PADAREAQRwLAERLLAQMGFTPAvmEQQT-ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL-ESFL 168
Cdd:cd03293 99 elqGVPKAEARE-RAEELLELVGLSGF--ENAYpHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLqEELL 175
|
170
....*....|....*.
gi 1439757928 169 QTWQG---SFVLVSHD 181
Cdd:cd03293 176 DIWREtgkTVLLVTHD 191
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-184 |
2.42e-22 |
|
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: 95.63 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA---------RVEQ--------HLpetLHTQSLL 86
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelaafRRRHigfvfqsfNL---LPDLTAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 QAVLAPL---PADAREAQRWlAERLLAQMGFtPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP-GNhLDLPT-- 160
Cdd:cd03255 101 ENVELPLllaGVPKKERRER-AEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPtGN-LDSETgk 177
|
170 180
....*....|....*....|....*.
gi 1439757928 161 --LLWLESFLQTWQGSFVLVSHDNTL 184
Cdd:cd03255 178 evMELLRELNKEAGTTIVVVTHDPEL 203
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-181 |
2.89e-22 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 96.75 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL-------------PEtlhtQSLLQA-V 89
Cdd:TIGR04521 25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrkkvglvfqfPE----HQLFEEtV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 L-----AP--LPADAREAQRwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlP--- 159
Cdd:TIGR04521 101 YkdiafGPknLGLSEEEAEE-RVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD-Pkgr 178
|
170 180
....*....|....*....|....
gi 1439757928 160 -TLLWLESFLQTWQG-SFVLVSHD 181
Cdd:TIGR04521 179 kEILDLFKRLHKEKGlTVILVTHS 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-181 |
3.05e-22 |
|
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: 94.89 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR---------VEQHlPET 79
Cdd:cd03259 5 GLSKTYGsvRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVpperrnigmVFQD-YAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 LHTQSLLQAVLAPL-----PADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:cd03259 84 FPHLTVAENIAFGLklrgvPKAEIRAR---VRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|.
gi 1439757928 155 HLDLPTLLWLESFLQTWQGSF----VLVSHD 181
Cdd:cd03259 160 ALDAKLREELREELKELQRELgittIYVTHD 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-181 |
6.07e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 95.54 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPET---------LHTQSLLQA 88
Cdd:COG1116 25 TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK----PVTGPGPDRgvvfqepalLPWLTVLDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 89 VLAPLPA---DAREAQRWlAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT--LLW 163
Cdd:COG1116 101 VALGLELrgvPKAERRER-ARELLELVGLAGF-EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTreRLQ 178
|
170 180
....*....|....*....|.
gi 1439757928 164 LEsFLQTWQG---SFVLVSHD 181
Cdd:COG1116 179 DE-LLRLWQEtgkTVLFVTHD 198
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-157 |
6.19e-22 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 92.83 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmarveqhlpetlhtqsllqavlaplpaDA 97
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV-----------------------------DL 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 98 RE-AQRWLAERLlaqmgftpAVMEQQT----AT-----LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03228 67 RDlDLESLRKNI--------AYVPQDPflfsGTireniLSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-186 |
6.91e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.34 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVEtaFG------PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------ 68
Cdd:COG1136 1 MSPLLELRNLTKS--YGtgegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 69 -MAR--------VEQ--HLPETLhtqSLLQAVLAPL---PADAREAQRWlAERLLAQMGFTpAVMEQQTATLSGGQHTRL 134
Cdd:COG1136 79 eLARlrrrhigfVFQffNLLPEL---TALENVALPLllaGVSRKERRER-ARELLERVGLG-DRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 135 LLARALIRQPDLLLLDEP-GNhLDLPT------LlwLESFLQTWQGSFVLVSHDNTLLD 186
Cdd:COG1136 154 AIARALVNRPKLILADEPtGN-LDSKTgeevleL--LRELNRELGTTIVMVTHDPELAA 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-188 |
1.11e-21 |
|
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: 98.68 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE--TLHTQ-------SLLQA 88
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRriAVVPQrphlfdtTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 89 VL--APlpaDAREAQRWLAerlLAQMGFTPAVMEQQT----------ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:COG4987 429 LRlaRP---DATDEELWAA---LERVGLGDWLAALPDgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190
....*....|....*....|....*....|....
gi 1439757928 157 DLPT-LLWLESFLQTWQG-SFVLVSHDNTLLDAV 188
Cdd:COG4987 503 DAATeQALLADLLEALAGrTVLLITHRLAGLERM 536
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-181 |
1.46e-21 |
|
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: 93.94 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE----------------TLHTQSLL 86
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRigvvfgqktqlwwdlpVIDSFYLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 QAVLAPLPADAREAQRWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLES 166
Cdd:cd03267 120 AAIYDLPPARFKKRLDELSELL--DLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170
....*....|....*....
gi 1439757928 167 FLQTW----QGSFVLVSHD 181
Cdd:cd03267 195 FLKEYnrerGTTVLLTSHY 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-181 |
1.53e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH--LPETLHTqSLLQAV------ 89
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRseVPDSLPL-TVRDLVamgrwa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 ----LAPLPADAREAqrwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:NF040873 85 rrglWRRLTRDDRAA----VDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170
....*....|....*....
gi 1439757928 166 SFLQTWQG---SFVLVSHD 181
Cdd:NF040873 160 ALLAEEHArgaTVVVVTHD 178
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-186 |
2.44e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 92.88 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 2 STLLTAHALH--VETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MA 70
Cdd:COG4181 6 APIIELRGLTktVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedaRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 71 RV-----------EQHLPetlhTQSLLQAVLAPLP-ADAREAQRwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLAR 138
Cdd:COG4181 86 RLrarhvgfvfqsFQLLP----TLTALENVMLPLElAGRRDARA-RARALLERVGLG-HRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928 139 ALIRQPDLLLLDEP-GNhLDLPT------LLwlesF-LQTWQGS-FVLVSHDNTLLD 186
Cdd:COG4181 160 AFATEPAILFADEPtGN-LDAATgeqiidLL----FeLNRERGTtLVLVTHDPALAA 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-181 |
3.02e-21 |
|
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: 92.53 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR------VEQH---LPETLHTQSLLQAVLAPL 93
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdrmvVFQNyslLPWLTVRENIALAVDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 94 PADAREAQRWLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL-ESFLQTWQ 172
Cdd:TIGR01184 84 PDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqEELMQIWE 162
|
170
....*....|..
gi 1439757928 173 GS---FVLVSHD 181
Cdd:TIGR01184 163 EHrvtVLMVTHD 174
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-181 |
4.16e-21 |
|
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: 90.71 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLLQ-AVLAPlpadare 99
Cdd:cd03229 17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGMVFQdFALFP------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 100 aqrwlaerllaqmgfTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSF---- 175
Cdd:cd03229 90 ---------------HLTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgitv 154
|
....*.
gi 1439757928 176 VLVSHD 181
Cdd:cd03229 155 VLVTHD 160
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-188 |
6.13e-21 |
|
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: 89.97 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmARVEQHLPETL--HTQSLLQAVLAplpa 95
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----ADISQWDPNELgdHVGYLPQDDEL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 dareaqrwlaerllaqmgFTPAVMEqqtATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQ--- 172
Cdd:cd03246 88 ------------------FSGSIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaag 146
|
170
....*....|....*.
gi 1439757928 173 GSFVLVSHDNTLLDAV 188
Cdd:cd03246 147 ATRIVIAHRPETLASA 162
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
18-184 |
7.96e-21 |
|
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: 92.18 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----------CLMARVEQHLPETLHTQSLL 86
Cdd:TIGR03873 15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglsrraraRRVALVEQDSDTAVPLTVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 QAVLAPLP-----ADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL 161
Cdd:TIGR03873 95 VVALGRIPhrslwAGDSPHDAAVVDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQ 173
|
170 180
....*....|....*....|....*.
gi 1439757928 162 LWLESFLQTWQGSFVLVS---HDNTL 184
Cdd:TIGR03873 174 LETLALVRELAATGVTVVaalHDLNL 199
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
21-152 |
1.63e-20 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 90.89 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQH--LPE------ 78
Cdd:COG3638 20 DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgralrrlrrrIGMIFQQfnLVPrlsvlt 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 79 -----TLHTQSLLQAVLAPLPADAREaqrwLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG3638 100 nvlagRLGRTSTWRSLLGLFPPEDRE----RALEALERVGLADK-AYQRADQLSGGQQQRVAIARALVQEPKLILADEP 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-189 |
4.62e-20 |
|
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: 88.80 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG----QCLMARVEQHLPETLHTQSLLQA------VLA 91
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirQLDPADLRRNIGYVPQDVTLFYGtlrdniTLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 92 PLPADAREAQRwlAERLLAQMGFT---PAVMEQQT----ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03245 102 APLADDERILR--AAELAGVTDFVnkhPNGLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL 179
|
170 180
....*....|....*....|....*..
gi 1439757928 165 ESFLQTWQG--SFVLVSHDNTLLDAVT 189
Cdd:cd03245 180 KERLRQLLGdkTLIIITHRPSLLDLVD 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-188 |
5.92e-20 |
|
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: 93.46 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLLQA 88
Cdd:TIGR03719 327 NLTKAFGdkLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 89 V---LAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:TIGR03719 407 IsggLDIIKLGKREIP---SRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALE 483
|
170 180
....*....|....*....|...
gi 1439757928 166 SFLQTWQGSFVLVSHDNTLLDAV 188
Cdd:TIGR03719 484 EALLNFAGCAVVISHDRWFLDRI 506
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-218 |
1.88e-19 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 91.74 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 17 GPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQHlpETLHTQSL 85
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsdldpaswrrqIAWVPQN--PYLFAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 86 LQAVLAPLPaDAREAQRWLAERLLAQMGFTPAvMEQQTAT--------LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4988 428 RENLRLGRP-DASDEELEAALEAAGLDEFVAA-LPDGLDTplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 158 LPT-LLWLESFLQTWQGSFVL-VSHDntlLDAVTNSSWILRdqtLHSFALPCSAARQALQEQD 218
Cdd:COG4988 506 AETeAEILQALRRLAKGRTVIlITHR---LALLAQADRILV---LDDGRIVEQGTHEELLAKN 562
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-181 |
3.03e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 87.94 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQHLPETLHTQ 83
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldrkqrrafrrdVQLVFQDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 SLLQAVLA-PL----PADAREAQRWLAErLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDL 158
Cdd:TIGR02769 105 MTVRQIIGePLrhltSLDESEQKARIAE-LLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180
....*....|....*....|....*..
gi 1439757928 159 ----PTLLWLESFLQTWQGSFVLVSHD 181
Cdd:TIGR02769 184 vlqaVILELLRKLQQAFGTAYLFITHD 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-157 |
3.48e-19 |
|
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: 91.43 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQ-------------S 84
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI----DLRQIDPASLRRQigvvlqdvflfsgT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQ--AVLAPLPADAReaqrwlAERLLAQMGFTPAVMEQ----QT------ATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG2274 565 IREniTLGDPDATDEE------IIEAARLAGLHDFIEALpmgyDTvvgeggSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
....*
gi 1439757928 153 GNHLD 157
Cdd:COG2274 639 TSALD 643
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
320-485 |
4.17e-19 |
|
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: 84.22 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpglrlhprlhpgyydqTLAQLPDEASLLEALTPFAPSADTRKRALI 399
Cdd:cd00267 22 LKAGEIVALVGPNGSGKSTLLRAI--------------------------AGLLKPTSGEILIDGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 400 AAgfgwarhsqkVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG---VLLVSHDRQLISE 476
Cdd:cd00267 76 GY----------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgrtVIIVTHDPELAEL 145
|
....*....
gi 1439757928 477 SCNRFWLID 485
Cdd:cd00267 146 AADRVIVLK 154
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-181 |
6.19e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.28 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVE----------QH--- 75
Cdd:COG1118 7 NISKRFGsfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPprerrvgfvfQHyal 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 76 -------------LPetlhtqsllqaVLAPLPADARE-AQRWL--------AERLLAQmgftpavmeqqtatLSGGQHTR 133
Cdd:COG1118 87 fphmtvaeniafgLR-----------VRPPSKAEIRArVEELLelvqleglADRYPSQ--------------LSGGQRQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 134 LLLARALIRQPDLLLLDEPGNHLD--LPTLL--WLESFLQTWQGSFVLVSHD 181
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDakVRKELrrWLRRLHDELGGTTVFVTHD 193
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-157 |
9.77e-19 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 84.89 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------------MARVEQH 75
Cdd:cd03262 5 NLHKSFGDFhvLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkkninelrqkVGMVFQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 76 LPETLHTQSLLQAVLAPLPA---DAREAQRwLAERLLAQMGFTpavmEQQT---ATLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:cd03262 85 FNLFPHLTVLENITLAPIKVkgmSKAEAEE-RALELLEKVGLA----DKADaypAQLSGGQQQRVAIARALAMNPKVMLF 159
|
....*...
gi 1439757928 150 DEPGNHLD 157
Cdd:cd03262 160 DEPTSALD 167
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-181 |
1.04e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.84 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP---TSGSVSLAGQCLmarveQHLP-ETLHTQSLLQ-AVLAP 92
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-----TALPaEQRRIGILFQdDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 93 -----------LPAD-AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:COG4136 90 hlsvgenlafaLPPTiGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180
....*....|....*....|....*
gi 1439757928 161 LLWLESF----LQTWQGSFVLVSHD 181
Cdd:COG4136 169 RAQFREFvfeqIRQRGIPALLVTHD 193
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-181 |
1.09e-18 |
|
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: 84.86 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---MARVEQH---------LPETLHTQSLLQ- 87
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdRKAARQSlgycpqfdaLFDELTVREHLRf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 -AVLAPLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPT---LLW 163
Cdd:cd03263 99 yARLKGLPKSEIKEE---VELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PAsrrAIW 173
|
170 180
....*....|....*....|
gi 1439757928 164 leSFLQTWQG--SFVLVSHD 181
Cdd:cd03263 174 --DLILEVRKgrSIILTTHS 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-157 |
1.32e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 85.31 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQHLPET------- 79
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqlrrqIGMIFQQFNLIerlsvle 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 ------LHTQSLLQAVLAPLPadarEAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:cd03256 98 nvlsgrLGRRSTWRSLFGLFP----KEEKQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
....
gi 1439757928 154 NHLD 157
Cdd:cd03256 173 ASLD 176
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
21-181 |
2.84e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 86.31 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQcLMARV--EQ--------------HLpetlhtqS 84
Cdd:COG3842 22 DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-DVTGLppEKrnvgmvfqdyalfpHL-------T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQAVLAPL-----PADAREAQrwlAERLLAQMGftpavMEQQ----TATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:COG3842 94 VAENVAFGLrmrgvPKAEIRAR---VAELLELVG-----LEGLadryPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190
....*....|....*....|....*....|
gi 1439757928 156 LDLP----TLLWLESFLQTWQGSFVLVSHD 181
Cdd:COG3842 166 LDAKlreeMREELRRLQRELGITFIYVTHD 195
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-157 |
4.28e-18 |
|
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: 83.10 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 8 HALHVETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH---LPE---- 78
Cdd:cd03269 2 EVENVTKRFGRvtALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigyLPEergl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 ----TLHTQSLLQAVLAPLPadAREAQRWlAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:cd03269 82 ypkmKVIDQLVYLAQLKGLK--KEEARRR-IDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
...
gi 1439757928 155 HLD 157
Cdd:cd03269 158 GLD 160
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-181 |
5.91e-18 |
|
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: 87.03 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG-------QCLMARVEQHLPETLH--TQSLLQA 88
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldQDEVRRRVSVCAQDAHlfDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 89 VLAPLPaDAREAQRW-------LAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT- 160
Cdd:TIGR02868 429 LRLARP-DATDEELWaalervgLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETa 507
|
170 180
....*....|....*....|..
gi 1439757928 161 LLWLESFLQTWQG-SFVLVSHD 181
Cdd:TIGR02868 508 DELLEDLLAALSGrTVVLITHH 529
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-181 |
6.39e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.76 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM------ARVEQH---LPetlhTQSLLQAV---- 89
Cdd:COG4525 26 VSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgadrGVVFQKdalLP----WLNVLDNVafgl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 -LAPLPADAREAQrwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT------LL 162
Cdd:COG4525 102 rLRGVPKAERRAR---AEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTreqmqeLL 177
|
170 180
....*....|....*....|..
gi 1439757928 163 wlesfLQTWQGS---FVLVSHD 181
Cdd:COG4525 178 -----LDVWQRTgkgVFLITHS 194
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-189 |
7.36e-18 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 87.23 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG----QCLMARVEQH---LPE--TLHTQSLLQ--AV 89
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdirQIDPADLRRNigyVPQdpRLFYGTLRDniAL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 LAPLPADA---REAQRWLAERLLAQ--MGFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:TIGR03375 562 GAPYADDEeilRAAELAGVTEFVRRhpDGLDMQIGER-GRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERF 640
|
170 180
....*....|....*....|....*..
gi 1439757928 165 ESFLQTWQG--SFVLVSHDNTLLDAVT 189
Cdd:TIGR03375 641 KDRLKRWLAgkTLVLVTHRTSLLDLVD 667
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-181 |
7.95e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 86.57 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 17 GPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE---------TLHTQSLLQ 87
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDqiawvpqhpFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 AV-LAPLPADAREAQRwlAERLLAQMGFTPA-------VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLP 159
Cdd:TIGR02857 415 NIrLARPDASDAEIRE--ALERAGLDEFVAAlpqgldtPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180
....*....|....*....|....
gi 1439757928 160 T-LLWLESFLQTWQG-SFVLVSHD 181
Cdd:TIGR02857 493 TeAEVLEALRALAQGrTVLLVTHR 516
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-157 |
8.92e-18 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 82.63 E-value: 8.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQHLpETLHTQ 83
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgkelrkarrrIGMIFQHF-NLLSSR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 84 SLLQAVLAPL-----PADAREAQrwlAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03258 98 TVFENVALPLeiagvPKAEIEER---VLELLELVGLEDKA-DAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-158 |
1.54e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.47 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARVEQHL 76
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawspweLARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 77 PEtlHTQ-----SLLQAV---LAPLPADAREAQRwLAERLLAQMGfTPAVMEQQTATLSGGQHTRLLLARAL--IRQPD- 145
Cdd:COG4559 81 PQ--HSSlafpfTVEEVValgRAPHGSSAAQDRQ-IVREALALVG-LAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVd 156
|
170
....*....|....*..
gi 1439757928 146 ----LLLLDEPGNHLDL 158
Cdd:COG4559 157 ggprWLFLDEPTSALDL 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-179 |
1.89e-17 |
|
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: 81.11 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLPETL-HTQSLLQAvlaplPA---- 95
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIEALrRIGALIEA-----PGfypn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 -DAREAQRWLA----------ERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03268 87 lTARENLRLLArllgirkkriDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170
....*....|....*..
gi 1439757928 165 ESFLQTW--QGSFVLVS 179
Cdd:cd03268 166 RELILSLrdQGITVLIS 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-186 |
1.97e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 85.56 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHlPETLH-TQSLLQ 87
Cdd:PRK11819 329 NLSKSFGDrlLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS-RDALDpNKTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 AVlaplpADARE----AQRWLAER-LLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLL 162
Cdd:PRK11819 408 EI-----SGGLDiikvGNREIPSRaYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLR 482
|
170 180
....*....|....*....|....
gi 1439757928 163 WLESFLQTWQGSFVLVSHDNTLLD 186
Cdd:PRK11819 483 ALEEALLEFPGCAVVISHDRWFLD 506
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-181 |
2.38e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 81.58 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG---PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETL------- 80
Cdd:cd03295 5 NVTKRYGggkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIgyviqqi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 81 ----HTQSLLQAVLAP-LPADAREAQRWLAERLLAQMGFTPA-VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:cd03295 85 glfpHMTVEENIALVPkLLKWPKEKIRERADELLALVGLDPAeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190
....*....|....*....|....*....|.
gi 1439757928 155 HLDLPTLLWL-ESFL---QTWQGSFVLVSHD 181
Cdd:cd03295 165 ALDPITRDQLqEEFKrlqQELGKTIVFVTHD 195
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
319-489 |
2.44e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 80.63 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL------------WQQMN-NASPLPGLR-----LHPRlhPGYYDQTLAQ-LPDEAS 379
Cdd:COG4619 22 TLEAGECVAITGPSGSGKSTLLRALadldpptsgeiyLDGKPlSAMPPPEWRrqvayVPQE--PALWGGTVRDnLPFPFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 380 LLEAltpfAPSADTRKRALIAAGFGWARHSQKVSTLSGGERSRLLFV-GLSLARySLLLLDEPTNHLDMEGKAALAQTLR 458
Cdd:COG4619 100 LRER----KFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIrALLLQP-DVLLLDEPTSALDPENTRRVEELLR 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1439757928 459 DYP----GGVLLVSHDRQLISESCNRFWLIDSAGL 489
Cdd:COG4619 175 EYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-218 |
3.39e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--------------HLPET-LHTQ 83
Cdd:PRK13643 22 LFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpvrkkvgvvfQFPESqLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 SLLQAV-LAP--LPADAREAQRWLAERlLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD--- 157
Cdd:PRK13643 101 TVLKDVaFGPqnFGIPKEKAEKIAAEK-LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpka 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 158 -LPTLLWLESFLQTWQgSFVLVSHdntLLDAVTN-SSWILRDQTLHsfALPCSAARQALQEQD 218
Cdd:PRK13643 180 rIEMMQLFESIHQSGQ-TVVLVTH---LMDDVADyADYVYLLEKGH--IISCGTPSDVFQEVD 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-181 |
3.87e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.18 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--------------HLPET-LHTQSLLQ 87
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkklrkkvslvfQFPEAqLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 AV-LAPLPADAREAQ-RWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:PRK13641 106 DVeFGPKNFGFSEDEaKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170
....*....|....*....
gi 1439757928 166 SFLQTWQG---SFVLVSHD 181
Cdd:PRK13641 186 QLFKDYQKaghTVILVTHN 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-180 |
4.09e-17 |
|
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: 79.01 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlpetlhtqsllQAVLAPLPADAREA 100
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------------KEVSFASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 101 qrwlaerllaqmgftPAVMEQQtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQ--TWQG-SFVL 177
Cdd:cd03216 76 ---------------GIAMVYQ---LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRrlRAQGvAVIF 137
|
...
gi 1439757928 178 VSH 180
Cdd:cd03216 138 ISH 140
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-185 |
4.38e-17 |
|
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: 80.27 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQC-----LMARVEQHLP--ETLHtqsLLQAVLAPLPA 95
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssllgLGGGFNPELTgrENIY---LNGRLLGLSRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 DAREAQRWLAErlLAQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEpgnhldlptllWL----ESF---- 167
Cdd:cd03220 118 EIDEKIDEIIE--FSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE-----------VLavgdAAFqekc 181
|
170 180
....*....|....*....|....
gi 1439757928 168 ---LQTWQ---GSFVLVSHDNTLL 185
Cdd:cd03220 182 qrrLRELLkqgKTVILVSHDPSSI 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-181 |
5.49e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.27 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 2 STLLTAHALHVETAFGPLF---------NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA-- 70
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 71 ------------RVEQHLPETLHTQSLLQAVLAP----LPADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRL 134
Cdd:PRK10419 81 raqrkafrrdiqMVFQDSISAVNPRKTVREIIREplrhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 135 LLARALIRQPDLLLLDEPGNHLDL----PTLLWLESFLQTWQGSFVLVSHD 181
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHD 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
24-157 |
5.53e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 80.81 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--------------MARVEQH---------LPETL 80
Cdd:TIGR02315 22 NLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgkklrklrrrIGMIFQHynlierltvLENVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 81 H----TQSLLQAVLAPLPadarEAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:TIGR02315 102 HgrlgYKPTWRSLLGRFS----EEDKERALSALERVGLA-DKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASL 176
|
.
gi 1439757928 157 D 157
Cdd:TIGR02315 177 D 177
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-152 |
5.81e-17 |
|
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: 80.41 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 2 STLLTAHALHVetAFGP---LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MAR 71
Cdd:COG0410 1 MPMLEVENLHA--GYGGihvLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglpphrIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 72 -----------------VEQHLpetlhtqsllqaVLAPLPADAREAQRWLAERL------LAQMgftpavMEQQTATLSG 128
Cdd:COG0410 78 lgigyvpegrrifpsltVEENL------------LLGAYARRDRAEVRADLERVyelfprLKER------RRQRAGTLSG 139
|
170 180
....*....|....*....|....
gi 1439757928 129 GQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
18-187 |
6.62e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.71 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPET-------------LHTQS 84
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrrigvvfqdfrlLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQAVLAPL---PADAREAQRWLAErLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTL 161
Cdd:COG2884 96 VYENVALPLrvtGKSRKEIRRRVRE-VLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLD-PET 172
|
170 180 190
....*....|....*....|....*....|..
