|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-514 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 645.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 4 MQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVP-GSDRRAVD 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPlDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 83 YVLDGDAELRDLQRRLEQAN--------DGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMR 154
Cdd:COG0488 81 TVLDGDAELRALEAELEELEaklaepdeDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 155 LGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALYAGSYTHAEAK 234
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 235 RAEAIVQSEAAAARVAAERAHLEDFVRRFRAKASKARQAQSRLKRLERMDEVAVIRAARPIHLEIPTPGRLPDPLLALDH 314
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 315 AEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQrEQLDLEASPLVH 394
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 395 LQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYA 474
Cdd:COG0488 400 LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 648648866 475 GGLVVVAHDRELLARVCDRFWTVEAGRLSPFDGDLDDYAR 514
Cdd:COG0488 480 GTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-621 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 580.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVPGSDRRA 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDGDAELRDLQRRLEQA---NDGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGL 157
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDAnerNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALYAGSYTHAEAKRAE 237
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 238 AIVQSEAAAARVAAERAHLEDFVRRFRAKASKARQAQSRLKRLERMDEVAVIRAARPIHLEIPTPGRLPDPLLALDHAEV 317
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 318 CTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQREQLDLEASPLVHLQR 397
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 398 QDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGL 477
Cdd:PRK10636 401 LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 478 VVVAHDRELLARVCDRFWTVEAGRLSPFDGDLDDYARALQARQREAARSAAETPPQAASDAPVRSQKERRQqaAQKRAAL 557
Cdd:PRK10636 481 VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENNANSAQARKDQKRRE--AELRTQT 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 558 RPLQQRADRAERDCSQTQERLQTLESELADPDLYAGDHAERLAALTREQGELCARLEALEAEWM 621
Cdd:PRK10636 559 QPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWL 622
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-518 |
2.31e-109 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 345.31 E-value: 2.31e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALqgelALDAgeIEQ-PPEWVVAHLPQEVPGSDRRA 80
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM----AMHA--IDGiPKNCQILHVEQEVVGDDTTA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDGDAEL--------------RDLQRRLEQANDGAEQ-------------ARLYAALEAIDGWSAEARARRLLAGL 133
Cdd:PLN03073 252 LQCVLNTDIERtqlleeeaqlvaqqRELEFETETGKGKGANkdgvdkdavsqrlEEIYKRLELIDAYTAEARAASILAGL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 134 GFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHV 213
Cdd:PLN03073 332 SFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 214 AHIERGTIALYAGSYTHAEAKRAEAIVQSEAAAARVAAERAHLEDFVRRFRAKASKARQAQSRLKRLERMDEVAVIRAAR 293
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDP 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 294 PIHLEIPTPGRLPD-PLLALDHAEV-CTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPA 371
Cdd:PLN03073 492 DYKFEFPTPDDRPGpPIISFSDASFgYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 372 LQVGYFAQHQREQLDLEASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLL 451
Cdd:PLN03073 572 VRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 452 DEPTNHLDLDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSPFDGDLDDYARALQA 518
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTLQS 718
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-514 |
1.90e-97 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 308.74 E-value: 1.90e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVPG-SDRR 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAfEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 80 AVDYVLDGDAEL------RDLQRRLEQAN--DGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGW 151
Cdd:PRK15064 81 VLDTVIMGHTELwevkqeRDRIYALPEMSeeDGMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 152 RMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALYAGSYTH- 230
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEy 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 231 -------------AEAKRAEAIVQseaaaarvaaerahLEDFVRRFRAKASKARQAQSRLKRLER--MDEVAV------- 288
Cdd:PRK15064 241 mtaatqarerllaDNAKKKAQIAE--------------LQSFVSRFSANASKAKQATSRAKQIDKikLEEVKPssrqnpf 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 289 IR--AARPIHleiptpgRLPDPLLALDHAevcTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGER 366
Cdd:PRK15064 307 IRfeQDKKLH-------RNALEVENLTKG---FDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 367 RVDPALQVGYFAQHQREQLDLEASPLVHL-QRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQA 445
Cdd:PRK15064 377 KWSENANIGYYAQDHAYDFENDLTLFDWMsQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 446 PSLLLLDEPTNHLDLDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSPFDGDLDDYAR 514
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLR 525
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-524 |
3.81e-85 |
|
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: 277.20 E-value: 3.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQGelaLDA---GEIEQPPEWVVAHLPQEVPGSDRRAV-DYVLDG 87
Cdd:TIGR03719 17 KKEIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKdfnGEARPQPGIKVGYLPQEPQLDPTKTVrENVEEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 88 DAELRDLQRRLEQAND------------GAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAerPMRDFSGGWRMRL 155
Cdd:TIGR03719 93 VAEIKDALDRFNEISAkyaepdadfdklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDA--DVTKLSGGERRRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 156 GLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALYAGSYTH-AEAK 234
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSwLEQK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 235 RAEAIVQSEAAAARVAAERAHLEdFVRrfraKASKARQAQS--RLKRLERMDEVAVIRAARPIHLEIPTPGRLPDPLLAL 312
Cdd:TIGR03719 251 QKRLEQEEKEESARQKTLKRELE-WVR----QSPKGRQAKSkaRLARYEELLSQEFQKRNETAEIYIPPGPRLGDKVIEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 313 DHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQhQREQLDLEAS-- 390
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ-SRDALDPNKTvw 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 391 -----PLVHLQ---RQDPRaeeqrlRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDM 462
Cdd:TIGR03719 405 eeisgGLDIIKlgkREIPS------RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 463 REALAEALENYAGGLVVVAHDRELLARVCDRFWTVEA-GRLSPFDGDLDDYARALQARQREAA 524
Cdd:TIGR03719 479 LRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGdSHVEWFEGNFSEYEEDKKRRLGEDA 541
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-618 |
1.79e-84 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 277.60 E-value: 1.79e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVPgsdrRA 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPP----RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 V-----DYVLDGDAELRDLQRRLEQANDGAEQ----------ARLYAALEAIDGWSAEARARRLLAGLGFapaDAERPMR 145
Cdd:PRK11147 79 VegtvyDFVAEGIEEQAEYLKRYHDISHLVETdpseknlnelAKLQEQLDHHNLWQLENRINEVLAQLGL---DPDAALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALYA 225
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 226 GSY-----THAEAKRAEAIvQSeaaaarvaaerahlEDFVRRF--------------------RAKASKARQaQSRLKRL 280
Cdd:PRK11147 236 GNYdqyllEKEEALRVEEL-QN--------------AEFDRKLaqeevwirqgikarrtrnegRVRALKALR-RERSERR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 281 ERMDEV--AVIRAARpihleiptPGRLpdpLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGE 358
Cdd:PRK11147 300 EVMGTAkmQVEEASR--------SGKI---VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 359 LLPTAGERRVDPALQVGYFAQHqREQLDLEASPLVHLQ--RQD------PRAEEQRLRNFLggmgFPGDKADGPVGQCSG 430
Cdd:PRK11147 369 LQADSGRIHCGTKLEVAYFDQH-RAELDPEKTVMDNLAegKQEvmvngrPRHVLGYLQDFL----FHPKRAMTPVKALSG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 431 GERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEA-GRLSPFDGDL 509
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGnGKIGRYVGGY 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 510 DDyaralqARQREAARSAAETPPQAASDAPVRSQKERRQQAAQKRA--ALRPLQQRADRAErdcsQTQERLQTLESELAD 587
Cdd:PRK11147 524 HD------ARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSKKLSykLQRELEQLPQLLE----DLEAEIEALQAQVAD 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 648648866 588 PDLYAGDHAE---RLAALTREQGEL---CARLEALEA 618
Cdd:PRK11147 594 ADFFSQPHEQtqkVLADLADAEQELevaFERWEELEA 630
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-491 |
3.20e-78 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 258.90 E-value: 3.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQGelaLDA---GEIEQPPEWVVAHLPQEVPGSDRRAV-DYVLDG 87
Cdd:PRK11819 19 KKQIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKefeGEARPAPGIKVGYLPQEPQLDPEKTVrENVEEG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 88 DAELRDLQRRLEQ-----ANDGA-------EQARLYAALEAIDGWSAEARARRLLAGLGFAPADAerPMRDFSGGWRMRL 155
Cdd:PRK11819 95 VAEVKAALDRFNEiyaayAEPDAdfdalaaEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDA--KVTKLSGGERRRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 156 GLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALYAGSY-THAEAK 234
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYsSWLEQK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 235 RAEAIVQSEAAAARVAAERAHLEdFVRrfraKASKARQAQS--RLKRLERMDEVAVIRAARPIHLEIPTPGRLPDPLLAL 312
Cdd:PRK11819 253 AKRLAQEEKQEAARQKALKRELE-WVR----QSPKARQAKSkaRLARYEELLSEEYQKRNETNEIFIPPGPRLGDKVIEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 313 DHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHqREQLDLEAS-- 390
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS-RDALDPNKTvw 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 391 -------PLVHL-QRQDP-RAeeqrlrnFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:PRK11819 407 eeisgglDIIKVgNREIPsRA-------YVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
490 500 510
....*....|....*....|....*....|
gi 648648866 462 MREALAEALENYAGGLVVVAHDRELLARVC 491
Cdd:PRK11819 480 TLRALEEALLEFPGCAVVISHDRWFLDRIA 509
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-220 |
1.52e-53 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 179.95 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQevpgsdrrav 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyvldgdaelrdlqrrleqandgaeqarlyaaleaidgwsaeararrllaglgfapadaerpmrdFSGGWRMRLGLARTL 161
Cdd:cd03221 71 -----------------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGT 220
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-229 |
2.10e-51 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 185.65 E-value: 2.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEvpgsdrRA 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH------QE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdyVLDGDAELRDLqrrLEQANDGAEqarlyaaleaidgwsaEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLART 160
Cdd:COG0488 389 ---ELDPDKTVLDE---LRDGAPGGT----------------EQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALYAGSYT 229
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYD 515
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
320-569 |
2.29e-45 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 168.70 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQREQLDLEA--------SP 391
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVldtvldgdAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 392 LVHLQRQDPRAE----------------------------EQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIW 443
Cdd:COG0488 89 LRALEAELEELEaklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 444 QAPSLLLLDEPTNHLDLDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSPFDGDLDDYARALQARQREA 523
Cdd:COG0488 169 SEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 648648866 524 ARSAAetppqaasdapvRSQKERRQQ-------AAQKRAALRPlQQRADRAER 569
Cdd:COG0488 249 AAAYA------------KQQKKIAKEeefirrfRAKARKAKQA-QSRIKALEK 288
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
320-501 |
8.13e-43 |
|
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: 150.68 E-value: 8.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFaqhqrEQLdleasplvhlqrqd 399
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYF-----EQL-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 400 praeeqrlrnflggmgfpgdkadgpvgqcSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGLVV 479
Cdd:cd03221 72 -----------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVIL 122
|
170 180
....*....|....*....|..
gi 648648866 480 VAHDRELLARVCDRFWTVEAGR 501
Cdd:cd03221 123 VSHDRYFLDQVATKIIELEDGK 144
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-227 |
2.45e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.79 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewVVAHLPQEVPGSDRRAV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR-----VLGEDVARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGDAELRDLqrrleqanDGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTL 161
Cdd:COG1131 76 GYVPQEPALYPDL--------TVRENLRFFARLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARY--PGTVIVIA-HDRRFLDSVCTHVAHIERGTIaLYAGS 227
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVAIIDKGRI-VADGT 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-209 |
7.27e-31 |
|
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: 119.89 E-value: 7.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWVVAHLPQEVPGSDRRA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV-----LWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDGDAELRDLqrrleqanDGAEQARLYAALEAIDGwsAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLART 160
Cdd:COG4133 77 LAYLGHADGLKPEL--------TVRENLRFWAALYGLRA--DREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETILWLEDWLARYP---GTVIVIAHDRRFLDSV 209
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-221 |
1.95e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI---------EQPPEWV--VAHLP 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsaMPPPEWRrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 71 QE-VPGSDRravdyVldGDAELRDLQRRLEQANdgaeqarlyaaleaidgwsaEARARRLLAGLGFAPADAERPMRDFSG 149
Cdd:COG4619 81 QEpALWGGT-----V--RDNLPFPFQLRERKFD--------------------RERALELLERLGLPPDILDKPVERLSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 150 GWRMRLGLARTLMTRSDLLLLDEPTNHLDVET----ILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:COG4619 134 GERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-221 |
9.02e-30 |
|
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: 115.57 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewVVAHLPQEVPGSDRRAV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-----VLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLdgdaelrdlqrrleqandgaEQARLYAALeaidgwsaeaRARRLLaglgfapadaerpmrDFSGGWRMRLGLARTL 161
Cdd:cd03230 76 GYLP--------------------EEPSLYENL----------TVRENL---------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARY---PGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-516 |
5.65e-29 |
|
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: 121.16 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 7 IELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGEL---ALDAGEIeqppewvvahlpqEVPGSDRRAVDY 83
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEV-------------LLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 84 VLDGDAELRDLQRRLEQANDG--AEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAERPMrDFSGGWRMRLGLARTL 161
Cdd:COG1123 79 ALRGRRIGMVFQDPMTQLNPVtvGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-QLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 162 MTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPG-TVIVIAHDRRFLDSVCTHVAHIERGTIalyagsythAEAKRAE 237
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI---------VEDGPPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 238 AIvqseaaaarvaaerahledfvrrfrakaskarqaqsrlkrLERMDEVAVIRAARPIHLEIPTPGRLPDPLLALDHA-- 315
Cdd:COG1123 229 EI----------------------------------------LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLsk 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 316 --EVCTGERVR-LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD----PAL----------QVGYFA 378
Cdd:COG1123 269 ryPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdlTKLsrrslrelrrRVQMVF 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 379 QHQREQLD-----LE--ASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLL 451
Cdd:COG1123 349 QDPYSSLNprmtvGDiiAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLIL 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 452 DEPTNHLDLDMREALAEALENYA----GGLVVVAHDRELLARVCDRFWTVEAGRL----SP---FDGDLDDYARAL 516
Cdd:COG1123 429 DEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHDLAVVRYIADRVAVMYDGRIvedgPTeevFANPQHPYTRAL 504
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.20e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPPEWV---VAHLPQEVP 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgKPPRRArrrIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 75 gSDR----RAVDYVLDGdaelRDLQRRLEQANDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGG 150
Cdd:COG1121 86 -VDWdfpiTVRDVVLMG----RYGRRGLFRRPSRADREAVDEALERVG-----------LEDL------ADRPIGELSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 151 WRMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATeeaLYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-238 |
3.61e-28 |
|
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: 113.41 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeQPPEWVVAHLPQEVpgsdRRA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-LIDGEDVRKEPREA----RRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDgdaelrdlQRRLEQANDGAEQARLYAALEAIDGWSAEARARRLLAGLGFaPADAERPMRDFSGGWRMRLGLART 160
Cdd:COG4555 76 IGVLPD--------ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETILWLED---WLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIaLYAGSYTHAEAKRAE 237
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV-VAQGSLDELREEIGE 225
|
.
gi 648648866 238 A 238
Cdd:COG4555 226 E 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
310-502 |
4.13e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.22 E-value: 4.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD---------PAL--QVGYFa 378
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkplsamppPEWrrQVAYV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 379 qHQREQLdLEASPLVHLQR----QDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEP 454
Cdd:COG4619 80 -PQEPAL-WGGTVRDNLPFpfqlRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648648866 455 TNHLDLDMREALAEALENYA----GGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:COG4619 158 TSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-235 |
9.63e-28 |
|
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: 117.73 E-value: 9.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEvpgsdRRAv 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS-----RDA- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyvLDGDAELrdlqrrLEQANDGAEQARLyaaleaidgWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTL 161
Cdd:TIGR03719 397 ---LDPNKTV------WEEISGGLDIIKL---------GKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIE-RGTIALYAGSYTHAEAKR 235
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEEDK 533
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-175 |
1.73e-26 |
|
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: 105.42 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppEWVVAHLPQEVPGSDRRAVDYVLDGDAELRDLQr 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI----LLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLT- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 97 rleqandGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAERP---MRDFSGGWRMRLGLARTLMTRSDLLLLDEP 173
Cdd:pfam00005 76 -------VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 648648866 174 TN 175
Cdd:pfam00005 149 TA 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-213 |
7.38e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 112.13 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEvpgsdRRAvdyvLDGDAEL 91
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS-----RDA----LDPNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 92 rdlqrrLEQANDGAEQARLyaaleaidGwSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLD 171
Cdd:PRK11819 406 ------WEEISGGLDIIKV--------G-NREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLD 470
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 648648866 172 EPTNHLDVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHV 213
Cdd:PRK11819 471 EPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI 512
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-222 |
1.22e-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: 104.92 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 3 RMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPPEWV---VAHLPQeVPGS 76
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgKPLEKErkrIGYVPQ-RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 DR----RAVDYVLDGdaelRDLQRRLEQANDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGWR 152
Cdd:cd03235 80 DRdfpiSVRDVVLMG----LYGHKGLFRRLSKADKAKVDEALERVG-----------LSEL------ADRQIGELSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 153 MRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPGTVIVIAHDrrfLDSV---CTHVAHIERGTIA 222
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTqedIYELLRELRREGMTILVVTHD---LGLVleyFDRVLLLNRTVVA 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-222 |
4.32e-25 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 104.74 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI--------EQPPEWV---VAHL 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaSLSRRELarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 70 PQEVPGSDR-RAVDYVLDGdaelrdlqrrleqandgaeqarLYAALEAIDGWSAE--ARARRLLAGLGFApADAERPMRD 146
Cdd:COG1120 81 PQEPPAPFGlTVRELVALG----------------------RYPHLGLFGRPSAEdrEAVEEALERTGLE-HLADRPVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 147 FSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD----VETILWLEDWLARYPGTVIVIAHD----RRFldsvCTHVAHIER 218
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHDlnlaARY----ADRLVLLKD 213
|
....
gi 648648866 219 GTIA 222
Cdd:COG1120 214 GRIV 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-220 |
5.69e-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: 101.55 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 3 RMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqevpgsdrravd 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 83 yvldgdaelrdlqrrleqandgaeqarlyaaleaIDG-WSAEARARRLLAGLGFAPadaerpmrDFSGGWRMRLGLARTL 161
Cdd:cd00267 58 ----------------------------------IDGkDIAKLPLEELRRRIGYVP--------QLSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARYPG---TVIVIAHDRRFLDSVCTHVAHIERGT 220
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-221 |
6.07e-25 |
|
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: 103.07 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQ-PPEWVVAHLPQEVPGSdrra 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRIGA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdyVLDGDAELRDLQRRleqandgaEQARLYAALEAIDgwsaEARARRLLAGLGFApADAERPMRDFSGGWRMRLGLART 160
Cdd:cd03268 77 ---LIEAPGFYPNLTAR--------ENLRLLARLLGIR----KKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETILWLEDWLARYP---GTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
320-501 |
1.28e-24 |
|
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: 100.40 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPalqvgyfaqhqreqLDLEASPLVHLQRQd 399
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG--------------KDIAKLPLEELRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 400 praeeqrlrnflggMGFpgdkadgpVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--- 476
Cdd:cd00267 75 --------------IGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgrt 132
|
170 180
....*....|....*....|....*
gi 648648866 477 LVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:cd00267 133 VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-222 |
3.45e-23 |
|
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: 99.11 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRG----RQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvvahLPQEV 73
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgRP-------VTRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 74 PGSDRRAVDYVL-DGDAELrDLQRRLEQAndgaeqarLYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWR 152
Cdd:COG1124 74 RKAFRRRVQMVFqDPYASL-HPRHTVDRI--------LAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 153 MRLGLARTLMTRSDLLLLDEPTNHLDVET---IL-WLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:COG1124 145 QRVAIARALILEPELLLLDEPTSALDVSVqaeILnLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
3.78e-23 |
|
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: 103.69 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRR--GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---------QPPEW--VVAH 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 69 LPQEVpgsdrravdYVLDGDaeLRD-LqrRLeqANDGAEQARLYAALEA--IDGWsaearARRLLAGLGFAPADAERPmr 145
Cdd:COG4987 414 VPQRP---------HLFDTT--LREnL--RL--ARPDATDEELWAALERvgLGDW-----LAALPDGLDTWLGEGGRR-- 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 146 dFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETI-LWLEDWLARYPG-TVIVIAHDRRFLDSVcTHVAHIERGTIA 222
Cdd:COG4987 472 -LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLERM-DRILVLEDGRIV 548
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-220 |
3.87e-22 |
|
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: 94.84 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 11 RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVpgsdRRAVDYVLDgDAE 90
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----RRKVGLVFQ-NPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 LRDLQRRLEQ------ANDGAEQARlyaaleaidgwsAEARARRLLAGLGFApADAERPMRDFSGGWRMRLGLARTLMTR 164
Cdd:cd03225 86 DQFFGPTVEEevafglENLGLPEEE------------IEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 165 SDLLLLDEPTNHLDVETILWLEDWLARYPG---TVIVIAHDRRFLDSVCTHVAHIERGT 220
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-221 |
4.29e-22 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 94.04 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 5 QDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqevpgsdrravdyv 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 LDGDaELRDLQRRleqandgaEQARLYA----ALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGWRMRLGLART 160
Cdd:cd03214 58 LDGK-DLASLSPK--------ELARKIAyvpqALELLG-----------LAHL------ADRPFNELSGGERQRVLLARA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 161 LMTRSDLLLLDEPTNHLD----VETILWLEDwLARYPG-TVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDiahqIELLELLRR-LARERGkTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
320-529 |
4.67e-22 |
|
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: 100.39 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQ--------REQLDLEASP 391
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPqldptktvRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 392 LVHLQRQ---------------DPRAEEQ-RLRNFLGGMGF-----------------PGDkadGPVGQCSGGERVRLVL 438
Cdd:TIGR03719 96 IKDALDRfneisakyaepdadfDKLAAEQaELQEIIDAADAwdldsqleiamdalrcpPWD---ADVTKLSGGERRRVAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 439 ALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGLVVVAHDRELLARVCDrfWTVEA--GRLSPFDGDLDDYARAL 516
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILELdrGRGIPWEGNYSSWLEQK 250
|
250
....*....|...
gi 648648866 517 QARQREAARSAAE 529
Cdd:TIGR03719 251 QKRLEQEEKEESA 263
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
319-501 |
1.14e-21 |
|
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: 93.69 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 319 TGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP-----------ALQVGYFAQHQREQL-- 385
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelRRKVGLVFQNPDDQFfg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 -----DLEASPlvhLQRQDPRAE-EQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD 459
Cdd:cd03225 91 ptveeEVAFGL---ENLGLPEEEiEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 648648866 460 LDMREALAEALENYAG---GLVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:cd03225 167 PAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
309-502 |
3.36e-21 |
|
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: 93.18 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 309 LLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE-----------RRVDPALQVGYF 377
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlaslSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 378 AQHQREQLDLEA------------SPLVHLQRQDPRAEEQRLRNFlgGMgfpGDKADGPVGQCSGGERVRLVLALLIWQA 445
Cdd:COG1120 81 PQEPPAPFGLTVrelvalgryphlGLFGRPSAEDREAVEEALERT--GL---EHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 446 PSLLLLDEPTNHLDLDMREALAEALENYAG----GLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARergrTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
311-502 |
6.08e-21 |
|
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: 90.57 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 311 ALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP-----------ALQVGYFAQ 379
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlaslspkelARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 380 hQREQLDLEasplvhlqrqdpraeeqrlrnflggmgfpgDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD 459
Cdd:cd03214 81 -ALELLGLA------------------------------HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648648866 460 LDMREALAEALENYA---GGLVVVA-HDRELLARVCDRFWTVEAGRL 502
Cdd:cd03214 130 IAHQIELLELLRRLArerGKTVVMVlHDLNLAARYADRVILLKDGRI 176
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-202 |
7.95e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVPGSDR---RAVDYVLDGD 88
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlplTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 89 AELRDLQRRLeqanDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGWRMRLGLARTLMTRSDLL 168
Cdd:NF040873 83 WARRGLWRRL----TRDDRAAVDDALERVG-----------LADL------AGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 648648866 169 LLDEPTNHLDVETILWLEDWLARYPG---TVIVIAHD 202
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-221 |
9.80e-21 |
|
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: 90.78 E-value: 9.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 3 RMQDIELRRGRQI-LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVPGSDRRAV 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGDAELRDLQRRLEQANDGAEQARlyAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGWRMRLGLARTL 161
Cdd:cd03226 81 DYQLFTDSVREELLLGLKELDAGNEQAE--TVLKDLD-----------LYAL------KERHPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDW---LARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
312-493 |
1.06e-20 |
|
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: 90.67 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 312 LDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPA------LQVGYFAQhqREQL 385
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerKRIGYVPQ--RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 DLE---------ASPLVH---LQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDE 453
Cdd:cd03235 80 DRDfpisvrdvvLMGLYGhkgLFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 454 PTNHLDLDMREALAEALENYAG---GLVVVAHDRELLARVCDR 493
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDR 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
2.47e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 94.82 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRR-GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---------QPPEW--VVAHL 69
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdlDPASWrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 70 PQE---VPGSdrravdyvldgdaeLRD-LqrRLeqANDGAEQARLYAALEAidgwsaeARARRLLAGLgfaPADAERPM- 144
Cdd:COG4988 417 PQNpylFAGT--------------IREnL--RL--GRPDASDEELEAALEA-------AGLDEFVAAL---PDGLDTPLg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 145 ---RDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAHDRRFLDSvCTHVAHIERG 219
Cdd:COG4988 469 eggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQ-ADRILVLDDG 547
|
...
gi 648648866 220 TIA 222
Cdd:COG4988 548 RIV 550
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
325-456 |
5.66e-20 |
|
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: 86.93 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD-----------PALQVGYFAQHQ--------REQL 385
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQDPqlfprltvRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 386 DlEASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTN 456
Cdd:pfam00005 81 R-LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-222 |
6.54e-20 |
|
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: 94.13 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELR--RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPqevPGS 76
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgID----LRQID---PAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 DRRAVDYVLDgDAEL--RDLQRRLEQANDGAEQARLYAALEaidgwsaeararrlLAGL-GFApadAERPM--------- 144
Cdd:COG2274 547 LRRQIGVVLQ-DVFLfsGTIRENITLGDPDATDEEIIEAAR--------------LAGLhDFI---EALPMgydtvvgeg 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 145 -RDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---IL-----WLEDWlarypgTVIVIAHDRRFLDSvCTHVAH 215
Cdd:COG2274 609 gSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiILenlrrLLKGR------TVIIIAHRLSTIRL-ADRIIV 681
|
....*..
gi 648648866 216 IERGTIA 222
Cdd:COG2274 682 LDKGRIV 688
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
214-294 |
1.14e-19 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 83.78 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 214 AHIERGTIALYAGSYTHAEAKRAEAIVQSEAAAARVAAERAHLEDFVRRFRAKASKARQAQSRLKRLERMDEVAVIRAAR 293
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
.
gi 648648866 294 P 294
Cdd:pfam12848 81 P 81
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
320-554 |
1.35e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 92.49 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQhqrE-QLDLE---------- 388
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ---EpQLDPEktvrenveeg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 389 ASPLVHLQRQ---------------DPRAEEQ-RLRNFLggmgfpgDKADG---------------------PVGQCSGG 431
Cdd:PRK11819 95 VAEVKAALDRfneiyaayaepdadfDALAAEQgELQEII-------DAADAwdldsqleiamdalrcppwdaKVTKLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 432 ERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGLVVVAHDRELLARVCDrfWTVEA--GRLSPFDGDL 509
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILELdrGRGIPWEGNY 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 510 DDY-----------ARALQARQR------EAARSAAETpPQAASDAPVRSQKERRQQAAQKR 554
Cdd:PRK11819 246 SSWleqkakrlaqeEKQEAARQKalkrelEWVRQSPKA-RQAKSKARLARYEELLSEEYQKR 306
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
320-511 |
2.36e-19 |
|
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: 87.61 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------RRVDPAL--QVGYFAQHQ-------- 381
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidgedvRKEPREArrQIGVLPDERglydrltv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLEASplvhLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:COG4555 92 RENIRYFAE----LYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648648866 462 MREALAEALENYA--GGLVVVA-HDRELLARVCDRFWTVEAGRLsPFDGDLDD 511
Cdd:COG4555 167 ARRLLREILRALKkeGKTVLFSsHIMQEVEALCDRVVILHKGKV-VAQGSLDE 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-198 |
2.70e-19 |
|
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: 87.83 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGeieqppewvvahlpQEVpgsdrra 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG--------------NDV------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdYVLD---GDAELRDLQRR-------LEQANDGAEQAR------------LYAALEAIDgwsaEARARRLLAGLGFApA 138
Cdd:COG1119 62 --RLFGerrGGEDVWELRKRiglvspaLQLRFPRDETVLdvvlsgffdsigLYREPTDEQ----RERARELLELLGLA-H 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 139 DAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDW---LARYPGTVIV 198
Cdd:COG1119 135 LADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALldkLAAEGAPTLV 197
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-221 |
2.91e-19 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 87.34 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWVvahLPQEVPGSDRRa 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI-----LV---DGQDITGLSEK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdyvldgdaELRDLQRR---LEQanDGA----------------EQARLYAALeaidgwsAEARARRLLAGLGFAPADAE 141
Cdd:COG1127 76 ---------ELYELRRRigmLFQ--GGAlfdsltvfenvafplrEHTDLSEAE-------IRELVLEKLELVGLPGAADK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 142 RPmRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD-------VETILWLEDwlaRYPGTVIVIAHDRRFLDSVCTHVA 214
Cdd:COG1127 138 MP-SELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsaviDELIRELRD---ELGLTSVVVTHDLDSAFAIADRVA 213
|
....*..