gi 1439757928 162 LW-----LESFLQTwqGSFVLV-SHDNTLLDA 187
Cdd:COG2884 173 SWeimelLEEINRR--GTTVLIaTHDLELVDR 202
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-152 |
8.61e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 79.40 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM-----ARVEQ---HLPET---LHTQSLLQAVLA 91
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpphERARAgigYVPEGrriFPELTVEENLLL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 92 PLPADAREAQRWLAERLLAQmgFtPAVME---QQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:cd03224 99 GAYARRRAKRKARLERVYEL--F-PRLKErrkQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-181 |
9.43e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 3 TLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARV--- 72
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlssrqLARRlal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 73 --EQHL-PETLHTQSLLQAVLAP-LPADAREAQ--RWLAERLLAQMGfTPAVMEQQTATLSGGQHTRLLLARALIRQPDL 146
Cdd:PRK11231 81 lpQHHLtPEGITVRELVAYGRSPwLSLWGRLSAedNARVNQAMEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1439757928 147 LLLDEPGNHLDLP---TLLWLESFLQTWQGSFVLVSHD 181
Cdd:PRK11231 160 VLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-234 |
1.70e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--HLPE 78
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 TLHTQSLLQAVLAP-------LPAdareAQRWLAERLLaqmgftpavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK09544 81 TLPLTVNRFLRLRPgtkkediLPA----LKRVQAGHLI----------DAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 152 PGNHLDLPTLLWLESF---LQTWQGSFVL-VSHDNTLLDAVTNSSWILRDQtlhsfaLPCSAARQALQEQDESAAL--RH 225
Cdd:PRK09544 147 PTQGVDVNGQVALYDLidqLRRELDCAVLmVSHDLHLVMAKTDEVLCLNHH------ICCSGTPEVVSLHPEFISMfgPR 220
|
....*....
gi 1439757928 226 KAEQKEIDR 234
Cdd:PRK09544 221 GAEQLGIYR 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-190 |
1.75e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA--------RVEQHL------PET-LHTQ 83
Cdd:PRK13649 23 LFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdikQIRKKVglvfqfPESqLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 SLLQAV-LAP--LPADAREAQRwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD--- 157
Cdd:PRK13649 102 TVLKDVaFGPqnFGVSQEEAEA-LAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDpkg 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1439757928 158 ---LPTLlwlesFLQTWQG--SFVLVSHdntLLDAVTN 190
Cdd:PRK13649 181 rkeLMTL-----FKKLHQSgmTIVLVTH---LMDDVAN 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-181 |
1.76e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmaRVeqhlpetlhtQSLLqAVLAPLPAD--ARE- 99
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----RV----------SALL-ELGAGFHPEltGREn 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 100 AqrwlaeRLLAQ-MGFTPAVMEQQTA-----------------TLSGGQHTRLLLARALIRQPDLLLLDEpgnhldlptl 161
Cdd:COG1134 109 I------YLNGRlLGLSRKEIDEKFDeivefaelgdfidqpvkTYSSGMRARLAFAVATAVDPDILLVDE---------- 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1439757928 162 lWL---------------ESFLQTwQGSFVLVSHD 181
Cdd:COG1134 173 -VLavgdaafqkkclariRELRES-GRTVIFVSHS 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-157 |
3.11e-16 |
|
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: 78.24 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGS---------VSLAG----QCLMAR------VEQHLpE 78
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwVDLAQasprEILALRrrtigyVSQFL-R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 TLHTQSLLQAVLAPLPAD--AREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:COG4778 104 VIPRVSALDVVAEPLLERgvDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASL 183
|
.
gi 1439757928 157 D 157
Cdd:COG4778 184 D 184
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-181 |
3.86e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.87 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-CLMARVEQ--------------HLpetlhtqSLLQA 88
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdLTALPPAErpvsmlfqennlfpHL-------TVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 89 VLAPLPADAR--EAQRWLAERLLAQMGFTPavMEQQT-ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTL---- 161
Cdd:COG3840 92 IGLGLRPGLKltAEQRAQVEQALERVGLAG--LLDRLpGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD-PALrqem 168
|
170 180
....*....|....*....|.
gi 1439757928 162 LWLESFLQTWQGSFVL-VSHD 181
Cdd:COG3840 169 LDLVDELCRERGLTVLmVTHD 189
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-181 |
4.36e-16 |
|
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: 77.93 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL--MARVEQhlpETLHTQ--- 83
Cdd:cd03261 5 GLTKSFGgrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsgLSEAEL---YRLRRRmgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 -----------SLLQAVLAPLPADAREAQRWLAERL---LAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:cd03261 82 lfqsgalfdslTVFENVAFPLREHTRLSEEEIREIVlekLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1439757928 150 DEPGNHLDLPTLLWLESFLQTWQGSF----VLVSHD 181
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHD 196
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-152 |
5.12e-16 |
|
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: 77.71 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPEtLHTQ----- 83
Cdd:COG1127 10 NLTKSFGdrVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE-LRRRigmlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 ---------SLLQAVLAPL-------PADAREaqrwLAERLLAQMGFtPAVMEQQTATLSGGQHTRLLLARALIRQPDLL 147
Cdd:COG1127 89 qggalfdslTVFENVAFPLrehtdlsEAEIRE----LVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
....*
gi 1439757928 148 LLDEP 152
Cdd:COG1127 164 LYDEP 168
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-152 |
5.18e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 77.73 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-------------VEQ- 74
Cdd:COG1126 6 NLHKSFGDLevLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkdinklrrkvgmVFQq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 75 -----HLpetlhtqSLLQAV-LAPL------PADAREaqrwLAERLLAQMGftpavMEQQT----ATLSGGQHTRLLLAR 138
Cdd:COG1126 86 fnlfpHL-------TVLENVtLAPIkvkkmsKAEAEE----RAMELLERVG-----LADKAdaypAQLSGGQQQRVAIAR 149
|
170
....*....|....
gi 1439757928 139 ALIRQPDLLLLDEP 152
Cdd:COG1126 150 ALAMEPKVMLFDEP 163
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-157 |
6.93e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.38 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETL--- 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 81 H---TQSLLQAV-----LAPLPADAREAQRWLAerlLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK13538 81 HqpgIKTELTALenlrfYQRLHGPGDDEALWEA---LAQVGLA-GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
....*
gi 1439757928 153 GNHLD 157
Cdd:PRK13538 157 FTAID 161
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-158 |
8.43e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR----VEQHLPETL 80
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 81 HTQSLL------QAV-LAPLPADAR-----EAQRWLAERLLAQMGfTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:PRK09536 84 QDTSLSfefdvrQVVeMGRTPHRSRfdtwtETDRAAVERAMERTG-VAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170
....*....|
gi 1439757928 149 LDEPGNHLDL 158
Cdd:PRK09536 163 LDEPTASLDI 172
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
23-157 |
1.00e-15 |
|
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: 76.45 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL-----APTSGSVSLAGQCLMARveQHLPETLHTQ-------------S 84
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDL--DVDVLELRRRvgmvfqkpnpfpgS 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928 85 LLQAVLAPLPA---DAREAQRWLAERLLAQMGFTPAVMEQQTAT-LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03260 97 IYDNVAYGLRLhgiKLKEELDERVEEALRKAALWDEVKDRLHALgLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-157 |
1.02e-15 |
|
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: 75.86 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmARVEQHLPETLH--- 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 82 TQSLLQAVLAPLP------ADAREAQRwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:TIGR01189 80 HLPGLKPELSALEnlhfwaAIHGGAQR-TIEDALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
..
gi 1439757928 156 LD 157
Cdd:TIGR01189 158 LD 159
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-158 |
1.11e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.12 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 3 TLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARVEQH 75
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwspaeLARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 76 LPEtlhtQSLL------QAV----LAPLPADAREAQRwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIR--- 142
Cdd:PRK13548 81 LPQ----HSSLsfpftvEEVvamgRAPHGLSRAEDDA-LVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAQlwe 154
|
170
....*....|....*....
gi 1439757928 143 ---QPDLLLLDEPGNHLDL 158
Cdd:PRK13548 155 pdgPPRWLLLDEPTSALDL 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-157 |
1.47e-15 |
|
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: 75.69 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 20 FNSLSFTLKKGdRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ------HLP------------ETLH 81
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrrigYLPqefgvypnftvrEFLD 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 82 TQSLLQAVlaplpADAREAQRwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03264 95 YIAWLKGI-----PSKEVKAR--VDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-157 |
1.47e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 75.87 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR----------VEQHL---PETLHTQSL-L 86
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREprevrrrigiVFQDLsvdDELTGWENLyI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 87 QAVLAPLPADAReAQRwlAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03265 97 HARLYGVPGAER-RER--IDELLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-152 |
1.56e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 76.02 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 7 AHALHvetafgplfnSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM-----ARVEQ---HLPE 78
Cdd:TIGR03410 13 SHILR----------GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITklpphERARAgiaYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 ------TLHTQSLLQAVLAPLPADAREaqrwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:TIGR03410 83 greifpRLTVEENLLTGLAALPRRSRK----IPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-181 |
1.99e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 75.74 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------MARVEQHLPET 79
Cdd:cd03300 5 NVSKFYGgfVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlpphkrpVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 LHTqSLLQAV-----LAPLPADAREAQrwlAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:cd03300 85 PHL-TVFENIafglrLKKLPKAEIKER---VAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190
....*....|....*....|....*....|.
gi 1439757928 155 HLDLPTLLWLESFLQTWQGS----FVLVSHD 181
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKElgitFVFVTHD 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-157 |
2.00e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 78.96 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAPTSGSVSLAGQCLMA----------------------------RV 72
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGlsrralrplrrrmqvvfqdpfgslsprmTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 73 EQHLPETLHtqsllqaVLAP-LPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:COG4172 382 GQIIAEGLR-------VHGPgLSAAERRAR---VAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
....*.
gi 1439757928 152 PGNHLD 157
Cdd:COG4172 452 PTSALD 457
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-181 |
2.20e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.43 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQC-------LMARV-------EQ---HLP--ETLH 81
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrkeFARRIgvvfgqrSQlwwDLPaiDSFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 82 tqsLLQAVLAPLPADAREAQRWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP--GnhLDLP 159
Cdd:COG4586 119 ---LLKAIYRIPDAEYKKRLDELVELL--DLG---ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPtiG--LDVV 188
|
170 180
....*....|....*....|....*.
gi 1439757928 160 TLLWLESFL----QTWQGSFVLVSHD 181
Cdd:COG4586 189 SKEAIREFLkeynRERGTTILLTSHD 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-157 |
2.35e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 74.27 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlpetlHTQSLLQAVLaplpada 97
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG---------------VPVSDLEKAL------- 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 98 REAQRWLAERLLAqmgFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03247 74 SSLISVLNQRPYL---FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-181 |
3.64e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKST----LLQvldgtLAPTSGSVSLAGQCLMA-RVEQHLPETLHTQSLLQ---AVLAP 92
Cdd:PRK15134 303 KNISFTLRPGETLGLVGESGSGKSTtglaLLR-----LINSQGEIWFDGQPLHNlNRRQLLPVRHRIQVVFQdpnSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 93 ------------------LPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:PRK15134 378 rlnvlqiieeglrvhqptLSAAQREQQ---VIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|.
gi 1439757928 155 HLDLPT----LLWLESFLQTWQGSFVLVSHD 181
Cdd:PRK15134 455 SLDKTVqaqiLALLKSLQQKHQLAYLFISHD 485
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-203 |
3.71e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 78.16 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmARVEQHLPETL--HTQSLLQAV------ 89
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG----ADLKQWDRETFgkHIGYLPQDVelfpgt 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 ----LAPLPADArEAQRWLAERLLAQ---------MGFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:TIGR01842 408 vaenIARFGENA-DPEKIIEAAKLAGvhelilrlpDGYDTVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1439757928 157 DLPTLLWLESFLQTWQ---GSFVLVSHDNTLLDAVtNSSWILRDQTLHSF 203
Cdd:TIGR01842 486 DEEGEQALANAIKALKargITVVVITHRPSLLGCV-DKILVLQDGRIARF 534
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
307-489 |
3.96e-15 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 74.55 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 307 PGQPSLFTTGVA-RLRSGDRVAIMGRNGGGKSSLLRL---LWQQMNNASPLPGL---RLHP---RLHPGYYDQTLAQLpd 376
Cdd:cd03245 13 PNQEIPALDNVSlTIRAGEKVAIIGRVGSGKSTLLKLlagLYKPTSGSVLLDGTdirQLDPadlRRNIGYVPQDVTLF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 377 EASLLEALTPFAPSADTRK--RALIAAGFG--WARH--------SQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNH 444
Cdd:cd03245 91 YGTLRDNITLGAPLADDERilRAAELAGVTdfVNKHpngldlqiGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1439757928 445 LDMEGKAALAQTLRDYPGG--VLLVSHdRQLISESCNRFWLIDSAGL 489
Cdd:cd03245 171 MDMNSEERLKERLRQLLGDktLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-157 |
4.81e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 74.88 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----------CLMARVEQ--HLPET----- 79
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrSQIGLVSQepVLFDGtiaen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 ----LHTQSLLQAVLAPLPADAREAQRWLAERLLAQMGftpavmeQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:cd03249 97 irygKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVG-------ERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
..
gi 1439757928 156 LD 157
Cdd:cd03249 170 LD 171
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-181 |
4.85e-15 |
|
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: 76.69 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmARVEQHLPETLHTQSL----LQAVLAPLPA--- 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL-FDSRKGIFLPPEKRRIgyvfQEARLFPHLSvrg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 -------DAREAQRWLA-ERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT----LLW 163
Cdd:TIGR02142 95 nlrygmkRARPSERRISfERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPY 173
|
170
....*....|....*...
gi 1439757928 164 LESFLQTWQGSFVLVSHD 181
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHS 191
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-157 |
4.89e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.83 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ--------------HLPET-LHTQSLLQAV- 89
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkplrkkvgivfQFPEHqLFEETVEKDIc 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 90 LAPL-----PADAREaqrwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13634 109 FGPMnfgvsEEDAKQ----KAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
21-181 |
5.00e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVsLAGQCLMARVEQHlpetlhTQSLLQ-AVLAP------- 92
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEARED------TRLMFQdARLLPwkkvidn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 93 ----LPADAREAqrwlAERLLAQMGFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFL 168
Cdd:PRK11247 102 vglgLKGQWRDA----ALQALAAVGLADRANEW-PAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLI 176
|
170
....*....|....*..
gi 1439757928 169 QT-WQG---SFVLVSHD 181
Cdd:PRK11247 177 ESlWQQhgfTVLLVTHD 193
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-498 |
5.19e-15 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 74.74 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLH------PRLHPGYYDQTLA---QLPdeASLLE------ 382
Cdd:COG1121 28 TIPPGEFVAIVGPNGAGKSTLLKAI---LGLLPPTSGtVRLFgkpprrARRRIGYVPQRAEvdwDFP--ITVRDvvlmgr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 ----ALTPFAPSADTRK--RALIAAGFgWARHSQKVSTLSGGERSRLLfvglsLARY-----SLLLLDEPTNHLDMEGKA 451
Cdd:COG1121 103 ygrrGLFRRPSRADREAvdEALERVGL-EDLADRPIGELSGGQQQRVL-----LARAlaqdpDLLLLDEPFAGVDAATEE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1439757928 452 ALAQTLRDYPG---GVLLVSHDRQLISESCNRFWLIDSaGLTEWHSLEEV 498
Cdd:COG1121 177 ALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEV 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-470 |
5.31e-15 |
|
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: 74.05 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--------NASPLPGLRLHPRLHPGYYDQTLAqLPDEASLLE------AL 384
Cdd:COG4133 24 TLAAGEALALTGPNGSGKTTLLRILAGLLPpsagevlwNGEPIRDAREDYRRRLAYLGHADG-LKPELTVREnlrfwaAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSADTRKRALiaAGFGWARHSQK-VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYP-- 461
Cdd:COG4133 103 YGLRADREAIDEAL--EAVGLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLar 180
|
170
....*....|
gi 1439757928 462 -GGVLLVSHD 470
Cdd:COG4133 181 gGAVLLTTHQ 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-181 |
8.15e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQS--------LLQAVLAP 92
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSyalfphmtVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 93 LPADaREAQRWLAERLLAQMGFtpaVMEQQTAT-----LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD--LPTLLWLE 165
Cdd:PRK11607 116 LKQD-KLPKAEIASRVNEMLGL---VHMQEFAKrkphqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLE 191
|
170
....*....|....*...
gi 1439757928 166 --SFLQTWQGSFVLVSHD 181
Cdd:PRK11607 192 vvDILERVGVTCVMVTHD 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-157 |
1.27e-14 |
|
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: 72.91 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 5 LTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmARVEQHLPETLHTQS 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQAVLAPLpaDAREAQRWLA--------ERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:cd03231 80 HAPGIKTTL--SVLENLRFWHadhsdeqvEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
.
gi 1439757928 157 D 157
Cdd:cd03231 157 D 157
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
319-475 |
1.60e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLpglrlhprlhpGYYDQTLAQLPDEASLLEALTPfAPSADTRKRAL 398
Cdd:COG2401 52 EIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA-----------GCVDVPDNQFGREASLIDAIGR-KGDFKDAVELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 399 IAAGFG----WARhsqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLD----MEGKAALAQTLRDYPGGVLLVSHD 470
Cdd:COG2401 120 NAVGLSdavlWLR---RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGITLVVATHH 196
|
....*
gi 1439757928 471 RQLIS 475
Cdd:COG2401 197 YDVID 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-157 |
1.65e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLaPTSGSVSLAGQCL----MARVEQHL------PETLHtQSLLQAVLAP 92
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELreldPESWRKHLswvgqnPQLPH-GTLRDNVLLG 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 93 LPaDAREAQRWLAerlLAQMG---FTPA-------VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11174 447 NP-DASDEQLQQA---LENAWvseFLPLlpqgldtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-180 |
1.90e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.08 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA---------------------RVEQHLPETLHT 82
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtppsrrpvsmlfqennlfshlTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 83 QSLLQAvlaplpadareAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTL- 161
Cdd:PRK10771 99 GLKLNA-----------AQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD-PALr 165
|
170 180
....*....|....*....|...
gi 1439757928 162 ----LWLESFLQTWQGSFVLVSH 180
Cdd:PRK10771 166 qemlTLVSQVCQERQLTLLMVSH 188
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-485 |
1.93e-14 |
|
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: 71.27 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG----LRLHPRLHPGYYDQTLAQLPDEASLLEALTPfapsadtrk 395
Cdd:cd03230 23 VEKGEIYGLLGPNGAGKTTLIKII---LGLLKPDSGeikvLGKDIKKEPEEVKRRIGYLPEEPSLYENLTV--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 396 RALIaagfgwarhsqkvsTLSGGERSRLLFVgLSLARY-SLLLLDEPTNHLDMEGKAALAQTLRDY---PGGVLLVSHDR 471
Cdd:cd03230 91 RENL--------------KLSGGMKQRLALA-QALLHDpELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHIL 155
|
170
....*....|....
gi 1439757928 472 QLISESCNRFWLID 485
Cdd:cd03230 156 EEAERLCDRVAILN 169
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
319-485 |
2.07e-14 |
|
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: 72.50 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL------------WQQMN-NASPLPGLRLH-------PRlhpgyyDQTLAQLPDE- 377
Cdd:cd03225 23 TIKKGEFVLIVGPNGSGKSTLLRLLngllgptsgevlVDGKDlTKLSLKELRRKvglvfqnPD------DQFFGPTVEEe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 378 -ASLLEALTpfAPSADTRKRALIAAGFG--WARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALA 454
Cdd:cd03225 97 vAFGLENLG--LPEEEIEERVEEALELVglEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....
gi 1439757928 455 QTLRDYPG---GVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03225 175 ELLKKLKAegkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-152 |
2.20e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 16 FGPLF--NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MAR--------------- 71
Cdd:PRK11300 15 FGGLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqIARmgvvrtfqhvrlfre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 72 --------VEQHlpetLHTQSLLQAVLAPLPAdAREAQRWLAERL---LAQMGFTPaVMEQQTATLSGGQHTRLLLARAL 140
Cdd:PRK11300 95 mtvienllVAQH----QQLKTGLFSGLLKTPA-FRRAESEALDRAatwLERVGLLE-HANRQAGNLAYGQQRRLEIARCM 168
|
170
....*....|..
gi 1439757928 141 IRQPDLLLLDEP 152
Cdd:PRK11300 169 VTQPEILMLDEP 180
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-181 |
2.47e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------MARVEQH-- 75
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpgaeRGVVFQNeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 76 -LPetlhTQSLLQAV-----LAPLPADAREAqrwLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:PRK11248 81 lLP----WRNVQDNVafglqLAGVEKMQRLE---IAHQMLKKVGLEGA-EKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1439757928 150 DEPGNHLDLPTLLWLES-FLQTWQGS---FVLVSHD 181
Cdd:PRK11248 153 DEPFGALDAFTREQMQTlLLKLWQETgkqVLLITHD 188
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-157 |
2.55e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 72.40 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG-------QCLMARVEQH-----LPETLHTQSLLQ-- 87
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepAEARRRLGFVsdstgLYDRLTARENLEyf 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 88 AVLAPLPADAREAQ-RWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03266 103 AGLYGLKGDELTARlEELADRL--GME---ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-181 |
2.57e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.66 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARV-EQHL-------------PET-LHTQSLLQ 87
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIrpvrkrigmvfqfPESqLFEDTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 AVL-AP--LPADAREAQRWlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT---L 161
Cdd:PRK13646 106 EIIfGPknFKMNLDEVKNY-AHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqV 184
|
170 180
....*....|....*....|.
gi 1439757928 162 LWLESFLQTWQG-SFVLVSHD 181
Cdd:PRK13646 185 MRLLKSLQTDENkTIILVSHD 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-152 |
3.03e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.00 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM-ARVEQHLPETLHTQ--------SL------LQA 88
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITgLSGRELRPLRRRMQmvfqdpyaSLnprmtvGDI 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 89 VLAPL----PADAREAQRWLAErLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG4608 118 IAEPLrihgLASKAERRERVAE-LLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
21-152 |
3.51e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.37 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL----M---AR-----------------VEQHL 76
Cdd:COG1137 20 KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpMhkrARlgigylpqeasifrkltVEDNI 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 77 petlhtqsllQAVL--APLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG1137 100 ----------LAVLelRKLSKKEREER---LEELLEEFGITH-LRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-181 |
3.58e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 72.68 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------------MARVEQH---LPEtlht 82
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsrkelrelrrkkISMVFQSfalLPH---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 83 QSLLQAV-----LAPLPADAREAQrwlAERLLAQMGFTPavMEQQTAT-LSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:cd03294 117 RTVLENVafgleVQGVPRAEREER---AAEALELVGLEG--WEHKYPDeLSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190
....*....|....*....|....*....|...
gi 1439757928 157 DlPT--------LLWLESFLQTwqgSFVLVSHD 181
Cdd:cd03294 192 D-PLirremqdeLLRLQAELQK---TIVFITHD 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
23-157 |
3.88e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.95 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------MARVEQ------HLpetlhtqSLLQ 87
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdrnIAMVFQsyalypHM-------TVYE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 88 AVLAPL-----PADAREAQ-RWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG3839 95 NIAFPLklrkvPKAEIDRRvREAAELL--GLE---DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-197 |
3.97e-14 |
|
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: 74.84 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSL-----------AGQCLMARVEQHLpETLHTQ------ 83
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPDGRGRAKRYI-GILHQEydlyph 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 -----SLLQAVLAPLPadaREAQRWLAERLLAQMGFTP----AVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:TIGR03269 380 rtvldNLTEAIGLELP---DELARMKAVITLKMVGFDEekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1439757928 155 HLDLPTLLWL-ESFLQT---WQGSFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:TIGR03269 457 TMDPITKVDVtHSILKAreeMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-186 |
4.64e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.84 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 5 LTAHALHVETAFG-PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAP-TSGSVSL-AGQCLMArveqhLPET-- 79
Cdd:COG4178 363 LALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARpAGARVLF-----LPQRpy 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 LHTQSLLQAVLapLPADAREAQRWLAERLLAQMG---FTPAVMEQQ--TATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:COG4178 437 LPLGTLREALL--YPATAEAFSDAELREALEAVGlghLAERLDEEAdwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|....
gi 1439757928 155 HLDLPTLLWLESFLQT--WQGSFVLVSHDNTLLD 186
Cdd:COG4178 515 ALDEENEAALYQLLREelPGTTVISVGHRSTLAA 548
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-181 |
4.78e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.77 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----MARVE------------QHLpetLHTQSL 85
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssAAKAElrnqklgfiyqfHHL---LPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 86 LQAVLAPL------PADAREAqrwlAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLP 159
Cdd:PRK11629 105 LENVAMPLligkkkPAEINSR----ALEMLAAVGLEHRA-NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180
....*....|....*....|....*.
gi 1439757928 160 T---LLWLESFLQTWQGS-FVLVSHD 181
Cdd:PRK11629 180 NadsIFQLLGELNRLQGTaFLVVTHD 205
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-181 |
5.31e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.07 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA----------------------------RV 72
Cdd:PRK11308 32 DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeaqkllrqkiqivfqnpygslnprkKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 73 EQHLPETLhtqsllqAVLAPLPADAREAQrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK11308 112 GQILEEPL-------LINTSLSAAERREK---ALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190
....*....|....*....|....*....|...
gi 1439757928 153 GNHLDLPT---LLWLESFLQTWQG-SFVLVSHD 181
Cdd:PRK11308 182 VSALDVSVqaqVLNLMMDLQQELGlSYVFISHD 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-157 |
5.86e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------------------------MARVEQHLPE 78
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadknqlrllrtrLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 TLHTQSLLQAVLAPL------PADAREAqrwlAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK10619 104 WSHMTVLENVMEAPIqvlglsKQEARER----AVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
....*
gi 1439757928 153 GNHLD 157
Cdd:PRK10619 180 TSALD 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-180 |
6.30e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 70.98 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQ--------SLLQAV-LAPL 93
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQennlfahlTVEQNVgLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 94 PA-DAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTL------LWLES 166
Cdd:cd03298 97 PGlKLTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALraemldLVLDL 174
|
170
....*....|....