gi 648648866 215 HIERGTI 221
Cdd:COG1127 214 VLADGKI 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
320-508 |
5.79e-19 |
|
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: 86.23 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD---------PAL--QVGYFAQHQREQL--- 385
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkditkknlRELrrKVGLVFQNPDDQLfap 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 ----DLEASPlvhLQRQDPRAE-EQRLRNFLGGMGFpGDKADGPVGQCSGGERVRL----VLALliwqAPSLLLLDEPTN 456
Cdd:COG1122 92 tveeDVAFGP---ENLGLPREEiRERVEEALELVGL-EHLADRPPHELSGGQKQRVaiagVLAM----EPEVLVLDEPTA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 457 HLDLDMREALAEALENYAG---GLVVVAHDRELLARVCDRFWTVEAGRLSpFDGD 508
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIV-ADGT 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-220 |
1.09e-18 |
|
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: 85.56 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 9 LRRGRQI-LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI--EQPPEWV-VAHL-PQEVPGSDRRAVDY 83
Cdd:COG4778 18 LQGGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvRHDGGWVdLAQAsPREILALRRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 84 V------------LDGDAE-LRDLqrrleqandGAEQARlyaaleaidgwsAEARARRLLAGLGFAPADAERPMRDFSGG 150
Cdd:COG4778 98 VsqflrviprvsaLDVVAEpLLER---------GVDREE------------ARARARELLARLNLPERLWDLPPATFSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 151 WRMRLGLARTLMTRSDLLLLDEPTNHLDVET----ILWLEDWLARypGTVIV-IAHDRRFLDSVCTHVAHIERGT 220
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKAR--GTAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-223 |
1.25e-18 |
|
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: 85.08 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewVVAHLPQEVpgsdRRAVDYVLDgDAE--- 90
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgKD---ITKKNLREL----RRKVGLVFQ-NPDdql 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 ------------LRDLQRRLEQAndgaeQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGWRMRLGLA 158
Cdd:COG1122 89 faptveedvafgPENLGLPREEI-----RERVEEALELVG-----------LEHL------ADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 159 RTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG---TVIVIAHDRRFLDSVCTHVAHIERGTIAL 223
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-219 |
1.84e-18 |
|
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: 83.20 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELR---RGRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqevpgsdr 78
Cdd:cd03228 1 IEFKNVSFSypgRPKPVL-KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 79 ravdyvLDGDaELRDLQRRleqandgaeqarlyaaleaidgwsaEARARrllagLGFAPADA---ERPMRD--FSGGWRM 153
Cdd:cd03228 61 ------IDGV-DLRDLDLE-------------------------SLRKN-----IAYVPQDPflfSGTIREniLSGGQRQ 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 154 RLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAHdRRFLDSVCTHVAHIERG 219
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRIIVLDDG 170
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
306-493 |
1.84e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 85.14 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 306 PDPLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD------PALQVGYFAQ 379
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 380 HQREQLDLEAS----------PLVHLQRQDPRAEEQRLRNFLG--GMgfpGDKADGPVGQCSGGERVRLVLALLIWQAPS 447
Cdd:COG1121 83 RAEVDWDFPITvrdvvlmgryGRRGLFRRPSRADREAVDEALErvGL---EDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 648648866 448 LLLLDEPTNHLDLDMREALAEALENYAG---GLVVVAHDRELLARVCDR 493
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDR 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-221 |
1.93e-18 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 84.86 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDRRAV 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL-------------IDGEDISGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyvldGDAELRDLQRR---LEQanDGAeqarLYAALEAIDG-------------WSAEARARRLLAGLGFAPADAERPmR 145
Cdd:cd03261 68 -----SEAELYRLRRRmgmLFQ--SGA----LFDSLTVFENvafplrehtrlseEEIREIVLEKLEAVGLRGAEDLYP-A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD-------VETILWLEDwlaRYPGTVIVIAHDRRFLDSVCTHVAHIER 218
Cdd:cd03261 136 ELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKK---ELGLTSIMVTHDLDTAFAIADRIAVLYD 212
|
...
gi 648648866 219 GTI 221
Cdd:cd03261 213 GKI 215
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
310-502 |
3.75e-18 |
|
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: 84.48 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE-----------RRVDPALQVGYFA 378
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTvdlagvdlhglSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 379 QHQREQLDLEASPLVHLQR--------QDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLL 450
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRiphrslwaGDSPHDAAVVDRALARTEL-SHLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 451 LDEPTNHLDLDMREALAEALENYAG-GLVVVA--HDRELLARVCDRFWTVEAGRL 502
Cdd:TIGR03873 161 LDEPTNHLDVRAQLETLALVRELAAtGVTVVAalHDLNLAASYCDHVVVLDGGRV 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-511 |
4.14e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 83.96 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV---DPALQ-------VGYFAQHQ-------- 381
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgeDVARDpaevrrrIGYVPQEPalypdltv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLEASplvhLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:COG1131 91 RENLRFFAR----LYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648648866 462 MREALAEALENYA--GGLVVVA-HDRELLARVCDRFWTVEAGRLSpFDGDLDD 511
Cdd:COG1131 166 ARRELWELLRELAaeGKTVLLStHYLEEAERLCDRVAIIDKGRIV-ADGTPDE 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-222 |
6.31e-18 |
|
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: 83.19 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWVVAHLPQEVPGSDRRAVDYVLDgdaelrdlQRRLEQ 100
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA-----TVAGHDVVREPREVRRRIGIVFQ--------DLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 101 ANDGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVE 180
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEA-ADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 181 TI--LW--LEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:cd03265 166 TRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-221 |
7.36e-18 |
|
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: 82.94 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 10 RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwVVAHLPQEVPGSDRRAVDYVL-DGD 88
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK-DLLKLSRRLRKIRRKEIQMVFqDPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 89 AELRDLQRRLEQANDGAEQARLYAALEAIdgwsaEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLL 168
Cdd:cd03257 93 SSLNPRMTIGEQIAEPLRIHGKLSKKEAR-----KEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 169 LLDEPTNHLDVET---ILWLEDWL-ARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03257 168 IADEPTSALDVSVqaqILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-222 |
1.85e-17 |
|
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: 81.65 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDI----ELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPeWVVAHLPQEVpgs 76
Cdd:cd03266 1 MITADALtkrfRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 dRRAVDYVLDGDAelrdLQRRLEqandGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLG 156
Cdd:cd03266 77 -RRRLGFVSDSTG----LYDRLT----ARENLEYFAGLYGLKGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 157 LARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG---TVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-202 |
2.20e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHL-PQEVpgS 76
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngRP----LADWsPAEL--A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 DRRAV--------------DYVLDGDAELRDLQRRLEQANDgaeqarlyAALEAIDgwsaeararrlLAGLgfapadAER 142
Cdd:PRK13548 76 RRRAVlpqhsslsfpftveEVVAMGRAPHGLSRAEDDALVA--------AALAQVD-----------LAHL------AGR 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 143 PMRDFSGGWRMRLGLARTLMTRSD------LLLLDEPTNHLDV---ETILWLEDWLAR-YPGTVIVIAHD 202
Cdd:PRK13548 131 DYPQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLahqHHVLRLARQLAHeRGLAVIVVLHD 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
320-502 |
2.21e-17 |
|
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: 79.95 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPAlqvgyfaqhqreqldleasplvHLQRQD 399
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA----------------------DISQWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 400 PRAeeqrLRNFLGGMG-----FPGDKADGPVgqcSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALEN-- 472
Cdd:cd03246 71 PNE----LGDHVGYLPqddelFSGSIAENIL---SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlk 143
|
170 180 190
....*....|....*....|....*....|.
gi 648648866 473 -YAGGLVVVAHDRELLARvCDRFWTVEAGRL 502
Cdd:cd03246 144 aAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-221 |
3.56e-17 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 81.09 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDI----ELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGs 76
Cdd:cd03258 1 MIELKNVskvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVL-------------VDG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 drraVDYVLDGDAELRDLQRR---------LEQANDGAEQARLyaALEaIDGWS---AEARARRLLAGLGFA-PADAeRP 143
Cdd:cd03258 67 ----TDLTLLSGKELRKARRRigmifqhfnLLSSRTVFENVAL--PLE-IAGVPkaeIEERVLELLELVGLEdKADA-YP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 144 mRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPG-TVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:cd03258 139 -AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKG 217
|
..
gi 648648866 220 TI 221
Cdd:cd03258 218 EV 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
321-502 |
5.48e-17 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 80.33 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 321 ERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------RRVDPAL---QVGYFAQHQ-------R 382
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgtdiRQLDPADlrrNIGYVPQDVtlfygtlR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 383 EQLDLEAsplvhlqrqdPRAEEQRL---RNFLGGMGFPGDKADG---PVG----QCSGGERVRLVLALLIWQAPSLLLLD 452
Cdd:cd03245 96 DNITLGA----------PLADDERIlraAELAGVTDFVNKHPNGldlQIGergrGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648648866 453 EPTNHLDLDMREALAEALENYAGG--LVVVAHDRELLArVCDRFWTVEAGRL 502
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-202 |
1.15e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 80.13 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELR----RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvVAHLPQEVPGS 76
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVL------VDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 DRRAV--DY-------VLDgDAELrdlqrrleqandGAEQARLYAAleaidgwSAEARARRLLAGLGFAPADAERPmRDF 147
Cdd:COG1116 81 DRGVVfqEPallpwltVLD-NVAL------------GLELRGVPKA-------ERRERARELLELVGLAGFEDAYP-HQL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLAR----YPGTVIVIAHD 202
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwqeTGKTVLFVTHD 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-202 |
1.18e-16 |
|
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: 83.18 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRR-GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewVVAHLPQEVPGSDRRA 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT-----LDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDGDAELRD--LQRRLEQANDGAEQARLYAALEAidgwsaeARARRLLAGLgfaPADAERPM----RDFSGGWRMR 154
Cdd:TIGR02868 410 RVSVCAQDAHLFDttVRENLRLARPDATDEELWAALER-------VGLADWLRAL---PDGLDTVLgeggARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 648648866 155 LGLARTLMTRSDLLLLDEPTNHLDVETIL-WLEDWLARYPG-TVIVIAHD 202
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-222 |
1.35e-16 |
|
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: 78.77 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWrVGLTGANGSGKSSLLAALQGELALDAGEIE--------QPPEW--VVAHLPQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQKLrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 72 EVPGSD----RRAVDYVldgdaelrdlqrrleqandgaeqarlyAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDF 147
Cdd:cd03264 80 EFGVYPnftvREFLDYI---------------------------AWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVI--AHDRRFLDSVCTHVAHIERGTIA 222
Cdd:cd03264 132 SGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-222 |
1.54e-16 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 79.86 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEieqppewvvahlpqevpgsdrrav 81
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGT------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyVLDGDAELRDLQRR--------LEQANDGAEQARL----------YAALEAIDGWSAEARARRLLAGLGfAPADAERP 143
Cdd:TIGR03873 58 --VDLAGVDLHGLSRRararrvalVEQDSDTAVPLTVrdvvalgripHRSLWAGDSPHDAAVVDRALARTE-LSHLADRD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 144 MRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDV----ETILWLEDwLARYPGTVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:TIGR03873 135 MSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVraqlETLALVRE-LAATGVTVVAALHDLNLAASYCDHVVVLDGG 213
|
...
gi 648648866 220 TIA 222
Cdd:TIGR03873 214 RVV 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-202 |
1.63e-16 |
|
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: 79.05 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 10 RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvVAHLPQEVPGSDRRavdYVLDGDA 89
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL------VDGEPVTGPGPDRG---YVFQQDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 EL--RDLQR----RLEQANDGAEQARlyaaleaidgwsaeARARRLLAGLGFAPADAERPmRDFSGGWRMRLGLARTLMT 163
Cdd:cd03293 84 LLpwLTVLDnvalGLELQGVPKAEAR--------------ERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 164 RSDLLLLDEPTNHLDVETILWLEDWLAR----YPGTVIVIAHD 202
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
337-527 |
2.47e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 82.25 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 337 RIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQ-------------------------REQL------ 385
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQfafeeftvldtvimghtelwevkqeRDRIyalpem 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 ---------DLEASplvhLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTN 456
Cdd:PRK15064 109 seedgmkvaDLEVK----FAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 457 HLDLDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSPFDGDLDDY-ARALQARQREAARSA 527
Cdd:PRK15064 185 NLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYmTAATQARERLLADNA 256
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
324-493 |
2.83e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 77.68 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 324 RLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD----PALQ----VGYFAQHQREQLdLEASPLVHL 395
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpiKAKErrksIGYVMQDVDYQL-FTDSVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 396 QRQDPRAEE--QRLRNFLGGMGFPGDKADGPVgQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENY 473
Cdd:cd03226 94 LLGLKELDAgnEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL 172
|
170 180
....*....|....*....|...
gi 648648866 474 A--GGLVVVA-HDRELLARVCDR 493
Cdd:cd03226 173 AaqGKAVIVItHDYEFLAKVCDR 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-221 |
3.19e-16 |
|
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: 78.93 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE--------QPPEWVVAH-------LPQEVPGSDrrAV 81
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditgLPPHRIARLgiartfqNPRLFPELT--VL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGdaelrdlqrRLEQANDGAEQARLYAALEAIDGWSAEARARRLLAGLGFApADAERPMRDFSGGWRMRLGLARTL 161
Cdd:COG0411 98 ENVLVA---------AHARLGRGLLAALLRLPRARREEREARERAEELLERVGLA-DRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 162 MTRSDLLLLDEPT---NHLDVETILWLEDWLARYPG-TVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:COG0411 168 ATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
308-490 |
4.43e-16 |
|
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: 77.13 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 308 PLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE----------RRVDPALQVGYF 377
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepirdAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 378 AQHQ--------REQLDLeasplvHLQRQDPRAEEQRLRNFLGGMGFPGdKADGPVGQCSGGERVRLVLALLIWQAPSLL 449
Cdd:COG4133 81 GHADglkpeltvRENLRF------WAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648648866 450 LLDEPTNHLDLDMREALAEALENYA--GGLVVVA-HDRELLARV 490
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLarGGAVLLTtHQPLELAAA 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-493 |
4.47e-16 |
|
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: 81.75 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 30 VGLTGANGSGKSSLLAALQGELALDAGEIEQPPEW--V----------------------VAHLPQevpgsdrrAVDY-- 83
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWdeVlkrfrgtelqdyfkklangeikVAHKPQ--------YVDLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 84 -VLDGDAelRDLqrrLEQANDgaeqarlyaaleaidgwsaEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTLM 162
Cdd:COG1245 174 kVFKGTV--REL---LEKVDE-------------------RGKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 163 TRSDLLLLDEPTNHLDV-----------EtilwledwLARYPGTVIVIAHDRRFLDSVCTHVaHIERGTIALYaGSYTHA 231
Cdd:COG1245 229 RDADFYFFDEPSSYLDIyqrlnvarlirE--------LAEEGKYVLVVEHDLAILDYLADYV-HILYGEPGVY-GVVSKP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 232 EAKRaEAIVQseaaaarvaaeraHLEDFVR----RFRakaskarqaqsrlkrlermDEvaviraarPIHLEIPTPGRLP- 306
Cdd:COG1245 299 KSVR-VGINQ-------------YLDGYLPeenvRIR-------------------DE--------PIEFEVHAPRREKe 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 307 -DPLLALDHAEVCTGE-RVRLQPTTLRlrPEDRIGILGPNGAGKSTLLTLLAGELLPTAGErrVDPALQVGYFAQHQREQ 384
Cdd:COG1245 338 eETLVEYPDLTKSYGGfSLEVEGGEIR--EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYKPQYISPD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 385 LDLEAsplvhlqrqdpraeEQRLRNFLGGMgFPGDKA--------------DGPVGQCSGGERVRLVLALLIWQAPSLLL 450
Cdd:COG1245 414 YDGTV--------------EEFLRSANTDD-FGSSYYkteiikplglekllDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 648648866 451 LDEPTNHLDLDMREALAEAL----ENYAGGLVVVAHDRELLARVCDR 493
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIrrfaENRGKTAMVVDHDIYLIDYISDR 525
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-220 |
5.45e-16 |
|
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: 76.07 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDrrav 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-------------IDGED---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyVLDGDAELRDLQRRLeqandGA--EQARLYAALEAIDgwsaeararRLLAGLgfapadaerpmrdfSGGWRMRLGLAR 159
Cdd:cd03229 64 --LTDLEDELPPLRRRI-----GMvfQDFALFPHLTVLE---------NIALGL--------------SGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 160 TLMTRSDLLLLDEPTNHLDVETILWLEDWL----ARYPGTVIVIAHDRRFLDSVCTHVAHIERGT 220
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-224 |
5.46e-16 |
|
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: 76.94 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAhlpqevpgSDRRAV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI--------AARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVldgdAELRDLQRRLEQandgAEQARLYAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTL 161
Cdd:cd03269 73 GYL----PEERGLYPKMKV----IDQLVYLAQLKGLKKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 162 MTRSDLLLLDEPTNHLD---VETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALY 224
Cdd:cd03269 144 IHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-220 |
5.56e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGR-QILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGelaL---DAGEIEQPPEWVVAHLPQEV--- 73
Cdd:COG4178 362 ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG---LwpyGSGRIARPAGARVLFLPQRPylp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 74 PGSDRRAVDYVLD----GDAELRDLqrrLEQANDGaeqaRLYAALEAIDGWSaearaRRLlaglgfapadaerpmrdfSG 149
Cdd:COG4178 439 LGTLREALLYPATaeafSDAELREA---LEAVGLG----HLAERLDEEADWD-----QVL------------------SL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 150 GWRMRLGLARTLMTRSDLLLLDEPTNHLDVETilwlEDWL-----ARYPG-TVIVIAHdRRFLDSVCTHVAHIERGT 220
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEEN----EAALyqllrEELPGtTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
5.89e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 78.23 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPPEwvvAHLPQEVpgSD 77
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngRPLA---AWSPWEL--AR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 78 RRAV---DYVLDGDAELRD---LQRRLEQANDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGW 151
Cdd:COG4559 76 RRAVlpqHSSLAFPFTVEEvvaLGRAPHGSSAAQDRQIVREALALVG-----------LAHL------AGRSYQTLSGGE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 152 RMRLGLARTL-------MTRSDLLLLDEPTNHLDV---ETILWLEDWLARYPGTVIVIAHD 202
Cdd:COG4559 139 QQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLahqHAVLRLARQLARRGGGVVAVLHD 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-221 |
5.98e-16 |
|
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: 77.14 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQIL----LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSD 77
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR-------------VDGTD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 78 RRAVDyvldgDAELRDLQRR----------LEQANDGAEQARLYAALEAIDGWSAEARARRLLAGLGFApADAERPMRDF 147
Cdd:cd03255 68 ISKLS-----EKELAAFRRRhigfvfqsfnLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLG-DRLNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPG-TVIVIAHDRRfLDSVCTHVAHIERGTI 221
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETgkeVMELLRELNKEAGtTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
6.14e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.40 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELR-RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWV----VAHLPQ-EVP 74
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQV-----LVngqdLSRLKRrEIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 75 GSdRRAVDYVLDgDAELrdLQRRLEQANdgaeqarLYAALEAIdGWS---AEARARRLLAGLGFAPADAERPMRdFSGGW 151
Cdd:COG2884 76 YL-RRRIGVVFQ-DFRL--LPDRTVYEN-------VALPLRVT-GKSrkeIRRRVREVLDLVGLSDKAKALPHE-LSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 152 RMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYpGTVIVIA-HDRRFLDSVCTHVAHIERGTI 221
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETsweIMELLEEINRR-GTTVLIAtHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-221 |
6.81e-16 |
|
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: 76.80 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDrrav 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII-------------IDGLK---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyVLDGDAELRDLQRRL----EQANdgaeqarLYAALEAID----------GWS---AEARARRLLAGLGFAPADAERPm 144
Cdd:cd03262 64 --LTDDKKNINELRQKVgmvfQQFN-------LFPHLTVLEnitlapikvkGMSkaeAEERALELLEKVGLADKADAYP- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 145 RDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETI---LWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVgevLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
9.84e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 76.62 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRG----RQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWV----VAHLpqe 72
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV-----LIdgqdISSL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 73 vpgsdrravdyvldGDAELRDLQRR-----LEQAN-----DGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAER 142
Cdd:COG1136 76 --------------SERELARLRRRhigfvFQFFNllpelTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 143 PmRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPG-TVIVIAHDRRfLDSVCTHVAHIER 218
Cdd:COG1136 142 P-SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeeVLELLRELNRELGtTIVMVTHDPE-LAARADRVIRLRD 219
|
...
gi 648648866 219 GTI 221
Cdd:COG1136 220 GRI 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-222 |
1.15e-15 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 76.40 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwVVAHLPQEvpgsdRRAV 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-DVTGVPPE-----RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGDAELRDLQRR------LEQANDGAEQARlyaaleaidgwsaeARARRLLAGLGFAPaDAERPMRDFSGGWRMRL 155
Cdd:cd03259 75 GMVFQDYALFPHLTVAeniafgLKLRGVPKAEIR--------------ARVRELLELVGLEG-LLNRYPHELSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 156 GLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG----TVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
329-502 |
1.38e-15 |
|
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: 74.74 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpalqvGyfaqhqreqldleasplvhlqrQDPRAEEQRLR 408
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-----G----------------------KDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 409 NFLG----GMGFPGDKAdgpVGQ---CSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYA--GGLVV 479
Cdd:cd03230 73 RRIGylpeEPSLYENLT---VREnlkLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkeGKTIL 149
|
170 180
....*....|....*....|....
gi 648648866 480 VA-HDRELLARVCDRFWTVEAGRL 502
Cdd:cd03230 150 LSsHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-230 |
1.62e-15 |
|
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: 76.00 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 10 RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWVVAHLPQEVPGSDRRAVDYVLDGDA 89
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-----YINGYSIRTDRKAARQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 ELRDLQrrleqandGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPaDAERPMRDFSGGWRMRLGLARTLMTRSDLLL 169
Cdd:cd03263 86 LFDELT--------VREHLRFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 170 LDEPTNHLDVET--ILWleDWLARY-PGTVIVIA-HDRRFLDSVCTHVAHIERGTIaLYAGSYTH 230
Cdd:cd03263 157 LDEPTSGLDPASrrAIW--DLILEVrKGRSIILTtHSMDEAEALCDRIAIMSDGKL-RCIGSPQE 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-224 |
2.26e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 75.65 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 9 LRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQppewvvahlpqevpgsdRRAVDYVLDG- 87
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-----------------RGRVSSLLGLg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 88 ---DAELrdlqrrleqanDGAEQARLYAALEAIDGWSAEARARRLL--AGLGfapADAERPMRDFSGGWRMRLGLARTLM 162
Cdd:cd03220 93 ggfNPEL-----------TGRENIYLNGRLLGLSRKEIDEKIDEIIefSELG---DFIDLPVKTYSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 163 TRSDLLLLDEPTNHLDVET----ILWLEDWLARyPGTVIVIAHDRRFLDSVCTHVAHIERGTIALY 224
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFqekcQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
286-497 |
2.47e-15 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 79.25 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 286 VAVIRAARPIHLEIPTPGRLPDPLLALDHAEVC-TGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAG 364
Cdd:TIGR02857 298 FAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 365 ERRVDPALQVGYFAQHQREQLD--------LEASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVG---------- 426
Cdd:TIGR02857 378 SIAVNGVPLADADADSWRDQIAwvpqhpflFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGldtpigegga 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 427 QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--LVVVAHDRELLARvCDRFWTV 497
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAAL-ADRIVVL 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
324-502 |
5.87e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 324 RLQPTTLRLRPEDRIGILGPNGAGKSTlLTLLAGELLPTAGERRVDP-----------ALQVGYFAQHQR--------EQ 384
Cdd:COG4138 11 RLGPISAQVNAGELIHLIGPNGAGKST-LLARMAGLLPGQGEILLNGrplsdwsaaelARHRAYLSQQQSppfampvfQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 385 LDLeasplvHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGE--RVRLVLALL-IW----QAPSLLLLDEPTNH 457
Cdd:COG4138 90 LAL------HQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEwqRVRLAAVLLqVWptinPEGQLLLLDEPMNS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648648866 458 LDLDMREALAEALENY--AGGLVVV-AHDRELLARVCDRFWTVEAGRL 502
Cdd:COG4138 164 LDVAQQAALDRLLRELcqQGITVVMsSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
307-485 |
1.02e-14 |
|
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: 74.35 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 307 DPLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTA-------GERR------------ 367
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYgndvrlfGERRggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 368 --VDPALQvgyfAQHQREQ--LDLEASPL---VHLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERvRLVL-- 438
Cdd:COG1119 81 glVSPALQ----LRFPRDEtvLDVVLSGFfdsIGLYREPTDEQRERARELLELLGL-AHLADRPFGTLSQGEQ-RRVLia 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648648866 439 -ALLIwqAPSLLLLDEPTNHLDLDMREALAEALENYAGG----LVVVAHDRE 485
Cdd:COG1119 155 rALVK--DPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTHHVE 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-494 |
1.31e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 30 VGLTGANGSGKSSLLAALQGELALDAGEIEQPPEW--V----------------------VAHLPQEVpgsdrravDY-- 83
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWdeVlkrfrgtelqnyfkklyngeikVVHKPQYV--------DLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 84 -VLDGDAelRDLqrrleqandgaeqarlyaaLEAIDgwsaEARARRLLAG-LGFAPAdAERPMRDFSGGWRMRLGLARTL 161
Cdd:PRK13409 174 kVFKGKV--REL-------------------LKKVD----ERGKLDEVVErLGLENI-LDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARY-PG-TVIVIAHDRRFLDSVCTHVaHIERGTIALYaGSYTHAEAKRaEAI 239
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELaEGkYVLVVEHDLAVLDYLADNV-HIAYGEPGAY-GVVSKPKGVR-VGI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 240 VQseaaaarvaaeraHLEDFVR----RFRAKASKAR-QAQSRLKRLERMDEVAVIRAarpihleiptpgRLPDPLLALDH 314
Cdd:PRK13409 305 NE-------------YLKGYLPeenmRIRPEPIEFEeRPPRDESERETLVEYPDLTK------------KLGDFSLEVEG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 315 AEVCTGErVrlqpttlrlrpedrIGILGPNGAGKSTLLTLLAGELLPTAGErrVDPALQVGYFAQHQREQLDLEASPLvh 394
Cdd:PRK13409 360 GEIYEGE-V--------------IGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPELKISYKPQYIKPDYDGTVEDL-- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 395 LQRQDPRAEEQRLRN-FLGGMGFPgDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENY 473
Cdd:PRK13409 421 LRSITDDLGSSYYKSeIIKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
490 500
....*....|....*....|....*
gi 648648866 474 A----GGLVVVAHDRELLARVCDRF 494
Cdd:PRK13409 500 AeereATALVVDHDIYMIDYISDRL 524
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-203 |
1.43e-14 |
|
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: 76.56 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 11 RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewVV--AHLPQEVPGSDRRAVDYVLdgd 88
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI------AVngVPLADADADSWRDQIAWVP--- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 89 aelrdlQRRLEQANDGAEQARLY---AALEAIDGWSAEARARRLLAGLgfaPADAERPM----RDFSGGWRMRLGLARTL 161
Cdd:TIGR02857 403 ------QHPFLFAGTIAENIRLArpdASDAEIREALERAGLDEFVAAL---PQGLDTPIgeggAGLSGGQAQRLALARAF 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAHDR 203
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-502 |
1.97e-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: 76.38 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQG--ELALDAGEI------------EQPPEWVVA 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 68 HLPQEVPGSDRRAVDYVLDGDAELRDLQRR------------------------LEQANDGAEQArLYAALEAIDGWSAE 123
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDFWNLSDKLRRRIRKRiaimlqrtfalygddtvldnvleaLEEIGYEGKEA-VGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 124 ARARRLlaglgfapadaerpMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLAR----YPGTVIVI 199
Cdd:TIGR03269 160 HRITHI--------------ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkaSGISMVLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 200 AHDRRFLDSVCTHVAHIERGTIALyAGSYTHAEAKRAEAIVQSEAAAARVAAerahlEDFVrrfrakasKARQAQSRLKR 279
Cdd:TIGR03269 226 SHWPEVIEDLSDKAIWLENGEIKE-EGTPDEVVAVFMEGVSEVEKECEVEVG-----EPII--------KVRNVSKRYIS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 280 LERmdevAVIRAARPIHLEIptpgrlpdpllalDHAEVctgervrlqpttlrlrpedrIGILGPNGAGKSTLLTLLAGEL 359
Cdd:TIGR03269 292 VDR----GVVKAVDNVSLEV-------------KEGEI--------------------FGIVGTSGAGKTTLSKIIAGVL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 360 LPTAGERRV----------DPALQ--------VGYFaqHQREQLDLEASPLVHLQRQ---DPRAEEQRLRNF--LGGMGF 416
Cdd:TIGR03269 335 EPTSGEVNVrvgdewvdmtKPGPDgrgrakryIGIL--HQEYDLYPHRTVLDNLTEAiglELPDELARMKAVitLKMVGF 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 417 PGDKA----DGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYAGGLVVVAHDRELLA 488
Cdd:TIGR03269 413 DEEKAeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVL 492
|
570
....*....|....
gi 648648866 489 RVCDRFWTVEAGRL 502
Cdd:TIGR03269 493 DVCDRAALMRDGKI 506
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
320-489 |
2.45e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQR--EQLDLEASPLVHLQR 397
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEvpDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 398 QDPRAEEQRLR--------NFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEA 469
Cdd:NF040873 83 WARRGLWRRLTrddraavdDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170 180
....*....|....*....|...
gi 648648866 470 LENYAG---GLVVVAHDRELLAR 489
Cdd:NF040873 162 LAEEHArgaTVVVVTHDLELVRR 184
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
324-502 |
3.08e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 324 RLQPTTLRLRPEDRIGILGPNGAGKSTlLTLLAGELLPTAGERRVDP-----------ALQVGYFAQHQR--------EQ 384
Cdd:PRK03695 11 RLGPLSAEVRAGEILHLVGPNGAGKST-LLARMAGLLPGSGSIQFAGqpleawsaaelARHRAYLSQQQTppfampvfQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 385 LDLEASPLVHLqrQDPRAEEQRLRNFLGgmgfPGDKADGPVGQCSGGE--RVRLVLALL-IWQA--PS--LLLLDEPTNH 457
Cdd:PRK03695 90 LTLHQPDKTRT--EAVASALNEVAEALG----LDDKLGRSVNQLSGGEwqRVRLAAVVLqVWPDinPAgqLLLLDEPMNS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648648866 458 LDLDMREALAEALENYA--GGLVVVA-HDRELLARVCDRFWTVEAGRL 502
Cdd:PRK03695 164 LDVAQQAALDRLLSELCqqGIAVVMSsHDLNHTLRHADRVWLLKQGKL 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
308-487 |
3.10e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 308 PLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQ--HQREQL 385
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 DLEASPLVHL----QRQDPRAEEQRLRnflggmgfPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:PRK09544 83 PLTVNRFLRLrpgtKKEDILPALKRVQ--------AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190
....*....|....*....|....*....|
gi 648648866 462 MREALAEALEN----YAGGLVVVAHDRELL 487
Cdd:PRK09544 155 GQVALYDLIDQlrreLDCAVLMVSHDLHLV 184
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
334-504 |
4.39e-14 |
|
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: 71.56 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 334 PEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpalqvGYFAQHQREQLDL------------EASPLVHL------ 395
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN-----GTVLFDSRKKINLppqqrkiglvfqQYALFPHLnvrenl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 396 ----QRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREA----LA 467
Cdd:cd03297 97 afglKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQllpeLK 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 648648866 468 EALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSP 504
Cdd:cd03297 176 QIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
320-502 |
5.46e-14 |
|
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: 75.18 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD---------PAL--QVGYFAQHQ------- 381
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvdlsdldpASWrrQIAWVPQNPylfagti 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLeASPLVHLQRQDPRAEEQRLRNFLggMGFPgDKADGPVGQC----SGGERVRLVLALLIWQAPSLLLLDEPTNH 457
Cdd:COG4988 428 RENLRL-GRPDASDEELEAALEAAGLDEFV--AALP-DGLDTPLGEGgrglSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648648866 458 LDLDMREALAEALENYAGG--LVVVAHDRELLARvCDRFWTVEAGRL 502
Cdd:COG4988 504 LDAETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
310-507 |
7.29e-14 |
|
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: 71.07 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGERVRLQPTTLRLrPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--------PALQ--VGYFAQ 379
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgqdvlkqpQKLRrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 380 H--------QREQLDLEASplvhLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLL 451
Cdd:cd03264 80 EfgvypnftVREFLDYIAW----LKGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 452 DEPTNHLDLDMREALAEALENYAGGLVVV--AHDRELLARVCDRFWTVEAGRLSpFDG 507
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
329-502 |
8.53e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 70.86 E-value: 8.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV-------DPA---LQVGYFAQHQREQLDLEASPLVHLQRQ 398
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvrEPRevrRRIGIVFQDLSVDDELTGWENLYIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 399 ---DPRAE-EQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALE--N 472
Cdd:cd03265 100 lygVPGAErRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklK 178
|
170 180 190
....*....|....*....|....*....|..
gi 648648866 473 YAGGLVVV--AHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03265 179 EEFGMTILltTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
325-501 |
9.39e-14 |
|
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: 69.72 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpalqvgyfaqhqreQLDLEASPLVHLQR------Q 398
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID--------------GVDLRDLDLESLRKniayvpQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 399 DPR------AEeqrlrNFLggmgfpgdkadgpvgqcSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALEN 472
Cdd:cd03228 84 DPFlfsgtiRE-----NIL-----------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRA 141
|
170 180 190
....*....|....*....|....*....|.
gi 648648866 473 YAGG--LVVVAHdRELLARVCDRFWTVEAGR 501
Cdd:cd03228 142 LAKGktVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
329-502 |
1.11e-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: 74.49 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------RRVDPAL---QVGYFAQHQ-------REQLDLEas 390
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgidlRQIDPASlrrQIGVVLQDVflfsgtiRENITLG-- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 391 plvhlqrqDPRAEEQRLRN---------FLGGM--GFpgdkaDGPVG----QCSGGERVRLVLALLIWQAPSLLLLDEPT 455
Cdd:COG2274 573 --------DPDATDEEIIEaarlaglhdFIEALpmGY-----DTVVGeggsNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 648648866 456 NHLDLDMREALAEALENYAGG--LVVVAHDRELLaRVCDRFWTVEAGRL 502
Cdd:COG2274 640 SALDAETEAIILENLRRLLKGrtVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-518 |
1.14e-13 |
|
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: 70.99 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 330 LRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE---------RRVDPAL--QVGYFAQHQREQLD----LEAS---P 391
Cdd:COG1124 26 LEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdgrpvtRRRRKAFrrRVQMVFQDPYASLHprhtVDRIlaeP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 392 LVHLQRQDpraEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMR----EALA 467
Cdd:COG1124 106 LRIHGLPD---REERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQaeilNLLK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 468 EALENYAGGLVVVAHDRELLARVCDRFWTVEAGRL-------SPFDGDLDDYARALQA 518
Cdd:COG1124 183 DLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIveeltvaDLLAGPKHPYTRELLA 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-209 |
1.22e-13 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 70.31 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQPPewvvahlPQEVpgsdRRAVDYVLDgDA 89
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLaglykptSGSVLLDGTDIRQLD-------PADL----RRNIGYVPQ-DV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 EL-----RDlqrRLEQANDGAEQARLYAALEaidgwsaeararrlLAGLG-FA---PADAERPMRD----FSGGWRMRLG 156
Cdd:cd03245 88 TLfygtlRD---NITLGAPLADDERILRAAE--------------LAGVTdFVnkhPNGLDLQIGErgrgLSGGQRQAVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 157 LARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAHDRRFLDSV 209
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLV 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
340-502 |
1.42e-13 |
|
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: 70.13 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVD-------PALQVGYFAQH------------QREQLDLEASPLVHLQRQdP 400
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKigvvfqdfrllpDRNVYENVAFALEVTGVP-P 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 401 RAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALE--NYAGGLV 478
Cdd:cd03292 111 REIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKkiNKAGTTV 189
|
170 180
....*....|....*....|....*
gi 648648866 479 VVA-HDRELLARVCDRFWTVEAGRL 502
Cdd:cd03292 190 VVAtHAKELVDTTRHRVIALERGKL 214
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
320-541 |
1.65e-13 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 71.65 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV-------DPAL---QVGYFAQHQREQLDLEA 389
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVagydvvrEPRKvrrSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 390 SP--LVHLQRQD-PRAE-EQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREA 465
Cdd:TIGR01188 84 REnlEMMGRLYGlPKDEaEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 466 ---LAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSPFDGD-----------LDDYARALQARQREAARSAAETP 531
Cdd:TIGR01188 163 iwdYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPeelkrrlgkdtLESRPRDIQSLKVEVSMLIAELG 242
|
250
....*....|
gi 648648866 532 PQAASDAPVR 541
Cdd:TIGR01188 243 ETGLGLLAVT 252
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
17-213 |
1.82e-13 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 70.11 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI--EQPPEWV--VAHLPQEVPGSDRRAVDYVldgDAELR 92
Cdd:TIGR02324 24 LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRIlvRHEGAWVdlAQASPREVLEVRRKTIGYV---SQFLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 93 DLQRRleqandgaeQARLYAALEAID-GWS---AEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLL 168
Cdd:TIGR02324 101 VIPRV---------SALEVVAEPLLErGVPreaARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648648866 169 LLDEPTNHLDV---ETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHV 213
Cdd:TIGR02324 172 LLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRV 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
395-589 |
1.93e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 73.74 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 395 LQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYA 474
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 475 GGLVVVAHDRELLARVCDRFWTVEAGRLSPFDGDLDDYARAlQARQREAARSAAETPPQAASDAPVRSQKERRQqaaQKR 554
Cdd:PLN03073 392 KTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERT-REEQLKNQQKAFESNERSRSHMQAFIDKFRYN---AKR 467
|
170 180 190
....*....|....*....|....*....|....*
gi 648648866 555 AALrpLQQRAdraerdcsQTQERLQTLESELADPD 589
Cdd:PLN03073 468 ASL--VQSRI--------KALDRLGHVDAVVNDPD 492
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-222 |
2.05e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.12 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDrra 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI-------------VDGLK--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdyVLDGDAELRDLqrRLEqANDGAEQARLYAALEAID----------GWS---AEARARRLLAGLGFAPADAERPmRDF 147
Cdd:PRK09493 65 ---VNDPKVDERLI--RQE-AGMVFQQFYLFPHLTALEnvmfgplrvrGASkeeAEKQARELLAKVGLAERAHHYP-SEL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVE---TILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:PRK09493 138 SGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-226 |
2.13e-13 |
|
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: 70.05 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 4 MQDIELRRGRQI-LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvVAHLpqeVPGSDRRAVd 82
Cdd:cd03267 23 LKSLFKRKYREVeALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR------VAGL---VPWKRRKKF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 83 yvldgdaeLRDLQRRLEQAND------GAEQARLYAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLG 156
Cdd:cd03267 93 --------LRRIGVVFGQKTQlwwdlpVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEEL-LDTPVRQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 157 LARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARY----PGTVIVIAHDRRFLDSVCTHVAHIERGTIaLYAG 226
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-201 |
2.69e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.89 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 6 DIELRR------GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPQEvpgS 76
Cdd:COG1132 339 EIEFENvsfsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgVD----IRDLTLE---S 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 DRRAVDYVLDgDAELrdLQRRLEQ----ANDGAEQARLYAALEAidgwsaeARARRLLAGL--GFapaDA---ERPMRdF 147
Cdd:COG1132 412 LRRQIGVVPQ-DTFL--FSGTIREniryGRPDATDEEVEEAAKA-------AQAHEFIEALpdGY---DTvvgERGVN-L 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAH 201
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH 533
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-221 |
2.89e-13 |
|
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: 69.77 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGE-------IEQPPEWVVAHL--------PQEVPGSDrrav 81
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgedITGLPPHEIARLgigrtfqiPRLFPELT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyVLDG--DAELRDLQRRLEQANDGAEQARlyaaleaidgwsAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLAR 159
Cdd:cd03219 92 --VLENvmVAAQARTGSGLLLARARREERE------------ARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 160 TLMTRSDLLLLDEPT---NHLDVETIL-WLEDwLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03219 157 ALATDPKLLLLDEPAaglNPEETEELAeLIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-221 |
3.31e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.00 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 6 DIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGelaldageIEQPPEWVVAHLPQEVP-GSDRRAVDYV 84
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINF--------LEKPSEGSIVVNGQTINlVRDKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 LDGDaELRDLQRRL----EQANDGAEQARLYAALEA---IDGWS-AEARAR--RLLAGLGFAPADAERPMRDFSGGWRMR 154
Cdd:PRK10619 82 ADKN-QLRLLRTRLtmvfQHFNLWSHMTVLENVMEApiqVLGLSkQEARERavKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 155 LGLARTLMTRSDLLLLDEPTNHLDVE---TILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-181 |
4.15e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 68.11 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 14 QILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahLPQEVPgsdrravdyVLDGDAELRD 93
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI----------TLDGVP---------VSDLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 94 LQRRLEQandgaeQARLYAAleaidgwsaeararRLLAGLGfapadaerpmRDFSGGWRMRLGLARTLMTRSDLLLLDEP 173
Cdd:cd03247 76 LISVLNQ------RPYLFDT--------------TLRNNLG----------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
....*...
gi 648648866 174 TNHLDVET 181
Cdd:cd03247 126 TVGLDPIT 133
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
338-507 |
4.19e-13 |
|
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: 69.28 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 338 IGILGPNGAGKSTLLTLLAGELLPTAGERRV---DPALQVGYFAQH------QREQL--DLEA----SPLVHLQRQDPRA 402
Cdd:cd03267 50 VGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglVPWKRRKKFLRRigvvfgQKTQLwwDLPVidsfYLLAAIYDLPPAR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 403 EEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRL-VLALLIWQaPSLLLLDEPTNHLDL----DMREALAEALENYAGGL 477
Cdd:cd03267 130 FKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAeIAAALLHE-PEILFLDEPTIGLDVvaqeNIRNFLKEYNRERGTTV 207
|
170 180 190
....*....|....*....|....*....|
gi 648648866 478 VVVAHDRELLARVCDRFWTVEAGRLSpFDG 507
Cdd:cd03267 208 LLTSHYMKDIEALARRVLVIDKGRLL-YDG 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
339-502 |
6.38e-13 |
|
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: 68.01 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 339 GILGPNGAGKSTLLTLLAGELLPTAGERRVD---------PALQVG--------YFAQHQREQLDLEAsplvhLQRQDPR 401
Cdd:cd03268 30 GFLGPNGAGKTTTMKIILGLIKPDSGEITFDgksyqknieALRRIGalieapgfYPNLTARENLRLLA-----RLLGIRK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 402 AEEQRLRNFLGgmgfPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAeALENYAGGL 477
Cdd:cd03268 105 KRIDEVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdgiKELRELIL-SLRDQGITV 179
|
170 180
....*....|....*....|....*
gi 648648866 478 VVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03268 180 LISSHLLSEIQKVADRIGIINKGKL 204
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-221 |
6.54e-13 |
|
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: 69.45 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 10 RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGelaldageIEQPPEWVVAHLPQEVP---GSDRRAVDyvld 86
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG--------LEKPAQGTVSFRGQDLYqldRKQRRAFR---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 87 gdaelRDLQRRLeQANDGAEQARLYAA---------LEAIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGL 157
Cdd:TIGR02769 88 -----RDVQLVF-QDSPSAVNPRMTVRqiigeplrhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLDV----ETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-187 |
7.08e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEvpgsdrra 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdyvLDGDAELRDLQRRLEQANDGAEQARLYAALEAIdgwsaeaRARRLLaglgfapadaERPMRDFSGGWRMRLGLART 160
Cdd:PRK09544 76 ----LYLDTTLPLTVNRFLRLRPGTKKEDILPALKRV-------QAGHLI----------DAPMQKLSGGETQRVLLARA 134
|
170 180
....*....|....*....|....*..
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETILWLED 187
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
7.10e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.83 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwvvahlpqEVPGSDRRAV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE--------PVPSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYV--------LDGDAELRdlqrrleqandgaEQARLYAALEaidGWSAEARARRLLAGLGFAPAD--AERPMRDFSGGW 151
Cdd:PRK13537 80 QRVgvvpqfdnLDPDFTVR-------------ENLLVFGRYF---GLSAAAARALVPPLLEFAKLEnkADAKVGELSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 152 RMRLGLARTLMTRSDLLLLDEPTNHLDVET--ILW--LEDWLARyPGTVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-174 |
7.43e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.69 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqevpgsdrrav 81
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyVLDGD----AELRDLQRRLeqA--------NdgaeqarLYAAL---EAID------GWSAEARARR---LLAGLGFAP 137
Cdd:NF033858 60 --VLGGDmadaRHRRAVCPRI--AympqglgkN-------LYPTLsvfENLDffgrlfGQDAAERRRRideLLRATGLAP 128
|
170 180 190
....*....|....*....|....*....|....*..
gi 648648866 138 AdAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPT 174
Cdd:NF033858 129 F-ADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-182 |
8.45e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 10 RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwvvahlPQEVPgSDRRAVDYVLDGDA 89
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDP-DVAEACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 ELRDL--QRRLE--QANDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGWRMRLGLARTLMTRS 165
Cdd:PRK13539 84 MKPALtvAENLEfwAAFLGGEELDIAAALEAVG-----------LAPL------AHLPFGYLSAGQKRRVALARLLVSNR 146
|
170
....*....|....*..
gi 648648866 166 DLLLLDEPTNHLDVETI 182
Cdd:PRK13539 147 PIWILDEPTAALDAAAV 163
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-178 |
8.81e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.74 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELR----RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewVVAHLPQEVPGS 76
Cdd:COG4525 3 MLTVRHVSVRypggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI------TLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 DRrAVdyVLDGDAELRDLqrrleqanDGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLG 156
Cdd:COG4525 77 DR-GV--VFQKDALLPWL--------NVLDNVAFGLRLRGVPKAERRARAEELLALVGLADF-ARRRIWQLSGGMRQRVG 144
|
170 180
....*....|....*....|..
gi 648648866 157 LARTLMTRSDLLLLDEPTNHLD 178
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALD 166
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
329-502 |
1.03e-12 |
|
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: 67.90 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP---------------ALQVGY-FAQHQ-------REQL 385
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafrRRHIGFvFQSFNllpdltaLENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 DLeasPLvHLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREA 465
Cdd:cd03255 104 EL---PL-LLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648648866 466 LAEALENYAG----GLVVVAHDRElLARVCDRFWTVEAGRL 502
Cdd:cd03255 179 VMELLRELNKeagtTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
320-502 |
1.14e-12 |
|
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: 67.56 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE----RRVDPALQVGYFAQHQ---REQLDLEASpL 392
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvtvrGRVSSLLGLGGGFNPEltgRENIYLNGR-L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 393 VHLQRQDPRAEEQRLRNF--LggmgfpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPT----NHLDLDMREAL 466
Cdd:cd03220 112 LGLSRKEIDEKIDEIIEFseL------GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEKCQRRL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 648648866 467 AEALENyAGGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03220 186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-459 |
1.24e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.43 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPPewvvAHLPQEvpgsdrravdyvldgdaelrD 93
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqfSHI----TRLSFE--------------------Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 94 LQRRLEQA-----NDG---AEQARLYAALEAI-DGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTLMTR 164
Cdd:PRK10938 75 LQKLVSDEwqrnnTDMlspGEDDTGRTTAEIIqDEVKDPARCEQLAQQFGITAL-LDRRFKYLSTGETRKTLLCQALMSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 165 SDLLLLDEPTNHLDVETILWLEDWLARYPG---TVIVIAHdrRFlDSVCTHVAHIerGTIAlyagSYTHAEAKRAEAIVQ 241
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLN--RF-DEIPDFVQFA--GVLA----DCTLAETGEREEILQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 242 seaaaarvaaerahledfvrrfrakasKARQAQsrLKRLERMDEVAVIRAARPIHLEiptpgRLPD--PLLALDHAEVCT 319
Cdd:PRK10938 225 ---------------------------QALVAQ--LAHSEQLEGVQLPEPDEPSARH-----ALPAnePRIVLNNGVVSY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTlLTLLAGELLPTA--------GERR------VDPALQVGYFAqhQREQL 385
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKST-LLSLITGDHPQGysndltlfGRRRgsgetiWDIKKHIGYVS--SSLHL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 DLEASPLVH------------LQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERvRLVL---ALLiwQAPSLLL 450
Cdd:PRK10938 348 DYRVSTSVRnvilsgffdsigIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQ-RLALivrALV--KHPTLLI 424
|
....*....
gi 648648866 451 LDEPTNHLD 459
Cdd:PRK10938 425 LDEPLQGLD 433
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
325-502 |
1.92e-12 |
|
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: 67.15 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP--------------ALQVGYFAQHQREQLD---- 386
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirRKEIQMVFQDPMSSLNprmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 387 ----LEASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDM 462
Cdd:cd03257 101 igeqIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648648866 463 REALAEAL----ENYAGGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03257 181 QAQILDLLkklqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
319-493 |
2.11e-12 |
|
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: 66.76 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 319 TGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE---------RRVDPALQ-VGYFAQHqrEQLDLE 388
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayingysirTDRKAARQsLGYCPQF--DALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 389 ASPLVHLQ-----RQDPRAEEQRLR-NFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDM 462
Cdd:cd03263 90 LTVREHLRfyarlKGLPKSEIKEEVeLLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190
....*....|....*....|....*....|...
gi 648648866 463 REALAEALENYAGGLVVV--AHDRELLARVCDR 493
Cdd:cd03263 169 RRAIWDLILEVRKGRSIIltTHSMDEAEALCDR 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-221 |
2.99e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 3 RMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI---EQP-PEW-------VVAHLPQ 71
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldAQPlESWsskafarKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 72 EVPGSDRRAVdyvldgdAELRDLQRrleqandgaeqarlYAALEAIDGWSAEARAR--RLLAGLGFAPAdAERPMRDFSG 149
Cdd:PRK10575 93 QLPAAEGMTV-------RELVAIGR--------------YPWHGALGRFGAADREKveEAISLVGLKPL-AHRLVDSLSG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 150 GWRMRLGLARTLMTRSDLLLLDEPTNHLDVE---TILWLEDWLARYPG-TVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-202 |
3.85e-12 |
|
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: 66.05 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQ------------GELALDAGEIEQPPEWVVAH- 68
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndlipgapdeGEVLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 69 --------LPQEVPGSDRRAVDYVLdgdaelRDLQRRLEQANDgaeqARLYAALEAIDGWsaEARARRLLAglgfapada 140
Cdd:cd03260 81 rrvgmvfqKPNPFPGSIYDNVAYGL------RLHGIKLKEELD----ERVEEALRKAALW--DEVKDRLHA--------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 141 erpmRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARY--PGTVIVIAHD 202
Cdd:cd03260 140 ----LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-221 |
4.18e-12 |
|
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: 64.93 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRG--RQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahlpqevpgsdrr 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 80 avdyVLDGdaelrdlqrrleqandgaeqarlyaalEAIDGWSAEARARRLlaglGFAPADAER---PMRD--FSGGWRMR 154
Cdd:cd03246 60 ----RLDG---------------------------ADISQWDPNELGDHV----GYLPQDDELfsgSIAEniLSGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 155 LGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYP---GTVIVIAHDRRFLDSvCTHVAHIERGTI 221
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
280-502 |
4.21e-12 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 69.02 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 280 LERMDEVAvirAARPIHLEIPTPGRLPDPL-LALDHAEVC--TGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLA 356
Cdd:COG4987 306 ARRLNELL---DAPPAVTEPAEPAPAPGGPsLELEDVSFRypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 357 GELLPTAGE--------RRVDPAL---QVGYFAQHqreqldleasplVHLQRQ---------DPRAEEQRLR-------- 408
Cdd:COG4987 383 RFLDPQSGSitlggvdlRDLDEDDlrrRIAVVPQR------------PHLFDTtlrenlrlaRPDATDEELWaalervgl 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 409 -NFLGGMGfpgDKADGPVG----QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--LVVVA 481
Cdd:COG4987 451 gDWLAALP---DGLDTWLGeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLIT 527
|
250 260
....*....|....*....|.
gi 648648866 482 HDRELLARVcDRFWTVEAGRL 502
Cdd:COG4987 528 HRLAGLERM-DRILVLEDGRI 547
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-501 |
4.40e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 303 GRLPDPLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV--DPALQVGYFAQH 380
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 381 ------QREQLDLEASPLVHLQ---------------RQDPRAEEQRLRNflggmgfpgdKADGPVGQCSGGERVRLVLA 439
Cdd:PRK13537 81 rvgvvpQFDNLDPDFTVRENLLvfgryfglsaaaaraLVPPLLEFAKLEN----------KADAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 440 LLIWQAPSLLLLDEPTNHLDLDMREALAEALEN-YAGG--LVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGktILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
329-493 |
4.54e-12 |
|
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: 66.31 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD-------PA--------------------------LQVG 375
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglPPheiarlgigrtfqiprlfpeltvlenVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 376 yfAQHQREQLDLEASPLVHLQRQDPRAEEqrLRNFLGgmgfPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPT 455
Cdd:cd03219 100 --AQARTGSGLLLARARREEREARERAEE--LLERVG----LADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648648866 456 NHLDLDMREALAEALE--NYAG-GLVVVAHDRELLARVCDR 493
Cdd:cd03219 172 AGLNPEETEELAELIRelRERGiTVLLVEHDMDVVMSLADR 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-181 |
5.01e-12 |
|
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: 66.05 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWV--------------VAHLPQEVPGSD 77
Cdd:cd03256 13 GKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqlrrqIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 78 R-RAVDYVLDGDAELRDLQRRLEQANDGAEQARLYAALEAIDgwsaeararrlLAGLGFAPADAerpmrdFSGGWRMRLG 156
Cdd:cd03256 92 RlSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVG-----------LLDKAYQRADQ------LSGGQQQRVA 154
|
170 180
....*....|....*....|....*
gi 648648866 157 LARTLMTRSDLLLLDEPTNHLDVET 181
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPAS 179
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-188 |
5.20e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.58 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDA---GEIeqppeWV----VAHLPQEv 73
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEV-----LLngrrLTALPAE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 74 pgsdRRAVDYvLDGDAEL-------RDLQRRLEQANDGAE-QARLYAALEAIDgwsaeararrlLAGLgfapadAERPMR 145
Cdd:COG4136 75 ----QRRIGI-LFQDDLLfphlsvgENLAFALPPTIGRAQrRARVEQALEEAG-----------LAGF------ADRDPA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDW 188
Cdd:COG4136 133 TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
309-502 |
5.22e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 66.29 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 309 LLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--------P---ALQVGYF 377
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawsPwelARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 378 AQHQREQLDLEASPLVHL----QRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGE--RVRL--VLAlLIWQA---- 445
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALgrapHGSSAAQDRQIVREALALVGL-AHLAGRSYQTLSGGEqqRVQLarVLA-QLWEPvdgg 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 446 PSLLLLDEPTNHLDLDMREALAEALENYA---GGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLArrgGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
7.33e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.81 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQ--PPEWV--VAHL 69
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDKPISMlsSRQLArrLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 70 PQEVPG----SDRRAVDYvldGDAELRDLQRRLEQAndgaEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMR 145
Cdd:PRK11231 82 PQHHLTpegiTVRELVAY---GRSPWLSLWGRLSAE----DNARVNQAMEQTR-----------INHL------ADRRLT 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD----VEtILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:PRK11231 138 DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVE-LMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-511 |
1.15e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 337 RIGILGPNGAGKSTLLTLLAGELLPTAGERRV---DPALQVGYFAQH------QREQL--DLEASPLVHLQRQ----DPR 401
Cdd:COG4586 50 IVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyVPFKRRKEFARRigvvfgQRSQLwwDLPAIDSFRLLKAiyriPDA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 402 AEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVR--LVLALLiwQAPSLLLLDEPTNHLDLDM----REALAEALENYAG 475
Cdd:COG4586 130 EYKKRLDELVELLDL-GELLDTPVRQLSLGQRMRceLAAALL--HRPKILFLDEPTIGLDVVSkeaiREFLKEYNRERGT 206
|
170 180 190
....*....|....*....|....*....|....*.
gi 648648866 476 GLVVVAHDRELLARVCDRFWTVEAGRLSpFDGDLDD 511
Cdd:COG4586 207 TILLTSHDMDDIEALCDRVIVIDHGRII-YDGSLEE 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
307-515 |
1.41e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 307 DPLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPA-----------LQVG 375
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 376 YFAQHQREQLDLEASPLV---HLQRQDPraEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLD 452
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpwQIRNQQP--DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 453 EPTNHLDLDMREALAEALENYAG----GLVVVAHDRELLARvCDRFWTveagrLSPFDGDLDD--YARA 515
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVReqniAVLWVTHDKDEINH-ADKVIT-----LQPHAGEMQEarYELA 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
308-502 |
1.47e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 308 PLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD-----------PALQVGY 376
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 377 FAQHQREQLDLEASPLV------HLQRQDP-----RAEEQRLRNFLGGMGFpgdkADGPVGQCSGGERVRLVLALLIWQA 445
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVemgrtpHRSRFDTwtetdRAAVERAMERTGVAQF----ADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 446 PSLLLLDEPTNHLDLDMR-EALAEALENYAGGLVVVA--HDRELLARVCDRFWTVEAGRL 502
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAaiHDLDLAARYCDELVLLADGRV 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
1.77e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.16 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELR--RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQPPEWV----VAH 68
Cdd:PRK11160 339 LTLNNVSFTypDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtrawdpqQGEILLNGQPIADYSEAAlrqaISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 69 LPQEVpgsdrravdYVLDGdaELRD-LQRRLEQANDGA-----EQARLYAALEAIDGwsaeararrLLAGLGfapaDAER 142
Cdd:PRK11160 419 VSQRV---------HLFSA--TLRDnLLLAAPNASDEAlievlQQVGLEKLLEDDKG---------LNAWLG----EGGR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 143 PMrdfSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPgTVIVIAHDRRFLDSVcTHVAHIERG 219
Cdd:PRK11160 475 QL---SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILELLAEHAQNK-TVLMITHRLTGLEQF-DRICVMDNG 549
|
..
gi 648648866 220 TI 221
Cdd:PRK11160 550 QI 551
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-223 |
1.94e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.39 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILlqHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI--------EQPP-EWVVAHLPQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltALPPaERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 72 E--------VpgsdRRAVDYVLDGDAELRDlqrrleqandgAEQARLYAALEAIDgwsaeararrlLAGLGfapadaERP 143
Cdd:COG3840 79 EnnlfphltV----AQNIGLGLRPGLKLTA-----------EQRAQVEQALERVG-----------LAGLL------DRL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 144 MRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD----VETILWLEDWLARYPGTVIVIAHD----RRFldsvCTHVAH 215
Cdd:COG3840 127 PGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDpedaARI----ADRVLL 202
|
....*...
gi 648648866 216 IERGTIAL 223
Cdd:COG3840 203 VADGRIAA 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
338-501 |
2.00e-11 |
|
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: 63.99 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 338 IGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQV-------------------GYFAQHQRE-----QLDLEASPLV 393
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaqaspreilalrrrtiGYVSQFLRViprvsALDVVAEPLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 394 HLQRQDPRAEEqRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENY 473
Cdd:COG4778 120 ERGVDREEARA-RARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA 198
|
170 180 190
....*....|....*....|....*....|.
gi 648648866 474 -AGGLVVVA--HDRELLARVCDRFWTVEAGR 501
Cdd:COG4778 199 kARGTAIIGifHDEEVREAVADRVVDVTPFS 229
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
330-504 |
2.18e-11 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 63.91 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 330 LRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPA---------------LQVGYFAQHQREQLD---LE--A 389
Cdd:TIGR02211 26 LSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQslsklssneraklrnKKLGFIYQFHHLLPDftaLEnvA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 390 SPLVhLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEA 469
Cdd:TIGR02211 106 MPLL-IGKKSVKEAKERAYEMLEKVGL-EHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDL 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 648648866 470 L----ENYAGGLVVVAHDRELLARVcDRFWTVEAGRLSP 504
Cdd:TIGR02211 184 MlelnRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-201 |
2.59e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 63.28 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 11 RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVvahlpQEVPGSDRRAVDYVLDGDAe 90
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 lrdlqrrLEQANDGAEQARLYAALEAIDGwSAEARARRLLAGLGfapadaERPMRDFSGGWRMRLGLARTLMTRSDLLLL 170
Cdd:cd03231 84 -------IKTTLSVLENLRFWHADHSDEQ-VEEALARVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....
gi 648648866 171 DEPTNHLDVETILWLEDWLARYP---GTVIVIAH 201
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
329-502 |
2.65e-11 |
|
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: 63.54 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD-------PA---LQVGYFAQHQ--------REQLDLEAS 390
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvkePAearRRLGFVSDSTglydrltaRENLEYFAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 391 pLVHLQRQdprAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEAL 470
Cdd:cd03266 105 -LYGLKGD---ELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180 190
....*....|....*....|....*....|....*
gi 648648866 471 ENY-AGG--LVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03266 180 RQLrALGkcILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
308-502 |
3.48e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.02 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 308 PLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP-----------ALQVGY 376
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 377 FAQHQ--------REQLDLEASPLVHLQRQDPRAEEQRLRNfLGGMGFpgdkADGPVGQCSGGE--RVRL--VLALLiWQ 444
Cdd:PRK13548 81 LPQHSslsfpftvEEVVAMGRAPHGLSRAEDDALVAAALAQ-VDLAHL----AGRDYPQLSGGEqqRVQLarVLAQL-WE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 445 A---PSLLLLDEPTNHLDLDMREALAEALENYA----GGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK13548 155 PdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAhergLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-207 |
3.76e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWR-----VGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwvVAHLPQEVpgsdrrAVDYvldgDAELRDLq 95
Cdd:PRK13409 354 SLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--ISYKPQYI------KPDY----DGTVEDL- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 96 rrLEQANDGAEQARLYAalEAIDGWSAEararRLLaglgfapadaERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTN 175
Cdd:PRK13409 421 --LRSITDDLGSSYYKS--EIIKPLQLE----RLL----------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190
....*....|....*....|....*....|....*.
gi 648648866 176 HLDVETILWLEDWLARY----PGTVIVIAHDRRFLD 207
Cdd:PRK13409 483 HLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMID 518
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-182 |
4.02e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.76 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 5 QDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVvahlpQEVPGSDRRAVDYV 84
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 --LDG-DAELRDLQR-RLEQANDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGWRMRLGLART 160
Cdd:TIGR01189 79 ghLPGlKPELSALENlHFWAAIHGGAQRTIEDALAAVG-----------LTGF------EDLPAAQLSAGQQRRLALARL 141
|
170 180
....*....|....*....|..