gi 1439757928 167 FLQTwQGSFVLVSH 180
Cdd:cd03298 175 HAET-KMTVLMVTH 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-152 |
6.43e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 72.78 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP---TSGSVSLAGQCLMA--------------------------- 70
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekelrkirgreiqmifqdpmtslnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 71 --RVEQHLPETLHTQsllqavlapLPADAREAQRwLAERLLAQMGFTPA--VMEQ---QtatLSGGQHTRLLLARALIRQ 143
Cdd:COG0444 102 vmTVGDQIAEPLRIH---------GGLSKAEARE-RAIELLERVGLPDPerRLDRyphE---LSGGMRQRVMIARALALE 168
|
....*....
gi 1439757928 144 PDLLLLDEP 152
Cdd:COG0444 169 PKLLIADEP 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
319-485 |
6.54e-14 |
|
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: 71.03 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNAS------PLPGLRLHPRLhpGYYDQTLAQLPD-----EASLLEALTPF 387
Cdd:cd03235 21 EVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSgsirvfGKPLEKERKRI--GYVPQRRSIDRDfpisvRDVVLMGLYGH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 A-----PSADTRKRALIAAGFGWARH--SQKVSTLSGGERSRLLfvglsLARY-----SLLLLDEPTNHLDMEGKAALA- 454
Cdd:cd03235 99 KglfrrLSKADKAKVDEALERVGLSElaDRQIGELSGGQQQRVL-----LARAlvqdpDLLLLDEPFAGVDPKTQEDIYe 173
|
170 180 190
....*....|....*....|....*....|...
gi 1439757928 455 --QTLRDYPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03235 174 llRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-187 |
6.99e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 70.90 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARVEQHLPETLHTQSLL------Q 87
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgraIPYLRRKIGVVFQDFRLLpdrnvyE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 AVLAPLP---ADAREAQRWLAErLLAQMGFTPAVMEqQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPTLLW- 163
Cdd:cd03292 98 NVAFALEvtgVPPREIRKRVPA-ALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD-PDTTWe 174
|
170 180
....*....|....*....|....*....
gi 1439757928 164 ----LESFLQtwQGSFVLVS-HDNTLLDA 187
Cdd:cd03292 175 imnlLKKINK--AGTTVVVAtHAKELVDT 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-152 |
7.73e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 3 TLLTAHALHVetafGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-----VEQ--- 74
Cdd:COG1129 255 VVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsprdaIRAgia 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 75 HLPETLHTQSLLQ-------AVLAPLPADAR------EAQRWLAERLLAQMGFTPAVMEQQTATLSGG--QhtRLLLARA 139
Cdd:COG1129 331 YVPEDRKGEGLVLdlsirenITLASLDRLSRgglldrRRERALAEEYIKRLRIKTPSPEQPVGNLSGGnqQ--KVVLAKW 408
|
170
....*....|...
gi 1439757928 140 LIRQPDLLLLDEP 152
Cdd:COG1129 409 LATDPKVLILDEP 421
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
319-485 |
8.69e-14 |
|
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: 69.77 E-value: 8.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGLRLhprlhpgYYDQTLAQL-PDEASLLEALTPfapsadtrkRA 397
Cdd:cd03214 21 SIEAGEIVGILGPNGAGKSTLLKTL---AGLLKPSSGEIL-------LDGKDLASLsPKELARKIAYVP---------QA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 398 LIAAGFGWARHsQKVSTLSGGERSRLLfvglsLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDYPG----GVLLVS 468
Cdd:cd03214 82 LELLGLAHLAD-RPFNELSGGERQRVL-----LARAlaqepPILLLDEPTSHLDIAHQIELLELLRRLARergkTVVMVL 155
|
170
....*....|....*..
gi 1439757928 469 HDRQLISESCNRFWLID 485
Cdd:cd03214 156 HDLNLAARYADRVILLK 172
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
320-443 |
9.38e-14 |
|
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: 68.83 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQQM---------NNASPLPGLRLHPRLHPGYYDQTLAQLPDEA---SLLEALTPF 387
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLsptegtillDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTvreNLRLGLLLK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 388 APSADTRKR----ALIAAGFGWARH---SQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTN 443
Cdd:pfam00005 88 GLSKREKDAraeeALEKLGLGDLADrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-157 |
1.00e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.06 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH---LPE--------TLHTQSLLQAV 89
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigyLPEerglypkmKVGEQLVYLAR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 90 LAPLP-ADARE-AQRWLaERLlaqmgftpAVMEQQTA---TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4152 98 LKGLSkAEAKRrADEWL-ERL--------GLGDRANKkveELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
296-480 |
1.17e-13 |
|
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: 69.17 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 296 LEMDTLHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRL---LWQQMNNASPLPGLRLHpRLHPGYYDQTLA 372
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLilgLLRPTSGRVRLDGADIS-QWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 373 QLPDEASLLealtpfapsADTrkralIAAgfgwarhsqkvSTLSGGERSRllfVGLSLARY---SLLLLDEPTNHLDMEG 449
Cdd:cd03246 80 YLPQDDELF---------SGS-----IAE-----------NILSGGQRQR---LGLARALYgnpRILVLDEPNSHLDVEG 131
|
170 180 190
....*....|....*....|....*....|....
gi 1439757928 450 KAALAQTLRDYPGG---VLLVSHDRQLIsESCNR 480
Cdd:cd03246 132 ERALNQAIAALKAAgatRIVIAHRPETL-ASADR 164
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-157 |
1.22e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.58 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQHlPETlhtqsll 86
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseetvwdvrrqVGMVFQN-PDN------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 QAVLAPLPADA----------REAqrwLAERL---LAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:PRK13635 93 QFVGATVQDDVafglenigvpREE---MVERVdqaLRQVGMED-FLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
....
gi 1439757928 154 NHLD 157
Cdd:PRK13635 169 SMLD 172
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-157 |
1.23e-13 |
|
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: 70.90 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETlhtQSLLQAVLAPLPADAREAQRWLA 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADY---EGTVRDLLSSITKDFYTHPYFKT 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 106 ErLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03237 98 E-IAKPLQIEQ-ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-157 |
1.37e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 73.28 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQ-------------S 84
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV----DIRDLTLESLRRQigvvpqdtflfsgT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQAV-LAPLPAD-------AREAQrwlAERLLAQMgftP----AVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG1132 430 IRENIrYGRPDATdeeveeaAKAAQ---AHEFIEAL---PdgydTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
....*
gi 1439757928 153 GNHLD 157
Cdd:COG1132 504 TSALD 508
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-197 |
1.65e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 5 LTAHALHVETAFGPLfnslSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAPTSGSVSLAGQCL-------MARVEQHLP 77
Cdd:COG4138 1 LQLNDVAVAGRLGPI----SAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLsdwsaaeLARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 78 EtlhtQSLLQAVL---------APLPADAREAQRWLAErLLAQMGFTPAVMeQQTATLSGGQHTRLLLARALIR------ 142
Cdd:COG4138 76 Q----QQSPPFAMpvfqylalhQPAGASSEAVEQLLAQ-LAEALGLEDKLS-RPLTQLSGGEWQRVRLAAVLLQvwptin 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 143 -QPDLLLLDEPGNHLD----LPTLLWLESFLQTwQGSFVLVSHD--NTLLDAvtNSSWILRD 197
Cdd:COG4138 150 pEGQLLLLDEPMNSLDvaqqAALDRLLRELCQQ-GITVVMSSHDlnHTLRHA--DRVWLLKQ 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-502 |
1.83e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.09 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASP-----------LPGLRLHPRLHPGYydqtlaqLPDEASLLEALTP-- 386
Cdd:COG1131 23 VEPGEIFGLLGPNGAGKTTTIRML---LGLLRPtsgevrvlgedVARDPAEVRRRIGY-------VPQEPALYPDLTVre 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 387 ----FA-----PSADTRKRA--LIAAgFG-WARHSQKVSTLSGGERSRLlfvGLSLA---RYSLLLLDEPTNHLDMEGKA 451
Cdd:COG1131 93 nlrfFArlyglPRKEARERIdeLLEL-FGlTDAADRKVGTLSGGMKQRL---GLALAllhDPELLILDEPTSGLDPEARR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 452 ALAQTLRDYPGG---VLLVSHDRQLISESCNRFWLIDS---------AGLTEwHSLEEVYARL 502
Cdd:COG1131 169 ELWELLRELAAEgktVLLSTHYLEEAERLCDRVAIIDKgrivadgtpDELKA-RLLEDVFLEL 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
23-183 |
1.93e-13 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 69.59 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------MARVEQHLPETLHtQSLLQAVLAPL 93
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdrdIAMVFQNYALYPH-MTVYDNIAFGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 94 ------PADAREAQRWLAERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD----LPTLLW 163
Cdd:cd03301 98 klrkvpKDEIDERVREVAELL--QIE---HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAE 172
|
170 180
....*....|....*....|
gi 1439757928 164 LESFLQTWQGSFVLVSHDNT 183
Cdd:cd03301 173 LKRLQQRLGTTTIYVTHDQV 192
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
21-181 |
2.17e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.90 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLP-ETLHTQSLLQA-VLAP------ 92
Cdd:PRK09452 31 SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPaENRHVNTVFQSyALFPhmtvfe 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 93 ----------LPADarEAQRWLAERL----LAQMGftpavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD- 157
Cdd:PRK09452 106 nvafglrmqkTPAA--EITPRVMEALrmvqLEEFA------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDy 177
|
170 180
....*....|....*....|....*..
gi 1439757928 158 -LPTLLWLE-SFLQTWQG-SFVLVSHD 181
Cdd:PRK09452 178 kLRKQMQNElKALQRKLGiTFVFVTHD 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-181 |
2.24e-13 |
|
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: 71.67 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM---ARV--------------EQHLPETLHTQSLL 86
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsaRGIflpphrrrigyvfqEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 QAVLAPLPADAREAQRwlaERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT----LL 162
Cdd:COG4148 99 LYGRKRAPRAERRISF---DEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeiLP 174
|
170
....*....|....*....
gi 1439757928 163 WLESFLQTWQGSFVLVSHD 181
Cdd:COG4148 175 YLERLRDELDIPILYVSHS 193
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-198 |
2.40e-13 |
|
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: 69.67 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---------MARVEQ------HLPETLHTQSLL 86
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItnlppekrdISYVPQnyalfpHMTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 QAVLAPLPADAREAqRWLAERLlaqmGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLES 166
Cdd:cd03299 97 KKRKVDKKEIERKV-LEIAEML----GID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1439757928 167 FLQTWQGSF---VL-VSHDntLLDAvtnssWILRDQ 198
Cdd:cd03299 171 ELKKIRKEFgvtVLhVTHD--FEEA-----WALADK 199
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
319-480 |
2.46e-13 |
|
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: 72.94 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHP--------------RLHPGYYDQTLAQLPDEA-----S 379
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLL------------LGLYEptsgrilidgidlrQIDPASLRRQIGVVLQDVflfsgT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 380 LLEALTPFAPSADTRK--RALIAAGF---------GWARH-SQKVSTLSGGERSRLLfvglsLAR--Y---SLLLLDEPT 442
Cdd:COG2274 565 IRENITLGDPDATDEEiiEAARLAGLhdfiealpmGYDTVvGEGGSNLSGGQRQRLA-----IARalLrnpRILILDEAT 639
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1439757928 443 NHLDMEGKAALAQTLRDYPGG--VLLVSHDRQLIsESCNR 480
Cdd:COG2274 640 SALDAETEAIILENLRRLLKGrtVIIIAHRLSTI-RLADR 678
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-157 |
2.58e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG------------QCLMAR-----VEQ--HL-PE 78
Cdd:COG4161 18 LFD-INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpsekAIRLLRqkvgmVFQqyNLwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 TLHTQSLLQA---VLAPLPADAREAqrwlAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNH 155
Cdd:COG4161 97 LTVMENLIEApckVLGLSKEQAREK----AMKLLARLRLTDKA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
..
gi 1439757928 156 LD 157
Cdd:COG4161 172 LD 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-157 |
2.67e-13 |
|
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: 69.68 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR---------VEQHLPET 79
Cdd:cd03296 7 NVSKRFGdfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVpvqernvgfVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 LHtQSLLQAV--------LAPLPADAREAQR-----------WLAERLLAQmgftpavmeqqtatLSGGQHTRLLLARAL 140
Cdd:cd03296 87 RH-MTVFDNVafglrvkpRSERPPEAEIRAKvhellklvqldWLADRYPAQ--------------LSGGQRQRVALARAL 151
|
170
....*....|....*..
gi 1439757928 141 IRQPDLLLLDEPGNHLD 157
Cdd:cd03296 152 AVEPKVLLLDEPFGALD 168
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-157 |
3.46e-13 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 69.77 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqcLMARVEQHLPETLHTQSLL------QAVLA 91
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKKVGMVfqnpdnQFVGA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 92 PLPAD----------AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:TIGR04520 94 TVEDDvafglenlgvPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-151 |
3.69e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----------CLMARVEQHlP---------- 77
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeykraKYIGRVFQD-Pmmgtapsmti 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 78 -ETL-------HTQSLLQAVLAplpadareAQRWLAERLLAQMGF-TPAVMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:COG1101 100 eENLalayrrgKRRGLRRGLTK--------KRRELFRELLATLGLgLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLL 171
|
...
gi 1439757928 149 LDE 151
Cdd:COG1101 172 LDE 174
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-180 |
3.97e-13 |
|
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: 69.04 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE---------TLHTQSLLQA 88
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSkvslvgqepVLFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 89 VLAPLPADARE-----AQRWLAERLLAQM--GFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL 161
Cdd:cd03248 108 IAYGLQSCSFEcvkeaAQKAHAHSFISELasGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180
....*....|....*....|.
gi 1439757928 162 LWLESFLQTW--QGSFVLVSH 180
Cdd:cd03248 187 QQVQQALYDWpeRRTVLVIAH 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-157 |
4.24e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 71.70 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmARVEQHLPETL--HTQSLLQAV------ 89
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG----ADLSQWDREELgrHIGYLPQDVelfdgt 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 ----LAPLP-ADARE----AQRWLAERLLAQM--GF-TPavMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4618 422 iaenIARFGdADPEKvvaaAKLAGVHEMILRLpdGYdTR--IGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-181 |
4.32e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLH-TQSLLQAVLAPL------ 93
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSdIQMIFQDPLASLnprmti 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 94 ------------PADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL 161
Cdd:PRK15079 118 geiiaeplrtyhPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180
....*....|....*....|....
gi 1439757928 162 LWLESFLQTWQG----SFVLVSHD 181
Cdd:PRK15079 198 AQVVNLLQQLQRemglSLIFIAHD 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-152 |
4.54e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 67.84 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 3 TLLTAHALHVETAFGPLfnslSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARveqhlpetlHT 82
Cdd:cd03215 3 PVLEVRGLSVKGAVRDV----SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR---------SP 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 83 QSLLQAVLAPLPADAREaqrwlaERLLAQMGftpaVMEQQTAT--LSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:cd03215 70 RDAIRAGIAYVPEDRKR------EGLVLDLS----VAENIALSslLSGGNQQKVVLARWLARDPRVLILDEP 131
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-157 |
4.55e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.88 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 2 STLLTAHALHVETAFGP-LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------------ 68
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmklre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 69 -MARVEQHLPETLHTQSLLQ-----AVLAPLPADarEAQRWLaERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIR 142
Cdd:PRK13636 83 sVGMVFQDPDNQLFSASVYQdvsfgAVNLKLPED--EVRKRV-DNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170
....*....|....*
gi 1439757928 143 QPDLLLLDEPGNHLD 157
Cdd:PRK13636 159 EPKVLVLDEPTAGLD 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-152 |
4.62e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmarvEQHLPETLHTQSL-LQAV---LAPLP----A 95
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE------PVRFRSPRDAQAAgIAIIhqeLNLVPnlsvA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 96 D----AREAQRW----------LAERLLAQMGFT--PavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG1129 98 EniflGREPRRGglidwramrrRARELLARLGLDidP---DTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-152 |
5.20e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR----------------------VEQHLpeTLH 81
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGdiatrrrvgymsqafslygeltVRQNL--ELH 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 82 tqsllqAVLAPLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF033858 364 ------ARLFHLPAAEIAAR---VAEMLERFDLAD-VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
319-485 |
5.80e-13 |
|
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: 68.73 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGLRL----HPRLHPGYYDQTLAQLPDEASLLEALTP------FA 388
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRML---AGLLKPDSGSILidgeDVRKEPREARRQIGVLPDERGLYDRLTVreniryFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 PSADTRKRALIAA--------GFGWARHsQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQ---TL 457
Cdd:COG4555 100 ELYGLFDEELKKRieeliellGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREilrAL 178
|
170 180
....*....|....*....|....*...
gi 1439757928 458 RDYPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:COG4555 179 KKEGKTVLFSSHIMQEVEALCDRVVILH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
295-532 |
5.93e-13 |
|
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: 71.09 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 295 LLEMDTLHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqmNNASPLPG------------LRLHPRL 362
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL----MGLLPHGGrisgevlldgrdLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 363 HPGYYDQTLAQLPD--------EASLLEALTPFAPSADTRKR----ALIAAGFGwARHSQKVSTLSGGERSRLLFVGLSL 430
Cdd:COG1123 80 LRGRRIGMVFQDPMtqlnpvtvGDQIAEALENLGLSRAEARArvleLLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 431 ARYSLLLLDEPTNHLDMEGKAALAQTL----RDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQAVA 506
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLrelqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
250 260
....*....|....*....|....*.
gi 1439757928 507 PAPDSRLALQSTPAGADDDEEALLAR 532
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPLLEVR 264
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-152 |
5.98e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 68.34 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLPetLHTQSLL-------------- 86
Cdd:cd03218 17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-----TKLP--MHKRARLgigylpqeasifrk 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 87 ----QAVLAPLP--ADAREAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:cd03218 90 ltveENILAVLEirGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-499 |
6.19e-13 |
|
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: 68.92 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHPRLHpG--YYD-------------QTLAQLPDEASLLEA 383
Cdd:COG1120 23 SLPPGEVTALLGPNGSGKSTLLRAL------------AGLLKPSS-GevLLDgrdlaslsrrelaRRIAYVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 384 LT--------------PFA-PSADTRK---RALIAAGFGWARHsQKVSTLSGGERSRLLfvglsLARY-----SLLLLDE 440
Cdd:COG1120 90 LTvrelvalgryphlgLFGrPSAEDREaveEALERTGLEHLAD-RPVDELSGGERQRVL-----IARAlaqepPLLLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 441 PTNHLDMEGKAALAQTLRDY----PGGVLLVSHDRQLISESCNRFWLID-----SAG-----LTEwHSLEEVY 499
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKdgrivAQGppeevLTP-ELLEEVY 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-184 |
8.01e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.27 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 27 LKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH-----------------LPETLHTQSLLQaV 89
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvgfvfqsfmLIPTLNALENVE-L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 LAPLPADAREAQRWLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT------LLW 163
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiadLLF 190
|
170 180
....*....|....*....|.
gi 1439757928 164 leSFLQTWQGSFVLVSHDNTL 184
Cdd:PRK10584 191 --SLNREHGTTLILVTHDLQL 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
319-485 |
8.67e-13 |
|
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: 66.64 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpglrlhprlhPGYYDqtlaqlPDEASLL---EALTPFAPSADTRK 395
Cdd:cd03228 24 TIKPGEKVAIVGPSGSGKSTLLKLL--------------------LRLYD------PTSGEILidgVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 396 RALIaagfgwarhSQKV----ST-----LSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDYP 461
Cdd:cd03228 78 IAYV---------PQDPflfsGTireniLSGGQRQRI-----AIARAllrdpPILILDEATSALDPETEALILEALRALA 143
|
170 180
....*....|....*....|....*.
gi 1439757928 462 GG--VLLVSHDRQLIsESCNRFWLID 485
Cdd:cd03228 144 KGktVIVIAHRLSTI-RDADRIIVLD 168
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-157 |
1.56e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------------------MARVEQHL-PE 78
Cdd:PRK11124 18 LFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsdkairelrrnvgMVFQQYNLwPH 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 79 TLHTQSLLQAVLAPLPADAREAQRwLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11124 97 LTVQQNLIEAPCRVLGLSKDQALA-RAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-157 |
1.67e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.85 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE--TLHTQS--LLQAVL--- 90
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQaiSVVSQRvhLFSATLrdn 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 91 ----APLPADAReaqrwLAErLLAQMGFTpAVMEQQTA----------TLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:PRK11160 434 lllaAPNASDEA-----LIE-VLQQVGLE-KLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
.
gi 1439757928 157 D 157
Cdd:PRK11160 507 D 507
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-157 |
1.69e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 66.91 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL---APTSGSVSLAGQCL--------MARVEQH---LPETLHTQS 84
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRkpdqfqkcVAYVRQDdilLPGLTVRET 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 85 LLQAVLAPLP---ADAREAQRWlAERLLAQMGFTPA---VMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03234 102 LTYTAILRLPrksSDAIRKKRV-EDVLLRDLALTRIggnLVKG----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
319-490 |
1.73e-12 |
|
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: 66.51 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwQQMNNASP----LPGLRLHP--RLHPGYYdqtLAQLPD----EASLLEALTPFA 388
Cdd:cd03226 22 DLYAGEIIALTGKNGAGKTTLAKIL-AGLIKESSgsilLNGKPIKAkeRRKSIGY---VMQDVDyqlfTDSVREELLLGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 PSAD---TRKRALIAAGFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG--- 462
Cdd:cd03226 98 KELDagnEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgk 177
|
170 180
....*....|....*....|....*...
gi 1439757928 463 GVLLVSHDRQLISESCNRFWLIDSAGLT 490
Cdd:cd03226 178 AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-187 |
1.94e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVETAFG--------PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL--APTSGSVSLagqclma 70
Cdd:COG2401 19 SVLDLSERVAIVLEAFGvelrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 71 rVEQHLPETLhtqSLLQAVLAPLPADAreaqrwlAERLLAQMGFTPAV-MEQQTATLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:COG2401 92 -PDNQFGREA---SLIDAIGRKGDFKD-------AVELLNAVGLSDAVlWLRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1439757928 150 DEPGNHLDLPTL----LWLESFLQTWQGSFVLVSHDNTLLDA 187
Cdd:COG2401 161 DEFCSHLDRQTAkrvaRNLQKLARRAGITLVVATHHYDVIDD 202
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
319-469 |
1.99e-12 |
|
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: 65.25 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRL---LWQqmnnasplpglrlhprlhpgYYDQTLAQLPDEASLLEALTPFAPSAdTRK 395
Cdd:cd03223 23 EIKPGDRLLITGPSGTGKSSLFRAlagLWP--------------------WGSGRIGMPEGEDLLFLPQRPYLPLG-TLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 396 RALIaagFGWARhsqkvsTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSH 469
Cdd:cd03223 82 EQLI---YPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-157 |
2.34e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmARVEQHLPETLHTQSLLQAVLAPLP--- 94
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEACHYLGHRNAMKPALTvae 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 95 -----ADAREAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13539 93 nlefwAAFLGGEELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-202 |
2.65e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLaPTSGSVSLAGQCL-------MARV-----EQHLPETL----HTQSL 85
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLeawsaaeLARHraylsQQQTPPFAmpvfQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 86 LQAVLAPLpADAREAQRWLAERLLAQMgftpaVMEQQTATLSGGQHTRLLLArALIRQ--PD------LLLLDEPGNHLD 157
Cdd:PRK03695 93 HQPDKTRT-EAVASALNEVAEALGLDD-----KLGRSVNQLSGGEWQRVRLA-AVVLQvwPDinpagqLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1439757928 158 LPTLLWLESFLQTW--QGSFVLVS-HD--NTLLDAvtNSSWILRDQTLHS 202
Cdd:PRK03695 166 VAQQAALDRLLSELcqQGIAVVMSsHDlnHTLRHA--DRVWLLKQGKLLA 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-157 |
3.07e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLlqa 88
Cdd:PRK11432 11 NITKRFGSntVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSY--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 89 VLAP----------------LPADAREAQRWLAERLLAQMGFTPAVMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK11432 88 ALFPhmslgenvgyglkmlgVPKEERKQRVKEALELVDLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEP 163
|
....*
gi 1439757928 153 GNHLD 157
Cdd:PRK11432 164 LSNLD 168
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-157 |
3.07e-12 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 66.49 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG--------QCL---MARVEQhlpET-LHTQSL 85
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlASLrrqIGLVSQ---DVfLFNDTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 86 LQAVLAPLPaDAREAQRWLAERLLAQMGF---TP----AVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03251 93 AENIAYGRP-GATREEVEEAARAANAHEFimeLPegydTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-195 |
3.08e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.45 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarVEQHLPETLHTQSLL------QAVLA 91
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRHKIGMVfqnpdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 92 PLPAD----------AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD---- 157
Cdd:PRK13650 98 TVEDDvafglenkgiPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegr 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1439757928 158 LPTLLWLESFLQTWQGSFVLVSHDntlLDAVTNSSWIL 195
Cdd:PRK13650 177 LELIKTIKGIRDDYQMTVISITHD---LDEVALSDRVL 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-157 |
3.61e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 2 STLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA----RVEQHLP 77
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpeIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 78 ETLHTQSLL-----QAVLAP--LPADAREAQRWLAErlLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLD 150
Cdd:PRK10247 85 YCAQTPTLFgdtvyDNLIFPwqIRNQQPDPAIFLDD--LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
....*..