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETI 182
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKAGV 163
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
424-498 |
4.34e-11 |
|
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: 62.62 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 424 PVGQCSGGERV------RLVLALLIWQAPSLLLLDEPTNHLDLDMRE-ALAEALENYAGG----LVVVAHDRELLARVcD 492
Cdd:cd03240 112 MRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELVDAA-D 190
|
....*.
gi 648648866 493 RFWTVE 498
Cdd:cd03240 191 HIYRVE 196
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-213 |
4.66e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.58 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 30 VGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwVVAHLPQEVPGSDRRAVDYVLdgdaelrdlqrrLEQANDGAEQAr 109
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTVRDLL------------SSITKDFYTHP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 110 lYAALEAIDGWSAEararRLLaglgfapadaERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWL 189
Cdd:cd03237 94 -YFKTEIAKPLQIE----QIL----------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180
....*....|....*....|....*...
gi 648648866 190 ARY----PGTVIVIAHDRRFLDSVCTHV 213
Cdd:cd03237 159 RRFaennEKTAFVVEHDIIMIDYLADRL 186
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-224 |
4.91e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.18 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahlpqEVPGSdrraVDYVLD---G-DAELr 92
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-------------EVNGR----VSALLElgaGfHPEL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 93 dlqrrleqanDGAEQARLYAaleAIDGWSAEARARRL-----LAGLGfapaDA-ERPMRDFSGGWRMRLGLARTLMTRSD 166
Cdd:COG1134 104 ----------TGRENIYLNG---RLLGLSRKEIDEKFdeiveFAELG----DFiDQPVKTYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 167 LLLLDEptnhldvetilwledWLA------------------RYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALY 224
Cdd:COG1134 167 ILLVDE---------------VLAvgdaafqkkclarirelrESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-181 |
5.14e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 7 IELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGEL--ALDAGEIEQPPEwvvaHLPQEVPGSDRRAvdyv 84
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDN----QFGREASLIDAIG---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 LDGDAelrdlqrrleqandgaeqarlYAALEAIDGwsaeararrllAGLGFAPAdAERPMRDFSGGWRMRLGLARTLMTR 164
Cdd:COG2401 108 RKGDF---------------------KDAVELLNA-----------VGLSDAVL-WLRRFKELSTGQKFRFRLALLLAER 154
|
170
....*....|....*..
gi 648648866 165 SDLLLLDEPTNHLDVET 181
Cdd:COG2401 155 PKLLVIDEFCSHLDRQT 171
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-501 |
5.73e-11 |
|
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: 62.30 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPAlQVGYFAQHQ----------------RE 383
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-PLDIAARNRigylpeerglypkmkvID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 384 QLDLEASpLVHLQRQDPRAEEQRLRNFLGgmgfPGDKADGPVGQCSGG--ERVRLVLALLiwQAPSLLLLDEPTNHLDLD 461
Cdd:cd03269 90 QLVYLAQ-LKGLKKEEARRRIDEWLERLE----LSEYANKRVEELSKGnqQKVQFIAAVI--HDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 462 MREALAEALENYAGG---LVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:cd03269 163 NVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-210 |
6.25e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.86 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWV-----------VAHL 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaraasrrVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 70 PQEVpgsdrrAVDYVLDGdaelrdlqRRLEQANDGAEQARLYAALEAIDGWSAEARARrllaglGFAPADAERPMRDFSG 149
Cdd:PRK09536 83 PQDT------SLSFEFDV--------RQVVEMGRTPHRSRFDTWTETDRAAVERAMER------TGVAQFADRPVTSLSG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 150 GWRMRLGLARTLMTRSDLLLLDEPTNHLDVE---TILWLEDWLARYPGTVIVIAHD----RRFLDSVC 210
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINhqvRTLELVRRLVDDGKTAVAAIHDldlaARYCDELV 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-179 |
7.26e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.02 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDRRA 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-------------YRMRDGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDGDAELRDLQRR----LEQ-ANDGAEQA---------RLYAAleaidGW----SAEARARRLLAGLGFAPADAER 142
Cdd:PRK11701 73 RDLYALSEAERRRLLRTewgfVHQhPRDGLRMQvsaggnigeRLMAV-----GArhygDIRATAGDWLERVEIDAARIDD 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 648648866 143 PMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDV 179
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
325-502 |
7.72e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 62.37 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV---------DPAL------QVGY-FAQHQ------- 381
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdgqdisslsERELarlrrrHIGFvFQFFNllpelta 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLeasPLVhLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:COG1136 104 LENVAL---PLL-LAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 648648866 462 MREALAEALENYAG----GLVVVAHDRELLARvCDRFWTVEAGRL 502
Cdd:COG1136 179 TGEEVLELLRELNRelgtTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-201 |
7.92e-11 |
|
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: 62.13 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELR--RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQ-PPEWVVAHL-- 69
Cdd:cd03244 3 IEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALfrlvelsSGSILIDGVDISKiGLHDLRSRIsi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 70 -PQEV---PGSDRRAVDyvldgdaelrdlqrRLEQANDgaeqARLYAALEAIDGWSAEARarrLLAGLGfapADAERPMR 145
Cdd:cd03244 83 iPQDPvlfSGTIRSNLD--------------PFGEYSD----EELWQALERVGLKEFVES---LPGGLD---TVVEEGGE 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWL-ARYPG-TVIVIAH 201
Cdd:cd03244 139 NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFKDcTVLTIAH 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
307-537 |
9.29e-11 |
|
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: 64.54 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 307 DPLLALDHAEVC--TGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTA---GERRVDP----------- 370
Cdd:COG1123 2 TPLLEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGrdllelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 371 ALQVGYFAQHQREQLD--------LEASPLVHLQRQDPRAEEQRLRNFLGGMGFpgdkADGPVGQCSGGERVRLVLALLI 442
Cdd:COG1123 82 GRRIGMVFQDPMTQLNpvtvgdqiAEALENLGLSRAEARARVLELLEAVGLERR----LDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 443 WQAPSLLLLDEPTNHLD----LDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSpFDGDLDD---YARA 515
Cdd:COG1123 158 ALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV-EDGPPEEilaAPQA 236
|
250 260
....*....|....*....|..
gi 648648866 516 LQARQREAARSAAETPPQAASD 537
Cdd:COG1123 237 LAAVPRLGAARGRAAPAAAAAE 258
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
320-506 |
9.35e-11 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 61.77 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD-------PALQ--VGYFAQHQR--EQLDLE 388
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvPPERrnIGMVFQDYAlfPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 389 ---ASPLVHlqRQDPRAE-EQRLRNFLGGMGFPGDkADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMRE 464
Cdd:cd03259 91 eniAFGLKL--RGVPKAEiRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLRE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 465 ALAEALENY--AGGL--VVVAHDRELLARVCDRFWTVEAGRLSPFD 506
Cdd:cd03259 168 ELREELKELqrELGIttIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-221 |
9.77e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 62.32 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDrra 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIT-------------VDGED--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdyVLDGDAELRDLQRRL----EQANdgaeqarLYAALEAID----------GWS---AEARARRLLA--GLGfAPADAe 141
Cdd:COG1126 65 ---LTDSKKDINKLRRKVgmvfQQFN-------LFPHLTVLEnvtlapikvkKMSkaeAEERAMELLErvGLA-DKADA- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 142 RPmRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETI---------LWLEDWlarypgTVIVIAHDRRFLDSVCTH 212
Cdd:COG1126 133 YP-AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVgevldvmrdLAKEGM------TMVVVTHEMGFAREVADR 205
|
....*....
gi 648648866 213 VAHIERGTI 221
Cdd:COG1126 206 VVFMDGGRI 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
306-502 |
1.03e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 62.07 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 306 PDPLLALDHAEVC----TGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD----PAL----- 372
Cdd:COG4181 5 SAPIIELRGLTKTvgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgqdlFALdedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 373 ------QVGY-FaqhQREQL-----DLE--ASPLVHLQRQDPRaeeQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVL 438
Cdd:COG4181 85 arlrarHVGFvF---QSFQLlptltALEnvMLPLELAGRRDAR---ARARALLERVGL-GHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 439 ALLIWQAPSLLLLDEPTNHLDLDMREALAEALE--NYAGG--LVVVAHDRELLARvCDRFWTVEAGRL 502
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGttLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-202 |
1.06e-10 |
|
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: 62.66 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 5 QDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDRRAVDyv 84
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL-------------IDGQDIAAMS-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 ldgDAELRDLQRR-----------------LEQANDGAE------QARLYAALEAIDgwsaeararrlLAGLGfapADAE 141
Cdd:cd03294 93 ---RKELRELRRKkismvfqsfallphrtvLENVAFGLEvqgvprAEREERAAEALE-----------LVGLE---GWEH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 142 RPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD-------VETILWLEDWLARypgTVIVIAHD 202
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAELQK---TIVFITHD 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-221 |
1.14e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 14 QILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQ------------GELALDAGEIEQPPEWVVAHLPQEV-------- 73
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARSLSQQKGLIRQLRQHVgfvfqnfn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 74 --PgsDRRAVDYVLDGDAELRDLQRRleqandgaeqarlyaaleaidgwSAEARARRLLAGLGFAPADAERPMRdFSGGW 151
Cdd:PRK11264 96 lfP--HRTVLENIIEGPVIVKGEPKE-----------------------EATARARELLAKVGLAGKETSYPRR-LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 152 RMRLGLARTLMTRSDLLLLDEPTNHLDVE---TILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPElvgEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-207 |
1.16e-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: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGW-----RVGLTGANGSGKSSLLAALQGELALDAGEIEqpPEWVVAHLPQEVPGsdrravdyvlDGDAELRDLq 95
Cdd:COG1245 355 SLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYISP----------DYDGTVEEF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 96 rrLEQANDGAEQARLYAAlEAIDGWSAEararRLLaglgfapadaERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTN 175
Cdd:COG1245 422 --LRSANTDDFGSSYYKT-EIIKPLGLE----KLL----------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190
....*....|....*....|....*....|....*.
gi 648648866 176 HLDVETILWLEDWLARY----PGTVIVIAHDRRFLD 207
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLID 520
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
340-502 |
1.22e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 61.61 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVD------------PAL--QVGYFAQHQR--------EQLDLeasPLvHLQR 397
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlkrreiPYLrrRIGVVFQDFRllpdrtvyENVAL---PL-RVTG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 398 QDPRAEEQRLRNFLG--GMGfpgDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALE--NY 473
Cdd:COG2884 109 KSRKEIRRRVREVLDlvGLS---DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEeiNR 185
|
170 180 190
....*....|....*....|....*....|
gi 648648866 474 AGGLVVVA-HDRELLARVCDRFWTVEAGRL 502
Cdd:COG2884 186 RGTTVLIAtHDLELVDRMPKRVLELEDGRL 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-221 |
1.25e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.36 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIEL---RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQ-------GELALDAGEIEQPPEW------- 64
Cdd:TIGR00958 479 IEFQDVSFsypNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLDGVPLVQYDHHylhrqva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 65 VVAHLPQEVPGSDRRAVDYVLDgdaelrdlqrrleqandgaeqarlYAALEAIDGWSAEARARRLLAGL--GFAPADAER 142
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGLT------------------------DTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEK 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 143 PMRdFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHdRRFLDSVCTHVAHIERGTI 221
Cdd:TIGR00958 615 GSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSV 691
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-202 |
1.38e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 61.93 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDI-ELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDRRA 80
Cdd:cd03295 1 IEFENVtKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIF-------------IDGEDIRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVldgdaELRdlqRRLEQAndgAEQARLY---------AALEAIDGWSAE---ARARRLLAGLGFAPAD-AERPMRDF 147
Cdd:cd03295 68 QDPV-----ELR---RKIGYV---IQQIGLFphmtveeniALVPKLLKWPKEkirERADELLALVGLDPAEfADRYPHEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYP----GTVIVIAHD 202
Cdd:cd03295 137 SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelgKTIVFVTHD 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-222 |
1.50e-10 |
|
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: 61.16 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 29 RVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpeWVVAHLPQEVPgSDRRAVDYVLDGDAELRDLQRRleqandga 105
Cdd:cd03297 25 VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngTV--LFDSRKKINLP-PQQRKIGLVFQQYALFPHLNVR-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 106 eQARLYAALEAIDGwSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---- 181
Cdd:cd03297 94 -ENLAFGLKRKRNR-EDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlql 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648648866 182 ILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
300-501 |
1.50e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 300 PTPGRLPDplLALDHAEVCT--GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV----DPA-- 371
Cdd:PRK13536 32 SIPGSMST--VAIDLAGVSKsyGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpVPAra 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 372 ----LQVGYFAQHQReqLDLEASPLVHLQ------RQDPRAEEQRLRNFLGGMGFPgDKADGPVGQCSGGERVRLVLALL 441
Cdd:PRK13536 110 rlarARIGVVPQFDN--LDLEFTVRENLLvfgryfGMSTREIEAVIPSLLEFARLE-SKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 442 IWQAPSLLLLDEPTNHLDLDMREALAEALEN-YAGG--LVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGktILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-215 |
1.69e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPQevpgsdrravdyvldgdAELRDLQRR 97
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgQD----ITGLSG-----------------RELRPLRRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 98 LE---QanDGaeqarlYAAL-----------EAI------DGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGL 157
Cdd:COG4608 97 MQmvfQ--DP------YASLnprmtvgdiiaEPLrihglaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLDV----ETILWLEDWLARYPGTVIVIAHDrrfLdSVCTHVAH 215
Cdd:COG4608 169 ARALALNPKLIVCDEPVSALDVsiqaQVLNLLEDLQDELGLTYLFISHD---L-SVVRHISD 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-178 |
2.00e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 63.71 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 14 QILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL------QGELALDAGEIEQ--PPEWVvAHL------PQEVPGSDRr 79
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpyQGSLKINGIELREldPESWR-KHLswvgqnPQLPHGTLR- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 80 avDYVLDGDAELRD--LQRRLEQANdgaeqarlyaALEAIDgwsaeararRLLAGLGFAPADAerpMRDFSGGWRMRLGL 157
Cdd:PRK11174 441 --DNVLLGNPDASDeqLQQALENAW----------VSEFLP---------LLPQGLDTPIGDQ---AAGLSVGQAQRLAL 496
|
170 180
....*....|....*....|.
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLD 178
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLD 517
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
325-502 |
2.25e-10 |
|
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: 61.74 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------------------RRVDPALQVGYFAQHQREQ 384
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTvsfrgqdlyqldrkqrrafrRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 385 LD-LEASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMR 463
Cdd:TIGR02769 107 VRqIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 464 EALAEALENY--AGGL--VVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:TIGR02769 187 AVILELLRKLqqAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-221 |
2.32e-10 |
|
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: 60.88 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQIL-LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPQEVPGSD 77
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngQD----VSDLRGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 78 RRAVDYVLDgdaELRDLQRRLEQANdgaeqarLYAALEAIDGWSAEARAR--RLLAGLGFAPADAERPMrDFSGGWRMRL 155
Cdd:cd03292 77 RRKIGVVFQ---DFRLLPDRNVYEN-------VAFALEVTGVPPREIRKRvpAALELVGLSHKHRALPA-ELSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 156 GLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-179 |
2.67e-10 |
|
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: 63.16 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAAL------QGELALDAgeieqppewvvahlpQEVPGSDRRAvdyvldgdae 90
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALlrlipsEGEIRFDG---------------QDLDGLSRRA---------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 LRDLQRRLE---QanDGaeqarlYAAL------EAI---------DGWSA---EARARRLLAGLGFAPADAERPMRDFSG 149
Cdd:COG4172 357 LRPLRRRMQvvfQ--DP------FGSLsprmtvGQIiaeglrvhgPGLSAaerRARVAEALEEVGLDPAARHRYPHEFSG 428
|
170 180 190
....*....|....*....|....*....|
gi 648648866 150 GWRMRLGLARTLMTRSDLLLLDEPTNHLDV 179
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-223 |
2.71e-10 |
|
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: 60.53 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVPgsdRRAVDYVLDGDAELRDL-- 94
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---RAGIGYVPEGRRIFPELtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 95 -------QRRLEQANDGAEQARLYAALEAIdgwsAEARARRllAGlgfapadaerpmrDFSGGWRMRLGLARTLMTRSDL 167
Cdd:cd03224 93 eenlllgAYARRRAKRKARLERVYELFPRL----KERRKQL--AG-------------TLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 168 LLLDEPTNHLD---VETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIAL 223
Cdd:cd03224 154 LLLDEPSEGLApkiVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVL 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
306-502 |
2.74e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.34 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 306 PDPLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQhqreql 385
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 dLEASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQ-------------------------CSGGERVRLVLAL 440
Cdd:PRK10575 82 -AFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAadrekveeaislvglkplahrlvdsLSGGERQRAWIAM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 441 LIWQAPSLLLLDEPTNHLDLDMRE---ALAEALENYAGGLVV-VAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVdvlALVHRLSQERGLTVIaVLHDINMAARYCDYLVALRGGEM 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-221 |
2.74e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.63 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 10 RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPQEVPGSDRRAVDYVLD 86
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgEP----LAKLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 87 GDAELRDLQRRLeqandGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSD 166
Cdd:PRK10419 97 DSISAVNPRKTV-----REIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 167 LLLLDEPTNHLDV----ETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:PRK10419 172 LLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-222 |
3.29e-10 |
|
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: 62.05 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 20 ASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPE-WVVAHLPQEVPgSDRRAVDYVLdgdaelrdlqrrl 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtLFDSRKGIFLP-PEKRRIGYVF------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 99 eqandgaEQARLYAALEA----------IDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTLMTRSDLL 168
Cdd:TIGR02142 82 -------QEARLFPHLSVrgnlrygmkrARPSERRISFERVIELLGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 169 LLDEPTNHLDV----ETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:TIGR02142 154 LMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-201 |
4.18e-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: 62.83 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRG--RQILlQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELAL--------DAGEIEQppew 64
Cdd:TIGR01193 474 IVINDVSYSYGygSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLvgffqarSGEILLngfslkdiDRHTLRQ---- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 65 VVAHLPQEvpgsdrravDYVLDGDAelrdLQRRLEQANDGAEQARLYAALEAidgwsAEARARRLLAGLGFAPADAERPM 144
Cdd:TIGR01193 549 FINYLPQE---------PYIFSGSI----LENLLLGAKENVSQDEIWAACEI-----AEIKDDIENMPLGYQTELSEEGS 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 145 rDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD-------VETILWLEDwlarypGTVIVIAH 201
Cdd:TIGR01193 611 -SISGGQKQRIALARALLTDSKVLILDESTSNLDtitekkiVNNLLNLQD------KTIIFVAH 667
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
325-524 |
4.42e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP------ALQVGYfaqHQ----REQLDLEASpLVH 394
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsallELGAGF---HPeltgRENIYLNGR-LLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 395 LQRQDPRAEEQRLRNF--LggmgfpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDeptnhldldmrEALA----- 467
Cdd:COG1134 118 LSRKEIDEKFDEIVEFaeL------GDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVD-----------EVLAvgdaa 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 468 ------EALENY---AGGLVVVAHDRELLARVCDR-FWtVEAGRLSpFDGDLDDYARALQARQREAA 524
Cdd:COG1134 181 fqkkclARIRELresGRTVIFVSHSMGAVRRLCDRaIW-LEKGRLV-MDGDPEEVIAAYEALLAGRE 245
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-222 |
4.69e-10 |
|
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: 59.81 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILlqHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeQPPEWVVAHLPQEvpgsdRRAV 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-LINGVDVTAAPPA-----DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGDAELRDLQrrLEQANDGAEQARLYaaLEAIDGWSAEARARRLlaglGFAPADAERPmRDFSGGWRMRLGLARTL 161
Cdd:cd03298 73 SMLFQENNLFAHLT--VEQNVGLGLSPGLK--LTAEDRQAIEVALARV----GLAGLEKRLP-GELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 162 MTRSDLLLLDEPTNHLD----VETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIA 222
Cdd:cd03298 144 VRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
5-222 |
5.24e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 60.35 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 5 QDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL---------QGELALDAGEI-EQPPE-------WVVA 67
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpsyevtSGTILFKGQDLlELEPDeraraglFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 68 HLPQEVPGsdrravdyvldgdAELRDLQRrleqanDGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRD- 146
Cdd:TIGR01978 84 QYPEEIPG-------------VSNLEFLR------SALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 147 FSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARY--PGT-VIVIAHDRRFLDSVCTHVAHI-ERGTIA 222
Cdd:TIGR01978 145 FSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRsFLIITHYQRLLNYIKPDYVHVlLDGRIV 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-202 |
5.64e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvVAHLPQEVPGSDRrA 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSIT------LDGKPVEGPGAER-G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDGDAELRDLQRRLEqandgaeqarLYAALEAIDGWSAEARARRLLAGLGFAPADAeRPMRDFSGGWRMRLGLART 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVA----------FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648648866 161 LMTRSDLLLLDEPTNHLDVET-----ILWLEDWlARYPGTVIVIAHD 202
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTreqmqTLLLKLW-QETGKQVLLITHD 188
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
339-502 |
7.25e-10 |
|
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: 59.50 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 339 GILGPNGAGKST-----LLTLLAGELLPTAGERRVDPA-------------LQVGYFAQHQ-------REQLDLeasPLV 393
Cdd:cd03260 30 ALIGPSGCGKSTllrllNRLNDLIPGAPDEGEVLLDGKdiydldvdvlelrRRVGMVFQKPnpfpgsiYDNVAY---GLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 394 HLQRQDPRAEEQRLRNFLGGMGFPG---DKADGpvGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREAL 466
Cdd:cd03260 107 LHGIKLKEELDERVEEALRKAALWDevkDRLHA--LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDpistAKIEELI 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 648648866 467 AEALENYAggLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03260 185 AELKKEYT--IVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
310-502 |
7.33e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP-----------ALQVGYFA 378
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 379 QHQ--------REQLDLEASPLVHLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLL 450
Cdd:PRK11231 83 QHHltpegitvRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 451 LDEPTNHLDLD--------MREalaeaLENYAGGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK11231 162 LDEPTTYLDINhqvelmrlMRE-----LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-224 |
9.10e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppEWvvahLPQEVPGSDRRA 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV----LW----DGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDgdaelrdlQRRLEQANDGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLART 160
Cdd:COG4152 73 IGYLPE--------ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDR-ANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETILWLEDWLARY--PG-TVIVIAHDrrfLDSV---CTHVAHIERGTIALY 224
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQ---MELVeelCDRIVIINKGRKVLS 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-202 |
9.60e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALqgelaldaGEIEQPPEWVVahlpqEVPGSDRRAvdyvLDGD--AELRD- 93
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNIL--------GCLDKPTSGTY-----RVAGQDVAT----LDADalAQLRRe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 94 -----LQRRLEQANDGAEQ----ARLYAALEAIdgwSAEARARRLLAGLGFAPADAERPMRdFSGGWRMRLGLARTLMTR 164
Cdd:PRK10535 87 hfgfiFQRYHLLSHLTAAQnvevPAVYAGLERK---QRLLRAQELLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648648866 165 SDLLLLDEPTNHLD------VETILwleDWLARYPGTVIVIAHD 202
Cdd:PRK10535 163 GQVILADEPTGALDshsgeeVMAIL---HQLRDRGHTVIIVTHD 203
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-201 |
9.64e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI--------EQPPE------WvV 66
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirRQRDEyhqdllY-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 67 AHLPqevpgsdrrAVDYVLDGDAELRDLQRrleqANDGAEQARLYAALEAIDgwsaeararrlLAGLGFAPAdaerpmRD 146
Cdd:PRK13538 80 GHQP---------GIKTELTALENLRFYQR----LHGPGDDEALWEALAQVG-----------LAGFEDVPV------RQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 147 FSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYP---GTVIVIAH 201
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
320-502 |
1.12e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE------------RRVDPAL--QVGY-FAQHQ--- 381
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKiwfsghditrlkNREVPFLrrQIGMiFQDHHllm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 -REQLDLEASPLV--HLQRQDPRaeeQRLRNFLGGMGFPgDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHL 458
Cdd:PRK10908 93 dRTVYDNVAIPLIiaGASGDDIR---RRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648648866 459 DLDMREALAEALE--NYAGGLVVVA-HDRELLARVCDRFWTVEAGRL 502
Cdd:PRK10908 169 DDALSEGILRLFEefNRVGVTVLMAtHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-513 |
1.13e-09 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 59.12 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP---------AL-----QVGYFAQHQR--E 383
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkALrqlrrQIGMIFQQFNliE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 384 QLD-LEA---------SPLVHLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDE 453
Cdd:cd03256 92 RLSvLENvlsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 454 PTNHLDLDMREALAEALE--NYAGGLVVVA--HDRELLARVCDRFWTVEAGRLSpFDG---DLDDYA 513
Cdd:cd03256 171 PVASLDPASSRQVMDLLKriNREEGITVIVslHQVDLAREYADRIVGLKDGRIV-FDGppaELTDEV 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
1.14e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 58.98 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELR----RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGS 76
Cdd:COG4181 8 IIELRGLTKTvgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVR-------------LAGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 DRRAvdyvLDGDAELRDLQRR-----------------------LEQANDGaeqarlyaaleaidgwSAEARARRLLAGL 133
Cdd:COG4181 75 DLFA----LDEDARARLRARHvgfvfqsfqllptltalenvmlpLELAGRR----------------DARARARALLERV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 134 GFAPADAERPmRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET----ILWLEDWLARYPGTVIVIAHDRRfLDSV 209
Cdd:COG4181 135 GLGHRLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHDPA-LAAR 212
|
250
....*....|..
gi 648648866 210 CTHVAHIERGTI 221
Cdd:COG4181 213 CDRVLRLRAGRL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
329-502 |
1.15e-09 |
|
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: 59.13 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD---------PAL-----QVGYFAQH-----QREQLDLEA 389
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllsgKELrkarrRIGMIFQHfnllsSRTVFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 390 SPL----VHLQRQDPRAEEqrLRNFLGgmgfPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREA 465
Cdd:cd03258 105 LPLeiagVPKAEIEERVLE--LLELVG----LEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648648866 466 LAEALE--NYAGGL--VVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03258 179 ILALLRdiNRELGLtiVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-203 |
1.18e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.50 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI---EQppewVVAHLPQEvpgsd 77
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldGR----DVTGLPPE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 78 RRAV-----DY-------VLD----GdaeLRdlQRRLeqanDGAEqarlyaaleaidgwsAEARARRLLA--GL-GFApa 138
Cdd:COG3842 76 KRNVgmvfqDYalfphltVAEnvafG---LR--MRGV----PKAE---------------IRARVAELLElvGLeGLA-- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 139 daERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD----VETILWLEDWLARYPGTVIVIAHDR 203
Cdd:COG3842 130 --DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
338-520 |
1.30e-09 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 58.82 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 338 IGILGPNGAGKSTLLTLLAGELLPTAGERRVD------------PALQVGYFAQHQ---REqLDLEASPLVHLQRQ---D 399
Cdd:TIGR04406 30 VGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmherARLGIGYLPQEAsifRK-LTVEENIMAVLEIRkdlD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 400 PRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREaLAEALENYAG 475
Cdd:TIGR04406 109 RAEREERLEALLEEFQI-SHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavGDIKK-IIKHLKERGI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 476 GLVVVAHD-RELLArVCDRFWTVEAGRLSpFDGDLDDYARALQARQ 520
Cdd:TIGR04406 187 GVLITDHNvRETLD-ICDRAYIISDGKVL-AEGTPAEIVANEKVRR 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
1.43e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvVAhlpqevpgsdrrav 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLN------IA-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGDAELRDLQRRLEQANDGA--EQARLYAALEAID----------GWS---AEARARRLLAGLGFAPAdAER-PMR 145
Cdd:COG4161 63 GHQFDFSQKPSEKAIRLLRQKVGMvfQQYNLWPHLTVMEnlieapckvlGLSkeqAREKAMKLLARLRLTDK-ADRfPLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 146 dFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD-------VETILWLEDwlaryPG-TVIVIAHDRRFLDSVCTHVAHIE 217
Cdd:COG4161 142 -LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqvVEIIRELSQ-----TGiTQVIVTHEVEFARKVASQVVYME 215
|
....
gi 648648866 218 RGTI 221
Cdd:COG4161 216 KGRI 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
1.52e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.09 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDI----ELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGelaldageieqppewvvahlpQEVPGS 76
Cdd:COG1135 1 MIELENLsktfPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---------------------LERPTS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 DRRAVDYV----LDGdAELRDLQRRL----EQANdgaeqarLYAA----------LEaIDGWSAEARARR---LLA--GL 133
Cdd:COG1135 60 GSVLVDGVdltaLSE-RELRAARRKIgmifQHFN-------LLSSrtvaenvalpLE-IAGVPKAEIRKRvaeLLElvGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 134 GfAPADAeRPmRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLedwLAR----YPGTVIVIAHD---- 202
Cdd:COG1135 131 S-DKADA-YP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsILDL---LKDinreLGLTIVLITHEmdvv 204
|
250
....*....|....*....
gi 648648866 203 RRfldsVCTHVAHIERGTI 221
Cdd:COG1135 205 RR----ICDRVAVLENGRI 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
270-522 |
2.15e-09 |
|
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: 60.53 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 270 ARQAQSRLKRLERMdevaviRAARPIHLEIPTP-GRLpdpllALDHAEVCT--GERVRLQPTTLRLRPEDRIGILGPNGA 346
Cdd:COG4618 301 ARQAYRRLNELLAA------VPAEPERMPLPRPkGRL-----SVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 347 GKSTLLTLLAGELLPTAGERRVDPAL-----------QVGYFAQHqreqldleasplVHL---------QR-QDPRAEE- 404
Cdd:COG4618 370 GKSTLARLLVGVWPPTAGSVRLDGADlsqwdreelgrHIGYLPQD------------VELfdgtiaeniARfGDADPEKv 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 405 -------------QRLRNflggmGFpgdkaDGPVGQ----CSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALA 467
Cdd:COG4618 438 vaaaklagvhemiLRLPD-----GY-----DTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA 507
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 468 EALEN--YAGG-LVVVAHDRELLArVCDRFWTVEAGRLSPFdGDLDDYARALQARQRE 522
Cdd:COG4618 508 AAIRAlkARGAtVVVITHRPSLLA-AVDKLLVLRDGRVQAF-GPRDEVLARLARPAAA 563
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-217 |
2.18e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 56.78 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 14 QILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQE---VPGSDRRAVDYVldgdae 90
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRpylPLGTLREQLIYP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 lrdlqrrleqandgaeqarlyaaleaidgWSAEararrllaglgfapadaerpmrdFSGGWRMRLGLARTLMTRSDLLLL 170
Cdd:cd03223 88 -----------------------------WDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648648866 171 DEPTNHLDVETILWLEDWLARYPGTVIVIAHdRRFLDSVCTHVAHIE 217
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-201 |
2.47e-09 |
|
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: 58.01 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQppewvvahLPQEvpgSDRRAV--- 81
Cdd:cd03253 13 GRPVL-KDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvsSGSILIDGQDIRE--------VTLD---SLRRAIgvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 --DYVLDGDaelrDLQRRLEQANDGAEQARLYAALEAidgwsaeARARRLLAGL--GFAPADAERPMRdFSGGWRMRLGL 157
Cdd:cd03253 81 pqDTVLFND----TIGYNIRYGRPDATDEEVIEAAKA-------AQIHDKIMRFpdGYDTIVGERGLK-LSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAH 201
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-221 |
2.58e-09 |
|
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: 58.12 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEvpgsdrRAV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE------RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGDAELRDL------------QRRLEQANDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSG 149
Cdd:cd03296 77 GFVFQHYALFRHMtvfdnvafglrvKPRSERPPEAEIRAKVHELLKLVQ-----------LDWL------ADRYPAQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 150 GWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG----TVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03296 140 GQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-201 |
2.79e-09 |
|
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: 58.01 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSDRRAVDYvldgdAELRDLQR 96
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIL-------------IDGHDVRDYTL-----ASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 97 RLEQ---------------ANDGAEQARLYAALEAidgwsaeARARRLLAGL--GFAPADAERPMRdFSGGWRMRLGLAR 159
Cdd:cd03251 80 LVSQdvflfndtvaeniayGRPGATREEVEEAARA-------ANAHEFIMELpeGYDTVIGERGVK-LSGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648648866 160 TLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAH 201
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKnrTTFVIAH 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
310-481 |
2.93e-09 |
|
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: 57.37 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP---ALQVGYFAQH-----Q 381
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENilylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLEASPLVHLQ--RQDPRAEEQRLRNFLGGMGFPGdKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD 459
Cdd:TIGR01189 81 LPGLKPELSALENLHfwAAIHGGAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....
gi 648648866 460 LDMREALAEALENYA--GGLVVVA 481
Cdd:TIGR01189 160 KAGVALLAGLLRAHLarGGIVLLT 183
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-226 |
3.05e-09 |
|
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: 57.67 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 15 ILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQG---ELALDAGEI---EQPPEwvvahlPQEVpgsdRRAVDYVLDGD 88
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQIlfnGQPRK------PDQF----QKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 89 AELRDLQrrleqandgAEQARLYAALEAIDGWSAEARARR-----LLAGLGFAPADAERpMRDFSGGWRMRLGLARTLMT 163
Cdd:cd03234 91 ILLPGLT---------VRETLTYTAILRLPRKSSDAIRKKrvedvLLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 164 RSDLLLLDEPTNHLD----VETILWLEDwLARYPGTVIVIAHD-RRFLDSVCTHVAHIERGTIAlYAG 226
Cdd:cd03234 161 DPKVLILDEPTSGLDsftaLNLVSTLSQ-LARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV-YSG 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-174 |
3.24e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 57.68 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahlpqevpgsdrra 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI---------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdyVLDGdaelrdlqrrleqandgaeqarlyaalEAIDGWSAEARARR--------------------LLAGLGFAPADA 140
Cdd:COG0410 61 ---RFDG---------------------------EDITGLPPHRIARLgigyvpegrrifpsltveenLLLGAYARRDRA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648648866 141 ERPMR--------------------DFSGGWRMRLGLARTLMTRSDLLLLDEPT 174
Cdd:COG0410 111 EVRADlervyelfprlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-221 |
3.51e-09 |
|
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: 56.67 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqevpgsdrravdyvLDGdaelrdlqr 96
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT-------------------------LDG--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 97 rleqandgaeqarlyaalEAIDGWSAEARARrllAGLGFAPAD-------AERPMRD-------FSGGWRMRLGLARTLM 162
Cdd:cd03215 62 ------------------KPVTRRSPRDAIR---AGIAYVPEDrkreglvLDLSVAEnialsslLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 163 TRSDLLLLDEPTNHLDVETI-----LWLEdwLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKaeiyrLIRE--LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-179 |
3.63e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---------QPPEWV---VAHLPQevpgsDRRAVDYV 84
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirSPRDAIragIAYVPE-----DRKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 LDGD-------AELRDLQRRLeQANDGAEQARlyaaleaidgwsaearARRLLAGLGFAPADAERPMRDFSGGWRMRLGL 157
Cdd:COG1129 343 LDLSirenitlASLDRLSRGG-LLDRRRERAL----------------AEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVL 405
|
170 180
....*....|....*....|..
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLDV 179
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDV 427
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-232 |
4.25e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.58 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 23 TVHAGWRVGLTGANGSGKSSLLAALQGELA----------LDAGEIEQPPEWVVAHLPQEV-------PGSDRRAVDYVL 85
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFALMGLLAangriggsatFNGREILNLPEKELNKLRAEQismifqdPMTSLNPYMRVG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 86 DGDAELRDLQRRLEQANDGAEQARLyaaLEAIDgwSAEARARrllagLGFAPadaerpmRDFSGGWRMRLGLARTLMTRS 165
Cdd:PRK09473 118 EQLMEVLMLHKGMSKAEAFEESVRM---LDAVK--MPEARKR-----MKMYP-------HEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 166 DLLLLDEPTNHLDVET---ILWLEDWLARYPGT-VIVIAHDRRFLDSVCTHVahiergtIALYAG---SYTHAE 232
Cdd:PRK09473 181 KLLIADEPTTALDVTVqaqIMTLLNELKREFNTaIIMITHDLGVVAGICDKV-------LVMYAGrtmEYGNAR 247
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
338-494 |
4.26e-09 |
|
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: 57.42 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 338 IGILGPNGAGKSTLLTLLAGELLPTAGERRVDpALQVGYFAQHQREQLDLEASPLVHLQRQDPRAEEQRLRNFLGGMGFP 417
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTEIAKPLQIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 418 gDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYA----GGLVVVAHDRELLARVCDR 493
Cdd:cd03237 107 -QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAenneKTAFVVEHDIIMIDYLADR 185
|
.
gi 648648866 494 F 494
Cdd:cd03237 186 L 186
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-202 |
4.34e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.54 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAAL------QGELALDAGEIEQPPEWVVAH----LPQEVPGSDRRAVDYVLDgdae 90
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMagllpgQGEILLNGRPLSDWSAAELARhrayLSQQQSPPFAMPVFQYLA---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 lrdlqrrLEQAnDGAEQARLYAALEAIdgwsaeARARRLLAGLGfapadaeRPMRDFSGGWRMRLGLARTLMT------- 163
Cdd:COG4138 92 -------LHQP-AGASSEAVEQLLAQL------AEALGLEDKLS-------RPLTQLSGGEWQRVRLAAVLLQvwptinp 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 648648866 164 RSDLLLLDEPTNHLDVETILWLEDWLARYP---GTVIVIAHD 202
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
144-218 |
4.73e-09 |
|
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: 56.85 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 144 MRDF-SGGWRM------RLGLARTLMTRSDLLLLDEPTNHLDVETI-LWLEDWLARYPGT----VIVIAHDRRFLDSVcT 211
Cdd:cd03240 112 MRGRcSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQknfqLIVITHDEELVDAA-D 190
|
....*..
gi 648648866 212 HVAHIER 218
Cdd:cd03240 191 HIYRVEK 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-201 |
4.92e-09 |
|
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: 57.11 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 16 LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWVVAH-LPQEVPGSDRRAVDYVLDGDAEL-RD 93
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-----LVDGHdLALADPAWLRRQVGVVLQENVLFnRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 94 LQRRLEQANDGAEQARLYAALEAidgwsAEARARRLLAGLGFAPADAERPMrDFSGGWRMRLGLARTLMTRSDLLLLDEP 173
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAKL-----AGAHDFISELPEGYDTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190
....*....|....*....|....*....|..
gi 648648866 174 TNHLDVET----ILWLEDWLARYpgTVIVIAH 201
Cdd:cd03252 166 TSALDYESehaiMRNMHDICAGR--TVIIIAH 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-201 |
5.10e-09 |
|
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: 55.51 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahlpqevpgsdrrav 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 dyVLDGdaelrdlqrrleqandgaeqarlyaalEAIDGWSAeARARRllAGLGFAPadaerpmrDFSGGWRMRLGLARTL 161
Cdd:cd03216 58 --LVDG---------------------------KEVSFASP-RDARR--AGIAMVY--------QLSVGERQMVEIARAL 97
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARYPG---TVIVIAH 201
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-501 |
5.30e-09 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 56.04 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALqvgyfaqHQREQLDLEAsplvhlQRQD 399
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGED-------LTDLEDELPP------LRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 400 PRAEEQRLRNF-----LGGMGFPgdkadgpvgqCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDL----DMREALAEAL 470
Cdd:cd03229 78 IGMVFQDFALFphltvLENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPitrrEVRALLKSLQ 147
|
170 180 190
....*....|....*....|....*....|.
gi 648648866 471 ENYAGGLVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:cd03229 148 AQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-201 |
5.56e-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: 58.96 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 6 DIELR------RGRQI-LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahlpqevpgsdr 78
Cdd:TIGR02203 330 DVEFRnvtfryPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 79 ravdyVLDG----DAELRDLQRRLEQA-------NDGAEQARLYAALEAIDgwsaEARARRLLAG-----------LGFA 136
Cdd:TIGR02203 390 -----LLDGhdlaDYTLASLRRQVALVsqdvvlfNDTIANNIAYGRTEQAD----RAEIERALAAayaqdfvdklpLGLD 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 137 PADAERPMRdFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLAR-YPG-TVIVIAH 201
Cdd:TIGR02203 461 TPIGENGVL-LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERlMQGrTTLVIAH 526
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-219 |
6.14e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.95 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 9 LRR--GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL------QGELALDAGEIEQppewvvAHLPQEVPGsdRRA 80
Cdd:PRK15134 292 LKRtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALlrlinsQGEIWFDGQPLHN------LNRRQLLPV--RHR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVL-DGDAELRDLQRRLEQANDGAE--QARLYAAleaidgwSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGL 157
Cdd:PRK15134 364 IQVVFqDPNSSLNPRLNVLQIIEEGLRvhQPTLSAA-------QREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAI 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLD--VET-ILWLEDWL-ARYPGTVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDktVQAqILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
325-502 |
6.59e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.39 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------------------RRVDPALQVGYFAQHQREQ 384
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNvswrgeplaklnraqrkafrRDIQMVFQDSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 385 L-DLEASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMR 463
Cdd:PRK10419 108 VrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 464 E---ALAEALENYAG-GLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK10419 188 AgviRLLKKLQQQFGtACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
325-482 |
7.17e-09 |
|
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: 55.78 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERrvdpalqvgYFAQHQREQLDLEASPLVHLQRQDPRAEE 404
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLEKALSSLISVLNQRPYLFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 405 QRLRNFLGgmgfpgdkadgpvGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYAggLVVV 480
Cdd:cd03247 89 TTLRNNLG-------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKDKT--LIWI 153
|
..
gi 648648866 481 AH 482
Cdd:cd03247 154 TH 155
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-178 |
7.85e-09 |
|
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: 59.15 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAAL------QGELALDAGEIEQPP--EWVVAH--LPQEV---PGSDR 78
Cdd:TIGR01271 1231 GRAVL-QDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstEGEIQIDGVSWNSVTlqTWRKAFgvIPQKVfifSGTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 79 RAVD-YVLDGDAELRDLqrrleqandgAEQARLYAALEAIDGwsaeararrllaGLGFAPADAERPMrdfSGGWRMRLGL 157
Cdd:TIGR01271 1310 KNLDpYEQWSDEEIWKV----------AEEVGLKSVIEQFPD------------KLDFVLVDGGYVL---SNGHKQLMCL 1364
|
170 180
....*....|....*....|.
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLD 178
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLD 1385
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
336-502 |
8.49e-09 |
|
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: 55.96 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 336 DRIGILGPNGAGKSTLLTLLAGELLPTAG---------------ERRVDPALQV-GYFAQHQREQ-LDLEASPLVHLQRQ 398
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGrvlingvdvtaappaDRPVSMLFQEnNLFAHLTVEQnVGLGLSPGLKLTAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 399 DpraeEQRLRNFLGGMGFPGDKADGPvGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYA 474
Cdd:cd03298 105 D----RQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETK 179
|
170 180
....*....|....*....|....*...
gi 648648866 475 GGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-219 |
1.01e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.54 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 18 QHA----SLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQPPEWvvahlpqevpgsdRRAVDYVLD 86
Cdd:PRK11607 32 QHAvddvSLTIYKGEIFALLGASGCGKSTLLRMLagfeqptAGQIMLDGVDLSHVPPY-------------QRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 87 GDAELRDLQrrLEQ-ANDGAEQARLYAAleaidgwSAEARARRLLaGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRS 165
Cdd:PRK11607 99 SYALFPHMT--VEQnIAFGLKQDKLPKA-------EIASRVNEML-GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 166 DLLLLDEPTNHLD--VETILWLE--DWLARYPGTVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:PRK11607 169 KLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
306-502 |
1.27e-08 |
|
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: 56.20 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 306 PDPLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--------PA------ 371
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgrditglpPHriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 372 -------------------LQVGYFAqHQREQLDLEASPLVHLQRQDPRAEEqRLRNFLGGMGFpGDKADGPVGQCSGGE 432
Cdd:COG0411 81 iartfqnprlfpeltvlenVLVAAHA-RLGRGLLAALLRLPRARREEREARE-RAEELLERVGL-ADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 433 RVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG----LVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgitILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-492 |
1.28e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 321 ERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPalQVGYFAQ--------HQREQLDL---EA 389
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKdifqidaiKLRKEVGMvfqQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 390 SPLVHL-----------------QRQDPRAEEQRLRNfLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLD 452
Cdd:PRK14246 100 NPFPHLsiydniayplkshgikeKREIKKIVEECLRK-VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 648648866 453 EPTNHLDLDMREALAEALENYAG--GLVVVAHDRELLARVCD 492
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVAD 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-221 |
1.49e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.79 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQ-------GEL--ALDAGEIEQPPewvvahlpqe 72
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNllemprsGTLniAGNHFDFSKTP---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 73 vpgsdrravdyvldGDAELRDLQRrleqaNDGA--EQARLYAAL-------EA------IDGWSAEARARRLLAGLGFAP 137
Cdd:PRK11124 73 --------------SDKAIRELRR-----NVGMvfQQYNLWPHLtvqqnliEApcrvlgLSKDQALARAEKLLERLRLKP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 138 AdAER-PMRdFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVE---TILWLEDWLARYPGTVIVIAHDRRFLDSVCTHV 213
Cdd:PRK11124 134 Y-ADRfPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQIVSIIRELAETGITQVIVTHEVEVARKTASRV 211
|
....*...
gi 648648866 214 AHIERGTI 221
Cdd:PRK11124 212 VYMENGHI 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-222 |
1.66e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.84 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAAL---------QGELALDaGE--IEQPPEwVVAHL--------PQE 72
Cdd:COG0396 12 GKEIL-KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkyevtSGSILLD-GEdiLELSPD-ERARAgiflafqyPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 73 VPGsdrravdyVldgdaELRDLQRRLEQANDGaeqarlyaalEAIDGWSAEARARRLLAGLGFAPADAERPM-RDFSGGW 151
Cdd:COG0396 89 IPG--------V-----SVSNFLRTALNARRG----------EELSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 152 RMRLGLARTLMTRSDLLLLDEPTNHLDV-------ETILWLedwlaRYPGT-VIVIAHDRRFLDSVCTHVAHI-ERGTIA 222
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIdalrivaEGVNKL-----RSPDRgILIITHYQRILDYIKPDFVHVlVDGRIV 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-223 |
1.91e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.84 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 4 MQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahlpqevpgsdrravdy 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 84 vLDGDAEL---RDLQRRLEQandgaeQARLYAALEAID--------GWsaEARARRLLAGLGFAPADAERPMRdFSGGWR 152
Cdd:PRK11247 70 -LAGTAPLaeaREDTRLMFQ------DARLLPWKKVIDnvglglkgQW--RDAALQALAAVGLADRANEWPAA-LSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 153 MRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLAR----YPGTVIVIAHDRRFLDSVCTHVAHIERGTIAL 223
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwqqHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-202 |
2.01e-08 |
|
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: 55.16 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGelaldageIEQPPEWVVAHLPQEV--PGSDRRAV--DYVLDGDAELR 92
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG--------LAQPTSGGVILEGKQItePGPDRMVVfqNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 93 D-----LQRRLEQANDGAEQARLYAALEaidgwsaeararrlLAGLGFApadAERPMRDFSGGWRMRLGLARTLMTRSDL 167
Cdd:TIGR01184 73 EnialaVDRVLPDLSKSERRAIVEEHIA--------------LVGLTEA---ADKRPGQLSGGMKQRVAIARALSIRPKV 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 648648866 168 LLLDEPTNHLDVETILWLEDWLAR----YPGTVIVIAHD 202
Cdd:TIGR01184 136 LLLDEPFGALDALTRGNLQEELMQiweeHRVTVLMVTHD 174
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-224 |
2.13e-08 |
|
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: 57.07 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQppeW-------VVAHLPQEV---P 74
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvgvwpptAGSVRLDGADLSQ---WdreelgrHIGYLPQDVelfD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 75 GSdrravdyVLDGDAelrdlqrRLEQANDGA--EQARLYAALEAIdgwsaearaRRLLAGLGFAPADAERPMrdfSGGWR 152
Cdd:COG4618 420 GT-------IAENIA-------RFGDADPEKvvAAAKLAGVHEMI---------LRLPDGYDTRIGEGGARL---SGGQR 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 153 MRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARY---PGTVIVIAHDRRFLdSVCTHVAHIERGTIALY 224
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLL-AAVDKLLVLRDGRVQAF 547
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-201 |
2.21e-08 |
|
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: 55.24 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELR---RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQ-------GELALDAGEI-EQPPEWVVAHL- 69
Cdd:cd03249 1 IEFKNVSFRypsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGEILLDGVDIrDLNLRWLRSQIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 70 --PQE---VPGSDRRAVDYvldGDAELRDLQRrlEQAndgaeqARLYAALEAI----DGWSAE--ARARRLlaglgfapa 138
Cdd:cd03249 81 lvSQEpvlFDGTIAENIRY---GKPDATDEEV--EEA------AKKANIHDFImslpDGYDTLvgERGSQL--------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 139 daerpmrdfSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWL--ARYPGTVIVIAH 201
Cdd:cd03249 141 ---------SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALdrAMKGRTTIVIAH 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-173 |
2.23e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 55.24 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSS-------LLAALQGELALDAGEIEQPPEWVVAH-----L 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTtfymivgLVKPDSGKILLDGQDITKLPMHKRARlgigyL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 70 PQEVpgsdrravdyvldgdaelrDLQRRLEqandgAEQaRLYAALEAIDGWSAEARARR--LLAGLGFAPAdAERPMRDF 147
Cdd:cd03218 81 PQEA-------------------SIFRKLT-----VEE-NILAVLEIRGLSKKEREEKLeeLLEEFHITHL-RKSKASSL 134
|
170 180
....*....|....*....|....*.
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEP 173
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-220 |
2.46e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 54.40 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 16 LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwvVAHLPQE---VPGS-----------DRRAV 81
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEpwiQNGTirenilfgkpfDEERY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGDAELRDLQrrleqandgaeqarlyaALEAIDgwsaeararrlLAGLGfapadaERPMrDFSGGWRMRLGLARTL 161
Cdd:cd03250 98 EKVIKACALEPDLE-----------------ILPDGD-----------LTEIG------EKGI-NLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARYPG----TVIVIAHDRRFLdSVCTHVAHIERGT 220
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFENCILGLLlnnkTRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-181 |
3.29e-08 |
|
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: 57.23 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 16 LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwvVAHLPQE---VPGSDRRAVDYVLDGDaELR 92
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQTswiMPGTIKDNIIFGLSYD-EYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 93 dlqrrleqandgaeqarlyaaleaidgWSAEARARRLLAGLGFAPADAERPMRD----FSGGWRMRLGLARTLMTRSDLL 168
Cdd:TIGR01271 518 ---------------------------YTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLY 570
|
170
....*....|...
gi 648648866 169 LLDEPTNHLDVET 181
Cdd:TIGR01271 571 LLDSPFTHLDVVT 583
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-181 |
3.78e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI---EQP-----PEWVVAHLPQ--EVPGSDRRAV-DYVL 85
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilGQPtrqalQKNLVAYVPQseEVDWSFPVLVeDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 86 DGDAELRDLQRRlEQANDgaeQARLYAALEAIDgwSAEARARRLlaglgfapadaerpmRDFSGGWRMRLGLARTLMTRS 165
Cdd:PRK15056 103 MGRYGHMGWLRR-AKKRD---RQIVTAALARVD--MVEFRHRQI---------------GELSGGQKKRVFLARAIAQQG 161
|
170
....*....|....*.
gi 648648866 166 DLLLLDEPTNHLDVET 181
Cdd:PRK15056 162 QVILLDEPFTGVDVKT 177
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
314-487 |
4.03e-08 |
|
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: 53.68 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 314 HAEVctGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLA--GELLPTAGERRVD----PALQVgyfaqHQREQLDL 387
Cdd:cd03217 7 HVSV--GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKgediTDLPP-----EERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 388 EASPlvhlqrQDP-RAEEQRLRNFLGGM--GFpgdkadgpvgqcSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMRE 464
Cdd:cd03217 80 FLAF------QYPpEIPGVKNADFLRYVneGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180
....*....|....*....|....*.
gi 648648866 465 ALAEALENYAG---GLVVVAHDRELL 487
Cdd:cd03217 142 LVAEVINKLREegkSVLIITHYQRLL 167
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-242 |
4.08e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDageieQPPEWVVAHLPQEVPGSDRRA 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD-----KSAGSHIELLGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDyVLDGDAELRDLQRRLEQAND-GAEQARLYAALEAIDGWSA---------EARARRLLAGLGFAPADAERpMRDFSGG 150
Cdd:PRK09984 79 RD-IRKSRANTGYIFQQFNLVNRlSVLENVLIGALGSTPFWRTcfswftreqKQRALQALTRVGMVHFAHQR-VSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 151 WRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG----TVIVIAHDRRFLDSVCTHVAHIERGTIaLYAG 226
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGHV-FYDG 235
|
250
....*....|....*.
gi 648648866 227 SYTHAEAKRAEAIVQS 242
Cdd:PRK09984 236 SSQQFDNERFDHLYRS 251
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
325-502 |
4.31e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 56.27 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--PALQVGYFAQHQReqldleasplVHLQRQDP-- 400
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgvPLVQYDHHYLHRQ----------VALVGQEPvl 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 401 --------------RAEEQRLRN---------FLGGMGFPGDKADGPVG-QCSGGERVRLVLALLIWQAPSLLLLDEPTN 456
Cdd:TIGR00958 567 fsgsvreniaygltDTPDEEIMAaakaanahdFIMEFPNGYDTEVGEKGsQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 457 HLDLDMREALAEALENYAGGLVVVAHdRELLARVCDRFWTVEAGRL 502
Cdd:TIGR00958 647 ALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSV 691
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-209 |
4.50e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppeWVVAHL-PQEVPGSDRRAVDYVLDGDAELR--- 92
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE----WIFKDEkNKKKTKEKEKVLEKLVIQKTRFKkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 93 ---DLQRRLEQANDGAEQARLYAALE----------AIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLAR 159
Cdd:PRK13651 99 kikEIRRRVGVVFQFAEYQLFEQTIEkdiifgpvsmGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648648866 160 TLMTRSDLLLLDEPTNHLD---VETILWLEDWLARYPGTVIVIAHDrrfLDSV 209
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNV 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-222 |
4.91e-08 |
|
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: 53.68 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQG--ELALDAGEIeqppewvvahlpqevpgsdrravdyVLDGDa 89
Cdd:cd03217 12 GKEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI-------------------------LFKGE- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 ELRDLqrrleqandgaeqarlyaaleaidgwSAEARARRLLaGLGF-APADAE--------RPMRD-FSGGWRMRLGLAR 159
Cdd:cd03217 65 DITDL--------------------------PPEERARLGI-FLAFqYPPEIPgvknadflRYVNEgFSGGEKKRNEILQ 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 160 TLMTRSDLLLLDEPTNHLDVETILWLEDWLARY--PGT-VIVIAHDRRFLDSVCTHVAHI-ERGTIA 222
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLDYIKPDRVHVlYDGRIV 184
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-201 |
5.10e-08 |
|
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: 54.01 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIEL---RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQ-------GELALDAGEIEQPPE-------W 64
Cdd:cd03248 12 VKFQNVTFaypTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqgGQVLLDGKPISQYEHkylhskvS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 65 VVAHLPQEVPGSDRRAVDYVLdGDAELRdlqrRLEQANDGAEQARLYAALEaiDGWSAEARARRLLaglgfapadaerpm 144
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGL-QSCSFE----CVKEAAQKAHAHSFISELA--SGYDTEVGEKGSQ-------------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 145 rdFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLE----DWLARYpgTVIVIAH 201
Cdd:cd03248 151 --LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQqalyDWPERR--TVLVIAH 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-202 |
5.18e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.64 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELR--RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvVAH--LPQEVPGSD 77
Cdd:PRK13635 6 IRVEHISFRypDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT------VGGmvLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 78 RRAVDYVLD-------GDAELRDLQRRLEqaNDGAE----QARLYAALEAIdgwsaeararRLLAGLGFAPAdaerpmrD 146
Cdd:PRK13635 80 RRQVGMVFQnpdnqfvGATVQDDVAFGLE--NIGVPreemVERVDQALRQV----------GMEDFLNREPH-------R 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 147 FSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD-------VETILWLEDWLARypgTVIVIAHD 202
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQLKEQKGI---TVLSITHD 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-201 |
6.22e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 55.74 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqeVPGSD---------RRAVDYVLDg 87
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL-------------IDGTDirtvtraslRRNIAVVFQ- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 88 DAEL--RDLQRRLEQANDGAEQARLYAALEAidgwsAEARARRLLAGLGFAPADAERPmRDFSGGWRMRLGLARTLMTRS 165
Cdd:PRK13657 417 DAGLfnRSIEDNIRVGRPDATDEEMRAAAER-----AQAHDFIERKPDGYDTVVGERG-RQLSGGERQRLAIARALLKDP 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 648648866 166 DLLLLDEPTNHLDVETILWLEDWL--ARYPGTVIVIAH 201
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALdeLMKGRTTFIIAH 528
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
309-502 |
7.51e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 309 LLALDHAEVCTGERVrLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPAlQVGYFAQHQREQ---- 384
Cdd:PRK10895 4 LTAKNLAKAYKGRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE-DISLLPLHARARrgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 385 -LDLEASPLVHLQ-----------RQDPRAEEQRLRNFLGGMGFPGDKADGPVGQC-SGGERVRLVLALLIWQAPSLLLL 451
Cdd:PRK10895 82 yLPQEASIFRRLSvydnlmavlqiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSlSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 452 DEPTNHLD----LDMREaLAEALENYAGGLVVVAHD-RELLArVCDRFWTVEAGRL 502
Cdd:PRK10895 162 DEPFAGVDpisvIDIKR-IIEHLRDSGLGVLITDHNvRETLA-VCERAYIVSQGHL 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
340-483 |
8.56e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVDP-----------ALQVGYFAQHQREQLDLEASPLVHLQRQDPRAEEQRLR 408
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 409 N-----FLGGMGFPG--DKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYAGGL 477
Cdd:PRK10253 118 KedeeaVTKAMQATGitHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTL 197
|
....*.