gi 1439757928 151 EPGNHLD 157
Cdd:PRK10247 163 EITSALD 169
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-157 |
4.34e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.14 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH------LPE---- 78
Cdd:PRK13537 12 NVEKRYGDklVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArqrvgvVPQfdnl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 ----TLHTQSLLQAVLAPLPA-DAREAQRWLAE--RLLAQmgftpavMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK13537 92 dpdfTVRENLLVFGRYFGLSAaAARALVPPLLEfaKLENK-------ADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
....*.
gi 1439757928 152 PGNHLD 157
Cdd:PRK13537 165 PTTGLD 170
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-194 |
5.54e-12 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 67.13 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 35 LIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQSLLQA-VLAPLPADAREAQRWLAERLLAQMG 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE----DVTNVPPHLRHINMVFQSyALFPHMTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 114 FTPAVME------------QQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD--LPTLLWLEsfLQTWQG----SF 175
Cdd:TIGR01187 77 IKPRVLEalrlvqleefadRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQMQLE--LKTIQEqlgiTF 154
|
170
....*....|....*....
gi 1439757928 176 VLVSHDNTllDAVTNSSWI 194
Cdd:TIGR01187 155 VFVTHDQE--EAMTMSDRI 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
312-492 |
5.94e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.27 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 312 LFTTGVARLRSGDRVAIMGRNGGGKSSLLRLL----------------WQ-----QMNNASPLPGLRlhprlhpgYY--- 367
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadggsytfpgnWQlawvnQETPALPQPALE--------YVidg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 368 DQTLAQLpdEASLLEA--------LTPFAPSADT------RKRA---LIAAGFGWARHSQKVSTLSGGERSRLLFVGLSL 430
Cdd:PRK10636 88 DREYRQL--EAQLHDAnerndghaIATIHGKLDAidawtiRSRAaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 431 ARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEW 492
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-152 |
7.46e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMarveqhlpeTLHTQSLLQAVLAPLPADAREAQR 102
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---------DWQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 103 WLAERLLAQMGFT-----------------PAVME---QQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK11614 95 MTVEENLAMGGFFaerdqfqerikwvyelfPRLHErriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-157 |
7.51e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 65.59 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLlTAHALHVET---AFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH 75
Cdd:COG4598 1 MTDT-APPALEVRDlhkSFGDLevLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 76 LP---------ETLHTQ--------------SLLQAVL-APL------PADAREAqrwlAERLLAQMGFtPAVMEQQTAT 125
Cdd:COG4598 80 GElvpadrrqlQRIRTRlgmvfqsfnlwshmTVLENVIeAPVhvlgrpKAEAIER----AEALLAKVGL-ADKRDAYPAH 154
|
170 180 190
....*....|....*....|....*....|..
gi 1439757928 126 LSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-157 |
8.44e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.78 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 12 VETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlpetlhtqsllqav 89
Cdd:PRK13536 47 VSKSYGdkAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG------------------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 lAPLPADAREAQRWLA---------------ERLLAQMGF-----------TPAVME---------QQTATLSGGQHTRL 134
Cdd:PRK13536 103 -VPVPARARLARARIGvvpqfdnldleftvrENLLVFGRYfgmstreieavIPSLLEfarleskadARVSDLSGGMKRRL 181
|
170 180
....*....|....*....|...
gi 1439757928 135 LLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLD 204
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-156 |
8.81e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 64.41 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclMARVEQ---HLPETLHtqsllQAVLAPLP 94
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQepwIQNGTIR-----ENILFGKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 95 ADareaQRWLaERLLAQMGFTP--AVMEQ--QT------ATLSGGQHTRLLLARALIRQPDLLLLDEP--------GNHL 156
Cdd:cd03250 92 FD----EERY-EKVIKACALEPdlEILPDgdLTeigekgINLSGGQKQRISLARAVYSDADIYLLDDPlsavdahvGRHI 166
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-158 |
9.00e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL--------APTSGSVSLAGQCL------- 68
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLaaidapr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 69 MARVEQHLPETLHTQ---SLLQAVLAPLPADAREA------QRWLAERLLAQMGFTPAVMEQQTaTLSGGQHTRLLLARA 139
Cdd:PRK13547 81 LARLRAVLPQAAQPAfafSAREIVLLGRYPHARRAgalthrDGEIAWQALALAGATALVGRDVT-TLSGGELARVQFARV 159
|
170 180
....*....|....*....|....*...
gi 1439757928 140 L---------IRQPDLLLLDEPGNHLDL 158
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-181 |
9.60e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALhvETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV---------------SL 63
Cdd:PRK11701 3 DQPLLSVRGL--TKLYGPRkgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqlrdlyalSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 64 AGQCLMAR-----VEQHLPETLHTQ--------SLLQAVLAPLPADARE-AQRWLAERLLAqmgftPAVMEQQTATLSGG 129
Cdd:PRK11701 81 AERRRLLRtewgfVHQHPRDGLRMQvsaggnigERLMAVGARHYGDIRAtAGDWLERVEID-----AARIDDLPTTFSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 130 QHTRLLLARALIRQPDLLLLDEPGNHLDLPT----LLWLESFLQTWQGSFVLVSHD 181
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHD 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
291-473 |
9.66e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 291 PADRLLEMDTLHVSPAPGQPsLFTTGVARLRSGDRVAIMGRNGGGKSSLLRL---LWqqmNNAS-----PlPGLRL---- 358
Cdd:COG4178 358 SEDGALALEDLTLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAiagLW---PYGSgriarP-AGARVlflp 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 359 -HPRLHPG------YYDQTLAQLPDEA--SLLEA--LTPFAPSADTRKRaliaagfgWARhsqkvsTLSGGERSRLLFVG 427
Cdd:COG4178 433 qRPYLPLGtlrealLYPATAEAFSDAElrEALEAvgLGHLAERLDEEAD--------WDQ------VLSLGEQQRLAFAR 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 428 LSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVS----------HDRQL 473
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISvghrstlaafHDRVL 554
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-180 |
1.03e-11 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 64.50 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQHLPETLHTQSLLQAVLAP 92
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHtglapyqrpvsMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 93 -LPADAREAQRwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD----LPTLLWLESF 167
Cdd:TIGR01277 98 gLKLNAEQQEK--VVDAAQQVGIAD-YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLALVKQL 174
|
170
....*....|...
gi 1439757928 168 LQTWQGSFVLVSH 180
Cdd:TIGR01277 175 CSERQRTLLMVTH 187
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-160 |
1.03e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 65.65 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-CLMARVEQHLPETLHtqsllQAVLAPLPAD 96
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFSWIMPGTIK-----ENIIFGVSYD 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 97 AREAQR-----WLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:cd03291 126 EYRYKSvvkacQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-476 |
1.37e-11 |
|
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: 64.16 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 321 RSGDRVAIMGRNGGGKSSLLRLL-------------WQQ--MNNASPLPglrlhpRL-----HPGYYDQTLAQlpdEASL 380
Cdd:cd03268 24 KKGEIYGFLGPNGAGKTTTMKIIlglikpdsgeitfDGKsyQKNIEALR------RIgalieAPGFYPNLTAR---ENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 381 LEALTPFAPSADTrKRALIAAGFGWARHsQKVSTLSGGERSRLlfvGLSLA---RYSLLLLDEPTNHLDMEGKAALAQTL 457
Cdd:cd03268 95 LLARLLGIRKKRI-DEVLDVVGLKDSAK-KKVKGFSLGMKQRL---GIALAllgNPDLLILDEPTNGLDPDGIKELRELI 169
|
170 180
....*....|....*....|..
gi 1439757928 458 RDYP---GGVLLVSHdrqLISE 476
Cdd:cd03268 170 LSLRdqgITVLISSH---LLSE 188
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-201 |
1.74e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.56 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAP-TSGSVSLAGQCLMARVEQH--LPETlhtqSLLQAVLAPlp 94
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIGMPEGEDLLFLPQRpyLPLG----TLREQLIYP-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 95 adareaqrWlaerllaqmgftpavmeqqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGS 174
Cdd:cd03223 88 --------W-------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGIT 140
|
170 180
....*....|....*....|....*..
gi 1439757928 175 FVLVSHDNTLldavtnssWILRDQTLH 201
Cdd:cd03223 141 VISVGHRPSL--------WKFHDRVLD 159
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-157 |
1.98e-11 |
|
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: 63.34 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP--TSGSVSLAGQ--------CLMARVEQHlpETLHTQSllq 87
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrKIIGYVPQD--DILHPTL--- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 avlaplpaDAREAqrwlaerllaqMGFTpAVMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03213 98 --------TVRET-----------LMFA-AKLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-171 |
2.34e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQ-------------- 83
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV----PLVQYDHHYLHRQvalvgqepvlfsgs 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 -------SLLQAVLAPLPADAREAQrwlAERLLAQM--GFTPAVMEQQTaTLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:TIGR00958 571 vreniayGLTDTPDEEIMAAAKAAN---AHDFIMEFpnGYDTEVGEKGS-QLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170
....*....|....*..
gi 1439757928 155 HLDLPTllwlESFLQTW 171
Cdd:TIGR00958 647 ALDAEC----EQLLQES 659
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
296-501 |
2.55e-11 |
|
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: 66.32 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 296 LEMDTLHVSPAPGQPSLftTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--------NASPLPGLRL-------- 358
Cdd:COG4988 337 IELEDVSFSYPGGRPAL--DGLsLTIPPGERVALVGPSGAGKSTLLNLLLGFLPpysgsiliNGVDLSDLDPaswrrqia 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 359 ----HPRLHPGyydqtlaqlpdeaSLLEALTPFAPSADTR--KRALIAAGF---------GWARH-SQKVSTLSGGERSR 422
Cdd:COG4988 415 wvpqNPYLFAG-------------TIRENLRLGRPDASDEelEAALEAAGLdefvaalpdGLDTPlGEGGRGLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 423 LlfvglSLAR-----YSLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSHDRQLISEsCNRFWLIDSAGLTEWHSL 495
Cdd:COG4988 482 L-----ALARallrdAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
....*.
gi 1439757928 496 EEVYAR 501
Cdd:COG4988 556 EELLAK 561
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-469 |
3.33e-11 |
|
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: 63.57 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnNAsplpglRLHP---------------------RLHPGYYDQTLAQ-LPD 376
Cdd:COG1119 25 TVKPGEHWAILGPNGAGKSTLLSLI-----TG------DLPPtygndvrlfgerrggedvwelRKRIGLVSPALQLrFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 377 EASLLEA-LTPF--------APSADTRKRAL-IAAGFGWARHSQK-VSTLSGGERSRLLfvglsLARY-----SLLLLDE 440
Cdd:COG1119 94 DETVLDVvLSGFfdsiglyrEPTDEQRERAReLLELLGLAHLADRpFGTLSQGEQRRVL-----IARAlvkdpELLILDE 168
|
170 180 190
....*....|....*....|....*....|...
gi 1439757928 441 PTNHLDMEGKAALAQTLRDYPGG----VLLVSH 469
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEgaptLVLVTH 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-181 |
4.00e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclmaRVEQHLPETLHTQSLLQAVLAPLPADAREAQ 101
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE----HIQHYASKEVARRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 102 --------------RWLAE------RLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLP-- 159
Cdd:PRK10253 101 lvargryphqplftRWRKEdeeavtKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShq 179
|
170 180
....*....|....*....|....
gi 1439757928 160 -TLLWLESFLQTWQG-SFVLVSHD 181
Cdd:PRK10253 180 iDLLELLSELNREKGyTLAAVLHD 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-187 |
4.31e-11 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 63.01 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTqsLLQAVLApLPADARE--- 99
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV--VLQDTFL-FSGTIMEnir 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 100 -----AQRWLAERLLAQMGFTPAVM----------EQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:cd03254 99 lgrpnATDEEVIEAAKEAGAHDFIMklpngydtvlGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLI 178
|
170 180
....*....|....*....|....*.
gi 1439757928 165 ESFLQTWQG---SFVLVSHDNTLLDA 187
Cdd:cd03254 179 QEALEKLMKgrtSIIIAHRLSTIKNA 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-157 |
4.35e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 63.27 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG--------QCLMARVEQHLPE-TLHTQSLLQAVLAPL 93
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpAWLRRQVGVVLQEnVLFNRSIRDNIALAD 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 94 PADARE-----AQRWLAERLLAQM--GFTPAVMEQqTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:cd03252 101 PGMSMErvieaAKLAGAHDFISELpeGYDTIVGEQ-GAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-160 |
4.49e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.09 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-CLMARVEQHLPETLHtqsllQAVLAPLPAD 96
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTSWIMPGTIK-----DNIIFGLSYD 514
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 97 A-REAQRWLAERLLAQMGFTP----AVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:TIGR01271 515 EyRYTSVIKACQLEEDIALFPekdkTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
323-492 |
4.91e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRLLWQ-------QMNNASPLPGLRLH---PRLHPG-YYDQTLAQLPDEASLLEA------LT 385
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGevllddgRIIYEQDLIVARLQqdpPRNVEGtVYDFVAEGIEEQAEYLKRyhdishLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 PFAPSADTRKR-----ALIAAGFGWARHSQ--------------KVSTLSGGERSRllfVGLSLARYS---LLLLDEPTN 443
Cdd:PRK11147 109 ETDPSEKNLNElaklqEQLDHHNLWQLENRinevlaqlgldpdaALSSLSGGWLRK---AALGRALVSnpdVLLLDEPTN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1439757928 444 HLDMEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEW 492
Cdd:PRK11147 186 HLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSY 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-157 |
4.92e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.56 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ--------CLMAR-----VEQHLPETLHTQSLLQ 87
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksLLEVRktvgiVFQNPDDQLFAPTVEE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928 88 AV-LAP----LPADarEAQRWLAERLLA--QMGFTpavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13639 99 DVaFGPlnlgLSKE--EVEKRVKEALKAvgMEGFE----NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-157 |
5.01e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA------GQCLMA----RVEQHL---PETLHTQSLLQAVLAP 92
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPdydgTVEDLLrsiTDDLGSSYYKSEIIKP 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 93 LpadareaqrwLAERLlaqmgftpavMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13409 441 L----------QLERL----------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-157 |
5.32e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.47 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG------------QCLMARVEQHlPETLHTQSL 85
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgiRKLVGIVFQN-PETQFVGRT 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 86 LQAVLAPLPAD---AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13644 95 VEEDLAFGPENlclPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-158 |
5.60e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 22 SLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQHLPETLHT-QSLLQAV 89
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyrsqrIRMIFQDPSTSLNPrQRISQIL 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 90 LAPL------PADAREAQRWLAERllaQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDL 158
Cdd:PRK15112 111 DFPLrlntdlEPEQREKQIIETLR---QVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-181 |
6.05e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.33 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG--PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ---CLMAR------VEQHLPET 79
Cdd:PRK10851 7 NIKKSFGrtQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsRLHARdrkvgfVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 LHtQSLLQAV---LAPLPADAR---EAQRWLAERLLaQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:PRK10851 87 RH-MTVFDNIafgLTVLPRRERpnaAAIKAKVTQLL-EMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190
....*....|....*....|....*....|..
gi 1439757928 154 NHLDLPTLL----WLESFLQTWQGSFVLVSHD 181
Cdd:PRK10851 165 GALDAQVRKelrrWLRQLHEELKFTSVFVTHD 196
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
286-474 |
6.38e-11 |
|
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: 65.00 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 286 QGDALPAD-RLLEMDTLHVS-----PAPGQPSLfttgvaRLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--------NAS 351
Cdd:TIGR02857 311 KAPVTAAPaSSLEFSGVSVAypgrrPALRPVSF------TVPPGERVALVGPSGAGKSTLLNLLLGFVDptegsiavNGV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 352 PLPGLRLHprlhpGYYDQT--LAQLPD--EASLLEAL---TPFAPSADTRkRALIAAGF---------GWARHSQKVST- 414
Cdd:TIGR02857 385 PLADADAD-----SWRDQIawVPQHPFlfAGTIAENIrlaRPDASDAEIR-EALERAGLdefvaalpqGLDTPIGEGGAg 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928 415 LSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSHDRQLI 474
Cdd:TIGR02857 459 LSGGQAQRL-----ALARAflrdaPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALA 520
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-157 |
7.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.14 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-------------VEQHlPETLHTQSLLQ 87
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvklsdirkkvglVFQY-PEYQLFEETIE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 88 AVLAPLPADAREAQRWLAERLLAQM---GFTPAVMEQQTA-TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRAMnivGLDYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-474 |
8.66e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclMARVEQHLPET-LHT--QSL----LQAVLAP-----L 93
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS--WDEVLKRFRGTeLQNyfKKLyngeIKVVHKPqyvdlI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 94 P-------------ADAREAQRWLAERLlaqmGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:PRK13409 173 PkvfkgkvrellkkVDERGKLDEVVERL----GLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 161 LLWLESFLQTW-QGSFVL-VSHDNTLLDAVTNSSWILrdqtlhsfalpcsaarqalqeQDESAALrhkaeqkeiDRVSas 238
Cdd:PRK13409 248 RLNVARLIRELaEGKYVLvVEHDLAVLDYLADNVHIA---------------------YGEPGAY---------GVVS-- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 239 aRRLATwgRVYDNEDLA--RKAKQMekqvaRLKDEQTELSVGPPWRLVlqgdalPADRLLEMD---------TLHVSPap 307
Cdd:PRK13409 296 -KPKGV--RVGINEYLKgyLPEENM-----RIRPEPIEFEERPPRDES------ERETLVEYPdltkklgdfSLEVEG-- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 308 GQpslfttgvarLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--NASPLPGLRLHPRlhPGY----YDQTLAQLpdeaslL 381
Cdd:PRK13409 360 GE----------IYEGEVIGIVGPNGIGKTTFAKLLAGVLKpdEGEVDPELKISYK--PQYikpdYDGTVEDL------L 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 382 EALTPfaPSADTRKRALIAAGFGWAR-HSQKVSTLSGGERSRLLfVGLSLARYS-LLLLDEPTNHLDMEGKAALAQTLRD 459
Cdd:PRK13409 422 RSITD--DLGSSYYKSEIIKPLQLERlLDKNVKDLSGGELQRVA-IAACLSRDAdLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
490
....*....|....*....
gi 1439757928 460 Y----PGGVLLVSHDRQLI 474
Cdd:PRK13409 499 IaeerEATALVVDHDIYMI 517
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-157 |
1.09e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLA------GQclmaRVEQHLPETLhtQSLLQAVLAPLPADAre 99
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQ----YISPDYDGTV--EEFLRSANTDDFGSS-- 433
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 100 aqrWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG1245 434 ---YYKTEIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
286-501 |
1.29e-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: 64.02 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 286 QGDALPADRLLEMDTLHVS-PAPGQPSLftTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHPrLH 363
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRyPGAGRPVL--DGLsLTLPPGERVAIVGPSGSGKSTLLALL------------LRFLD-PQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 364 PGYY---DQTLAQLPDE-----------------ASLLEALTPFAPSADTRK--RALIAAGFG-WARHSQK-----V--- 412
Cdd:COG4987 389 SGSItlgGVDLRDLDEDdlrrriavvpqrphlfdTTLRENLRLARPDATDEElwAALERVGLGdWLAALPDgldtwLgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 413 -STLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSHDRQLIsESCNRFWLIDSAGL 489
Cdd:COG4987 469 gRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGL-ERMDRILVLEDGRI 547
|
250
....*....|..
gi 1439757928 490 TEWHSLEEVYAR 501
Cdd:COG4987 548 VEQGTHEELLAQ 559
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-219 |
1.30e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.09 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLL----------- 86
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLfqsgalftdmn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 --QAVLAPLpadaREAQRWLAERL-------LAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP---GN 154
Cdd:PRK11831 101 vfDNVAYPL----REHTQLPAPLLhstvmmkLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPfvgQD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 155 HLDLPTLLWLESFLQTWQG-SFVLVSHDNTLLDAVTNSSWILRDQTLHSFALPcsaarQALQEQDE 219
Cdd:PRK11831 176 PITMGVLVKLISELNSALGvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA-----QALQANPD 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-160 |
1.36e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 61.36 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLPetLHTqslLQAVLAPLPADA 97
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI-----SKIG--LHD---LRSRISIIPQDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 98 -------R----------EAQRW-------LAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:cd03244 88 vlfsgtiRsnldpfgeysDEELWqalervgLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
....*..
gi 1439757928 154 NHLDLPT 160
Cdd:cd03244 168 ASVDPET 174
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-160 |
1.39e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 63.99 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFG---PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQcLMARVEQH--------LPET 79
Cdd:TIGR01193 478 DVSYSYGygsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF-SLKDIDRHtlrqfinyLPQE 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 --LHTQSLLQAVLAPLPADAREAQRWLAERLLA--------QMGFTPAVMEQQTaTLSGGQHTRLLLARALIRQPDLLLL 149
Cdd:TIGR01193 557 pyIFSGSILENLLLGAKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGS-SISGGQKQRIALARALLTDSKVLIL 635
|
170
....*....|.
gi 1439757928 150 DEPGNHLDLPT 160
Cdd:TIGR01193 636 DESTSNLDTIT 646
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
319-469 |
1.40e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.84 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMN--------NASPLPGLRLHPRLHPGYYDQtLAQLPDEASLLEALTPFAPS 390
Cdd:TIGR01189 22 TLNAGEALQVTGPNGIGKTTLLRILAGLLRpdsgevrwNGTPLAEQRDEPHENILYLGH-LPGLKPELSALENLHFWAAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 391 ADTRKR----ALIAAGFGWARHSqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY---PGG 463
Cdd:TIGR01189 101 HGGAQRtiedALAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGI 179
|
....*.
gi 1439757928 464 VLLVSH 469
Cdd:TIGR01189 180 VLLTTH 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
286-470 |
1.40e-10 |
|
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: 63.92 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 286 QGDALPADRLLEMDTLHVSPAPGQPSLftTGV-ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGLRLHPRLHP 364
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVL--DGVsLDLPPGERVAILGPSGSGKSTLLATL---AGLLDPLQGEVTLDGVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 365 GYYDQT--------LAQLPD--EASLLEALTPFAPSADTRK--RALIAAGFG-WARH-----SQKV----STLSGGERSR 422
Cdd:TIGR02868 400 SSLDQDevrrrvsvCAQDAHlfDTTVRENLRLARPDATDEElwAALERVGLAdWLRAlpdglDTVLgeggARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1439757928 423 LLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSHD 470
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHH 529
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-158 |
1.46e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARVEQHLPETL-----HTQSLL 86
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskaFARKVAYLPQQLpaaegMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 87 QAV--------LAPLPADAREAqrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDL 158
Cdd:PRK10575 106 VAIgrypwhgaLGRFGAADREK----VEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-157 |
1.56e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.12 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGS---VSLAGQCLMAR-----------VEQHlPETlhtq 83
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKtvwdirekvgiVFQN-PDN---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 sllQAVLAPLPADA----------REAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:PRK13640 96 ---QFVGATVGDDVafglenravpRPEMIKIVRDVLADVGMLD-YIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
....
gi 1439757928 154 NHLD 157
Cdd:PRK13640 172 SMLD 175
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-157 |
1.67e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.69 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV-----------SLAGQ-CLMARVEQHLPETL-------H 81
Cdd:PRK11264 20 HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarSLSQQkGLIRQLRQHVGFVFqnfnlfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 82 TQSLLQAVLAPL--PADAREAQRWLAERLLAQMGFTpavmEQQTA---TLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:PRK11264 100 RTVLENIIEGPVivKGEPKEEATARARELLAKVGLA----GKETSyprRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
.
gi 1439757928 157 D 157
Cdd:PRK11264 176 D 176
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-160 |
1.76e-10 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 61.48 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveqhlpeTLHTQSLLQAVLAPLPAD- 96
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----------REVTLDSLRRAIGVVPQDt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 97 -----------------AREAQRWLAERlLAQMGFTPAVMEQQTAT--------LSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:cd03253 85 vlfndtigynirygrpdATDEEVIEAAK-AAQIHDKIMRFPDGYDTivgerglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
....*....
gi 1439757928 152 PGNHLDLPT 160
Cdd:cd03253 164 ATSALDTHT 172
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-157 |
1.83e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQclMARVEQHlpETLHTQSLLQAVLAPLPADA 97
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQ--AWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 98 REAQRWL-AERLLAQMGFTPA----VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:TIGR00957 728 KYYQQVLeACALLPDLEILPSgdrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
24-157 |
2.03e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.40 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM---------AR-----VEQH--LpetLHTQSLLQ 87
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalserelraARrkigmIFQHfnL---LSSRTVAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 AVLAPL-----PADAREAQrwlAERLLAQMGFT------PAvmeQqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:COG1135 102 NVALPLeiagvPKAEIRKR---VAELLELVGLSdkadayPS---Q----LSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
.