gi 648648866 478 VVVAHD 483
Cdd:PRK10253 198 AAVLHD 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-202 |
8.76e-08 |
|
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: 53.49 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI--------EQPPEWV-VAHLPQevpgsdrravDYVLDG 87
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditNLPPEKRdISYVPQ----------NYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 88 DAELRD-----LQRRLEQANDGAEQARLYAALEAIDgwsaeararRLLaglgfapadaERPMRDFSGGWRMRLGLARTLM 162
Cdd:cd03299 85 HMTVYKniaygLKKRKVDKKEIERKVLEIAEMLGID---------HLL----------NRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648648866 163 TRSDLLLLDEPTNHLDVET----ILWLEDWLARYPGTVIVIAHD 202
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-203 |
1.10e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 54.38 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI---EQppEWVVAHLPQEvpgsdr 78
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlnGR--DLFTNLPPRE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 79 RAVDYVLDGDAELRDLQRR------LEQANDGAEQARlyaaleaidgwsaeARARRLL-----AGLgfapadAERPMRDF 147
Cdd:COG1118 75 RRVGFVFQHYALFPHMTVAeniafgLRVRPPSKAEIR--------------ARVEELLelvqlEGL------ADRYPSQL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLAR----YPGTVIVIAHDR 203
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhdeLGGTTVFVTHDQ 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
320-502 |
1.13e-07 |
|
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: 52.92 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--------PAL-----QVGYFAQH-----Q 381
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglkltddkKNInelrqKVGMVFQQfnlfpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLEASPLVHLQRQDPRAEEQRLRNFLGGMGFPgDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD-- 459
Cdd:cd03262 91 LTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpe 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648648866 460 -----LDMREALAEalENYAggLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03262 170 lvgevLDVMKDLAE--EGMT--MVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-215 |
1.92e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.43 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQPPEWVVAHLPQEV------P-GS--DRRAVDYV 84
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLtmietptGGELYYQGQDLLKADPEAQKLLRQKIqivfqnPyGSlnPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 LDGDAELrdlqrrleQANDGAEQARlyaaleaidgwsaeARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTR 164
Cdd:PRK11308 115 LEEPLLI--------NTSLSAAERR--------------EKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 165 SDLLLLDEPTNHLDVET---ILWLEDWLARYPGTVIV-IAHDRrfldSVCTHVAH 215
Cdd:PRK11308 173 PDVVVADEPVSALDVSVqaqVLNLMMDLQQELGLSYVfISHDL----SVVEHIAD 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
317-535 |
1.97e-07 |
|
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: 53.58 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 317 VCTGERVRLQPTTL----RLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpalqvGYFAQHQREQLDL----- 387
Cdd:TIGR02142 1 LSARFSKRLGDFSLdadfTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-----GRTLFDSRKGIFLppekr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 388 -------EASPLVHL----------QRQDP---RAEEQRLRNFLGgmgfPGDKADGPVGQCSGGERVRLVLALLIWQAPS 447
Cdd:TIGR02142 76 rigyvfqEARLFPHLsvrgnlrygmKRARPserRISFERVIELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 448 LLLLDEPTNHLDLDMREALAEALENYAGGL----VVVAHDRELLARVCDRFWTVEAGRLSPFDgdlddyarALQARQREA 523
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEFgipiLYVSHSLQEVLRLADRVVVLEDGRVAAAG--------PIAEVWASP 223
|
250
....*....|..
gi 648648866 524 ARSAAETPPQAA 535
Cdd:TIGR02142 224 DLPWLAREDQGS 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-234 |
2.03e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.63 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 24 VHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLpqevpgSD-RRAVDYVLDGDAelrdlqrrLEQAN 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNI------SDvHQNMGYCPQFDA--------IDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 103 DGAEQARLYAALEAIDGWSAEARARRLLAGLGFApADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET- 181
Cdd:TIGR01257 2028 TGREHLYLYARLRGVPAEEIEKVANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAr 2106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 182 -ILW-LEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALYaGSYTHAEAK 234
Cdd:TIGR01257 2107 rMLWnTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCL-GTIQHLKSK 2160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
340-501 |
2.18e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGE-----RRVDPALQ--------VGYFAQHQREQL-------DLEASPlvhLQRQD 399
Cdd:PRK13636 37 ILGGNGAGKSTLFQNLNGILKPSSGRilfdgKPIDYSRKglmklresVGMVFQDPDNQLfsasvyqDVSFGA---VNLKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 400 PRAE-EQRLRNFLGGMGFPGDKaDGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYA 474
Cdd:PRK13636 114 PEDEvRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELG 192
|
170 180
....*....|....*....|....*..
gi 648648866 475 GGLVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:PRK13636 193 LTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
325-509 |
2.48e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE---------------RRVDPALQVGYFAQ--------HQ 381
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEvslvgqplhqmdeeaRAKLRAKHVGFVFQsfmliptlNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLEASplvhLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:PRK10584 106 LENVELPAL----LRGESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648648866 462 MREALAEAL----ENYAGGLVVVAHDRELLARvCDRfwtveagRLSPFDGDL 509
Cdd:PRK10584 181 TGDKIADLLfslnREHGTTLILVTHDLQLAAR-CDR-------RLRLVNGQL 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
329-525 |
2.89e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.89 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--------PALQ-VGYFAQHQ--------REQLDLEASP 391
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttpPSRRpVSMLFQENnlfshltvAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 392 ---LVHLQRqdpraeeQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLA-LLIWQAPsLLLLDEPTNHLD----LDMR 463
Cdd:PRK10771 99 glkLNAAQR-------EKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALArCLVREQP-ILLLDEPFSALDpalrQEML 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 464 EALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSpFDGDLDdyarALQARQREAAR 525
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA-WDGPTD----ELLSGKASASA 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-224 |
2.92e-07 |
|
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: 52.55 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 16 LLQHASLTVHAGWRVGLTGANGSGKSSLLAAL------QGELALDAGEIEQPP--EWVVAH--LPQEV---PGSDRRAVD 82
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntEGDIQIDGVSWNSVPlqKWRKAFgvIPQKVfifSGTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 83 -YVLDGDAELRDLqrrleqandgAEQARLYAALEAIDGwsaeararrllaGLGFAPADAERPMrdfSGGWRMRLGLARTL 161
Cdd:cd03289 99 pYGKWSDEEIWKV----------AEEVGLKSVIEQFPG------------QLDFVLVDGGCVL---SHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 162 MTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAHDRR---FLDsvCTHVAHIERGTIALY 224
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRieaMLE--CQRFLVIEENKVRQY 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
320-511 |
2.96e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.02 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD------PALQV-------GYFAQH-----Q 381
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglkvndPKVDErlirqeaGMVFQQfylfpH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLEASPLVHLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:PRK09493 92 LTALENVMFGPLRVRGASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648648866 462 MREALAEALENYAG---GLVVVAHDRELLARVCDRFWTVEAGRLSPfDGDLDD 511
Cdd:PRK09493 171 LRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAE-DGDPQV 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
320-481 |
2.97e-07 |
|
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: 51.34 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQREQLDL--------EASP 391
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLghapgiktTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 392 LVHLQRQDPRAEEQRLRNFLGGMGFPGDKaDGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALE 471
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|..
gi 648648866 472 NY--AGGLVVVA 481
Cdd:cd03231 170 GHcaRGGMVVLT 181
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-204 |
3.09e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.70 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 16 LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPQEVPGSDR-RAVDYVLDGDAEL 91
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgQP----LHQMDEEARAKLRaKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 92 RDLqrrleqanDGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRdFSGGWRMRLGLARTLMTRSDLLLLD 171
Cdd:PRK10584 101 PTL--------NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 648648866 172 EPTNHLDVETILWLEDWL----ARYPGTVIVIAHDRR 204
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQ 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-178 |
3.21e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.01 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 15 ILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPQEvpgsdRRAVdYV------- 84
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidgKD----VTKLPEY-----KRAK-YIgrvfqdp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 LDGDAE------------LRDLQRRLEQANDGAEQARLYAALEAIdgwsaeararrllaGLGFapadaERPMRD----FS 148
Cdd:COG1101 90 MMGTAPsmtieenlalayRRGKRRGLRRGLTKKRRELFRELLATL--------------GLGL-----ENRLDTkvglLS 150
|
170 180 190
....*....|....*....|....*....|
gi 648648866 149 GGWRMRLGLARTLMTRSDLLLLDEPTNHLD 178
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-219 |
3.31e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.53 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvAHLPQEVPGSDRRA---VDYVLDGD 88
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI--------TVLGVPVPARARLArarIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 89 aelrdlqrRLEQANDGAEQARLYAALEAIDGWSAEARARRLLAglgFA--PADAERPMRDFSGGWRMRLGLARTLMTRSD 166
Cdd:PRK13536 124 --------NLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLE---FArlESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 167 LLLLDEPTNHLD--VETILW--LEDWLARyPGTVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:PRK13536 193 LLILDEPTTGLDphARHLIWerLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
280-500 |
3.63e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 280 LERMDE-VAVIRAARPIHLEIPTPGRLPDPLLALDHAEVCTGE-RVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLlag 357
Cdd:COG4178 332 VDRLAGfEEALEAADALPEAASRIETSEDGALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 358 ellpTAG-----ERRVD-PAL-------QVGYF---------------AQHQREQLdLEASPLVHLQRQDPR-AEEQRLR 408
Cdd:COG4178 409 ----IAGlwpygSGRIArPAGarvlflpQRPYLplgtlreallypataEAFSDAEL-REALEAVGLGHLAERlDEEADWD 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 409 NFLggmgfpgdkadgpvgqcSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--LVVVAHdREL 486
Cdd:COG4178 484 QVL-----------------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGttVISVGH-RST 545
|
250
....*....|....
gi 648648866 487 LARVCDRFWTVEAG 500
Cdd:COG4178 546 LAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
337-502 |
4.10e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.11 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 337 RIGILGPNGAGKSTLLTLLAGELLPTAGER--RVDPALQ---------VGYFAQHQREQLdleASPLVHLQRQ------- 398
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVliRGEPITKenirevrkfVGLVFQNPDDQI---FSPTVEQDIAfgpinlg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 399 -DPRAEEQRLRNFLGGMGFPGDKADGPvGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEAL----ENY 473
Cdd:PRK13652 109 lDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLndlpETY 187
|
170 180
....*....|....*....|....*....
gi 648648866 474 AGGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK13652 188 GMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-181 |
4.99e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQI--LLQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQPPEW----VVAH 68
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALfriveleRGRILIDGCDISKFGLMdlrkVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 69 LPQEvPGSDRRAVDYVLDGDAELRDlqrrleqandgaeqARLYAALEaidgwsaeaRA------RRLLAGLgfapaDAE- 141
Cdd:PLN03130 1318 IPQA-PVLFSGTVRFNLDPFNEHND--------------ADLWESLE---------RAhlkdviRRNSLGL-----DAEv 1368
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648648866 142 -RPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET 181
Cdd:PLN03130 1369 sEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
332-494 |
5.04e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.09 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 332 LRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV----------DPALQVGYFAQHQ--------REQLDLEASplv 393
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagksiltnisDVHQNMGYCPQFDaiddlltgREHLYLYAR--- 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 394 hlQRQDPRAEEQRLRNF-LGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALEN 472
Cdd:TIGR01257 2039 --LRGVPAEEIEKVANWsIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180
....*....|....*....|....*
gi 648648866 473 Y---AGGLVVVAHDRELLARVCDRF 494
Cdd:TIGR01257 2116 IireGRAVVLTSHSMEECEALCTRL 2140
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
310-502 |
5.50e-07 |
|
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: 51.08 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--PALQVGyfaQHQRE---- 383
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkDITNLP---PHKRPvntv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 384 --------QLDLE---ASPLvHLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLD 452
Cdd:cd03300 78 fqnyalfpHLTVFeniAFGL-RLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648648866 453 EPTNHLDLDMREALAEALENYAGGL----VVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
325-502 |
5.65e-07 |
|
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: 50.24 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKST--LLTLLAGELLPTAGERRVD--------PALQVGYFAQHQ--------REQLD 386
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTllNALAGRRTGLGVSGEVLINgrpldkrsFRKIIGYVPQDDilhptltvRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 387 LEAsplvhlqrqdpraeeqRLRNFlggmgfpgdkadgpvgqcSGGERVRLVLAL-LIWQaPSLLLLDEPTNHLDLDMREA 465
Cdd:cd03213 105 FAA----------------KLRGL------------------SGGERKRVSIALeLVSN-PSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648648866 466 LAEALENYAGG---LVVVAHD-RELLARVCDRFWTVEAGRL 502
Cdd:cd03213 150 VMSLLRRLADTgrtIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-482 |
6.49e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 51.00 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------RRVDPAL---QVGYFAQhqrEQLDLEASPL- 392
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEilldgvdiRDLNLRWlrsQIGLVSQ---EPVLFDGTIAe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 393 -VHLQRQDPRAEEQR-------LRNFLggMGFPgDKADGPVG----QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDL 460
Cdd:cd03249 96 nIRYGKPDATDEEVEeaakkanIHDFI--MSLP-DGYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180
....*....|....*....|....
gi 648648866 461 DMREALAEALENYAGG--LVVVAH 482
Cdd:cd03249 173 ESEKLVQEALDRAMKGrtTIVIAH 196
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
340-485 |
7.16e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.76 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVDpALQVGYFAQHQRE------------QLDLEASPLVHLqRQD--PRAE-E 404
Cdd:PRK11607 50 LLGASGCGKSTLLRMLAGFEQPTAGQIMLD-GVDLSHVPPYQRPinmmfqsyalfpHMTVEQNIAFGL-KQDklPKAEiA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 405 QRLRNFLG---GMGFPGDKADgpvgQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREAL----AEALENYAGGL 477
Cdd:PRK11607 128 SRVNEMLGlvhMQEFAKRKPH----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILERVGVTC 203
|
....*...
gi 648648866 478 VVVAHDRE 485
Cdd:PRK11607 204 VMVTHDQE 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-201 |
7.91e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRR--GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQ----PPEWVVA 67
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALfriveleKGRIMIDDCDVAKfgltDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 68 HLPQEvPGSDRRAVDYVLDGDAELRDlqrrleqandgaeqARLYAALEaidgwsaEARARRLLAGLGFApADAE--RPMR 145
Cdd:PLN03232 1314 IIPQS-PVLFSGTVRFNIDPFSEHND--------------ADLWEALE-------RAHIKDVIDRNPFG-LDAEvsEGGE 1370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLAR--YPGTVIVIAH 201
Cdd:PLN03232 1371 NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAH 1428
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-179 |
7.98e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 19 HASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQE------VPGS-DRRAVDYVLDGDAE- 90
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangiVYISeDRKRDGLVLGMSVKe 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 ------LRDLQRRLEQANDGAEQArlyAALEAIDGWSAEARARrllaglgfapadaERPMRDFSGGWRMRLGLARTLMTR 164
Cdd:PRK10762 350 nmsltaLRYFSRAGGSLKHADEQQ---AVSDFIRLFNIKTPSM-------------EQAIGLLSGGNQQKVAIARGLMTR 413
|
170
....*....|....*
gi 648648866 165 SDLLLLDEPTNHLDV 179
Cdd:PRK10762 414 PKVLILDEPTRGVDV 428
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
280-480 |
8.86e-07 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 51.98 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 280 LERMDEV---AVIRAARPIHLEIPTPGRLPDPLLALDHAEVCTGERVrLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLA 356
Cdd:TIGR02868 304 AERIVEVldaAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 357 GELLPTAGERRVD-----------PALQVGYFAQhqREQLdLEASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPV 425
Cdd:TIGR02868 383 GLLDPLQGEVTLDgvpvssldqdeVRRRVSVCAQ--DAHL-FDTTVRENLRLARPDATDEELWAALERVGLADWLRALPD 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 426 G----------QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGLVVV 480
Cdd:TIGR02868 460 GldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVV 524
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-224 |
9.37e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.44 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 27 GWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWvvahlpqevpgsdrravDYVLDgdaELR--DLQRRLEQANDG 104
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDW-----------------DEILD---EFRgsELQNYFTKLLEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 105 ---AEQARLYAAL--EAIDGWSAEARARR--------LLAGLGFAPAdAERPMRDFSGGWRMRLGLARTLMTRSDLLLLD 171
Cdd:cd03236 86 dvkVIVKPQYVDLipKAVKGKVGELLKKKdergkldeLVDQLELRHV-LDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 172 EPTNHLDVE---TILWLEDWLARYPGTVIVIAHDRRFLDSVcTHVAHIERGTIALY 224
Cdd:cd03236 165 EPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYL-SDYIHCLYGEPGAY 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
320-520 |
9.93e-07 |
|
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: 50.23 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpALQVGYFAQHQREQLDL-----EASPLVH 394
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD-GQDITKLPMHKRARLGIgylpqEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 395 L-----------QRQDPRAE-EQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD--- 459
Cdd:cd03218 90 LtveenilavleIRGLSKKErEEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpia 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 460 -LDMREALAEaLENYAGGLVVVAHD-RELLArVCDRFWTVEAGRLSpFDGDLDDYARALQARQ 520
Cdd:cd03218 169 vQDIQKIIKI-LKDRGIGVLITDHNvRETLS-ITDRAYIIYEGKVL-AEGTPEEIAANELVRK 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-174 |
1.09e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvahlpqevpgsdrra 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 vdyvLDGdAEL-----RDLQRR--------LEQAND---------GAEQARLYaaleAIDgWSA-EARARRLLAGLGFaP 137
Cdd:COG1129 63 ----LDG-EPVrfrspRDAQAAgiaiihqeLNLVPNlsvaeniflGREPRRGG----LID-WRAmRRRARELLARLGL-D 131
|
170 180 190
....*....|....*....|....*....|....*..
gi 648648866 138 ADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPT 174
Cdd:COG1129 132 IDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-182 |
1.12e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE--------QPPEWV----VAHLPQevpgsDRRAVDYV 84
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgeditgLSPRERrrlgVAYIPE-----DRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 LDGDAE----LRDlQRRLEQANDGAeqarlyaaleaIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLART 160
Cdd:COG3845 349 PDMSVAenliLGR-YRRPPFSRGGF-----------LDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARE 416
|
170 180
....*....|....*....|..
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETI 182
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAI 438
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
321-502 |
1.15e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 321 ERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV----------DPAL-----QVGYFAQHQREQL 385
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetgNKNLkklrkKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 -------DLEASPLvHLQRQDPRAEEQRLRnFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHL 458
Cdd:PRK13641 99 fentvlkDVEFGPK-NFGFSEDEAKEKALK-WLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648648866 459 DLDMREALAEALENY--AGGLVV-VAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK13641 177 DPEGRKEMMQLFKDYqkAGHTVIlVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
122-202 |
1.18e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.20 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 122 AEARARRLLAGLGFAPADAERPmRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD---VETILWLEDWLARYPGTV-I 197
Cdd:PRK11629 122 INSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGTAfL 200
|
....*
gi 648648866 198 VIAHD 202
Cdd:PRK11629 201 VVTHD 205
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
310-488 |
1.30e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 48.69 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGE-RVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLlagellpTAG---------ERRVDPAL----QVG 375
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRA-------LAGlwpwgsgriGMPEGEDLlflpQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 376 YFAQHQ-REQLdleASPLvhlqrqdpraeEQRLrnflggmgfpgdkadgpvgqcSGGERVRLVLALLIWQAPSLLLLDEP 454
Cdd:cd03223 74 YLPLGTlREQL---IYPW-----------DDVL---------------------SGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|....
gi 648648866 455 TNHLDLDMREALAEALENYAGGLVVVAHDRELLA 488
Cdd:cd03223 119 TSALDEESEDRLYQLLKELGITVISVGHRPSLWK 152
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
321-502 |
1.43e-06 |
|
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: 49.79 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 321 ERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--------PAL---QVGYFAQHQ-------R 382
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlaladPAWlrrQVGVVLQENvlfnrsiR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 383 EQLDLeASPLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVGQ-CSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:cd03252 94 DNIAL-ADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAgLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 462 MREALAEALENYAGG--LVVVAHdRELLARVCDRFWTVEAGRL 502
Cdd:cd03252 173 SEHAIMRNMHDICAGrtVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
325-497 |
1.63e-06 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 48.58 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpalqvgyfaqhQREQldleasplvhlQRQDPRAEE 404
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----------GKEV-----------SFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 405 QRlrnflgGMGFpgdkadgpVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAG---GLVVVA 481
Cdd:cd03216 74 RA------GIAM--------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFIS 139
|
170
....*....|....*.
gi 648648866 482 HDRELLARVCDRFwTV 497
Cdd:cd03216 140 HRLDEVFEIADRV-TV 154
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-179 |
1.92e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 20 ASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEV--------PgSDRRAvdyvlDGDAEL 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiragimlcP-EDRKA-----EGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 92 RDLQrrlEQANDGAEQARLYAALEAIDGWSAEaRARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLD 171
Cdd:PRK11288 346 HSVA---DNINISARRHHLRAGCLINNRWEAE-NADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
....*...
gi 648648866 172 EPTNHLDV 179
Cdd:PRK11288 422 EPTRGIDV 429
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
414-482 |
2.15e-06 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 2.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 414 MGFPgDKADGPVGQ----CSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--LVVVAH 482
Cdd:cd03253 121 MRFP-DGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH 194
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-178 |
2.92e-06 |
|
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: 48.32 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 6 DIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGEL--ALDAGEIE-----QPPEW---VVAHLPQEvpg 75
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLingrpLDKRSfrkIIGYVPQD--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 76 sdrravDYVLdgdaelrdlqrrleqANDGAEQARLYAALeaidgwsaeararrllaglgfapadaerpMRDFSGGWRMRL 155
Cdd:cd03213 91 ------DILH---------------PTLTVRETLMFAAK-----------------------------LRGLSGGERKRV 120
|
170 180
....*....|....*....|...
gi 648648866 156 GLARTLMTRSDLLLLDEPTNHLD 178
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-221 |
3.05e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.74 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 11 RGRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwVVAHLPqeVPGSDRRAVDYVldgdAE 90
Cdd:PRK10895 14 KGRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE-DISLLP--LHARARRGIGYL----PQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 LRDLQRRLEQANDgaeqarLYAALEAIDGWSAEARARRllaglgfapadAERPMRDF-------------SGGWRMRLGL 157
Cdd:PRK10895 86 EASIFRRLSVYDN------LMAVLQIRDDLSAEQREDR-----------ANELMEEFhiehlrdsmgqslSGGERRRVEI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLDVETILWLE---DWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKriiEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-221 |
3.13e-06 |
|
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: 50.19 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELR-----RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE--QPPEWVvaHLPQEV 73
Cdd:TIGR03269 279 IIKVRNVSKRyisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWV--DMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 74 PGSDRRAVDYV--LDGDAEL---RDLQRRLEQAndgaeqarlyAALEAIDGWsAEARARRLLAGLGFAPADAE----RPM 144
Cdd:TIGR03269 357 PDGRGRAKRYIgiLHQEYDLyphRTVLDNLTEA----------IGLELPDEL-ARMKAVITLKMVGFDEEKAEeildKYP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 145 RDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD-------VETILWLEDWLARypgTVIVIAHDRRFLDSVCTHVAHIE 217
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMR 502
|
....
gi 648648866 218 RGTI 221
Cdd:TIGR03269 503 DGKI 506
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
320-511 |
3.17e-06 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 48.65 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPAlQVGYFAQHQREQLDLE----------- 388
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE-DISGLSEAELYRLRRRmgmlfqsgalf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 389 ---------ASPLvHLQRQDPRAE-EQRLRNFLGGMGFPGDkADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHL 458
Cdd:cd03261 90 dsltvfenvAFPL-REHTRLSEEEiREIVLEKLEAVGLRGA-EDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 459 D-----------LDMREALaealenyagGL--VVVAHDRELLARVCDRFWTVEAGRLsPFDGDLDD 511
Cdd:cd03261 168 DpiasgviddliRSLKKEL---------GLtsIMVTHDLDTAFAIADRIAVLYDGKI-VAEGTPEE 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
325-502 |
3.28e-06 |
|
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: 48.62 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQREQLDLEAS-------------- 390
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQepvlfarslqdnia 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 391 ---PLVHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPVG-QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREAL 466
Cdd:cd03248 110 yglQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGsQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 648648866 467 AEALE--NYAGGLVVVAHDRELLARVcDRFWTVEAGRL 502
Cdd:cd03248 190 QQALYdwPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
298-474 |
3.45e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 298 EIPTPGRLPDP----LLALDHAEVCTGERVR---LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTA------- 363
Cdd:TIGR00955 7 NSDVFGRVAQDgswkQLVSRLRGCFCRERPRkhlLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsgsvl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 364 --GERRVDPALQV--GYFAQHQ--------REQLDLEAspLVHLQRQDPRAEE-QRLRNFLGGMGFpGDKADGPVGQC-- 428
Cdd:TIGR00955 87 lnGMPIDAKEMRAisAYVQQDDlfiptltvREHLMFQA--HLRMPRRVTKKEKrERVDEVLQALGL-RKCANTRIGVPgr 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 648648866 429 ----SGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYA 474
Cdd:TIGR00955 164 vkglSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-201 |
3.63e-06 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 48.38 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahLPQEVPGSD------RRAVDYVLDGDAE 90
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI----------LIDGIDIRDisrkslRSMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 LRDLQRrleqanDGAEQARLYAALEAIDGWSAEARARRLLAGL--GFAPADAERPmRDFSGGWRMRLGLARTLMTRSDLL 168
Cdd:cd03254 89 FSGTIM------ENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENG-GNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 648648866 169 LLDEPTNHLDVETILWLEDWLARYPG--TVIVIAH 201
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKgrTSIIIAH 196
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
122-226 |
3.81e-06 |
|
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: 49.28 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 122 AEARARRLLAGLGFApaDAERPMRD----FSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVeTI------LwLEDWLAR 191
Cdd:COG0444 124 ARERAIELLERVGLP--DPERRLDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIqaqilnL-LKDLQRE 199
|
90 100 110
....*....|....*....|....*....|....*..
gi 648648866 192 YPGTVIVIAHDrrfLdSVcthVAHI-ERgtIA-LYAG 226
Cdd:COG0444 200 LGLAILFITHD---L-GV---VAEIaDR--VAvMYAG 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-181 |
3.83e-06 |
|
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: 49.08 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 16 LLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEwvVAHLPQE---VPGSDRRAVDYVLDGDaELR 92
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQFswiMPGTIKENIIFGVSYD-EYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 93 dlqrrleqandgaeqarlyaaleaidgWSAEARARRLLAGLGFAPADAERPMRD----FSGGWRMRLGLARTLMTRSDLL 168
Cdd:cd03291 129 ---------------------------YKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLY 181
|
170
....*....|...