gi 1439757928 157 D 157
Cdd:COG1135 172 D 172
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-161 |
2.31e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.88 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 12 VETAFGP--LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-------------VEQHL 76
Cdd:PRK09493 7 VSKHFGPtqVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvderlirqeagmVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 77 PETLHTQSLLQAVLAPLP--ADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:PRK09493 87 YLFPHLTALENVMFGPLRvrGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
....*..
gi 1439757928 155 HLDlPTL 161
Cdd:PRK09493 166 ALD-PEL 171
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-217 |
2.80e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------------MARVEQHlPETLHTQS 84
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllalrqqVATVFQD-PEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQAVLAPLPADAREAQRWLAERLLAQMGFTPA--VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLL 162
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAqhFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 163 WLESFLQ--TWQGSFVLV-SHDNTLLDAVTNSSWILRDQTLHSFALPCSA-ARQALQEQ 217
Cdd:PRK13638 174 QMIAIIRriVAQGNHVIIsSHDIDLIYEISDAVYVLRQGQILTHGAPGEVfACTEAMEQ 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-152 |
3.81e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ---------CLMARV-----EQHL-PETLHTQSLLqa 88
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaALAAGVaiiyqELHLvPEMTVAENLY-- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 89 vLAPLPA-----DAREAQRWLAERlLAQMG--FTPavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK11288 102 -LGQLPHkggivNRRLLNYEAREQ-LEHLGvdIDP---DTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-180 |
4.77e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 35 LIGHNGCGKSTLLQVLDGTL-----APTSGSVSLAGQC--------LMARVEQ--HLPETLHTQSLLQAV-----LAPLP 94
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDifkmdvieLRRRVQMvfQIPNPIPNLSIFENValglkLNRLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 95 ADAREAQ---RWLAERllAQM-GFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLES-FLQ 169
Cdd:PRK14247 114 KSKKELQervRWALEK--AQLwDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESlFLE 191
|
170
....*....|..
gi 1439757928 170 TWQG-SFVLVSH 180
Cdd:PRK14247 192 LKKDmTIVLVTH 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-157 |
4.80e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.43 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQC--------LMARVEQH----------LPETLHTQS 84
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldadaLAQLRREHfgfifqryhlLSHLTAAQN 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 85 L-LQAVLAPLPADAREAQrwlAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK10535 107 VeVPAVYAGLERKQRLLR---AQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-152 |
4.93e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 10 LHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARveqhlpetlHTQSLLQAV 89
Cdd:PRK10762 258 LKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR---------SPQDGLANG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 LAPLPAD-----------AREAQRWLAERLLAQMGF---------------------TPAvMEQQTATLSGGQHTRLLLA 137
Cdd:PRK10762 329 IVYISEDrkrdglvlgmsVKENMSLTALRYFSRAGGslkhadeqqavsdfirlfnikTPS-MEQAIGLLSGGNQQKVAIA 407
|
170
....*....|....*
gi 1439757928 138 RALIRQPDLLLLDEP 152
Cdd:PRK10762 408 RGLMTRPKVLILDEP 422
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-502 |
5.83e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.74 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGT--LAPTSGSV----------------SLAGQ----C------------- 67
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvCggtlepeevdfwn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 68 --------LMARVEQHLPETL---HTQSLLQAVLAPLPADAREAQRWL--AERLLAQMGFTPAVMeQQTATLSGGQHTRL 134
Cdd:TIGR03269 99 lsdklrrrIRKRIAIMLQRTFalyGDDTVLDNVLEALEEIGYEGKEAVgrAVDLIEMVQLSHRIT-HIARDLSGGEKQRV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 135 LLARALIRQPDLLLLDEPGNHLDLPTllwlesflqtwqgsfVLVSHdNTLLDAVTNS--SWILrdqTLHsfaLPcsaarQ 212
Cdd:TIGR03269 178 VLARQLAKEPFLFLADEPTGTLDPQT---------------AKLVH-NALEEAVKASgiSMVL---TSH---WP-----E 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 213 ALQEQDESAALRHKAEQKEI---DRVSasarrlatwgrvydnedlarkAKQMEkQVARLKDEqtelsvgppwRLVLQGDa 289
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEgtpDEVV---------------------AVFME-GVSEVEKE----------CEVEVGE- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 290 lPADRLLEMDTLHVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLL------------------WQQMNNAS 351
Cdd:TIGR03269 278 -PIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsgevnvrvgdeWVDMTKPG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 352 PLPGLRLHPRLhpGYYDQTLAQLPDEA---SLLEALTPFAPSADTRKRALI---AAGFG--WARH--SQKVSTLSGGERS 421
Cdd:TIGR03269 357 PDGRGRAKRYI--GILHQEYDLYPHRTvldNLTEAIGLELPDELARMKAVItlkMVGFDeeKAEEilDKYPDELSEGERH 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 422 RLLFVGLSLARYSLLLLDEPTNHLD-----------MEGKAALAQTLrdypggvLLVSHDRQLISESCNRFWLIDSAGLT 490
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDpitkvdvthsiLKAREEMEQTF-------IIVSHDMDFVLDVCDRAALMRDGKIV 507
|
570
....*....|..
gi 1439757928 491 EWHSLEEVYARL 502
Cdd:TIGR03269 508 KIGDPEEIVEEL 519
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
319-504 |
6.51e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLlwqqmnnasplpglrlhprlhpgyydqtLAQL--PDE---------ASLLEALTPF 387
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKL----------------------------IAGIlePTSgrvevngrvSALLELGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 APS------------------ADTRKR-ALIA--AGFGWARHsQKVSTLSGGERSRLLFvGLSLA-RYSLLLLDEptnhl 445
Cdd:COG1134 100 HPEltgreniylngrllglsrKEIDEKfDEIVefAELGDFID-QPVKTYSSGMRARLAF-AVATAvDPDILLVDE----- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 446 dmegkaALA--------------QTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQA 504
Cdd:COG1134 173 ------VLAvgdaafqkkclariRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEA 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-189 |
6.98e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPETLHTQSLLQAVLAPLPAD------- 96
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDvvmmgry 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 97 --------AREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFL 168
Cdd:PRK15056 107 ghmgwlrrAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
170 180
....*....|....*....|...
gi 1439757928 169 QTW--QGSFVLVSHDNtlLDAVT 189
Cdd:PRK15056 186 RELrdEGKTMLVSTHN--LGSVT 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-474 |
7.29e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.72 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 26 TLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPT-----------------SGS---------------VSLAGQclmaRVE 73
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTelqdyfkklangeikVAHKPQ----YVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 74 QhLPETLH--TQSLLQAVlaplpaDAREAQRWLAERLlaqmGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:COG1245 171 L-IPKVFKgtVRELLEKV------DERGKLDELAEKL----GLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 152 PGNHLDLPTLLWLESFLQTWQG---SFVLVSHDNTLLDAVTNSSWILrdqtlhsfalpcsaarqalqeQDESAALrhkae 228
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEegkYVLVVEHDLAILDYLADYVHIL---------------------YGEPGVY----- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 229 qkeiDRVSasaRRLATwgRVYDNEDLA--RKAKQMekqvaRLKDEQTELSVGPPwrlvlqGDALPADRLLEMDTLHVSPa 306
Cdd:COG1245 293 ----GVVS---KPKSV--RVGINQYLDgyLPEENV-----RIRDEPIEFEVHAP------RREKEEETLVEYPDLTKSY- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 307 pGQPSLFTTGvARLRSGDRVAIMGRNGGGKSSLLRLLW--QQMNNASPLPGLRLHPRlhPGY----YDQTLAQLpdeasL 380
Cdd:COG1245 352 -GGFSLEVEG-GEIREGEVLGIVGPNGIGKTTFAKILAgvLKPDEGEVDEDLKISYK--PQYispdYDGTVEEF-----L 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 381 LEALTPFAPSadTRKRALIAAGFGWAR-HSQKVSTLSGGERSRLLfVGLSLARYS-LLLLDEPTNHLDMEGKAALAQTLR 458
Cdd:COG1245 423 RSANTDDFGS--SYYKTEIIKPLGLEKlLDKNVKDLSGGELQRVA-IAACLSRDAdLYLLDEPSAHLDVEQRLAVAKAIR 499
|
490 500
....*....|....*....|
gi 1439757928 459 DYPGG----VLLVSHDRQLI 474
Cdd:COG1245 500 RFAENrgktAMVVDHDIYLI 519
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
321-458 |
7.93e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 58.72 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 321 RSGDRVAIMGRNGGGKSSLLRLLWQQMN----------NASPLPglRLHPRLHPGYYDQtlaqlpdEASLLEALTPfaps 390
Cdd:cd03213 33 KPGELTAIMGPSGAGKSTLLNALAGRRTglgvsgevliNGRPLD--KRSFRKIIGYVPQ-------DDILHPTLTV---- 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 391 adtrKRALiaagfgwaRHSQKVSTLSGGERSRLLfVGLSL-ARYSLLLLDEPTNHLDMEGKAALAQTLR 458
Cdd:cd03213 100 ----RETL--------MFAAKLRGLSGGERKRVS-IALELvSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
318-476 |
8.06e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.40 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 318 ARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPGYYDQTLA---QLPDEASLLEALTPFAP---- 389
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVL---AGVLRPTSGtVRRAGGARVAYVPQRSEvpdSLPLTVRDLVAMGRWARrglw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 390 ---SADTRK---RALIAAGFGWARHSQkVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG- 462
Cdd:NF040873 90 rrlTRDDRAavdDALERVGLADLAGRQ-LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAr 168
|
170
....*....|....*.
gi 1439757928 463 --GVLLVSHDRQLISE 476
Cdd:NF040873 169 gaTVVVVTHDLELVRR 184
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
15-151 |
8.63e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 15 AFGPLfnslSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL----MARVEQHLPETLHTQSLLQAVL 90
Cdd:PRK10522 338 SVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaeqPEDYRKLFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 91 AP--LPADAREAQRWLaERLlaQMGFTPAVMEQQTAT--LSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK10522 414 GPegKPANPALVEKWL-ERL--KMAHKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
319-480 |
9.42e-10 |
|
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: 59.06 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNAS--------PLPGLRLHPRLHPGYYDQTLAQLPDEA---------SLL 381
Cdd:cd03257 27 SIKKGETLGLVGESGSGKSTLARAILGLLKPTSgsiifdgkDLLKLSRRLRKIRRKEIQMVFQDPMSSlnprmtigeQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 382 EALT----PFAPSADTRKRALIAAGFGWARH--SQKVSTLSGGERSRLLFVgLSLA-RYSLLLLDEPTNHLDMEGKAALA 454
Cdd:cd03257 107 EPLRihgkLSKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVAIA-RALAlNPKLLIADEPTSALDVSVQAQIL 185
|
170 180 190
....*....|....*....|....*....|
gi 1439757928 455 QTLRD----YPGGVLLVSHDRQLISESCNR 480
Cdd:cd03257 186 DLLKKlqeeLGLTLLFITHDLGVVAKIADR 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
302-474 |
1.21e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 302 HVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPG-LRLHPRLHPGYYDQTL---AQLPDE 377
Cdd:PRK09544 9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV---LGLVAPDEGvIKRNGKLRIGYVPQKLyldTTLPLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 378 ASLLEALTPFAPSADTrkraLIAAGFGWARH--SQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAAL-- 453
Cdd:PRK09544 86 VNRFLRLRPGTKKEDI----LPALKRVQAGHliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALyd 161
|
170 180
....*....|....*....|...
gi 1439757928 454 --AQTLRDYPGGVLLVSHDRQLI 474
Cdd:PRK09544 162 liDQLRRELDCAVLMVSHDLHLV 184
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-158 |
1.43e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.94 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-------MARV------EQHLPETL---------- 80
Cdd:COG4604 21 SLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsreLAKRlailrqENHINSRLtvrelvafgr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 81 --HTQSLLQAvlaplpADAReaqrwLAERLLAQMGFTPavMEQQTA-TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4604 101 fpYSKGRLTA------EDRE-----IIDEAIAYLDLED--LADRYLdELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
.
gi 1439757928 158 L 158
Cdd:COG4604 168 M 168
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
36-181 |
1.58e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.03 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 36 IGHNGCGKSTLLQVLDGT--LAPT---SGSVSLAGQCLMAR-------------VEQH---LPETLHTQSLLQAVLAPLP 94
Cdd:PRK14243 42 IGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPdvdpvevrrrigmVFQKpnpFPKSIYDNIAYGARINGYK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 95 ADAREaqrwLAERLLAQMGFTPAV---MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTW 171
Cdd:PRK14243 122 GDMDE----LVERSLRQAALWDEVkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL 197
|
170
....*....|..
gi 1439757928 172 --QGSFVLVSHD 181
Cdd:PRK14243 198 keQYTIIIVTHN 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-181 |
1.75e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 34 GLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----MARVEQ-----------HLPETLHTQSLLQAVLAPLPA-- 95
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdIFQIDAiklrkevgmvfQQPNPFPHLSIYDNIAYPLKShg 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 --DAREAQRwLAERLLAQMGFTPAV---MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQT 170
Cdd:PRK14246 120 ikEKREIKK-IVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170
....*....|...
gi 1439757928 171 WQG--SFVLVSHD 181
Cdd:PRK14246 199 LKNeiAIVIVSHN 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-152 |
2.23e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 10 LHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMA-----RVEQ---HLPE--- 78
Cdd:PRK15439 269 LTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqRLARglvYLPEdrq 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 79 ----------TLHTQSLLQAVLAPLPADAREAQRWlaERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:PRK15439 349 ssglyldaplAWNVCALTHNRRGFWIKPARENAVL--ERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
....
gi 1439757928 149 LDEP 152
Cdd:PRK15439 427 VDEP 430
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
17-151 |
2.74e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.81 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 17 GPLfnslSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-MARVEQHlpetlhtQSLLQAVLA---- 91
Cdd:COG4615 349 GPI----DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAY-------RQLFSAVFSdfhl 417
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 92 -------PLPADAREAQRWLaERLlaQMGFTPAVMEQQTAT--LSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:COG4615 418 fdrllglDGEADPARARELL-ERL--ELDHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-188 |
3.01e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.15 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 10 LHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDG--TLAPTSGSVSLAGQclmarveqhlpetlhtqSLLQ 87
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE-----------------DITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 avlapLPADAReaqrwlaerllAQMGFT-----PAVMEQQT---------ATLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:cd03217 69 -----LPPEER-----------ARLGIFlafqyPPEIPGVKnadflryvnEGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 1439757928 154 NHLDLPTLLWLESFLQTWQG---SFVLVSHDNTLLDAV 188
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYI 170
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-157 |
3.43e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 59.31 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVetAFG------PLFNSLSFTLKKGDRIGLIGHNGCGKS----TLLQVLDGTLAPTSGSVSLAGQCLMA 70
Cdd:COG4172 3 SMPLLSVEDLSV--AFGqgggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 71 RVEQHL--------------PET----LHT--QSLLQAVLAPLPADAREAQRWLAErLLAQMGFTPAvmEQQTAT----L 126
Cdd:COG4172 81 LSERELrrirgnriamifqePMTslnpLHTigKQIAEVLRLHRGLSGAAARARALE-LLERVGIPDP--ERRLDAyphqL 157
|
170 180 190
....*....|....*....|....*....|.
gi 1439757928 127 SGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-157 |
6.37e-09 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 58.57 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG--------QCL---MARVEQHLpeTLHTQSLL 86
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlASLrrqVALVSQDV--VLFNDTIA 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 87 QAVLAPLPADAREAQRWLAERLLAQMGFTPAVME-------QQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
320-485 |
6.72e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 56.39 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpglrlhprlhPGYYdqtlaqLPDE---------ASLLEALTPFAPS 390
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLL--------------------AGIY------PPDSgtvtvrgrvSSLLGLGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 391 ADTRKRA-LIAAGFGWARHS-------------------QKVSTLSGGERSRLLFvGLSLA-RYSLLLLDEPTNHLD--- 446
Cdd:cd03220 99 LTGRENIyLNGRLLGLSRKEidekideiiefselgdfidLPVKTYSSGMKARLAF-AIATAlEPDILLIDEVLAVGDaaf 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1439757928 447 MEGKAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLE 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
319-486 |
6.88e-09 |
|
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: 56.29 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRL---LWQQMN-----NASPLPGLRLHPRLHPGyydqtLAQLPDEASLLEALTP---F 387
Cdd:cd03224 22 TVPEGEIVALLGRNGAGKTTLLKTimgLLPPRSgsirfDGRDITGLPPHERARAG-----IGYVPEGRRIFPELTVeenL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 APSADTRKRALIAAGFGWA---------RHSQKVSTLSGGERsRLLFVGLSL-ARYSLLLLDEPTnhldmEGKA------ 451
Cdd:cd03224 97 LLGAYARRRAKRKARLERVyelfprlkeRRKQLAGTLSGGEQ-QMLAIARALmSRPKLLLLDEPS-----EGLApkivee 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1439757928 452 --ALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDS 486
Cdd:cd03224 171 ifEAIRELRDEGVTILLVEQNARFALEIADRAYVLER 207
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
319-477 |
7.15e-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: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLW--------------QQMNNASP--LPGLRlhpRLHPGYYDQTLAQLPDeASLLE 382
Cdd:cd03255 26 SIEKGEFVAIVGPSGSGKSTLLNILGgldrptsgevrvdgTDISKLSEkeLAAFR---RRHIGFVFQSFNLLPD-LTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 -ALTPF----APSADTRKRA---LIAAGFGwARHSQKVSTLSGGERSRllfvgLSLARY-----SLLLLDEPTNHLDMEG 449
Cdd:cd03255 102 nVELPLllagVPKKERRERAeelLERVGLG-DRLNHYPSELSGGQQQR-----VAIARAlandpKIILADEPTGNLDSET 175
|
170 180 190
....*....|....*....|....*....|..
gi 1439757928 450 KAALAQTLRD----YPGGVLLVSHDRQLISES 477
Cdd:cd03255 176 GKEVMELLRElnkeAGTTIVVVTHDPELAEYA 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-163 |
7.30e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ------HLPE--------TLHTQ 83
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDvhqnmgYCPQfdaiddllTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 SLLQAVLAPLPADAREAqrwLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT--L 161
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEK---VANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQArrM 2108
|
..
gi 1439757928 162 LW 163
Cdd:TIGR01257 2109 LW 2110
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-152 |
7.86e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGdRI-GLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL------MAR------VEQH--LPETLhtqSLLQA 88
Cdd:COG3845 25 SLTVRPG-EIhALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsprDAIalgigmVHQHfmLVPNL---TVAEN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 89 V---LAPLPA---DAREAQRWLAErLLAQMGFT--PavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:COG3845 101 IvlgLEPTKGgrlDRKAARARIRE-LSERYGLDvdP---DAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-157 |
8.11e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.50 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPET-------------LHTQSLLQAVL 90
Cdd:PRK11153 25 SLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqigmifqhfnlLSSRTVFDNVA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 91 APLPA---DAREAQRWLAErLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11153 105 LPLELagtPKAEIKARVTE-LLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-158 |
8.13e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQClMARVEQ--------H 75
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRsrfmaylgH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 76 LPETLHTQSLLQAVLAPLPADAREAQRWLAERL--LAQMGFTPAVMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEPG 153
Cdd:PRK13543 90 LPGLKADLSTLENLHFLCGLHGRRAKQMPGSALaiVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....*
gi 1439757928 154 NHLDL 158
Cdd:PRK13543 166 ANLDL 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-152 |
8.18e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLM----ARVEQ-- 74
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpAKAHQlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 75 -----HLPETLHTQSLLQAVLAPLPADAREAQRwlAERLLAQMG--FTPAVmeqQTATLSGGQHTRLLLARALIRQPDLL 147
Cdd:PRK15439 88 iylvpQEPLLFPNLSVKENILFGLPKRQASMQK--MKQLLAALGcqLDLDS---SAGSLEVADRQIVEILRGLMRDSRIL 162
|
....*
gi 1439757928 148 LLDEP 152
Cdd:PRK15439 163 ILDEP 167
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-203 |
9.52e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 29 KGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlPETLHTQSLLQAVLAPLPADAREaqrwlaerl 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------GEDILEEVLDQLLLIIVGGKKAS--------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 109 laqmgftpavmeqqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSFVLVSHDNTLLDAV 188
Cdd:smart00382 61 -----------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
170
....*....|....*
gi 1439757928 189 TNSSWILRDQTLHSF 203
Cdd:smart00382 124 NDEKDLGPALLRRRF 138
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-197 |
1.11e-08 |
|
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: 57.53 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTL--APTSGSVSLAGQCLMAR------------VEQ 74
Cdd:TIGR02633 6 GIVKTFGGVkaLDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASnirdteragiviIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 75 HL---PET-------LHTQSLLQAVLAPLPADAREAQRWLAERLLAQMGFTPAVMEqqtatLSGGQHTRLLLARALIRQP 144
Cdd:TIGR02633 86 ELtlvPELsvaenifLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-----YGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 145 DLLLLDEPGNHL---DLPTLLWLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRD 197
Cdd:TIGR02633 161 RLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-157 |
1.32e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---MARVEQHL---PE---TLHTQSLLQA 88
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnLDAVRQSLgmcPQhniLFHHLTVAEH 1023
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 89 VL--APLPADAREAQRWLAERLLAQMGFTPAVMEqQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:TIGR01257 1024 ILfyAQLKGRSWEEAQLEMEAMLEDTGLHHKRNE-EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-459 |
1.62e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLR-----------------LLWQQMNNASPLPGLRLHPRLHPGYYDQTLaQLPDEASLLE 382
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRhlsglitgdksagshieLLGRTVQREGRLARDIRKSRANTGYIFQQF-NLVNRLSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 AL-------TP--------FAPSADTRK-RALIAAGFGWARHsQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLD 446
Cdd:PRK09984 106 NVligalgsTPfwrtcfswFTREQKQRAlQALTRVGMVHFAH-QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
170
....*....|...
gi 1439757928 447 MEGKAALAQTLRD 459
Cdd:PRK09984 185 PESARIVMDTLRD 197
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
323-485 |
1.71e-08 |
|
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: 55.59 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRLL---WQQMNNASPLPGLRLH--PRLHPGYYDQTLAQLPDEASLLEAL-------TPF--- 387
Cdd:TIGR03873 27 GSLTGLLGPNGSGKSTLLRLLagaLRPDAGTVDLAGVDLHglSRRARARRVALVEQDSDTAVPLTVRdvvalgrIPHrsl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 ----APSADTRKRALIAAGFGWARHSQKVSTLSGGERSRLlFVGLSLA-RYSLLLLDEPTNHLDMEGKAALAQTLRDYPG 462
Cdd:TIGR03873 107 wagdSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRV-HVARALAqEPKLLLLDEPTNHLDVRAQLETLALVRELAA 185
|
170 180
....*....|....*....|....*.
gi 1439757928 463 G---VLLVSHDRQLISESCNRFWLID 485
Cdd:TIGR03873 186 TgvtVVAALHDLNLAASYCDHVVVLD 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-157 |
1.76e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.91 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL----MARVEQHL------PETLHTQSLLQAVL 90
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLRKHIgivfqnPDNQFVGSIVKYDV 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 91 A------PLPADarEAQRWLAErLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13648 106 AfglenhAVPYD--EMHRRVSE-ALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-157 |
1.77e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.90 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL----------PETLHTQSLLQAVLAP 92
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdPDDQVFSSTVWDDVAF 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 93 LPADAREAQRWLAERL---LAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13647 104 GPVNMGLDKDEVERRVeeaLKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-65 |
2.29e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.38 E-value: 2.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 14 TAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG 65
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG 70
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
313-470 |
2.39e-08 |
|
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: 54.61 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 313 FTTGVARLRSGDRVAIMGRNGGGKSSLLRLL-----------------WQQMNNASPLPglrLHPRlHPGYYDQTLAQLP 375
Cdd:cd03297 13 FTLKIDFDLNEEVTGIFGASGAGKSTLLRCIaglekpdggtivlngtvLFDSRKKINLP---PQQR-KIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 376 D---EASLLEALTPFAPSADTRKRALIAAGFGWAR-HSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKA 451
Cdd:cd03297 89 HlnvRENLAFGLKRKRNREDRISVDELLDLLGLDHlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180
....*....|....*....|...
gi 1439757928 452 ALAQTLR----DYPGGVLLVSHD 470
Cdd:cd03297 169 QLLPELKqikkNLNIPVIFVTHD 191
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-190 |
2.41e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.73 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 27 LKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqclmarveqhlpetlhtqsllqavlaplpadareaqrwlae 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 107 rllaqmgFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLL----WLESFLQTWQGSFVLVSHDN 182
Cdd:cd03222 61 -------ITPVY-KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLnaarAIRRLSEEGKKTALVVEHDL 132
|
....*...
gi 1439757928 183 TLLDAVTN 190
Cdd:cd03222 133 AVLDYLSD 140
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-478 |
2.81e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKS-TLLQVLDGTLAP----TSGSVSLAGQCLMARVEQHLPET---------------- 79
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkiamifqepmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 --LHT-QSLLQAVLAPLPADAREAQRWLAERLLAQMGFTPAV--MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGN 154
Cdd:PRK15134 106 npLHTlEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAkrLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 155 HLDLPT----LLWLESFLQTWQGSFVLVSHDntlLDAVtnsswilrdqtlhsfalpcsaarqalqeqdesaalrhkaeqk 230
Cdd:PRK15134 186 ALDVSVqaqiLQLLRELQQELNMGLLFITHN---LSIV------------------------------------------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 231 eidrvsasaRRLAtwgrvyDNEDLARKAKQMEKQVARlkdeqtELSVGP--PWRLVL-----QGDALPADR----LLEMD 299
Cdd:PRK15134 221 ---------RKLA------DRVAVMQNGRCVEQNRAA------TLFSAPthPYTQKLlnsepSGDPVPLPEpaspLLDVE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 300 TLHVSpAPGQPSLFTTGVAR----------LRSGDRVAIMGRNGGGKSS----LLRLLWQQMN---NASPLPGLRLHPRL 362
Cdd:PRK15134 280 QLQVA-FPIRKGILKRTVDHnvvvknisftLRPGETLGLVGESGSGKSTtglaLLRLINSQGEiwfDGQPLHNLNRRQLL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 363 HPGYYDQTLAQLPDEA---------SLLEALTPFAP--SADTRKRALIAA----GFGWARHSQKVSTLSGGERSRLLFVG 427
Cdd:PRK15134 359 PVRHRIQVVFQDPNSSlnprlnvlqIIEEGLRVHQPtlSAAQREQQVIAVmeevGLDPETRHRYPAEFSGGQRQRIAIAR 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 428 LSLARYSLLLLDEPTNHLDMEGKA---ALAQTLR-DYPGGVLLVSHDRQLISESC 478
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAqilALLKSLQqKHQLAYLFISHDLHVVRALC 493
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
250-475 |
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 1439757928 250 DNEDLARKAKQMEKQvaRLKDEQTELS------VGPPWRLVLQG--DALPADRLLEMDTLHVSPapGQPSLFTTGVARLR 321
Cdd:PLN03073 126 DLAKIERRKRKEERQ--REVQYQAHVAemeaakAGMPGVYVNHDgnGGGPAIKDIHMENFSISV--GGRDLIVDASVTLA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 322 SGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRLHPRLHPGYYDQTLAQ------------LPDEASLL--EALTPF 387
Cdd:PLN03073 202 FGRHYGLVGRNGTGKTTFLRYMAMHAIDGIPKNCQILHVEQEVVGDDTTALQcvlntdiertqlLEEEAQLVaqQRELEF 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 -----------------------------------APSADTRKrALIAAGFGWARHSQ--KVSTLSGGERSRLLFVGLSL 430
Cdd:PLN03073 282 etetgkgkgankdgvdkdavsqrleeiykrlelidAYTAEARA-ASILAGLSFTPEMQvkATKTFSGGWRMRIALARALF 360
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1439757928 431 ARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLIS 475
Cdd:PLN03073 361 IEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLN 405
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-157 |
3.60e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLA--PTSGS-VSLAGQCLM--ARVEQHLPET-LHTQSLLQ------ 87
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQreGRLARDIRKSrANTGYIFQqfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 --AVLAPLPADA-------REAQRWL-------AERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK09984 100 rlSVLENVLIGAlgstpfwRTCFSWFtreqkqrALQALTRVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
....*.
gi 1439757928 152 PGNHLD 157
Cdd:PRK09984 179 PIASLD 184
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-186 |
4.04e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 28 KKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVS-----------LAGQCLMARVEQHLPETLHTQSLLQAV-LAPLPA 95
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKLLEGDVKVIVKPQYVdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 DA-------REAQRWLAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFL 168
Cdd:cd03236 104 KGkvgellkKKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170 180
....*....|....*....|.
gi 1439757928 169 Q---TWQGSFVLVSHDNTLLD 186
Cdd:cd03236 183 RelaEDDNYVLVVEHDLAVLD 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-160 |
5.62e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 53.57 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveQHLPetLHTqslLQAVLAPLPADA 97
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----STIP--LED---LRSSLTIIPQDP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 98 -------REAQRWLAERLLAQMgFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPT 160
Cdd:cd03369 92 tlfsgtiRSNLDPFDEYSDEEI-YGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-157 |
5.85e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG----------------QCLMARVEQHLpetLHTQSLL 86
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflrrQIGMIFQDHHL---LMDRTVY 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 87 QAVLAPL--PADAREAQRWLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKA-KNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-195 |
6.32e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.33 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHL----------PETLHTQSLLQAV 89
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrkigmvfqnPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 90 LA------PLPADarEAQRWLAERLLA--QMGFTpavmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDlPT- 160
Cdd:PRK13642 103 VAfgmenqGIPRE--EMIKRVDEALLAvnMLDFK----TREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD-PTg 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1439757928 161 ----LLWLESFLQTWQGSFVLVSHDntlLDAVTNSSWIL 195
Cdd:PRK13642 176 rqeiMRVIHEIKEKYQLTVLSITHD---LDEAASSDRIL 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-157 |
6.53e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.44 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP---TSGSVSLAG-----QCLMAR---VEQH---LP-----ET 79
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGmpidaKEMRAIsayVQQDdlfIPtltvrEH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 LHTQSLLQavlapLPADAREAQRWLA-ERLLAQMGFTPAvmeQQTAT--------LSGGQHTRLLLARALIRQPDLLLLD 150
Cdd:TIGR00955 120 LMFQAHLR-----MPRRVTKKEKRERvDEVLQALGLRKC---ANTRIgvpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
....*..
gi 1439757928 151 EPGNHLD 157
Cdd:TIGR00955 192 EPTSGLD 198
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-157 |
6.70e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.65 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 27 LKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQcLMARVEqhlPETLHTQSLLQA-VLAP------------- 92
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-RMNDVP---PAERGVGMVFQSyALYPhlsvaenmsfglk 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 93 -LPADAREAQRWL---AERLlaQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11000 102 lAGAKKEEINQRVnqvAEVL--QLA---HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
319-480 |
7.18e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.88 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNAS------PLPGLRLHPRLHPG-YYDQTLAQLPDEASLLEALTPFAP-- 389
Cdd:cd03231 22 TLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAgrvllnGGPLDFQRDSIARGlLYLGHAPGIKTTLSVLENLRFWHAdh 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 390 SADTRKRALIAAGFGWARHSqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG---VLL 466
Cdd:cd03231 102 SDEQVEEALARVGLNGFEDR-PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARggmVVL 180
|
170
....*....|....
gi 1439757928 467 VSHDRQLISESCNR 480
Cdd:cd03231 181 TTHQDLGLSEAGAR 194
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-185 |
7.23e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTlAPTSGSVSLAgqcLMAR----------VEQHL---PETLHTQ- 83
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGYSNDLT---LFGRrrgsgetiwdIKKHIgyvSSSLHLDy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 84 ------------------SLLQAVlaplpadaREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPD 145
Cdd:PRK10938 350 rvstsvrnvilsgffdsiGIYQAV--------SDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPT 421
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1439757928 146 LLLLDEPGNHLDLPTLLWLESFLQtwqgsfVLVSHDNTLL 185
Cdd:PRK10938 422 LLILDEPLQGLDPLNRQLVRRFVD------VLISEGETQL 455
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
320-473 |
7.60e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLW--------------QQMNNASPLPGLRLHPRlHPGYYDQTLAQLPDEASLLEALT 385
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGgldtptsgdvifngQPMSKLSSAAKAELRNQ-KLGFIYQFHHLLPDFTALENVAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 PF----APSADTRKRAL-IAAGFGWARHSQ-KVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTL-- 457
Cdd:PRK11629 111 PLligkKKPAEINSRALeMLAAVGLEHRANhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLge 190
|
170
....*....|....*...
gi 1439757928 458 --RDYPGGVLLVSHDRQL 473
Cdd:PRK11629 191 lnRLQGTAFLVVTHDLQL 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-157 |
7.65e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.04 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMAR-----------VEQHLPETLHTQSLLQAV 89
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevrkfvglVFQNPDDQIFSPTVEQDI 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 90 lAPLPADAREAQRWLAERL---LAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13652 101 -AFGPINLGLDEETVAHRVssaLHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-157 |
7.95e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVslagQCLMARVEQHLPETLhtQSLLQA--------VLAPLPA 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER----QSQFSHITRLSFEQL--QKLVSDewqrnntdMLSPGED 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 96 D----ARE------AQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK10938 97 DtgrtTAEiiqdevKDPARCEQLAQQFGIT-ALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-152 |
7.99e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGtLAPT---SGSVSLAGQCLMARveqHLPET-------LHTQSLLQAVL 90
Cdd:PRK13549 22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQAS---NIRDTeragiaiIHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 91 APL-----------------PADAREAQRWLAErllAQMGFTPA--VMEqqtatLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK13549 98 SVLeniflgneitpggimdyDAMYLRAQKLLAQ---LKLDINPAtpVGN-----LGLGQQQLVEIAKALNKQARLLILDE 169
|
.
gi 1439757928 152 P 152
Cdd:PRK13549 170 P 170
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-186 |
1.13e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL---MARVEQHLPETLHtQSLLQAVLAplp 94
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdLCTYQKQLCFVGH-RSGINPYLT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 95 adAREAQRWLAERLLAQMGFTPAV--------MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLES 166
Cdd:PRK13540 91 --LRENCLYDIHFSPGAVGITELCrlfslehlIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170 180
....*....|....*....|...
gi 1439757928 167 FLQTWQ---GSFVLVSHDNTLLD 186
Cdd:PRK13540 169 KIQEHRakgGAVLLTSHQDLPLN 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-152 |
1.31e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 3 TLLTAHALHVETAFG-PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----MARVEQ-- 74
Cdd:COG3845 256 VVLEVENLSVRDDRGvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspRERRRLgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 75 -HLPETLHTQ------SLLQ-AVL-----APLPA----DAREAQRWlAERLLAQMGFTPAVMEQQTATLSGG--QhtRLL 135
Cdd:COG3845 336 aYIPEDRLGRglvpdmSVAEnLILgryrrPPFSRggflDRKAIRAF-AEELIEEFDVRTPGPDTPARSLSGGnqQ--KVI 412
|
170
....*....|....*..
gi 1439757928 136 LARALIRQPDLLLLDEP 152
Cdd:COG3845 413 LARELSRDPKLLIAAQP 429
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-157 |
1.33e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 13 ETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV-----------------SLAG--------QC 67
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenlwdirNKAGmvfqnpdnQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 68 LMARVEQHL---PETLHTQsllqavlaplPADAREAqrwlAERLLAQMG------FTPAVmeqqtatLSGGQHTRLLLAR 138
Cdd:PRK13633 99 VATIVEEDVafgPENLGIP----------PEEIRER----VDESLKKVGmyeyrrHAPHL-------LSGGQKQRVAIAG 157
|
170
....*....|....*....
gi 1439757928 139 ALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLD 176
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
396-485 |
1.35e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 396 RALIAAGFGWARHSQKVSTLSGGERSRL---LFVGLSLARySLLLLDEPTNHLDMEGKAALA---QTLRDYPGGVLLVSH 469
Cdd:cd03238 69 QFLIDVGLGYLTLGQKLSTLSGGELQRVklaSELFSEPPG-TLFILDEPSTGLHQQDINQLLeviKGLIDLGNTVILIEH 147
|
90
....*....|....*.
gi 1439757928 470 DRQLISESCnrfWLID 485
Cdd:cd03238 148 NLDVLSSAD---WIID 160
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
319-475 |
1.61e-07 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 52.35 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpGLRLHP-----RLHpgyyDQTLAQLPDEAS-------------- 379
Cdd:COG1136 30 SIEAGEFVAIVGPSGSGKSTLLNIL-----------GGLDRPtsgevLID----GQDISSLSERELarlrrrhigfvfqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 380 --LLEALTPF-----------APSADTRKRALIAA---GFGwARHSQKVSTLSGGERSRllfvgLSLARY-----SLLLL 438
Cdd:COG1136 95 fnLLPELTALenvalplllagVSRKERRERARELLervGLG-DRLDHRPSQLSGGQQQR-----VAIARAlvnrpKLILA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1439757928 439 DEPTNHLDME-GKAALA--QTLRDYPG-GVLLVSHDRQLIS 475
Cdd:COG1136 169 DEPTGNLDSKtGEEVLEllRELNRELGtTIVMVTHDPELAA 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-152 |
2.05e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.20 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----CLMARVEQ---HLPET------LHTQSLLQA 88
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRgigYLPQEasifrrLSVYDNLMA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 89 VLAPLPADAREAQRWLAERLLAQMGFTpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:PRK10895 102 VLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-484 |
2.29e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 51.51 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQ---------QMNNAsplpGLRLHPRLHPGYydqtlaqLPDEASL------LEAL 384
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILGiilpdsgevLFDGK----PLDIAARNRIGY-------LPEERGLypkmkvIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSADTRKRALIAAGFGW-------ARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTL 457
Cdd:cd03269 92 VYLAQLKGLKKEEARRRIDEWlerlelsEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190
....*....|....*....|....*....|
gi 1439757928 458 RDYPGG---VLLVSHDRQLISESCNRFWLI 484
Cdd:cd03269 172 RELARAgktVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
319-474 |
2.65e-07 |
|
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: 51.64 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGL---------RLHPRLHPgYYDQTLAQLPDEASLLEALTPF-- 387
Cdd:cd03292 23 SISAGEFVFLVGPSGAGKSTLLKLI---YKEELPTSGTirvngqdvsDLRGRAIP-YLRRKIGVVFQDFRLLPDRNVYen 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 ---------APSADTRKR---ALIAAGFGwARHSQKVSTLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGK 450
Cdd:cd03292 99 vafalevtgVPPREIRKRvpaALELVGLS-HKHRALPAELSGGEQQRV-----AIARAivnspTILIADEPTGNLDPDTT 172
|
170 180
....*....|....*....|....*..
gi 1439757928 451 AALAQTLRDYPGG---VLLVSHDRQLI 474
Cdd:cd03292 173 WEIMNLLKKINKAgttVVVATHAKELV 199
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-181 |
3.23e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 35 LIGHNGCGKSTLLQVLDGTLAPTSG-----SVSLAGQCLM---------ARVEQ--HLPETLhTQSLLQAVLAPLPADA- 97
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFnyrdvlefrRRVGMlfQRPNPF-PMSIMDNVLAGVRAHKl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 98 --REAQRWLAERLLAQMGFTPAVMEQQTAT---LSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQ 172
Cdd:PRK14271 131 vpRKEFRGVAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170
....*....|.
gi 1439757928 173 G--SFVLVSHD 181
Cdd:PRK14271 211 DrlTVIIVTHN 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-66 |
3.86e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 3.86e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ 66
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE 86
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
318-533 |
4.43e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.54 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 318 ARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASP---LPGLRLHpRLHPGYYDQTLAQLPDEASL-----LEAL----- 384
Cdd:PRK09536 24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtvlVAGDDVE-ALSARAASRRVASVPQDTSLsfefdVRQVvemgr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TP----FAPSADTRKRAL---IAAGFGWARHSQKVSTLSGGERSRLLfVGLSLARYS-LLLLDEPTNHLDMEGKA---AL 453
Cdd:PRK09536 103 TPhrsrFDTWTETDRAAVeraMERTGVAQFADRPVTSLSGGERQRVL-LARALAQATpVLLLDEPTASLDINHQVrtlEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 454 AQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARlQAVAPAPDSRLALQSTPA----------GAD 523
Cdd:PRK09536 182 VRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA-DTLRAAFDARTAVGTDPAtgaptvtplpDPD 260
|
250
....*....|
gi 1439757928 524 DDEEALLARL 533
Cdd:PRK09536 261 RTEAAADTRV 270
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
290-485 |
5.06e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.93 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 290 LPADRLLEMDTL--HVSPAPGQPSLFTTGVARLRSGDRVAIMGRNGGGKSSLL--------------RLLWQQMNNASPL 353
Cdd:PRK10584 1 MPAENIVEVHHLkkSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLailaglddgssgevSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 354 PGLRLHPRlHPGYYDQTLAQLPDEASL----LEALTPFAPSADTRKRA---LIAAGFGwARHSQKVSTLSGGERSRLLFV 426
Cdd:PRK10584 81 ARAKLRAK-HVGFVFQSFMLIPTLNALenveLPALLRGESSRQSRNGAkalLEQLGLG-KRLDHLPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 427 GLSLARYSLLLLDEPTNHLDMEGKAALAQTL----RDYPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:PRK10584 159 RAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-156 |
5.33e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 11 HVETAFGPL--FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG--------------------QCL 68
Cdd:PRK09700 10 GIGKSFGPVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlgigiiyQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 69 MARVEQHLPETLHTQSLLQAVLAPLPADAREAQRWLAERLLAQMGFTPAvMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:PRK09700 90 SVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
....*...
gi 1439757928 149 LDEPGNHL 156
Cdd:PRK09700 169 MDEPTSSL 176
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
319-469 |
5.68e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL------------WQqmnnasplpGLRLHpRLHPGYYDQTL-----AQLPDEASLL 381
Cdd:PRK13538 23 TLNAGELVQIEGPNGAGKTSLLRILaglarpdagevlWQ---------GEPIR-RQRDEYHQDLLylghqPGIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 382 EALTPFAP-----SADTRKRALIAAGFGwARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQT 456
Cdd:PRK13538 93 ENLRFYQRlhgpgDDEALWEALAQVGLA-GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170
....*....|....*.
gi 1439757928 457 LRDY--PGG-VLLVSH 469
Cdd:PRK13538 172 LAQHaeQGGmVILTTH 187
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-157 |
6.77e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSL------AGQCLMARVEQHLPETLHTQSLLQAVLA--- 91
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNPYSKKIKNFKELRRRVSmvf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 92 -------------------PLP-ADAREAQRWLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK13631 123 qfpeyqlfkdtiekdimfgPVAlGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
....*.
gi 1439757928 152 PGNHLD 157
Cdd:PRK13631 203 PTAGLD 208
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-214 |
6.85e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVETAfGPLFNSLSFTLKKGDRIGLIGHNGCGKS----TLLQVLDGTLAPTSGSVSLAGQCLmarveqhL 76
Cdd:PRK10418 1 MPQQIELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV-------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 77 PETL---HTQSLLQA------VLAPLPADAREAQRWLA-----ERLLAQM-----GFTPAVMEQQTATLSGGQHTRLLLA 137
Cdd:PRK10418 73 PCALrgrKIATIMQNprsafnPLHTMHTHARETCLALGkpaddATLTAALeavglENAARVLKLYPFEMSGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 138 RALIRQPDLLLLDEPGNHLDLPT----LLWLESFLQTWQGSFVLVSHD----NTLLD--AVTNSSWILRDQTLHS-FALP 206
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDmgvvARLADdvAVMSHGRIVEQGDVETlFNAP 232
|
....*...
gi 1439757928 207 CSAARQAL 214
Cdd:PRK10418 233 KHAVTRSL 240
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
320-470 |
7.46e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 50.54 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQQMnnaSPLPG-LRLHPRLHPGYYDQTLAQ----LPDEASLLEALT--------- 385
Cdd:PRK13548 25 LRPGEVVAILGPNGAGKSTLLRALSGEL---SPDSGeVRLNGRPLADWSPAELARrravLPQHSSLSFPFTveevvamgr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 -PFAPSADTRKRALIAA-------GFGwarhSQKVSTLSGGERSRLlfvglSLAR-----------YSLLLLDEPTNHLD 446
Cdd:PRK13548 102 aPHGLSRAEDDALVAAAlaqvdlaHLA----GRDYPQLSGGEQQRV-----QLARvlaqlwepdgpPRWLLLDEPTSALD 172
|
170 180
....*....|....*....|....*...
gi 1439757928 447 MEGKAALAQTLRDY----PGGVLLVSHD 470
Cdd:PRK13548 173 LAHQHHVLRLARQLaherGLAVIVVLHD 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-157 |
8.23e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.03 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 33 IGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLmarveqhlpETLHTQSLLQ---------AVLA-------PLPAD 96
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL---------SSLSHSVLRQgvamvqqdpVVLAdtflanvTLGRD 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 97 AREAQRW-------LAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK10790 441 ISEEQVWqaletvqLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
319-480 |
8.80e-07 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 50.42 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL----------------------------------WQqmnNASPLPGLR------- 357
Cdd:COG0411 26 EVERGEIVGLIGPNGAGKTTLFNLItgfyrptsgrilfdgrditglpphriarlgiartFQ---NPRLFPELTvlenvlv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 358 -LHPRLHPGYYdqtlaqlpdeASLLEALTPFAPSADTRKRAL-IAAGFG-WARHSQKVSTLSGGERsRLLFVGLSLA-RY 433
Cdd:COG0411 103 aAHARLGRGLL----------AALLRLPRARREEREARERAEeLLERVGlADRADEPAGNLSYGQQ-RRLEIARALAtEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 434 SLLLLDEPTNHLDMEGKAALAQTLRDYPGG----VLLVSHDRQLISESCNR 480
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRDErgitILLIEHDMDLVMGLADR 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-160 |
1.06e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.50 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ---------------------CLMAR-VEQHL---- 76
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrniavvfqdaGLFNRsIEDNIrvgr 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 77 PETLHTQSLLQAVLAplpadarEAQRWLAERLlaqMGFTPAVMEQQTAtLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:PRK13657 434 PDATDEEMRAAAERA-------QAHDFIERKP---DGYDTVVGERGRQ-LSGGERQRLAIARALLKDPPILILDEATSAL 502
|
....
gi 1439757928 157 DLPT 160
Cdd:PRK13657 503 DVET 506
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
35-152 |
1.21e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.04 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 35 LIGHNGCGKSTLLQVL-------DGtlAPTSGSVSLAGQCLMAR-------------VEQH---LPET----------LH 81
Cdd:COG1117 42 LIGPSGCGKSTLLRCLnrmndliPG--ARVEGEILLDGEDIYDPdvdvvelrrrvgmVFQKpnpFPKSiydnvayglrLH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 82 ------------TQSLLQAVLaplpadareaqrW--LAERLlaqmgftpavmeQQTAT-LSGGQHTRLLLARALIRQPDL 146
Cdd:COG1117 120 gikskseldeivEESLRKAAL------------WdeVKDRL------------KKSALgLSGGQQQRLCIARALAVEPEV 175
|
....*.
gi 1439757928 147 LLLDEP 152
Cdd:COG1117 176 LLMDEP 181
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
318-460 |
1.31e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 49.58 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 318 ARLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPG---LRLHPRlHPGYYDQTLAQLPDEASLLEALT-----PFA- 388
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGqilFNGQPR-KPDQFQKCVAYVRQDDILLPGLTvretlTYTa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 --------PSADTRKRA----LIAAGFGWARHsQKVSTLSGGERSRllfvgLSLARY-----SLLLLDEPTNHLDMEGKA 451
Cdd:cd03234 107 ilrlprksSDAIRKKRVedvlLRDLALTRIGG-NLVKGISGGERRR-----VSIAVQllwdpKVLILDEPTSGLDSFTAL 180
|
....*....
gi 1439757928 452 ALAQTLRDY 460
Cdd:cd03234 181 NLVSTLSQL 189
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-157 |
1.33e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.17 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAG-------------QClmARVEQHLpetlHtqs 84
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQV--ALVSQNV----H--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQAVLAPLPADARE-----AQRWLAERLLAQMGFTPAvMEQ--------QTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK11176 428 LFNDTIANNIAYARTeqysrEQIEEAARMAYAMDFINK-MDNgldtvigeNGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
....*.
gi 1439757928 152 PGNHLD 157
Cdd:PRK11176 507 ATSALD 512
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
326-480 |
1.37e-06 |
|
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: 49.43 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 326 VAIMGRNGGGKSSLLRLLWQQMNNASP---LPGL-----RLHPRLHPGYYDQTLAqLPDEASLLEALTPFA-----PSAD 392
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGELRPTSGtayINGYsirtdRKAARQSLGYCPQFDA-LFDELTVREHLRFYArlkglPKSE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 393 TRKRA---LIAAGFGWARHSqKVSTLSGGERsRLLFVGLSLARYS-LLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLL 466
Cdd:cd03263 110 IKEEVellLRVLGLTDKANK-RARTLSGGMK-RKLSLAIALIGGPsVLLLDEPTSGLDPASRRAIWDLILEVRKGrsIIL 187
|
170
....*....|....