gi 648648866 169 LLDEPTNHLDVET 181
Cdd:cd03291 182 LLDSPFGYLDVFT 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
340-489 |
4.06e-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: 47.35 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFaqhqreqldleaSPLVHLQRQdpraeeqrlrnFLggmgfpgd 419
Cdd:cd03227 26 ITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCI------------VAAVSAELI-----------FT-------- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 420 kadgpVGQCSGGERVRLVLALLI----WQAPSLLLLDEPTNHLDLDMREALAEALENYAGG---LVVVAHDRELLAR 489
Cdd:cd03227 75 -----RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgaqVIVITHLPELAEL 146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-503 |
4.15e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE------QPPEWVVAH------LPQE---VPGSDRRav 81
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggnpcARLTPAKAHqlgiylVPQEpllFPNLSVK-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 DYVLDGDAELRDLQRRLEQandgaeqarlyaaleaidgwsaeararrLLAGLGF-----APAD----AERPMRDfsggwr 152
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQ----------------------------LLAALGCqldldSSAGslevADRQIVE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 153 mrlgLARTLMTRSDLLLLDEPTNHL---DVETIL-WLEDWLARYPGtVIVIAHDRRFLDSVCTHVAHIERGTIALyagSY 228
Cdd:PRK15439 151 ----ILRGLMRDSRILILDEPTASLtpaETERLFsRIRELLAQGVG-IVFISHKLPEIRQLADRISVMRDGTIAL---SG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 229 THAEAKRAEAIvqseaaaarvaaerahledfvrrfrakaskarQAQSRLKRLERMDEVAVIRAARPIHLEIPTPGRlpdP 308
Cdd:PRK15439 223 KTADLSTDDII--------------------------------QAITPAAREKSLSASQKLWLELPGNRRQQAAGA---P 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 309 LLALDHaevCTGERVRlqPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE----------RRVDPALQVG--Y 376
Cdd:PRK15439 268 VLTVED---LTGEGFR--NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRimlngkeinaLSTAQRLARGlvY 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 377 FAQ-HQREQLDLEA------SPLVHLQR---QDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAP 446
Cdd:PRK15439 343 LPEdRQSSGLYLDAplawnvCALTHNRRgfwIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASP 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 447 SLLLLDEPTNHLDLDMREALAEALENYAGGLVVV---AHDRELLARVCDRFWTVEAGRLS 503
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVlfiSSDLEEIEQMADRVLVMHQGEIS 482
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-181 |
4.27e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.33 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 10 RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSL-------LAALQGELALDAGEIEQ----PPEWVVAHLPQE---VPG 75
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtlglfriNESAEGEIIIDGLNIAKiglhDLRFKITIIPQDpvlFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 76 SDRRAvdyvLDGDAELRDlqrrlEQANDGAEQARLYAALEAidgwsaeararrLLAGLGFAPADAErpmRDFSGGWRMRL 155
Cdd:TIGR00957 1375 SLRMN----LDPFSQYSD-----EEVWWALELAHLKTFVSA------------LPDKLDHECAEGG---ENLSVGQRQLV 1430
|
170 180
....*....|....*....|....*.
gi 648648866 156 GLARTLMTRSDLLLLDEPTNHLDVET 181
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLET 1456
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-173 |
4.88e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 48.94 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMqDIELRRGRQILlqHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPE-WVVAHLPQEVPgSDRR 79
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvLQDSARGIFLP-PHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 80 AVDYV---------LDGDAELRDLQRRLEQANDGAEQARLYAALEaidgwsaeararrlLAGLgfapadAERPMRDFSGG 150
Cdd:COG4148 78 RIGYVfqearlfphLSVRGNLLYGRKRAPRAERRISFDEVVELLG--------------IGHL------LDRRPATLSGG 137
|
170 180
....*....|....*....|...
gi 648648866 151 WRMRLGLARTLMTRSDLLLLDEP 173
Cdd:COG4148 138 ERQRVAIGRALLSSPRLLLMDEP 160
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
320-502 |
4.94e-06 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 48.10 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------RRVDPA-LQVGYFAQH---------- 380
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTilfggedaTDVPVQeRNVGFVFQHyalfrhmtvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 381 QREQLDLEASPLvhlQRQDPRAE-EQRLRNFLGGMGFPGdKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD 459
Cdd:cd03296 93 DNVAFGLRVKPR---SERPPEAEiRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648648866 460 LDMREALAEALENYAGGL----VVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03296 169 AKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
320-481 |
4.96e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpalqvGYFAQHQREQL--DL---------- 387
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-----GEPIRRQRDEYhqDLlylghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 388 -EASPLVHL---QRQDPRAEEQRLRNFLGGMGFPGdKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMR 463
Cdd:PRK13538 87 tELTALENLrfyQRLHGPGDDEALWEALAQVGLAG-FEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|
gi 648648866 464 EALAEALENYA--GGLVVVA 481
Cdd:PRK13538 166 ARLEALLAQHAeqGGMVILT 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-178 |
5.05e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.46 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppeWvvahlpqevpgsDRRA 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVL----W------------QGKP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLDGdaeLRDLQRRLEQANDGAEQARLYAALEAIDGWS------AEAR-ARRLLAGLGFAPADAER--PMRDFSGGW 151
Cdd:PRK13638 65 LDYSKRG---LLALRQQVATVFQDPEQQIFYTDIDSDIAFSlrnlgvPEAEiTRRVDEALTLVDAQHFRhqPIQCLSHGQ 141
|
170 180
....*....|....*....|....*..
gi 648648866 152 RMRLGLARTLMTRSDLLLLDEPTNHLD 178
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
560-621 |
5.23e-06 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 44.38 E-value: 5.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 560 LQQRADRAERDCSQTQERLQTLESELADPDLYAGDhaERLAALTREQGELCARLEALEAEWM 621
Cdd:pfam16326 6 EQRELEELEAEIEKLEEEIAELEAQLADPELYSDY--EKLQELSAELEELEAELEELYERWE 65
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-203 |
5.27e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.95 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRR--GRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWVVAHLPQEVPGSD- 77
Cdd:PRK10908 1 MIRFEHVSKAYlgGRQAL-QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-----WFSGHDITRLKNREv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 78 ---RRAVDYVLDGDAELRDlqrRLEQANdgaeqarlYAALEAIDGWSAEARARRLLAGL---GFAPADAERPMRdFSGGW 151
Cdd:PRK10908 75 pflRRQIGMIFQDHHLLMD---RTVYDN--------VAIPLIIAGASGDDIRRRVSAALdkvGLLDKAKNFPIQ-LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 152 RMRLGLARTLMTRSDLLLLDEPTNHLD---VETILWLEDWLARYPGTVIVIAHDR 203
Cdd:PRK10908 143 QQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-173 |
5.33e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.10 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 11 RGRQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI---EQPpewvVAHLPQevpgsDRRA---VDYv 84
Cdd:COG1137 14 GKRTVV-KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIfldGED----ITHLPM-----HKRArlgIGY- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 ldgdaelrdL-Q-----RRL--EQaNdgaeqarLYAALEAIdGWSAEARARRL--------LAGLGFAPADAerpmrdFS 148
Cdd:COG1137 83 ---------LpQeasifRKLtvED-N-------ILAVLELR-KLSKKEREERLeelleefgITHLRKSKAYS------LS 138
|
170 180
....*....|....*....|....*
gi 648648866 149 GGWRMRLGLARTLMTRSDLLLLDEP 173
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEP 163
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-226 |
6.47e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.31 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQppewvvahlpqevpgsDRRAVDYVLDGDAELRDLQR 96
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILF----------------DGKPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 97 RLEQAND------GAEQARLYAALE-AIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTLMTRSDLLL 169
Cdd:PRK13636 86 MVFQDPDnqlfsaSVYQDVSFGAVNlKLPEDEVRKRVDNALKRTGIEHL-KDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 170 LDEPTNHLD---VETILWLEDWLARYPGTVIVIA-HDRRFLDSVCTHVAHIERGTIALYAG 226
Cdd:PRK13636 165 LDEPTAGLDpmgVSEIMKLLVEMQKELGLTIIIAtHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
321-501 |
6.63e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.12 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 321 ERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPA-------------LQVGYFAQHQREQL-- 385
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVditdkkvklsdirKKVGLVFQYPEYQLfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 -----DLEASPlVHLQRQDPRAEEqRLRNFLGGMGFPGDK-ADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD 459
Cdd:PRK13637 99 etiekDIAFGP-INLGLSEEEIEN-RVKRAMNIVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 460 LDMREALAEAL----ENYAGGLVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:PRK13637 177 PKGRDEILNKIkelhKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-202 |
6.79e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.01 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAAL------QGELALDAGEIEQPPEWVVAH----LPQEVPGSDRRAVDYVLDgdae 90
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMagllpgSGSIQFAGQPLEAWSAAELARhrayLSQQQTPPFAMPVFQYLT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 lrdlqrrLEQAnDGAEQARLYAALEAIdgwsaeARARRLLAGLGfapadaeRPMRDFSGG-W-RMRLGLA-----RTLMT 163
Cdd:PRK03695 92 -------LHQP-DKTRTEAVASALNEV------AEALGLDDKLG-------RSVNQLSGGeWqRVRLAAVvlqvwPDINP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 648648866 164 RSDLLLLDEPTNHLDVETILWLE---DWLARYPGTVIVIAHD 202
Cdd:PRK03695 151 AGQLLLLDEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHD 192
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-226 |
7.94e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEieqppewvVAHLPQEVPG---SDRRAV--DYVLDGDAELRDLQ 95
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGE--------VAWLGKDLLGmkdDEWRAVrsDIQMIFQDPLASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 96 RRLEQANDGAEQARLY----AALEAIDgwsaeaRARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLD 171
Cdd:PRK15079 113 PRMTIGEIIAEPLRTYhpklSRQEVKD------RVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 172 EPTNHLDVE---TILWLEDWLARYPG-TVIVIAHDRrfldSVcthVAHIERGTIALYAG 226
Cdd:PRK15079 187 EPVSALDVSiqaQVVNLLQQLQREMGlSLIFIAHDL----AV---VKHISDRVLVMYLG 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-174 |
8.43e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.57 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI----EQPPEWVVAHLPQE---- 72
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgKDITDWQTAKIMREavai 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 73 VPGSDRRAVDYVLDGD-------AELRDLQRRLEQANDgaeqarLYAALeaidgwsAEARARRllAGlgfapadaerpmr 145
Cdd:PRK11614 85 VPEGRRVFSRMTVEENlamggffAERDQFQERIKWVYE------LFPRL-------HERRIQR--AG------------- 136
|
170 180
....*....|....*....|....*....
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPT 174
Cdd:PRK11614 137 TMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-181 |
8.70e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvvaHLPQEVPGSDRRAVDyvldgDA------- 89
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIL--------YLGKEVTFNGPKSSQ-----EAgigiihq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 ELrDLQRRLEQAND---GAEQARlyaALEAIDGWSAEARARRLLAGLGFaPADAERPMRDFSGGWRMRLGLARTLMTRSD 166
Cdd:PRK10762 87 EL-NLIPQLTIAENiflGREFVN---RFGRIDWKKMYAEADKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170
....*....|....*.
gi 648648866 167 LLLLDEPTNHL-DVET 181
Cdd:PRK10762 162 VIIMDEPTDALtDTET 177
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-210 |
9.54e-06 |
|
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: 48.53 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILLQHASLTVHAGWRVGLTGANGSGKS----SLLAALQGELALDAGEIeqppewvvaHLpqevpgsdrRAVDYVLDG 87
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSI---------LF---------DGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 88 DAELRDLQ-RRL------------------EQAndgAEQARLYAALeaiDGWSAEARARRLLAGLGFApaDAERPMRDF- 147
Cdd:COG4172 83 ERELRRIRgNRIamifqepmtslnplhtigKQI---AEVLRLHRGL---SGAAARARALELLERVGIP--DPERRLDAYp 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 148 ---SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPGT-VIVIAHD----RRFLDSVC 210
Cdd:COG4172 155 hqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVqaqILDLLKDLQRELGMaLLLITHDlgvvRRFADRVA 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-525 |
1.01e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.78 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQREQLDLEASPLVHLQRQDP-------------RAEEQR 406
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPfpmsimdnvlagvRAHKLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 407 LRNFLGGMG------------FPGDKADGPVgQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYA 474
Cdd:PRK14271 132 PRKEFRGVAqarltevglwdaVKDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 475 GGL--VVVAHDRELLARVCDRFWTVEAGRL-----------SPFDGDLDDYARALQARQREAAR 525
Cdd:PRK14271 211 DRLtvIIVTHNLAQAARISDRAALFFDGRLveegpteqlfsSPKHAETARYVAGLSGDVKDAKR 274
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
310-501 |
1.07e-05 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 47.04 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD------------PALQVGYF 377
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglppherARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 378 AQHQR--------EQLDLEASPLVHLQRQDPRAEEQRLrnflggmgFP--GDKADGPVGQCSGGERVRLVLALLIWQAPS 447
Cdd:cd03224 81 PEGRRifpeltveENLLLGAYARRRAKRKARLERVYEL--------FPrlKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 448 LLLLDEPTNHLDLDMREALAEALENYAGG---LVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEgvtILLVEQNARFALEIADRAYVLERGR 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
320-502 |
1.09e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.44 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVrLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRV-----DPAL--------------QVGYFAQH 380
Cdd:PRK11264 15 GQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditiDTARslsqqkglirqlrqHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 381 -----QREQLD--LEASPLVhlqRQDPRAE-EQRLRNFLGGMGFPGdKADGPVGQCSGGERVRLVLALLIWQAPSLLLLD 452
Cdd:PRK11264 94 fnlfpHRTVLEniIEGPVIV---KGEPKEEaTARARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648648866 453 EPTNHLDLDM-REALA--EALENYAGGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK11264 170 EPTSALDPELvGEVLNtiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
337-501 |
1.14e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.42 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 337 RIGILGPNGAGKSTLLTLLAGELLPTAGE-----RRVDPALQ------VGYFAQHQREQL-------DLEASPLVhlQRQ 398
Cdd:PRK13647 33 KTALLGPNGAGKSTLLLHLNGIYLPQRGRvkvmgREVNAENEkwvrskVGLVFQDPDDQVfsstvwdDVAFGPVN--MGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 399 DPRAEEQRLRNFLGGMGFPgDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALE--NYAGG 476
Cdd:PRK13647 111 DKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDrlHNQGK 189
|
170 180
....*....|....*....|....*.
gi 648648866 477 LVVVA-HDRELLARVCDRFWTVEAGR 501
Cdd:PRK13647 190 TVIVAtHDVDLAAEWADQVIVLKEGR 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
336-459 |
1.15e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 336 DRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--------PAL-----QVGYFAQHQREQL-------DLEASPL-VH 394
Cdd:PRK13639 29 EMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikydkKSLlevrkTVGIVFQNPDDQLfaptveeDVAFGPLnLG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 395 LQRQDPraeEQRLRNFLGGMGFPGdKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD 459
Cdd:PRK13639 109 LSKEEV---EKRVKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
325-506 |
1.16e-05 |
|
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: 46.64 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpalqvgyfaqhqreQLDLEASPLVHLQR------Q 398
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID--------------GIDISTIPLEDLRSsltiipQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 399 DPRAEEQRLRNFLGGMGFPGD-------KADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEAL- 470
Cdd:cd03369 90 DPTLFSGTIRSNLDPFDEYSDeeiygalRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIr 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 648648866 471 ENYAGG-LVVVAHDRELLARvCDRFWTVEAGRLSPFD 506
Cdd:cd03369 170 EEFTNStILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-486 |
1.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 401 RAEEQRLRNFLGGMGfpgdkADGPVGQCSGGERV------RLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYA 474
Cdd:PRK03918 767 KAEENKVKLFVVYQG-----KERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYL 841
|
90
....*....|....*
gi 648648866 475 GGL---VVVAHDREL 486
Cdd:PRK03918 842 RKIpqvIIVSHDEEL 856
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
309-501 |
1.45e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 309 LLALDHAEvctgervrlqpttLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD-------PALQVG------ 375
Cdd:PRK11300 18 LLAVNNVN-------------LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieglPGHQIArmgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 376 -----------------YFAQHQReqldLEASPLVHL-----QRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGER 433
Cdd:PRK11300 85 tfqhvrlfremtvienlLVAQHQQ----LKTGLFSGLlktpaFRRAESEALDRAATWLERVGL-LEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 434 VRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNpketKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-201 |
1.46e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDageieqppewvvahlpqevpGSDRRavDYVLdgdA 89
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfydidEGEILLD--------------------GHDLR--DYTL---A 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 ELRDLQRRLEQA----NDGAEQARLYAALEAidgWSAE--ARARRLLAGLGFApadaeRPMRD------------FSGGW 151
Cdd:PRK11176 414 SLRNQVALVSQNvhlfNDTIANNIAYARTEQ---YSREqiEEAARMAYAMDFI-----NKMDNgldtvigengvlLSGGQ 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 648648866 152 RMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLA--RYPGTVIVIAH 201
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAH 537
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-177 |
1.48e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahLPQEVPGSDRRAVDYVLDGDAEL-RDLQ 95
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI----------LIDGQEMRFASTTAALAAGVAIIyQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 96 RRLEQANdgAEQ---ARLYAALEAIDGWSAEARARRLLAGLGFApADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDE 172
Cdd:PRK11288 90 LVPEMTV--AENlylGQLPHKGGIVNRRLLNYEAREQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
....*
gi 648648866 173 PTNHL 177
Cdd:PRK11288 167 PTSSL 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-227 |
1.69e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 47.39 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewvVAHLpqeVPGSDRRAVdyvldgdaeLRDL-----Q 95
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR------VLGY---VPFKRRKEF---------ARRIgvvfgQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 96 RrlEQ------ANDGaeqARLYAALEAIDgwsaEARARRLLAGLgfapadAE---------RPMRDFSGGWRMRLGLART 160
Cdd:COG4586 104 R--SQlwwdlpAIDS---FRLLKAIYRIP----DAEYKKRLDEL------VElldlgelldTPVRQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 161 LMTRSDLLLLDEPTNHLDVETILWLEDWL----ARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIaLYAGS 227
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLkeynRERGTTILLTSHDMDDIEALCDRVIVIDHGRI-IYDGS 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
321-502 |
1.91e-05 |
|
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: 47.79 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 321 ERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQREQLDLeASPLVHL----- 395
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL-VSQDVVLfndti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 396 --------QRQDPRAEEQR------LRNFLGGM--GFpgdkaDGPVGQ----CSGGERVRLVLALLIWQAPSLLLLDEPT 455
Cdd:TIGR02203 423 anniaygrTEQADRAEIERalaaayAQDFVDKLplGL-----DTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 648648866 456 NHLDLDMREALAEALENYAGG--LVVVAHdRELLARVCDRFWTVEAGRL 502
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQGrtTLVIAH-RLSTIEKADRIVVMDDGRI 545
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
1.97e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.44 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLL------------AALQGELALDAGEIEQPP------- 62
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlielypeARVSGEVYLDGQDIFKMDvielrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 63 EWVVAHLPQEVPGSDrravdyVLDGDAELRDLQRrleQANDGAE-QARLYAALEAIDGWsaEARARRLLAglgfapadae 141
Cdd:PRK14247 84 VQMVFQIPNPIPNLS------IFENVALGLKLNR---LVKSKKElQERVRWALEKAQLW--DEVKDRLDA---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 142 rPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWL--ARYPGTVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:PRK14247 143 -PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFleLKKDMTIVLVTHFPQQAARISDYVAFLYKG 221
|
..
gi 648648866 220 TI 221
Cdd:PRK14247 222 QI 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
325-493 |
2.43e-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: 45.93 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD------PALQVGYFAQHQR-------EQ---LDLE 388
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgPGPDRGYVFQQDAllpwltvLDnvaLGLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 389 AsplVHLQRQDPRAEEQRLRNFLGGMGFpgdkADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMRE 464
Cdd:cd03293 100 L---QGVPKAEARERAEELLELVGLSGF----ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQE 172
|
170 180
....*....|....*....|....*....
gi 648648866 465 ALAEALENYAGGLVVVAHDRELLARVCDR 493
Cdd:cd03293 173 ELLDIWRETGKTVLLVTHDIDEAVFLADR 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
426-492 |
2.44e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.37 E-value: 2.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 426 GQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYAggLVVVAHDRELLARVCD 492
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgtAKIEELLFELKKEYT--IVLVTHSPAQAARVSD 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
124-235 |
2.54e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 124 ARARRLLAGLGFAPAD--AERPMRdFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVI 199
Cdd:PRK14271 140 AQARLTEVGLWDAVKDrlSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIV 218
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 648648866 200 AHDRRFLDSVCTHVA------HIERGTIALYAGSYTHAEAKR 235
Cdd:PRK14271 219 THNLAQAARISDRAAlffdgrLVEEGPTEQLFSSPKHAETAR 260
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
329-527 |
2.69e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 45.90 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYfAQHQR------------EQLDLEA------S 390
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-PPAERpvsmlfqennlfPHLTVAQniglglR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 391 PLVHLQrqdpRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREAL 466
Cdd:COG3840 98 PGLKLT----AEQRAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 467 AEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSPfDGDLDdyarALQARQREAARSA 527
Cdd:COG3840 173 DELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA-DGPTA----ALLDGEPPPALAA 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
325-490 |
2.70e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.96 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE------------RRVDPAL---QVGYFAQHQREQLD--- 386
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvifngqpmsklsSAAKAELrnqKLGFIYQFHHLLPDfta 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 387 LE--ASPLVhLQRQDPRAEEQRLRNFLGGMGFPGDKADGPvGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDL---- 460
Cdd:PRK11629 105 LEnvAMPLL-IGKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnad 182
|
170 180 190
....*....|....*....|....*....|
gi 648648866 461 DMREALAEALENYAGGLVVVAHDRELLARV 490
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-201 |
2.72e-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: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIEL-RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVPGSDRR 79
Cdd:TIGR00954 451 GIKFENIPLvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 80 AVDYVLDGDAELrDLQRR------LEQAndgAEQARLYAALEAIDGWSAEARARRLLaglgfapadaerpmrdfSGGWRM 153
Cdd:TIGR00954 531 LRDQIIYPDSSE-DMKRRglsdkdLEQI---LDNVQLTHILEREGGWSAVQDWMDVL-----------------SGGEKQ 589
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648648866 154 RLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPGTVIVIAH 201
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-179 |
2.74e-05 |
|
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: 46.08 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPqevpgSDR 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILldgKD----ITNLP-----PHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 79 RAVDYVLDGDAELRDLQ--------RRLEQANDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGG 150
Cdd:cd03300 72 RPVNTVFQNYALFPHLTvfeniafgLRLKKLPKAEIKERVAEALDLVQ-----------LEGY------ANRKPSQLSGG 134
|
170 180
....*....|....*....|....*....
gi 648648866 151 WRMRLGLARTLMTRSDLLLLDEPTNHLDV 179
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
334-511 |
2.83e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 46.26 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 334 PEDRI-GILGPNGAGKSTLLTLLAGELLPTAGERRVD----------------------PALQVG----YFAQhqreqld 386
Cdd:COG4152 25 PKGEIfGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgepldpedrrrigylpeerglyPKMKVGeqlvYLAR------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 387 leasplvhLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGE--RVRLVLALLiwQAPSLLLLDEPTNHLDLDMRE 464
Cdd:COG4152 98 --------LKGLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNqqKVQLIAALL--HDPELLILDEPFSGLDPVNVE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 648648866 465 ALAEALENYA--GGLVVVA-HDRELLARVCDRFWTVEAGRLsPFDGDLDD 511
Cdd:COG4152 167 LLKDVIRELAakGTTVIFSsHQMELVEELCDRIVIINKGRK-VLSGSVDE 215
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
308-461 |
2.96e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.61 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 308 PLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------RRVDPALQVGYFAQ 379
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQiqidgktaTRGDRSRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 380 HQREQLDLEASPLVH-LQRQDPRAEEQRLRNFLGGMGFPGdKADGPVGQCSGGERVRLVLALLiWQAPS-LLLLDEPTNH 457
Cdd:PRK13543 90 LPGLKADLSTLENLHfLCGLHGRRAKQMPGSALAIVGLAG-YEDTLVRQLSAGQKKRLALARL-WLSPApLWLLDEPYAN 167
|
....
gi 648648866 458 LDLD 461
Cdd:PRK13543 168 LDLE 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-219 |
3.01e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDA--GEIEQPPEWVVAhlpQEVPGSDR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKA---SNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 79 RAVDYVLDGDAELRDLQRrLEQANDGAEqARLYAALEAIDgwSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLA 158
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSV-AENIFLGNE-ITLPGGRMAYN--AMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 159 RTLMTRSDLLLLDEPTNHL---DVETILWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERG 219
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
429-511 |
3.06e-05 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 45.79 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 429 SGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEAL----ENYAGGLVVVAHDRELLARVCDRFWTVEAGRLSP 504
Cdd:cd03299 131 SGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELkkirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
....*..
gi 648648866 505 FdGDLDD 511
Cdd:cd03299 211 V-GKPEE 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
341-506 |
3.29e-05 |
|
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: 45.75 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 341 LGPNGAGKSTLLTLLAGELLPTAGE--------RRVDP-ALQ--VGYFAQ------HQREQLDLEASPlvHLQRQDPRAE 403
Cdd:cd03295 33 IGPSGSGKTTTMKMINRLIEPTSGEifidgediREQDPvELRrkIGYVIQqiglfpHMTVEENIALVP--KLLKWPKEKI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 404 EQRLRNFLGGMGF-PGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGL----V 478
Cdd:cd03295 111 RERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgktiV 190
|
170 180
....*....|....*....|....*...
gi 648648866 479 VVAHDRELLARVCDRFWTVEAGRLSPFD 506
Cdd:cd03295 191 FVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
338-517 |
3.40e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 338 IGILGPNGAGKSTLLTLLAGELLPTAGERRVDpALQVGYFAQHqreqLDLeasplvhlqrqdpraeeqrlrnflggmgfp 417
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-GITPVYKPQY----IDL------------------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 418 gdkadgpvgqcSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEAL----ENYAGGLVVVAHDRELLARVCDR 493
Cdd:cd03222 73 -----------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIrrlsEEGKKTALVVEHDLAVLDYLSDR 141
|
170 180
....*....|....*....|....*....
gi 648648866 494 FWTVEA-----GRLSPFDGDLDDYARALQ 517
Cdd:cd03222 142 IHVFEGepgvyGIASQPKGTREGINRFLR 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
429-488 |
3.99e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 3.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 429 SGGERVRLVLALLIWQAP------SLLLLDEPTNHLDLDMREALAEALE---NYAGG---LVVVAHDRELLA 488
Cdd:PRK01156 803 SGGEKTAVAFALRVAVAQflnndkSLLIMDEPTAFLDEDRRTNLKDIIEyslKDSSDipqVIMISHHRELLS 874
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-189 |
4.90e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.85 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 12 GRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVvahlpQEVPGSDRRaVDYVLDGDAEL 91
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHARDRK-VGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 92 RD-------------LQRRlEQANDGAEQARLYAALEAIDgwsaeararrlLAGLgfapadAERPMRDFSGGWRMRLGLA 158
Cdd:PRK10851 87 RHmtvfdniafgltvLPRR-ERPNAAAIKAKVTQLLEMVQ-----------LAHL------ADRYPAQLSGGQKQRVALA 148
|
170 180 190
....*....|....*....|....*....|.
gi 648648866 159 RTLMTRSDLLLLDEPTNHLDVETILWLEDWL 189
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWL 179
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
325-506 |
5.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.77 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD----PA------------LQVGYFAQHQREQL--- 385
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaiPAnlkkikevkrlrKEIGLVFQFPEYQLfqe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 ----DLEASPlVHLQrQDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLD 461
Cdd:PRK13645 107 tiekDIAFGP-VNLG-ENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 648648866 462 MREALAEALE----NYAGGLVVVAHDRELLARVCDRFWTVEAGRL----SPFD 506
Cdd:PRK13645 185 GEEDFINLFErlnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVisigSPFE 237
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
429-501 |
6.56e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.49 E-value: 6.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 429 SGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMR----EALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQaqimTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-202 |
8.28e-05 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 44.17 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIeqppeWVVAHLPQEVPGSDRRAV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-----YIGGRDVTDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 82 ----DYVLDGDAELRD-----LQRRLEQANDGAEQARLYAALEAIDGwsaeararrLLaglgfapadaERPMRDFSGGWR 152
Cdd:cd03301 76 mvfqNYALYPHMTVYDniafgLKLRKVPKDEIDERVREVAELLQIEH---------LL----------DRKPKQLSGGQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648648866 153 MRLGLARTLMTRSDLLLLDEPTNHLD----VETILWLEDWLARYPGTVIVIAHD 202
Cdd:cd03301 137 QRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
429-506 |
8.28e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.77 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 429 SGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYAggLVVVAHDRELLARVCDR--FWTVEA--- 499
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDpistLRIEELMHELKEQYT--IIIVTHNMQQAARVSDMtaFFNVELteg 230
|
90
....*....|.
gi 648648866 500 ----GRLSPFD 506
Cdd:PRK14243 231 ggryGYLVEFD 241
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
427-502 |
8.36e-05 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 45.14 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 427 QCSGGERVRLVLAlliwQA----PSLLLLDEPTNHLD----LDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVE 498
Cdd:COG1118 133 QLSGGQRQRVALA----RAlavePEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMN 208
|
....
gi 648648866 499 AGRL 502
Cdd:COG1118 209 QGRI 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
306-485 |
8.99e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 45.09 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 306 PDPLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD-------PALQ--VGY 376
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglPPEKrnVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 377 FAQHqreqLDLeaSPlvHL-----------QRQDPRAE-EQRLRNFLG--GMGfpgDKADGPVGQCSGGE--RVRLVLAL 440
Cdd:COG3842 82 VFQD----YAL--FP--HLtvaenvafglrMRGVPKAEiRARVAELLElvGLE---GLADRYPHQLSGGQqqRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 648648866 441 LIwqAPSLLLLDEPTNHLDLDMREALAEALENYAGGL----VVVAHDRE 485
Cdd:COG3842 151 AP--EPRVLLLDEPLSALDAKLREEMREELRRLQRELgitfIYVTHDQE 197
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-227 |
9.56e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.65 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 143 PMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAHDRRFLDSVCTHVAHIERGT 220
Cdd:PRK14246 150 PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGE 229
|
....*..