gi 1439757928 467 VSHDRQLISESCNR 480
Cdd:cd03263 188 TTHSMDEAEALCDR 201
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
319-471 |
1.43e-06 |
|
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: 49.44 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLL--WQQMNNASPLPGLRLHPRLHPgyYDQTLAQLPDEASLLEALTPF--------- 387
Cdd:cd03259 22 TVEPGEFLALLGPSGCGKTTLLRLIagLERPDSGEILIDGRDVTGVPP--ERRNIGMVFQDYALFPHLTVAeniafglkl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 --APSADTRKRAL-IAAGFGWARHSQ-KVSTLSGGERSRllfVGL--SLARY-SLLLLDEPTNHLDMEGKAALAQTLRDY 460
Cdd:cd03259 100 rgVPKAEIRARVReLLELVGLEGLLNrYPHELSGGQQQR---VALarALAREpSLLLLDEPLSALDAKLREELREELKEL 176
|
170
....*....|....*
gi 1439757928 461 PGG----VLLVSHDR 471
Cdd:cd03259 177 QRElgitTIYVTHDQ 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
320-485 |
1.55e-06 |
|
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: 49.64 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL------------------WQQMN------------------NASPLPGLRLHP--- 360
Cdd:cd03267 44 IEKGEIVGFIGPNGAGKTTTLKILsgllqptsgevrvaglvpWKRRKkflrrigvvfgqktqlwwDLPVIDSFYLLAaiy 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 361 RLHPGYYDQTLAQLPDeasLLEaLTPFApsadtrkraliaagfgwarhSQKVSTLSGGERSRLLFVGLSLARYSLLLLDE 440
Cdd:cd03267 124 DLPPARFKKRLDELSE---LLD-LEELL--------------------DTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1439757928 441 PTNHLDMEGKAALAQTLRDY----PGGVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-179 |
1.55e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDgTLAPTSGSVSLAGQCLMARVEQH-------LPETLHTQS-LLQAVLAPLP 94
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTwrkafgvIPQKVFIFSgTFRKNLDPYE 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 95 ADARE---------AQRWLAERLLAQMGFtpaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:TIGR01271 1317 QWSDEeiwkvaeevGLKSVIEQFPDKLDF---VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
170
....*....|....*
gi 1439757928 166 SFL-QTWQGSFVLVS 179
Cdd:TIGR01271 1394 KTLkQSFSNCTVILS 1408
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
410-477 |
1.61e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 410 QKVSTLSGGERSRLLF-VGLSLARY-----SLLLLDEPTNHLDMEGKAALAQ----TLRDYPG--GVLLVSHDRQLISES 477
Cdd:PRK01156 797 EGIDSLSGGEKTAVAFaLRVAVAQFlnndkSLLIMDEPTAFLDEDRRTNLKDiieySLKDSSDipQVIMISHHRELLSVA 876
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
126-181 |
1.76e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.65 E-value: 1.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 126 LSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTW----QGSFVLVSHD 181
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-157 |
1.91e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.39 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 1 MSTLLTAHALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLD--GTLAP---TSGSVSLAGQCLMAR---- 71
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPrtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 72 ---------VEQH---LPETLH--------------TQSLLQAVLAPLpadaREAQRW--LAERLlaqmgftpavmEQQT 123
Cdd:PRK14239 82 vdlrkeigmVFQQpnpFPMSIYenvvyglrlkgikdKQVLDEAVEKSL----KGASIWdeVKDRL-----------HDSA 146
|
170 180 190
....*....|....*....|....*....|....
gi 1439757928 124 ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-151 |
2.11e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.66 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLP------ETLHTQSLLQAVlaplp 94
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNgqltgiENIELKGLMMGL----- 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 95 adAREAQRWLAERLL--AQMGftpAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PRK13545 116 --TKEKIKEIIPEIIefADIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
310-477 |
2.27e-06 |
|
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: 47.74 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 310 PSLFTTGVARLRSGDRVAIMGRNGGGKSSLLR----LLWQQMNNasplpgLRLHPRLHPGYYdqtlaqlpdeasllealt 385
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiglALGGAQSA------TRRRSGVKAGCI------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 pfapsadtrkRALIAAGFGWARHsqkvsTLSGGERSR----LLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYP 461
Cdd:cd03227 64 ----------VAAVSAELIFTRL-----QLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHL 128
|
170
....*....|....*....
gi 1439757928 462 GG---VLLVSHDRQLISES 477
Cdd:cd03227 129 VKgaqVIVITHLPELAELA 147
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-181 |
3.80e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 49.26 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 24 SFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQHLPE-------------------TLHTQS 84
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkkiamvfqsfalmphmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 85 LLQAVLAPLPADAREAQRWLAERLLAQMGFTPAVMEQqtatLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWL 164
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDE----LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180
....*....|....*....|.
gi 1439757928 165 ESFLQTWQG----SFVLVSHD 181
Cdd:PRK10070 204 QDELVKLQAkhqrTIVFISHD 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
320-480 |
4.14e-06 |
|
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: 48.20 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASP-----------LPGLRLHPRLHPG----------YYDQT------LA 372
Cdd:cd03219 23 VRPGEIHGLIGPNGAGKTTLFNLI---SGFLRPtsgsvlfdgedITGLPPHEIARLGigrtfqiprlFPELTvlenvmVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 373 QLPDEASLLEALTPFAPSADTRKRAL-IAAGFG-WARHSQKVSTLSGGERsRLLFVGLSLA-RYSLLLLDEPTNHLDMEG 449
Cdd:cd03219 100 AQARTGSGLLLARARREEREARERAEeLLERVGlADLADRPAGELSYGQQ-RRLEIARALAtDPKLLLLDEPAAGLNPEE 178
|
170 180 190
....*....|....*....|....*....|....
gi 1439757928 450 KAALAQTLRDYPG---GVLLVSHDRQLISESCNR 480
Cdd:cd03219 179 TEELAELIRELRErgiTVLLVEHDMDVVMSLADR 212
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-497 |
4.41e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.46 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnASPLP--------GLRLHpRLHPGYYDQTLA------QLPdEASLLEAL 384
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNAL------LGFLPyqgslkinGIELR-ELDPESWRKHLSwvgqnpQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSA-DTRKRALIAAGFGW---ARHSQKVSTLSgGERSRLLFVG----LSLAR-----YSLLLLDEPTNHLDMEGKA 451
Cdd:PRK11174 444 LLGNPDAsDEQLQQALENAWVSeflPLLPQGLDTPI-GDQAAGLSVGqaqrLALARallqpCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1439757928 452 ALAQTLRDYPGG--VLLVSHdrQLIS-ESCNRFWLIDSAGLTEWHSLEE 497
Cdd:PRK11174 523 LVMQALNAASRRqtTLMVTH--QLEDlAQWDQIWVMQDGQIVQQGDYAE 569
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
319-484 |
4.53e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRLHPRLhpGYYDQTLAQLPD------EASLLEALTP-FAPSA 391
Cdd:PRK13547 23 RIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDV--TLNGEPLAAIDAprlarlRAVLPQAAQPaFAFSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 392 DT------------------RKRALIAAGFGWARHS----QKVSTLSGGERSRLLFV-----------GLSLARYslLLL 438
Cdd:PRK13547 101 REivllgrypharragalthRDGEIAWQALALAGATalvgRDVTTLSGGELARVQFArvlaqlwpphdAAQPPRY--LLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1439757928 439 DEPTNHLDMEGKAALAQTL----RDYPGGVLLVSHDRQLISESCNRFWLI 484
Cdd:PRK13547 179 DEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAARHADRIAML 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-152 |
4.95e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVS-LAGQCLMARVEQHL-------PETL-----HTQSL---L 86
Cdd:NF033858 20 VSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVcpriaymPQGLgknlyPTLSVfenL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 87 Q--AVLAPLPADAREAQrwlAERLLAQMGFTPaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF033858 100 DffGRLFGQDAAERRRR---IDELLRATGLAP-FADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
319-469 |
5.22e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.39 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpglrlhprlhPGYYDQT----------LAQLPDEA---------- 378
Cdd:COG1132 362 TIPPGETVALVGPSGSGKSTLVNLL--------------------LRFYDPTsgrilidgvdIRDLTLESlrrqigvvpq 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 379 -------SLLEALTPFAPSADTR--KRALIAAGF-GWARH---------SQKVSTLSGGERSRLlfvglSLARY-----S 434
Cdd:COG1132 422 dtflfsgTIRENIRYGRPDATDEevEEAAKAAQAhEFIEAlpdgydtvvGERGVNLSGGQRQRI-----AIARAllkdpP 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 1439757928 435 LLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSH 469
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
124-180 |
5.49e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.72 E-value: 5.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1439757928 124 ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLP----TLLWLESFLQTWQGSFVLVSH 180
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPrkreLLPYLERLAREINIPILYVSH 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-186 |
5.57e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGqCLMARVEQH--------LPE--TLHTQSLlQAVLAP 92
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG-LNIAKIGLHdlrfkitiIPQdpVLFSGSL-RMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 93 LPADAREaQRWLAERLLAQMGFT---PAVMEQQTA----TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLE 165
Cdd:TIGR00957 1383 FSQYSDE-EVWWALELAHLKTFVsalPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
170 180
....*....|....*....|....
gi 1439757928 166 SFLQT-WQGSFVL-VSHD-NTLLD 186
Cdd:TIGR00957 1462 STIRTqFEDCTVLtIAHRlNTIMD 1485
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
322-477 |
6.00e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.14 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 322 SGDRVAIMGRNGGGKSSLLRLL--------WQQMNNASPLPGLRLHPRLHpgYYDQTLaqLP-----DEASLlealtpfA 388
Cdd:PRK11247 37 AGQFVAVVGRSGCGKSTLLRLLagletpsaGELLAGTAPLAEAREDTRLM--FQDARL--LPwkkviDNVGL-------G 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 PSADTRKRALIA-AGFGWARHSQK-VSTLSGGERSRllfVGLSLA---RYSLLLLDEPTNHLD----MEGKAALAQTLRD 459
Cdd:PRK11247 106 LKGQWRDAALQAlAAVGLADRANEwPAALSGGQKQR---VALARAlihRPGLLLLDEPLGALDaltrIEMQDLIESLWQQ 182
|
170
....*....|....*...
gi 1439757928 460 YPGGVLLVSHDrqlISES 477
Cdd:PRK11247 183 HGFTVLLVTHD---VSEA 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-469 |
6.72e-06 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 46.92 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqMNNASPLPGLRLHPRLHPGYYDQTLAQ----LPDEASLLealtpfapsaDTRK 395
Cdd:cd03247 25 LKQGEKIALLGRSGSGKSTLLQLL---TGDLKPQQGEITLDGVPVSDLEKALSSlisvLNQRPYLF----------DTTL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 396 RALIAAGFgwarhsqkvstlSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG--VLLVSH 469
Cdd:cd03247 92 RNNLGRRF------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDktLIWITH 155
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-181 |
7.17e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ---CLMARVEQHLPETLH------------TQSLLQ 87
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQfifqdpyasldpRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 88 AVLAPLPA----DAREAQRWLAErLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLW 163
Cdd:PRK10261 423 SIMEPLRVhgllPGKAAAARVAW-LLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180
....*....|....*....|..
gi 1439757928 164 LESFLQTWQG----SFVLVSHD 181
Cdd:PRK10261 502 IINLLLDLQRdfgiAYLFISHD 523
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-480 |
7.34e-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: 46.80 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL-----------------WQQMNNASPLPglrlhpRLHPGYYDQTlAQLPDEASLLE 382
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCIagleepdsgsilidgedLTDLEDELPPL------RRRIGMVFQD-FALFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 ALTpfapsadtrkraliaagFGwarhsqkvstLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKA---ALA 454
Cdd:cd03229 96 NIA-----------------LG----------LSGGQQQRV-----ALARAlamdpDVLLLDEPTSALDPITRRevrALL 143
|
170 180
....*....|....*....|....*..
gi 1439757928 455 QTLRDYPG-GVLLVSHDRQLISESCNR 480
Cdd:cd03229 144 KSLQAQLGiTVVLVTHDLDEAARLADR 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-157 |
8.88e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGS-----------------------VSLAGQCLMARVEQH 75
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDiiindshnlkdinlkwwrskigvVSQDPLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 76 LPETLHTQSLLQAVLAPLPADAREAQRWLAERL---------------------LAQM---------------------- 112
Cdd:PTZ00265 480 IKYSLYSLKDLEALSNYYNEDGNDSQENKNKRNscrakcagdlndmsnttdsneLIEMrknyqtikdsevvdvskkvlih 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 113 GFTPAVMEQ-------QTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PTZ00265 560 DFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
319-474 |
9.56e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 46.75 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLwqqMNnasplpglrlhprlHPGYY---------DQTLAQL-PDEasllealtpfa 388
Cdd:cd03217 22 TIKKGEVHALMGPNGSGKSTLAKTI---MG--------------HPKYEvtegeilfkGEDITDLpPEE----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 psadtrkRALIAAGFGWARHSQ----KVSTL--------SGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQ- 455
Cdd:cd03217 74 -------RARLGIFLAFQYPPEipgvKNADFlryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEv 146
|
170 180
....*....|....*....|.
gi 1439757928 456 --TLRDYPGGVLLVSHDRQLI 474
Cdd:cd03217 147 inKLREEGKSVLIITHYQRLL 167
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-195 |
1.23e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.56 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 18 PLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQcLMARVEQHLPETLHTQSLLQAVLAP--LPA 95
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSVAYAAQKPwlLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 96 DARE---------AQRWLAerLLAQMGFTPAV----------MEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:cd03290 94 TVEEnitfgspfnKQRYKA--VTDACSLQPDIdllpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1439757928 157 D--LPTLLWLE---SFLQTWQGSFVLVSHDntlLDAVTNSSWIL 195
Cdd:cd03290 172 DihLSDHLMQEgilKFLQDDKRTLVLVTHK---LQYLPHADWII 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-188 |
1.25e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.39 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV------------SLAGQCLMARVEQHLPET--------- 79
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkkTKEKEKVLEKLVIQKTRFkkikkikei 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 80 --------------LHTQSLLQAVL-APL-----PADAREaqrwLAERLLAQMGFTPAVMEQQTATLSGGQHTRLLLARA 139
Cdd:PRK13651 104 rrrvgvvfqfaeyqLFEQTIEKDIIfGPVsmgvsKEEAKK----RAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 140 LIRQPDLLLLDEPGNHLDlP--TLLWLESF--LQTWQGSFVLVSHDntlLDAV 188
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLD-PqgVKEILEIFdnLNKQGKTIILVTHD---LDNV 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
326-472 |
1.27e-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: 46.79 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 326 VAIMGRNGGGKSSLLRLLwQQMN--------------------------------------NASPLPG-----LRLHPRL 362
Cdd:cd03260 29 TALIGPSGCGKSTLLRLL-NRLNdlipgapdegevlldgkdiydldvdvlelrrrvgmvfqKPNPFPGsiydnVAYGLRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 363 HpGYYDQTLAQLPDEASLLEALTPfapsaDTRKRALIAAGfgwarhsqkvstLSGGERSRLlfvglSLARY-----SLLL 437
Cdd:cd03260 108 H-GIKLKEELDERVEEALRKAALW-----DEVKDRLHALG------------LSGGQQQRL-----CLARAlanepEVLL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1439757928 438 LDEPTNHLDMEGKAALAQTL----RDYPggVLLVSHDRQ 472
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIaelkKEYT--IVIVTHNMQ 201
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
407-508 |
1.31e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.92 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 407 RHsQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG---VLLVSHDRQLISESCNRFWL 483
Cdd:PRK13638 130 RH-QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYV 208
|
90 100
....*....|....*....|....*
gi 1439757928 484 IDSAGLTEWHSLEEVYARLQAVAPA 508
Cdd:PRK13638 209 LRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
124-180 |
1.31e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.76 E-value: 1.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 124 ATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTLLWLESFLQTWQGSF--VLVSH 180
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYtiVLVTH 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
415-519 |
1.64e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.72 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG----GVLLVSHDRQLISESCNRFWLIDSAGLT 490
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
90 100
....*....|....*....|....*....
gi 1439757928 491 EWHSLEEVYARLQAVAPApdsRLALQSTP 519
Cdd:PRK13652 218 AYGTVEEIFLQPDLLARV---HLDLPSLP 243
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-151 |
1.90e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.44 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLdGTLAPT-SGSVSLAGQCLMARVEQHLPETLHTqsLLQAVLAPlpaDA 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVyGGRLTKPAKGKLFYVPQRPYMTLGT--LRDQIIYP---DS 540
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 98 REAQ--RWLAERLLAQM--------------GFTpaVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:TIGR00954 541 SEDMkrRGLSDKDLEQIldnvqlthileregGWS--AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
379-518 |
1.99e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 379 SLLEALTPFAPSA-------DTRKRALIAAGFGWARHSQKVSTLSGGERSRL-----LFVGLSLARYsllLLDEPTNHL- 445
Cdd:PRK00635 434 IFLSQLPSKSLSIeevlqglKSRLSILIDLGLPYLTPERALATLSGGEQERTalakhLGAELIGITY---ILDEPSIGLh 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 446 --DMEGKAALAQTLRDYPGGVLLVSHDRQLISeSCNRfwLID---SAG---------------LTEWHSLEEVYARLQAV 505
Cdd:PRK00635 511 pqDTHKLINVIKKLRDQGNTVLLVEHDEQMIS-LADR--IIDigpGAGifggevlfngsprefLAKSDSLTAKYLRQELT 587
|
170
....*....|...
gi 1439757928 506 APAPDSRLALQST 518
Cdd:PRK00635 588 IPIPEKRTNSLGT 600
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
315-459 |
2.26e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 47.35 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 315 TGVARlrSGDRVAIMGRNGGGKSSLLRLLWQQMNNASPLPGLRL------------------------------------ 358
Cdd:TIGR00955 45 SGVAK--PGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLlngmpidakemraisayvqqddlfiptltvrehlmf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 359 --HPRLHPGYYDQTLAQLPDEasLLEALTpFAPSADTRkralIAAGfgwarhsQKVSTLSGGERSRLLFVGLSLARYSLL 436
Cdd:TIGR00955 123 qaHLRMPRRVTKKEKRERVDE--VLQALG-LRKCANTR----IGVP-------GRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180
....*....|....*....|...
gi 1439757928 437 LLDEPTNHLDMEGKAALAQTLRD 459
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKG 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-157 |
2.53e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.15 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 20 FNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQ---------------HLPETLHTQS 84
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkrlrkeiglvfQFPEYQLFQE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928 85 LLQAVLAPLP----ADAREAQRWLAErLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK13645 107 TIEKDIAFGPvnlgENKQEAYKKVPE-LLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
319-470 |
2.71e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.78 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMnnaSPLPGLRLHprlhpgyYDQTLAQLPDEA-----SLL--EALTPfapsA 391
Cdd:PRK11231 24 SLPTGKITALIGPNGCGKSTLLKCFARLL---TPQSGTVFL-------GDKPISMLSSRQlarrlALLpqHHLTP----E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 392 DTRKRALIAAGFG-----WARHSQK---------------------VSTLSGGERSRlLFVGLSLARYS-LLLLDEPTNH 444
Cdd:PRK11231 90 GITVRELVAYGRSpwlslWGRLSAEdnarvnqameqtrinhladrrLTDLSGGQRQR-AFLAMVLAQDTpVVLLDEPTTY 168
|
170 180
....*....|....*....|....*....
gi 1439757928 445 LDMEGKA---ALAQTLRDYPGGVLLVSHD 470
Cdd:PRK11231 169 LDINHQVelmRLMRELNTQGKTVVTVLHD 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
319-474 |
3.12e-05 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 45.43 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLW--------------QQMNNASP--LPGLRLH-------PRLHPgyyDQTLAQ-- 373
Cdd:COG2884 24 EIEKGEFVFLTGPSGAGKSTLLKLLYgeerptsgqvlvngQDLSRLKRreIPYLRRRigvvfqdFRLLP---DRTVYEnv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 374 -LPdeaslLEALTpfAPSADTRKRalIAAGFGW----ARHSQKVSTLSGGERSRLlfvglSLARY-----SLLLLDEPTN 443
Cdd:COG2884 101 aLP-----LRVTG--KSRKEIRRR--VREVLDLvglsDKAKALPHELSGGEQQRV-----AIARAlvnrpELLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|....
gi 1439757928 444 HLDMEGKAALAQTLRDYP-GG--VLLVSHDRQLI 474
Cdd:COG2884 167 NLDPETSWEIMELLEEINrRGttVLIATHDLELV 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-152 |
3.35e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.44 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 10 LHVETAFGP-LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCLMARVEQH--------LPETL 80
Cdd:PRK11288 258 LRLDGLKGPgLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairagimlCPEDR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 81 HTQSLLQ-----------AVLAPLPA-----DAREAQrwLAERLLAQMGF-TPAvMEQQTATLSGGQHTRLLLARALIRQ 143
Cdd:PRK11288 338 KAEGIIPvhsvadninisARRHHLRAgclinNRWEAE--NADRFIRSLNIkTPS-REQLIMNLSGGNQQKAILGRWLSED 414
|
....*....
gi 1439757928 144 PDLLLLDEP 152
Cdd:PRK11288 415 MKVILLDEP 423
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-486 |
3.78e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.95 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLR-LLWQQMNNA-------SPLPGLRLHPRLHPGYYDQtLAQLPDEASLLEALTPFA-- 388
Cdd:PRK13537 29 HVQRGECFGLLGPNGAGKTTTLRmLLGLTHPDAgsislcgEPVPSRARHARQRVGVVPQ-FDNLDPDFTVRENLLVFGry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 ---PSADTrkRALIAAGFGWARHSQK----VSTLSGGERSRllfvgLSLARY-----SLLLLDEPTNHLDMEGKAALAQT 456
Cdd:PRK13537 108 fglSAAAA--RALVPPLLEFAKLENKadakVGELSGGMKRR-----LTLARAlvndpDVLVLDEPTTGLDPQARHLMWER 180
|
170 180 190
....*....|....*....|....*....|...
gi 1439757928 457 LRDYPGG---VLLVSHDRQLISESCNRFWLIDS 486
Cdd:PRK13537 181 LRSLLARgktILLTTHFMEEAERLCDRLCVIEE 213
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
108-474 |
3.93e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 108 LLAQMGFTPAVMEQQTATLSGGQHTRLLLARAL-IRQPDLL-LLDEP--GNH-LDLPTLLwleSFLQTwqgsfvLVSHDN 182
Cdd:PRK00635 1370 FIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKIsSNLTDIIyLLEDPlsGLHpQDAPTLL---QLIKE------LVTNNN 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 183 TLLdaVTNSSWILR---DQTLH---------SFALPCSAARQ--------ALQEQDESAALRHKAEQKEIDRVSASARRL 242
Cdd:PRK00635 1441 TVI--ATDRSGSLAehaDHLIHlgpgsgpqgGYLLSTSALKQsqpdlhntRSSEETPTLSVSLSIHTIQNLNVSAPLHSL 1518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 243 ATWGRVYDNEDLARKAKQMEKQVARLKDEQTELSVGppwRLVLQGDALPADRLLEMDTlHVSPApgqPSL--FTTGVARL 320
Cdd:PRK00635 1519 VAISGVSGSGKTSLLLEGFYKQACALIEKGPSVFSE---IIFLDSHPQISSQRSDIST-YFDIA---PSLrnFYASLTQA 1591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 321 RSGDRVAIM---GRNGGGKSSLLRLLWQQMNNA------SPLP---GLRLHPR----LHPGYYDQTLAQLPDEASLLeaL 384
Cdd:PRK00635 1592 KALNISASMfstNTKQGQCSDCWGLGYQWIDRAfyalekRPCPtcsGFRIQPLaqevVYEGKHFGQLLQTPIEEVAE--T 1669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSADTRKRALIAAGFGWARHSQKVSTLSGGERsrllfVGLSLARY--------SLLLLDEPTNHLDMEGKAALAQT 456
Cdd:PRK00635 1670 FPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEK-----IAIKIAKFlylppkhpTLFLLDEIATSLDNQQKSALLVQ 1744
|
410 420
....*....|....*....|.
gi 1439757928 457 LRDYPG---GVLLVSHDRQLI 474
Cdd:PRK00635 1745 LRTLVSlghSVIYIDHDPALL 1765
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-157 |
3.94e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.99 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 23 LSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQ-----------CLMA----------RVEQHLPETLH 81
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVfqnyalyphmSVRENMAYGLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 82 tqsllqavLAPLPADAREAQRWLAERLLAQMGFtpavMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PRK11650 103 --------IRGMPKAEIEERVAEAARILELEPL----LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
415-473 |
4.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 415 LSGGERSRL-LFVGLSLARY-----SLLLLDEPTNHLDMEGKAAL----AQTLRDYPgGVLLVSHDRQL 473
Cdd:PRK03918 789 LSGGERIALgLAFRLALSLYlagniPLLILDEPTPFLDEERRRKLvdimERYLRKIP-QVIIVSHDEEL 856
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
323-459 |
5.03e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.36 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRLLWQQMnnaSPLPGLRLHPRLHPGYYDQT--------LAQ---LPDEASLLEALT----PF 387
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLM---TPAHGHVWLDGEHIQHYASKevarriglLAQnatTPGDITVQELVArgryPH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 AP--------SADTRKRALIAAGFGwARHSQKVSTLSGGERSRlLFVGLSLAR-YSLLLLDEPTNHLDMEGKAALAQTLR 458
Cdd:PRK10253 110 QPlftrwrkeDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQR-AWIAMVLAQeTAIMLLDEPTTWLDISHQIDLLELLS 187
|
.
gi 1439757928 459 D 459
Cdd:PRK10253 188 E 188
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
15-203 |
5.18e-05 |
|
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: 44.52 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 15 AFGPLFNSLSFTLKKGdrIGLI-GHNGCGKSTLLQ----VLDGTLAPTSgsvslagqclmaRVEQHLPETLHTQS-LLQA 88
Cdd:cd03240 8 NIRSFHERSEIEFFSP--LTLIvGQNGAGKTTIIEalkyALTGELPPNS------------KGGAHDPKLIREGEvRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 89 VLAPLPADAREaqrWLAERLLAQmgFTPAVMEQQ----------TATLSGGQHT------RLLLARALIRQPDLLLLDEP 152
Cdd:cd03240 74 KLAFENANGKK---YTITRSLAI--LENVIFCHQgesnwplldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 153 GNHLD-------LPTLlwLESFLQTWQGSFVLVSHDNTLLDAVTNSSWILRDQTLHSF 203
Cdd:cd03240 149 TTNLDeenieesLAEI--IEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGRQKSR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
125-157 |
5.72e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 5.72e-05
10 20 30
....*....|....*....|....*....|...
gi 1439757928 125 TLSGGQHTRLLLARALIRQPDLLLLDEPGNHLD 157
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
410-470 |
5.72e-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: 5.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1439757928 410 QKVSTLSGGERSRLLfVGLSLAR-YSLLLLDEPTNHLDMEGKAALAQTLRDY----PGGVLLVSHD 470
Cdd:cd03237 111 REVPELSGGELQRVA-IAACLSKdADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHD 175
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-470 |
5.81e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 44.75 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLL------------RLLWQQMNNASPLPGLR------------------------LHPRLHpgy 366
Cdd:COG3840 25 GERVAILGPSGAGKSTLLnliagflppdsgRILWNGQDLTALPPAERpvsmlfqennlfphltvaqniglgLRPGLK--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 367 ydqtlaqlpdeaslleaLTPfapsADTRKRALIAAGFGWARHSQ-KVSTLSGGERSRllfVGLS---LARYSLLLLDEPT 442
Cdd:COG3840 102 -----------------LTA----EQRAQVEQALERVGLAGLLDrLPGQLSGGQRQR---VALArclVRKRPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|..
gi 1439757928 443 NHLD----MEGKAALAQTLRDYPGGVLLVSHD 470
Cdd:COG3840 158 SALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
320-513 |
6.09e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 45.23 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQQMN------------NASPLPGLR----------------LHPRLHP--GYYDQ 369
Cdd:cd03289 27 ISPGQRVGLLGRTGSGKSTLLSAFLRLLNtegdiqidgvswNSVPLQKWRkafgvipqkvfifsgtFRKNLDPygKWSDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 370 TLAQLPDEASLLEALTPFAPSADTrkrALIAAGFgwarhsqkvsTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEG 449
Cdd:cd03289 107 EIWKVAEEVGLKSVIEQFPGQLDF---VLVDGGC----------VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 450 KAALAQTLRDYPGG--VLLVSHDRQLISEsCNRFWLIDSAGLTEWHSLEEVYARL----QAVAPAPDSRL 513
Cdd:cd03289 174 YQVIRKTLKQAFADctVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKshfkQAISPSDRLKL 242
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
412-470 |
6.12e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.92 E-value: 6.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 412 VSTLSGGE--RSRLLFVGLSLARYS-----LLLLDEPTNHLDMEGKAALAQTLRDYP---GGVLLVSHD 470
Cdd:PRK03695 124 VNQLSGGEwqRVRLAAVVLQVWPDInpagqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-470 |
6.19e-05 |
|
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: 44.38 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLWQ---------QMNNAsPLPGlrlhPRLHPGYYDQTLAQLP-----DEASL-LEAl 384
Cdd:cd03293 27 VEEGEFVALVGPSGCGKSTLLRIIAGlerptsgevLVDGE-PVTG----PGPDRGYVFQQDALLPwltvlDNVALgLEL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 tPFAPSADTRKRA--LIA----AGFGWARHSQkvstLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKAAL 453
Cdd:cd03293 101 -QGVPKAEARERAeeLLElvglSGFENAYPHQ----LSGGMRQRV-----ALARAlavdpDVLLLDEPFSALDALTREQL 170
|
170 180
....*....|....*....|.
gi 1439757928 454 AQTL----RDYPGGVLLVSHD 470
Cdd:cd03293 171 QEELldiwRETGKTVLLVTHD 191
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
416-530 |
7.27e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.10 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 416 SGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTL----RDYPGGVLLVSHDRQLISESCNRFwLIDSAGLT- 490
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITHDLGVVAGICDKV-LVMYAGRTm 241
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1439757928 491 EWHSLEEVYARlqavaPA-PDSRLALQSTPAgADDDEEALL 530
Cdd:PRK09473 242 EYGNARDVFYQ-----PShPYSIGLLNAVPR-LDAEGESLL 276
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
8-195 |
7.50e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.47 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 8 HALHVETAFGPLFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSVSLAGQCL-----------MARVEQhl 76
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldswrsrLAVVSQ-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 77 PETLHTQSLLQAVLAPLPaDAREAQRWLAERL---------LAQmGFTPAVMEqQTATLSGGQHTRLLLARALIRQPDLL 147
Cdd:PRK10789 397 TPFLFSDTVANNIALGRP-DATQQEIEHVARLasvhddilrLPQ-GYDTEVGE-RGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1439757928 148 LLDEPGNHLDLPTLLWLESFLQTW-QGSFVLVSHDNtlLDAVTNSSWIL 195
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWgEGRTVIISAHR--LSALTEASEIL 520
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
320-503 |
1.08e-04 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 43.72 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL-----------------WQQMNNAsplpGLRlHPRLHPGYYDQTLaqlpdeaSLLE 382
Cdd:cd03258 28 VPKGEIFGIIGRSGAGKSTLIRCInglerptsgsvlvdgtdLTLLSGK----ELR-KARRRIGMIFQHF-------NLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 ALTPF-----------APSADTRKRA--LIA-AGFGwARHSQKVSTLSGGERSRllfVGL--SLARY-SLLLLDEPTNHL 445
Cdd:cd03258 96 SRTVFenvalpleiagVPKAEIEERVleLLElVGLE-DKADAYPAQLSGGQKQR---VGIarALANNpKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 446 DMEGKAALAQTLRDYPG----GVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQ 503
Cdd:cd03258 172 DPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
319-503 |
1.30e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 43.73 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQM-----------NNASPLPglrLHPRLHPGyydqtLAQLPDEASLLEALTPF 387
Cdd:PRK10895 25 TVNSGEIVGLLGPNGAGKTTTFYMVVGIVprdagniiiddEDISLLP---LHARARRG-----IGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 --------------APSADTRKRALIAAGFGWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLD---MEGK 450
Cdd:PRK10895 97 dnlmavlqirddlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 451 AALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQ 503
Cdd:PRK10895 177 KRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
412-524 |
1.32e-04 |
|
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: 44.33 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 412 VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLR------DYPggVLLVSHDRQLISESCNRFWLID 485
Cdd:TIGR02142 129 PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLErlhaefGIP--ILYVSHSLQEVLRLADRVVVLE 206
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1439757928 486 SAGLTEWHSLEEVYARLQ-AVAPAPDSRLALQSTPAGADD 524
Cdd:TIGR02142 207 DGRVAAAGPIAEVWASPDlPWLAREDQGSLIEGVVAEHDQ 246
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
411-470 |
1.39e-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: 43.48 E-value: 1.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 411 KVSTLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKAALAQTLRD----YPGGVLLVSHD 470
Cdd:cd03299 126 KPETLSGGEQQRV-----AIARAlvvnpKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
407-499 |
1.73e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.50 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 407 RHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG--GVLLVSHDRQLISESCNRFWLI 484
Cdd:PRK14246 146 RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFL 225
|
90
....*....|....*
gi 1439757928 485 DSAGLTEWHSLEEVY 499
Cdd:PRK14246 226 YNGELVEWGSSNEIF 240
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
322-474 |
1.74e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 322 SGDRVAIMGRNGGGKSSLLRLLwqqmnnasplpgLRLHPRLHPGYYDQTLAQLPDEASLLEALTPFAPsadtrkraliaa 401
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL------------ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGG------------ 56
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1439757928 402 gfgwarhsqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGGVLLVSHDRQLI 474
Cdd:smart00382 57 ---------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
413-470 |
1.76e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 43.57 E-value: 1.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1439757928 413 STLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLR----DYPGGVLLVSHD 470
Cdd:PRK13650 139 ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKgirdDYQMTVISITHD 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
319-442 |
2.09e-04 |
|
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: 43.05 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKSSLLRLLWQQMNNAS--------PLPGLRLHPRLHPGyydqtLAQLPDEASLLEALT----- 385
Cdd:COG0410 25 EVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSgsirfdgeDITGLPPHRIARLG-----IGYVPEGRRIFPSLTveenl 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 ---PFAPSADTRKRALIAAGFGW-----ARHSQKVSTLSGGER-----SRLLfvglsLARYSLLLLDEPT 442
Cdd:COG0410 100 llgAYARRDRAEVRADLERVYELfprlkERRRQRAGTLSGGEQqmlaiGRAL-----MSRPKLLLLDEPS 164
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-157 |
2.38e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDG--TLAPTSGSVSLAG----QCLMARV----EQ---HLPETLHTQSL 85
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGrkTGGYIEGDIRISGfpkkQETFARIsgycEQndiHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 86 LQAVLAPLPADAREAQRwlaerllaqMGFTPAVME--------------QQTATLSGGQHTRLLLARALIRQPDLLLLDE 151
Cdd:PLN03140 975 IYSAFLRLPKEVSKEEK---------MMFVDEVMElveldnlkdaivglPGVTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
....*.
gi 1439757928 152 PGNHLD 157
Cdd:PLN03140 1046 PTSGLD 1051
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
414-484 |
2.69e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 414 TLSGGERSRL-LFVGLSLARY-----SLLLLDEPTNHLDMEGKA-ALAQTLRDYPGG----VLLVSHDRQLIsESCNRFW 482
Cdd:cd03240 115 RCSGGEKVLAsLIIRLALAETfgsncGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELV-DAADHIY 193
|
..
gi 1439757928 483 LI 484
Cdd:cd03240 194 RV 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
320-480 |
3.05e-04 |
|
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: 42.42 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL------------------WQQMNNASPLPGLRLHpRLHPGYYDQTLAQLP-----D 376
Cdd:COG4778 34 VAAGECVALTGPSGAGKSTLLKCIygnylpdsgsilvrhdggWVDLAQASPREILALR-RRTIGYVSQFLRVIPrvsalD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 377 --EASLLEALTPfAPSADTRKRALIAAgFGWARHSQKVS--TLSGGERSRLlfvglSLAR-----YSLLLLDEPTNHLDM 447
Cdd:COG4778 113 vvAEPLLERGVD-REEARARARELLAR-LNLPERLWDLPpaTFSGGEQQRV-----NIARgfiadPPLLLLDEPTASLDA 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1439757928 448 EGKAALAQTLRDY-PGGVLLVS--HDRQLISESCNR 480
Cdd:COG4778 186 ANRAVVVELIEEAkARGTAIIGifHDEEVREAVADR 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
319-503 |
3.10e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 319 RLRSGDRVAIMGRNGGGKS----SLLRLLWQQMNNASPLPG-LRLHPRLHPGYYDQTLAQL-----PDEASLLE----AL 384
Cdd:PRK10261 38 SLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMlLRRRSRQVIELSEQSAAQMrhvrgADMAMIFQepmtSL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 385 TPFAPSAD------------TRKRALIAAGF---------GWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTN 443
Cdd:PRK10261 118 NPVFTVGEqiaesirlhqgaSREEAMVEAKRmldqvripeAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTT 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 444 HLDMEGKAALAQTLR----DYPGGVLLVSHDRQLISESCNRFWLIDSAGLTEWHSLEEVYARLQ 503
Cdd:PRK10261 198 ALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
382-485 |
3.61e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.60 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 382 EALTPFA--PSADTRKRALIAAGFGWARHSQKVSTLSGGERSRllfVGLS--LARYS----LLLLDEPTNHLDMEGKAAL 453
Cdd:cd03271 135 EALEFFEniPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQR---IKLAkeLSKRStgktLYILDEPTTGLHFHDVKKL 211
|
90 100 110
....*....|....*....|....*....|....*
gi 1439757928 454 A---QTLRDYPGGVLLVSHDRQLIsESCNrfWLID 485
Cdd:cd03271 212 LevlQRLVDKGNTVVVIEHNLDVI-KCAD--WIID 243
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-195 |
3.74e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 21 NSLSFTLKKGDRIGLIGHNGCGKSTLLQvldgtlaptsgsvslagQCLMARVEQHLPETLHTQSLLQAV-LAPLpadare 99
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLPKFSRNKLIfIDQL------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 100 aqrwlaeRLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPD--LLLLDEPG---NHLDLPTLL-WLESFLQtwQG 173
Cdd:cd03238 69 -------QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPStglHQQDINQLLeVIKGLID--LG 139
|
170 180
....*....|....*....|...
gi 1439757928 174 -SFVLVSHDNTLLDAvtnSSWIL 195
Cdd:cd03238 140 nTVILIEHNLDVLSS---ADWII 159
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
393-485 |
3.74e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.24 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 393 TRKRALIAAGFGWARHSQKVSTLSGGE--RSRL---LFVGLSLARYsllLLDEPTNHLDMEGKAALAQT---LRDYPGGV 464
Cdd:cd03270 116 ERLGFLVDVGLGYLTLSRSAPTLSGGEaqRIRLatqIGSGLTGVLY---VLDEPSIGLHPRDNDRLIETlkrLRDLGNTV 192
|
90 100
....*....|....*....|.
gi 1439757928 465 LLVSHDRQLISESCnrfWLID 485
Cdd:cd03270 193 LVVEHDEDTIRAAD---HVID 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-157 |
3.98e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.33 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTS--GSVSLAGQCL----MAR---VEQ------HLP--ETLH 81
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPtkqiLKRtgfVTQddilypHLTvrETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 82 TQSLLQavlapLPAD-AREAQRWLAERLLAQMGFTPA----VMEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHL 156
Cdd:PLN03211 163 FCSLLR-----LPKSlTKQEKILVAESVISELGLTKCentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
.
gi 1439757928 157 D 157
Cdd:PLN03211 238 D 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
415-500 |
4.71e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.51 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPGG---VLLVSHDRQLISESCNRFWLIDSAGLTE 491
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
....*....
gi 1439757928 492 WHSLEEVYA 500
Cdd:PRK13641 226 HASPKEIFS 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
414-470 |
6.18e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 41.61 E-value: 6.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1439757928 414 TLSGGERSRLlFVGLSLA---RYslLLLDEPTNHLDMEGKAALAQTLR----DYPGGVLLVSHD 470
Cdd:COG4604 135 ELSGGQRQRA-FIAMVLAqdtDY--VLLDEPLNNLDMKHSVQMMKLLRrladELGKTVVIVLHD 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
320-474 |
8.56e-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: 41.30 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLLwqqmNNASPLPGLRLHPRLHP------GYYDQTLAQLPDEASL------------- 380
Cdd:cd03248 37 LHPGEVTALVGPSGSGKSTVVALL----ENFYQPQGGQVLLDGKPisqyehKYLHSKVSLVGQEPVLfarslqdniaygl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 381 ----LEALTPFAPSADTRKR-ALIAAGFgWARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQ 455
Cdd:cd03248 113 qscsFECVKEAAQKAHAHSFiSELASGY-DTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQ 191
|
170 180
....*....|....*....|.
gi 1439757928 456 TLRDYPGG--VLLVSHDRQLI 474
Cdd:cd03248 192 ALYDWPERrtVLVIAHRLSTV 212
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
412-470 |
1.18e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 412 VSTLSGGERSRllfvgLSLARYSLLLLDepTNHLDMEGKAALAQTLRDypggVLLVSHD 470
Cdd:COG0419 156 IETLSGGERLR-----LALADLLSLILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-485 |
1.23e-03 |
|
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: 40.56 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL-----------------WQQMNNASplpglRLHPRLHPGYYDQTLAqlpdeasLLE 382
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIvgllrpdsgevlidgedISGLSEAE-----LYRLRRRMGMLFQSGA-------LFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 383 ALTPFA------------PSADTRKRA---LIAAGFGWARHsQKVSTLSGGERSRLlfvglSLARY-----SLLLLDEPT 442
Cdd:cd03261 91 SLTVFEnvafplrehtrlSEEEIREIVlekLEAVGLRGAED-LYPAELSGGMKKRV-----ALARAlaldpELLLYDEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1439757928 443 NHLDMEGKAALAQTLRD----YPGGVLLVSHDRQLISESCNRFWLID 485
Cdd:cd03261 165 AGLDPIASGVIDDLIRSlkkeLGLTSIMVTHDLDTAFAIADRIAVLY 211
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-157 |
1.71e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 4 LLTAHALHVETAFGPLFNsLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAPTSGSV---------------SLAGQCL 68
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninniakpycTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 69 MARVEQHLPETLHTQSLLQAVLAPLPAdareAQRWLAERLLaqmgftpavMEQQTATLSGGQHTRLLLARALIRQPDLLL 148
Cdd:PRK13541 80 GLKLEMTVFENLKFWSEIYNSAETLYA----AIHYFKLHDL---------LDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
....*....
gi 1439757928 149 LDEPGNHLD 157
Cdd:PRK13541 147 LDEVETNLS 155
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
327-470 |
1.74e-03 |
|
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: 40.85 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 327 AIMGRNGGGKSSLLRLL-----------------WQQMNNASPLPglrLHPRlHPGYYDQtlaqlpdEASLLEALT---- 385
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIaglerpdsgrirlggevLQDSARGIFLP---PHRR-RIGYVFQ-------EARLFPHLSvrgn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 386 -----PFAPSADTRKR--ALIAA-GFGwarH--SQKVSTLSGGERSRllfVGLS---LARYSLLLLDEPTNHLDMEGKA- 451
Cdd:COG4148 98 llygrKRAPRAERRISfdEVVELlGIG---HllDRRPATLSGGERQR---VAIGralLSSPRLLLMDEPLAALDLARKAe 171
|
170 180
....*....|....*....|....*
gi 1439757928 452 ------ALAQTLrDYPggVLLVSHD 470
Cdd:COG4148 172 ilpyleRLRDEL-DIP--ILYVSHS 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
323-480 |
1.96e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.16 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRLL--WQQMNNASPLPGLRLHPRLHPGYYDQTLAQLPDEASLLEALTpfapsadtrKRALIA 400
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLgrHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMT---------VRELVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 401 AG----------FGWARHSQK----------------VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKA--- 451
Cdd:PRK10575 108 IGrypwhgalgrFGAADREKVeeaislvglkplahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVdvl 187
|
170 180 190
....*....|....*....|....*....|
gi 1439757928 452 ALAQTLRDYPG-GVLLVSHDRQLISESCNR 480
Cdd:PRK10575 188 ALVHRLSQERGlTVIAVLHDINMAARYCDY 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
105-152 |
2.30e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1439757928 105 AERLLAQMGF-TPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEP 152
Cdd:NF040905 384 AEEYRKKMNIkTPSV-FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
323-484 |
2.39e-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: 39.66 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 323 GDRVAIMGRNGGGKSSLLRL---LWQQMNNASPLPGLRLHPrlHPGYYDQTLAQLPDEASLLEALTpfapsadTRKRALI 399
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMlagLLEPDAGFATVDGFDVVK--EPAEARRRLGFVSDSTGLYDRLT-------ARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 400 AAGF-GWARHSQK-------------------VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRD 459
Cdd:cd03266 102 FAGLyGLKGDELTarleeladrlgmeelldrrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ 181
|
170 180
....*....|....*....|....*...
gi 1439757928 460 YPGG---VLLVSHDRQLISESCNRFWLI 484
Cdd:cd03266 182 LRALgkcILFSTHIMQEVERLCDRVVVL 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
97-179 |
2.64e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 97 AREAQRWLAERLLAQMGFTPAVmEQQTATLSGGQHTRLLLARALIRQPDLLLLDEPGNHLDLPTL--LWLESFLQTWQGS 174
Cdd:NF000106 117 SRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRneVWDEVRSMVRDGA 195
|
....*
gi 1439757928 175 FVLVS 179
Cdd:NF000106 196 TVLLT 200
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
327-485 |
2.72e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 40.09 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 327 AIMGRNGGGKSSLLRLLwqqMNNASPLPG--------LRLHPRLHPGYydqtlaqLPDEASL------LEALTPFA---- 388
Cdd:COG4152 31 GLLGPNGAGKTTTIRII---LGILAPDSGevlwdgepLDPEDRRRIGY-------LPEERGLypkmkvGEQLVYLArlkg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 389 -PSADTRKRAL-------IAagfGWARHsqKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY 460
Cdd:COG4152 101 lSKAEAKRRADewlerlgLG---DRANK--KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL 175
|
170 180
....*....|....*....|....*...
gi 1439757928 461 --PG-GVLLVSHDRQLISESCNRFWLID 485
Cdd:COG4152 176 aaKGtTVIFSSHQMELVEELCDRIVIIN 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
415-510 |
2.83e-03 |
|
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: 40.56 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVgLSLARYSLLLL-DEPTNHLDMEG----KAALAQTLRDYPGGVLLVSHDRQLISESCNRFWLIDSAGL 489
Cdd:TIGR03269 169 LSGGEKQRVVLA-RQLAKEPFLFLaDEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEI 247
|
90 100
....*....|....*....|.
gi 1439757928 490 TEWHSLEEVYARLQAVAPAPD 510
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGVSEVE 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
415-538 |
3.29e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.07 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDYPG----GVLLVSHDRQLISEscnrfwLIDS-AGL 489
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRK------LADRvAVM 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1439757928 490 TEWHSLEEVYARLQAVAPA-PDSRLALQSTPAGADDDEEALLARLIDLEQ 538
Cdd:PRK15134 231 QNGRCVEQNRAATLFSAPThPYTQKLLNSEPSGDPVPLPEPASPLLDVEQ 280
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
415-469 |
3.29e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 39.65 E-value: 3.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKA---ALAQTLRD-YPGGVLLVSH 469
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDeilNKIKELHKeYNMTIILVSH 203
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
410-470 |
3.35e-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: 38.71 E-value: 3.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1439757928 410 QKVStLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY----PGGVLLVSHD 470
Cdd:cd03222 68 QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHD 131
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
412-485 |
3.51e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 39.69 E-value: 3.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1439757928 412 VSTLSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY--PGG--VLLVSHDRQLISESCNRFWLID 485
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGttILLTSHDMDDIEALCDRVIVID 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
320-491 |
3.97e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.19 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 320 LRSGDRVAIMGRNGGGKSSLLRLL---WQQMNNASPLPGLRLHprlhpGYYDQTL-------AQLPD--EASLLEALTPF 387
Cdd:PRK11160 363 IKAGEKVALLGRTGCGKSTLLQLLtraWDPQQGEILLNGQPIA-----DYSEAALrqaisvvSQRVHlfSATLRDNLLLA 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 388 APSADTRKRALIAAGFGWARHSQKVS-----------TLSGGERSRLlfvglSLARY-----SLLLLDEPTNHLDMEGKA 451
Cdd:PRK11160 438 APNASDEALIEVLQQVGLEKLLEDDKglnawlgeggrQLSGGEQRRL-----GIARAllhdaPLLLLDEPTEGLDAETER 512
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1439757928 452 ALAQTLRDYPGG--VLLVSHdRQLISESCNRFWLIDSAGLTE 491
Cdd:PRK11160 513 QILELLAEHAQNktVLMITH-RLTGLEQFDRICVMDNGQIIE 553
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
393-485 |
5.00e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 393 TRKRALIAAGFGWARHSQKVSTLSGGERSRL-----LFVGLSLARYsllLLDEPTNHLDMEGKAALAQT---LRDYPGGV 464
Cdd:TIGR00630 467 ERLGFLIDVGLDYLSLSRAAGTLSGGEAQRIrlatqIGSGLTGVLY---VLDEPSIGLHQRDNRRLINTlkrLRDLGNTL 543
|
90 100
....*....|....*....|.
gi 1439757928 465 LLVSHDRQLISESCnrfWLID 485
Cdd:TIGR00630 544 IVVEHDEDTIRAAD---YVID 561
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
415-501 |
6.26e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 38.84 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY--PGG--VLLVSHDrqlISE--SCNRFWLIDSAG 488
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGitVLSITHD---LDEaaQADRVIVMNKGE 217
|
90
....*....|...
gi 1439757928 489 LTEWHSLEEVYAR 501
Cdd:PRK13635 218 ILEEGTPEEIFKS 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
307-484 |
6.29e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 38.47 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 307 PGQPSLFTTGVaRLRSGDRVAIMGRNGGGKSSLLRLLWQQM---------NNASPLPGLRLHPRLHPGYYDQTLAQLP-- 375
Cdd:cd03290 12 SGLATLSNINI-RIPTGQLTMIVGQVGCGKSSLLLAILGEMqtlegkvhwSNKNESEPSFEATRSRNRYSVAYAAQKPwl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 376 DEASLLEALTPFAPSADTRKRALIAA----------GFG-WARHSQKVSTLSGGERSRLLFVGLSLARYSLLLLDEPTNH 444
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDAcslqpdidllPFGdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1439757928 445 LDMEGKAALAQT-----LRDYPGGVLLVSHDRQLISESCnrfWLI 484
Cdd:cd03290 171 LDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYLPHAD---WII 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-157 |
8.87e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.32 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 19 LFNSLSFTLKKGDRIGLIGHNGCGKSTLLQVLDGTLAP---TSGSVSLAGQCL---MAR----VEQ---HLPETLHTQSL 85
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLdssFQRsigyVQQqdlHLPTSTVRESL 857
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1439757928 86 LQAVLAPLPADA--REAQRWLAE--RLLAQMGFTPAVMEQQTATLSGGQHTRLLLARALIRQPDLLL-LDEPGNHLD 157
Cdd:TIGR00956 858 RFSAYLRQPKSVskSEKMEYVEEviKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
415-508 |
9.54e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 38.13 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1439757928 415 LSGGERSRLLFVGLSLARYSLLLLDEPTNHLDMEGKAALAQTLRDY--PGGVLLVS-HDRQLISESCNRFWLIDSAGLTE 491
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKIIK 217
|
90
....*....|....*..
gi 1439757928 492 WHSLEEVYARLQAVAPA 508
Cdd:PRK13639 218 EGTPKEVFSDIETIRKA 234
|
|
|