gi 648648866 221 IALYAGS 227
Cdd:PRK14246 230 LVEWGSS 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
329-482 |
1.00e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 45.54 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 329 TLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDpalqvGYfaqhqreqlDLEASPLVHLQRQ---------- 398
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID-----GV---------DIRDLTLESLRRQigvvpqdtfl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 399 ------------DPRAEEQRLRN---------FLggMGFPgDKADGPVGQ----CSGGERVRLVLALLIWQAPSLLLLDE 453
Cdd:COG1132 426 fsgtirenirygRPDATDEEVEEaakaaqaheFI--EALP-DGYDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190
....*....|....*....|....*....|.
gi 648648866 454 PTNHLDLDMREALAEALENYAGG--LVVVAH 482
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
140-459 |
1.01e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 140 AERPMRDF----SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPG-TVIVIAHD----RRFLD 207
Cdd:PRK15134 146 AAKRLTDYphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELQQELNmGLLFITHNlsivRKLAD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 208 SVcthvahiergtialyagsythaeakraeAIVQSEAAaarvaaerahledfVRRFRAKASKARQAQSRLKRLermdeva 287
Cdd:PRK15134 226 RV----------------------------AVMQNGRC--------------VEQNRAATLFSAPTHPYTQKL------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 288 viRAARPIHLEIPTPGRLPdPLLALDHAEVC-----------TGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLA 356
Cdd:PRK15134 257 --LNSEPSGDPVPLPEPAS-PLLDVEQLQVAfpirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 357 GELlPTAGE--------------------RRVDPALQVGYFAQHQR---EQLdLEASPLVHLQRQDPRAEEQRLRNFLGG 413
Cdd:PRK15134 334 RLI-NSQGEiwfdgqplhnlnrrqllpvrHRIQVVFQDPNSSLNPRlnvLQI-IEEGLRVHQPTLSAAQREQQVIAVMEE 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 648648866 414 MGFPGDKADGPVGQCSGGERVRLVLA-LLIWQaPSLLLLDEPTNHLD 459
Cdd:PRK15134 412 VGLDPETRHRYPAEFSGGQRQRIAIArALILK-PSLIILDEPTSSLD 457
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
325-459 |
1.06e-04 |
|
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: 44.18 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKST---LLTLLAGELLPTAGE-----RRVDPAL---QVGYFAQHQ--------REQL 385
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQilfngQPRKPDQfqkCVAYVRQDDillpgltvRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 386 DLeaSPLVHLQR------QDPRAEEQRLRnflggmgfpgDKADGPVG-----QCSGGERVRLVLALLIWQAPSLLLLDEP 454
Cdd:cd03234 103 TY--TAILRLPRkssdaiRKKRVEDVLLR----------DLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
....*
gi 648648866 455 TNHLD 459
Cdd:cd03234 171 TSGLD 175
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-470 |
1.26e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 44.08 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD------PALQVGYFAQHQ-----REQLDLEASPLv 393
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDgvpvtgPGADRGVVFQKDallpwLNVLDNVAFGL- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648648866 394 HLQRQDPRAEEQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEAL 470
Cdd:COG4525 102 RLRGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
330-488 |
1.35e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.79 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 330 LRLRPEDRIGILGPNGAGKST--LLTLLAGELLPTAGERRVDPalqvgyfaqhqrEQLDLEASPLVHLQRQDPRAEEQRL 407
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTllRLLAGALKGTPVAGCVDVPD------------NQFGREASLIDAIGRKGDFKDAVEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 408 rnfLGGMGFpgdkADG-----PVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALA----EALENYAGGLV 478
Cdd:COG2401 119 ---LNAVGL----SDAvlwlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVArnlqKLARRAGITLV 191
|
170
....*....|
gi 648648866 479 VVAHDRELLA 488
Cdd:COG2401 192 VATHHYDVID 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
325-483 |
1.53e-04 |
|
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: 43.61 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD--------PALQVgYFAQHQ-------REQLDLEa 389
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkqitepgPDRMV-VFQNYSllpwltvRENIALA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 390 splVHLQRQDPRAEEQR--LRNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALA 467
Cdd:TIGR01184 79 ---VDRVLPDLSKSERRaiVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180
....*....|....*....|
gi 648648866 468 EAL----ENYAGGLVVVAHD 483
Cdd:TIGR01184 155 EELmqiwEEHRVTVLMVTHD 174
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-459 |
1.58e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.92 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 321 ERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPAlQVGYFAQHQREQldleasplvHLQR--Q 398
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-DVTKLPEYKRAK---------YIGRvfQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 399 DP-------------------------------RAEEQRLRNFLG--GMGFPgDKADGPVGQCSGGER--VRLVLALLiw 443
Cdd:COG1101 88 DPmmgtapsmtieenlalayrrgkrrglrrgltKKRRELFRELLAtlGLGLE-NRLDTKVGLLSGGQRqaLSLLMATL-- 164
|
170
....*....|....*.
gi 648648866 444 QAPSLLLLDEPTNHLD 459
Cdd:COG1101 165 TKPKLLLLDEHTAALD 180
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
325-502 |
1.59e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.84 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELlPTAGERRVD----PALQVGYFAQH-----QREQLdLEASPLVHL 395
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINgielRELDPESWRKHlswvgQNPQL-PHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 396 QRQDPRAEEQRLRNFLggmgfpgDKA-------------DGPVGQCSGGERV----RLVLALLIWQAPSLLLLDEPTNHL 458
Cdd:PRK11174 444 LLGNPDASDEQLQQAL-------ENAwvseflpllpqglDTPIGDQAAGLSVgqaqRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 459 DLDMREALAEALENYAGG--LVVVAHDRELLARvCDRFWTVEAGRL 502
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRqtTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-226 |
1.59e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.82 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAAL-------QGELALDAGEIEQPPEWVVAhlpqevp 74
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLsrlmtpaHGHVWLDGEHIQHYASKEVA------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 75 gsdRR----AVDYVLDGDAELRDLQRRLEqandgaeqarlYAALEAIDGWSAE--ARARRLLAGLGFAPAdAERPMRDFS 148
Cdd:PRK10253 81 ---RRigllAQNATTPGDITVQELVARGR-----------YPHQPLFTRWRKEdeEAVTKAMQATGITHL-ADQSVDTLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 149 GGWRMRLGLARTLMTRSDLLLLDEPTNHLDVE---TILWLEDWLARYPG-TVIVIAHDrrfLDSVCTHVAHIergtIALY 224
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShqiDLLELLSELNREKGyTLAAVLHD---LNQACRYASHL----IALR 218
|
..
gi 648648866 225 AG 226
Cdd:PRK10253 219 EG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
321-482 |
1.66e-04 |
|
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: 43.37 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 321 ERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQREQLDLeASPLVHL----- 395
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL-VSQDVFLfndtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 396 ----QRQDPRAEEQRLR---------NFLggMGFPgDKADGPVGQ----CSGGERVRLVLALLIWQAPSLLLLDEPTNHL 458
Cdd:cd03251 93 aeniAYGRPGATREEVEeaaraanahEFI--MELP-EGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180
....*....|....*....|....*.
gi 648648866 459 DLDMREALAEALENYAGG--LVVVAH 482
Cdd:cd03251 170 DTESERLVQAALERLMKNrtTFVIAH 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
325-459 |
1.72e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.43 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQREQLDLeASPLVH---------L 395
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV-VSQRVHlfsatlrdnL 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 396 QRQDPRAEEQRLRNFLGGMGFpGDKADGPVG----------QCSGGERVRLVLA-LLIWQAPsLLLLDEPTNHLD 459
Cdd:PRK11160 435 LLAAPNASDEALIEVLQQVGL-EKLLEDDKGlnawlgeggrQLSGGEQRRLGIArALLHDAP-LLLLDEPTEGLD 507
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-202 |
1.76e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 32 LTGANGSGKSSLLAALqgELAL-------------------DAGEIE-----QPPEWVV-------AHLPQEVPGSDRRA 80
Cdd:COG0419 28 IVGPNGAGKSTILEAI--RYALygkarsrsklrsdlinvgsEEASVElefehGGKRYRIerrqgefAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 81 VDYVLdGDAELRDLQRRLEQANDGAEQArlYAALEAIDGwsAEARARRLLAGLGfapadaerPMRDFSGGWRMRLGLART 160
Cdd:COG0419 106 LKRLL-GLEIYEELKERLKELEEALESA--LEELAELQK--LKQEILAQLSGLD--------PIETLSGGERLRLALADL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 648648866 161 LMtrsdlLLLDepTNHLDVETILWLEDWLARypgtVIVIAHD 202
Cdd:COG0419 173 LS-----LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
309-470 |
2.14e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 43.53 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 309 LLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD------PALQVGYFAQHQ- 381
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 ----REQLDLEASPLvHLQRQDPRAEEQRLRNFLGGMGFPGDKADgPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNH 457
Cdd:PRK11248 81 llpwRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKR-YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170
....*....|...
gi 648648866 458 LDLDMREALAEAL 470
Cdd:PRK11248 159 LDAFTREQMQTLL 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-201 |
2.29e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.32 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 11 RGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI--EQPPEWVVAH--LPQEVPGSDRRAV---DY 83
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrlDGRPLSSLSHsvLRQGVAMVQQDPVvlaDT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 84 VLDGDAELRDLqrrleqandgaEQARLYAALEAIDgwsaeararrlLAGLgfapadaerpMRDFSGGWRMRLG------- 156
Cdd:PRK10790 431 FLANVTLGRDI-----------SEEQVWQALETVQ-----------LAEL----------ARSLPDGLYTPLGeqgnnls 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 157 --------LARTLMTRSDLLLLDEPTNHLDVETILWLEDWLA--RYPGTVIVIAH 201
Cdd:PRK10790 479 vgqkqllaLARVLVQTPQILILDEATANIDSGTEQAIQQALAavREHTTLVVIAH 533
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
76-221 |
2.33e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 76 SDRRAVDYVLDGDAELRDLQRrleQANDGAEQARLYAALEAIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRL 155
Cdd:NF000106 78 ANRRALRRTIG*HRPVR*GRR---ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEA-AGRAAAKYSGGMRRRL 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 156 GLARTLMTRSDLLLLDEPTNHLDVETI--LWLE-DWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRneVWDEvRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
132-208 |
2.37e-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: 42.31 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 132 GLGFAPADaeRPMRDFSGGWRMRLGLARTLMTRSD--LLLLDEPTNHLDVETILWLEDWLARY---PGTVIVIAHDRRFL 206
Cdd:cd03238 75 GLGYLTLG--QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVL 152
|
..
gi 648648866 207 DS 208
Cdd:cd03238 153 SS 154
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-221 |
2.59e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.15 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 2 IRMQDIELRRGRqILLQHASLTVHAGWRVGLTGANGSGKS-SLLAAL----------QGELALDAGEIEqpPEWVVAHLP 70
Cdd:PRK10418 5 IELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpagvrqtAGRVLLDGKPVA--PCALRGRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 71 QEVPGSDRRAVDYVLDGDAELRDLQRRLEQANDgaeQARLYAALEAidgwsaeararrllAGLGFAPADAERPMRDFSGG 150
Cdd:PRK10418 82 ATIMQNPRSAFNPLHTMHTHARETCLALGKPAD---DATLTAALEA--------------VGLENAARVLKLYPFEMSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 151 WRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLA-----RYPGTVIViAHDRRFLDSVCTHVAHIERGTI 221
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLEsivqkRALGMLLV-THDMGVVARLADDVAVMSHGRI 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
427-493 |
2.83e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.53 E-value: 2.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 427 QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGL----VVVAHDRELLARVCDR 493
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDQEEAMEVADR 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
341-502 |
3.12e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.19 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 341 LGPNGAGKSTLLTLLAGELLPTAGERRVDPAL---------------QVGYFAQHQREQLdLEASPL--VHLQRQD---- 399
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQFPESQL-FEETVLkdVAFGPQNfgvs 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 400 PRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALEN-YAGGL- 477
Cdd:PRK13649 118 QEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMt 197
|
170 180
....*....|....*....|....*.
gi 648648866 478 -VVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK13649 198 iVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-202 |
3.68e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.83 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI----EQPPEWVVAHLPQEvpgs 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgENIPAMSRSRLYTV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 77 dRRAVDYVLDGDAELRDLQRRLEQANDGAEQARLYAA-LEAIDGWSAEARARRLLAGLgfAPAdaerpmrDFSGGWRMRL 155
Cdd:PRK11831 83 -RKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPlLHSTVMMKLEAVGLRGAAKL--MPS-------ELSGGMARRA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648648866 156 GLARTLMTRSDLLLLDEPTNHLDVET---ILWLEDWLARYPG-TVIVIAHD 202
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITmgvLVKLISELNSALGvTCVVVSHD 203
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
427-502 |
4.14e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 427 QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEAL------ENYAggLVVVAHDRELLARVCDRFWTVEAG 500
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLlelqqkENMA--LVLITHDLALVAEAAHKIIVMYAG 230
|
..
gi 648648866 501 RL 502
Cdd:PRK11022 231 QV 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-202 |
4.15e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 10 RRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPpewvvahlpqevpgsdrrAVDYVLDGDA 89
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID------------------GVDIAKISDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 ELRDLQRRleQANDGAEQARLYAALEAID---------GWSAEARARRLLAGL---GFAPADAERPmRDFSGGWRMRLGL 157
Cdd:PRK10070 99 ELREVRRK--KIAMVFQSFALMPHMTVLDntafgmelaGINAEERREKALDALrqvGLENYAHSYP-DELSGGMRQRVGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 648648866 158 ARTLMTRSDLLLLDEPTNHLDVETILWLEDWL----ARYPGTVIVIAHD 202
Cdd:PRK10070 176 ARALAINPDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-276 |
4.22e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVV----AHLPQEVPGSDRRAVDYVLDG--DAE 90
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSViaisAGLSGQLTGIENIEFKMLCMGfkRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 91 LRDLQRRLEQANDGAEqaRLYaaleaidgwsaeararrllaglgfapadaeRPMRDFSGGWRMRLGLARTLMTRSDLLLL 170
Cdd:PRK13546 120 IKAMTPKIIEFSELGE--FIY------------------------------QPVKKYSSGMRAKLGFSINITVNPDILVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 171 DEPtnhLDVETILWLEDWLARY------PGTVIVIAHDRRFLDSVCTHVAHIERGTIALYAgsythaeakraeaivqsea 244
Cdd:PRK13546 168 DEA---LSVGDQTFAQKCLDKIyefkeqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG------------------- 225
|
250 260 270
....*....|....*....|....*....|..
gi 648648866 245 aaaRVAAERAHLEDFVRRFRaKASKARQAQSR 276
Cdd:PRK13546 226 ---ELDDVLPKYEAFLNDFK-KKSKAEQKEFR 253
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
333-487 |
4.24e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.35 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 333 RPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP------------ALQvGYFAQHQREQLDLEASP--------- 391
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeildefrgsELQ-NYFTKLLEGDVKVIVKPqyvdlipka 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 392 -----LVHLQRQDPRA------EEQRLRNFLggmgfpgdkaDGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDL 460
Cdd:cd03236 103 vkgkvGELLKKKDERGkldelvDQLELRHVL----------DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190
....*....|....*....|....*....|
gi 648648866 461 DMREALAEA---LENYAGGLVVVAHDRELL 487
Cdd:cd03236 173 KQRLNAARLireLAEDDNYVLVVEHDLAVL 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-201 |
4.47e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 43.27 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 13 RQILlQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE---QPpewvVAHLPQEvpgSDRRAV-----DYV 84
Cdd:COG5265 371 RPIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILidgQD----IRDVTQA---SLRAAIgivpqDTV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 85 LDGDaelrDLQRRLEQANDGAEQARLYAALEAidgwsaeARARRLLAGL--GFAPADAERPMRdFSGGWRMRLGLARTLM 162
Cdd:COG5265 443 LFND----TIAYNIAYGRPDASEEEVEAAARA-------AQIHDFIESLpdGYDTRVGERGLK-LSGGEKQRVAIARTLL 510
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 648648866 163 TRSDLLLLDEPTNHLDVET---ILWLEDWLARypG-TVIVIAH 201
Cdd:COG5265 511 KNPPILIFDEATSALDSRTeraIQAALREVAR--GrTTLVIAH 551
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
315-506 |
4.68e-04 |
|
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: 43.36 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 315 AEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLpTAGERRVDP------ALQ------------VGY 376
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswnsvTLQtwrkafgvipqkVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 377 FAQHQREQLDleasPlvHLQRQDPR----AEEQRLRNFLggMGFPgDKADGPV--GQC--SGGERVRLVLALLIWQAPSL 448
Cdd:TIGR01271 1304 FSGTFRKNLD----P--YEQWSDEEiwkvAEEVGLKSVI--EQFP-DKLDFVLvdGGYvlSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 449 LLLDEPTNHLD----LDMREALAEALENYAggLVVVAHDRELLARvCDRFWTVEAGRLSPFD 506
Cdd:TIGR01271 1375 LLLDEPSAHLDpvtlQIIRKTLKQSFSNCT--VILSEHRVEALLE-CQQFLVIEGSSVKQYD 1433
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
320-483 |
5.02e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 42.38 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 320 GERVRLQPTTLRLrPEDRI-GILGPNGAGKSTLLTLLAGELLPTAGERRVDP-----------ALQVGYFAQHQREQLDL 387
Cdd:COG4604 12 GGKVVLDDVSLTI-PKGGItALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelAKRLAILRQENHINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 388 EASPLV----------HLQRQDPRAEEQRLRnFLGGMGFpgdkADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNh 457
Cdd:COG4604 91 TVRELVafgrfpyskgRLTAEDREIIDEAIA-YLDLEDL----ADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLN- 164
|
170 180 190
....*....|....*....|....*....|..
gi 648648866 458 lDLDMREALA--EALENYAGGL----VVVAHD 483
Cdd:COG4604 165 -NLDMKHSVQmmKLLRRLADELgktvVIVLHD 195
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
424-488 |
5.08e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 5.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648648866 424 PVGQCSGGERvRLVLALLIW----QAPSLLLLDEPTNHLDLDMREALAEALENYAGG---LVVVAHDRELLA 488
Cdd:pfam13304 233 PAFELSDGTK-RLLALLAALlsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgaqLILTTHSPLLLD 303
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
427-526 |
6.10e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 427 QCSGGERVRLVLAL-LIWQAPsLLLLDEPTNHLDL--DMR--EALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:PRK10418 140 EMSGGMLQRMMIALaLLCEAP-FIIADEPTTDLDVvaQARilDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGR 218
|
90 100
....*....|....*....|....*
gi 648648866 502 LSpfdgDLDDYARALQARQREAARS 526
Cdd:PRK10418 219 IV----EQGDVETLFNAPKHAVTRS 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-220 |
7.10e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.90 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQG-------ELALDAGEIEQPPEWVVAhlpqev 73
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfykptggTILLRGQHIEGLPGHQIA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 74 pgsdRRAVdyvldgdaeLRDLQrrleqandgaeQARLYAALEAIDG-WSAEAR--ARRLLAGLGFAPA--DAERPMRDFS 148
Cdd:PRK11300 79 ----RMGV---------VRTFQ-----------HVRLFREMTVIENlLVAQHQqlKTGLFSGLLKTPAfrRAESEALDRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 149 GGWRMRLGL---------------------ARTLMTRSDLLLLDEPT---NHLDVETILWLEDWLARYPG-TVIVIAHDR 203
Cdd:PRK11300 135 ATWLERVGLlehanrqagnlaygqqrrleiARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNEHNvTVLLIEHDM 214
|
250
....*....|....*..
gi 648648866 204 RFLDSVCTHVAHIERGT 220
Cdd:PRK11300 215 KLVMGISDRIYVVNQGT 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
319-502 |
7.17e-04 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 41.86 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 319 TGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP------------ALQVGYFA---QH--- 380
Cdd:cd03294 34 TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrELRRKKISmvfQSfal 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 381 --QREQLDLEASPLvHLQRQDPRAEEQRLRNFLGGMGFPGDKADGPvGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHL 458
Cdd:cd03294 114 lpHRTVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 648648866 459 D----LDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:cd03294 192 DplirREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
140-202 |
7.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648648866 140 AERPMRDFSGGWRMRLGLA-RTLMT-----RSDLLLLDEPTNHLDVETILWLEDWLARY----PgTVIVIAHD 202
Cdd:PRK03918 782 KERPLTFLSGGERIALGLAfRLALSlylagNIPLLILDEPTPFLDEERRRKLVDIMERYlrkiP-QVIIVSHD 853
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
306-493 |
7.36e-04 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 41.61 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 306 PDPLLALDHA----EVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVD------PALQVG 375
Cdd:COG1116 4 AAPALELRGVskrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtgPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 376 YFAQHQR-------EQ---LDLEAsplvhlqRQDPRAE-EQRLRNFLGGMGFpGDKADGPVGQCSGGERVRLVLA--LLI 442
Cdd:COG1116 84 VVFQEPAllpwltvLDnvaLGLEL-------RGVPKAErRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIAraLAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 648648866 443 wqAPSLLLLDEPTNHLD----LDMREALAEALENYAGGLVVVAHDRELLARVCDR 493
Cdd:COG1116 156 --DPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTHDVDEAVFLADR 208
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
310-487 |
7.43e-04 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 41.48 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 310 LALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLA--GELLPTAGERRVDP----ALQV------GYF 377
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGqdllELEPderaraGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 378 A--QHQREQLDLEASPLVH----LQRQDPRAEEQRLRNF-------LGGMGFPGDKADGPVGQ-CSGGERVR---LVLAL 440
Cdd:TIGR01978 81 LafQYPEEIPGVSNLEFLRsalnARRSARGEEPLDLLDFekllkekLALLDMDEEFLNRSVNEgFSGGEKKRneiLQMAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 648648866 441 LiwqAPSLLLLDEPTNHLDLDMREALAEALENYAG---GLVVVAHDRELL 487
Cdd:TIGR01978 161 L---EPKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLL 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-178 |
7.76e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.49 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRgrQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEI---------EQPPEWVVAHLPQ 71
Cdd:PRK10771 1 MLKLTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhttTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 72 E--------VpgsdRRAVDYVLDGDAELRDLQRrlEQANDGAEQARLYAALEaidgwsaeararRLLAGLgfapadaerp 143
Cdd:PRK10771 79 EnnlfshltV----AQNIGLGLNPGLKLNAAQR--EKLHAIARQMGIEDLLA------------RLPGQL---------- 130
|
170 180 190
....*....|....*....|....*....|....*
gi 648648866 144 mrdfSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD 178
Cdd:PRK10771 131 ----SGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
325-502 |
8.11e-04 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 41.54 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE-----------RRVDPAL------QVGY-FAQ-----HQ 381
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqfdfsQKPSEKAirllrqKVGMvFQQynlwpHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 382 REQLDLEASP--LVHLQRQDPRAEEQRLRNFLGgmgfPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD 459
Cdd:COG4161 98 TVMENLIEAPckVLGLSKEQAREKAMKLLARLR----LTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 460 LDMREALAEALENYAG-GL--VVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:COG4161 174 PEITAQVVEIIRELSQtGItqVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-179 |
8.14e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 41.74 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 1 MIRMQDIELRRGRQILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGEL---------------ALDAGEIEQPPEWV 65
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgarvtgdvTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 66 VAHLPQEVPGSDRRAVDYVLDgdaELRDLQRrleqandgAEQARLYAALEAIDG---WSAEARARrllaglgfAPADAER 142
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAR---EIVLLGR--------YPHARRAGALTHRDGeiaWQALALAG--------ATALVGR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648648866 143 PMRDFSGGWRMRLGLARTL---------MTRSDLLLLDEPTNHLDV 179
Cdd:PRK13547 142 DVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
325-466 |
8.16e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.70 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 325 LQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDP-ALQVG---YFAQHQREQLDLEASPLVHLQR--- 397
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhPLHFGdysYRSQRIRMIFQDPSTSLNPRQRisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 398 -----------QDPRAEEQRLRNFLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREAL 466
Cdd:PRK15112 109 ildfplrlntdLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
117-221 |
8.32e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 117 IDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDV----ETILWLEDWLARY 192
Cdd:PRK10261 434 LPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDF 513
|
90 100
....*....|....*....|....*....
gi 648648866 193 PGTVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:PRK10261 514 GIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
427-501 |
8.61e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 8.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 427 QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMR----EALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGR 501
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-224 |
1.01e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 41.33 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 29 RVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVpgsdRRAVDYVLdgdaelrdlQRRLEQA-NDGAEQ 107
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV----RKFVGLVF---------QNPDDQIfSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 108 ARLYAALE-AIDGWSAEARARRLLAGLGFAPAdAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD----VETI 182
Cdd:PRK13652 99 DIAFGPINlGLDEETVAHRVSSALHMLGLEEL-RDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 648648866 183 LWLEDWLARYPGTVIVIAHDRRFLDSVCTHVAHIERGTIALY 224
Cdd:PRK13652 178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
340-486 |
1.02e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.04 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVDPALQVGYFAQHQ-------REQLDLEASPLVHLQR----QDPRA--EEQR 406
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPymtlgtlRDQIIYPDSSEDMKRRglsdKDLEQilDNVQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 407 LRNFL---GGMGFPGDKADgpvgQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGLVVVAHD 483
Cdd:TIGR00954 563 LTHILereGGWSAVQDWMD----VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHR 638
|
...
gi 648648866 484 REL 486
Cdd:TIGR00954 639 KSL 641
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-217 |
1.07e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.99 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 24 VHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEqppewVVAHlpqEVPGSDR-RAVDYVLDGDAELRDLQRrLEQAN 102
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQ-----IDGK---TATRGDRsRFMAYLGHLPGLKADLST-LENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 103 dgaeqarlyaALEAIDGWSAEARARRLLAGLGFApADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETI 182
Cdd:PRK13543 105 ----------FLCGLHGRRAKQMPGSALAIVGLA-GYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 648648866 183 LWLEDWLA---RYPGTVIVIAHDRRFLDSVCTHVAHIE 217
Cdd:PRK13543 174 TLVNRMISahlRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
419-459 |
1.17e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.05 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 648648866 419 DKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD 459
Cdd:PRK14247 138 DRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
141-178 |
1.52e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.17 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|....*...
gi 648648866 141 ERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD 178
Cdd:PRK11000 128 DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
122-228 |
1.59e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.99 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 122 AEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLD-------VETILwledwLARYPG 194
Cdd:PRK13631 152 AKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgehemMQLIL-----DAKANN 226
|
90 100 110
....*....|....*....|....*....|....*
gi 648648866 195 -TVIVIAHDRRFLDSVCTHVAHIERGTIALYAGSY 228
Cdd:PRK13631 227 kTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPY 261
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-209 |
1.60e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 40.87 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSS-------LLAALQGELALDAGEIEQPPEWVVAHLPQEV-PGSDRRAVDYVLDGD 88
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTtvrlidgLLEAESGQIIIDGDLLTEENVWDIRHKIGMVfQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 89 A---------ELRDLQRRLEQAndgaeqarlyaaleaidgwsaeararrlLAGLGFAPADAERPMRdFSGGWRMRLGLAR 159
Cdd:PRK13650 103 VafglenkgiPHEEMKERVNEA----------------------------LELVGMQDFKEREPAR-LSGGQKQRVAIAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648648866 160 TLMTRSDLLLLDEPTNHLD----VETILWLEDWLARYPGTVIVIAHDrrfLDSV 209
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEV 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-178 |
1.60e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 40.77 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 17 LQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELaldageieQPPEWVVaHLPQEVPGSDRRAVDyvldgdaeLRDLQR 96
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL--------QPTSGTV-TIGERVITAGKKNKK--------LKPLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 97 RLEQANDGAEqARLYAALEAID--------GWS---AEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRS 165
Cdd:PRK13634 86 KVGIVFQFPE-HQLFEETVEKDicfgpmnfGVSeedAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170
....*....|...
gi 648648866 166 DLLLLDEPTNHLD 178
Cdd:PRK13634 165 EVLVLDEPTAGLD 177
|
|
| RecA-like_BCS1 |
cd19510 |
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ... |
28-125 |
1.65e-03 |
|
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410918 [Multi-domain] Cd Length: 153 Bit Score: 39.64 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 28 WRVG--LTGANGSGKSSLLAALQGELALDAGEIEqppewvvahLPQEVPGSDR----------RAVDYVLDGDAELRDLQ 95
Cdd:cd19510 22 YRRGylLYGPPGTGKSSFIAALAGELDYDICDLN---------LSEVVLTDDRlnhllntapkQSIILLEDIDAAFESRE 92
|
90 100 110
....*....|....*....|....*....|...
gi 648648866 96 RRLEQANDGAEQARLYAA--LEAIDG-WSAEAR 125
Cdd:cd19510 93 HNKKNPSAYGGLSRVTFSglLNALDGvASSEER 125
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
429-482 |
1.75e-03 |
|
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: 40.29 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 648648866 429 SGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--LVVVAH 482
Cdd:cd03254 141 SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
338-454 |
2.11e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 40.01 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 338 IGILGPNGAGKSTLLTLLAGELLPTAGERRVD-------P-----ALQVGYFAQHQ--------REQLD--LEASPLVHL 395
Cdd:COG1137 32 VGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgedithlPmhkraRLGIGYLPQEAsifrkltvEDNILavLELRKLSKK 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 396 QRQDpRAEE-------QRLRNFLGgmgfpgdkadgpvGQCSGGERVRLVLA--LLIwqAPSLLLLDEP 454
Cdd:COG1137 112 EREE-RLEElleefgiTHLRKSKA-------------YSLSGGERRRVEIAraLAT--NPKFILLDEP 163
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
340-468 |
2.15e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 40.86 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVDpALQVGYFAQHQREQLDLEAS----PlvHLQRQD-----------PRAE- 403
Cdd:PRK11432 37 LLGPSGCGKTTVLRLVAGLEKPTEGQIFID-GEDVTHRSIQQRDICMVFQSyalfP--HMSLGEnvgyglkmlgvPKEEr 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 404 EQRLRNFL-----GGMGfpgdkaDGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAE 468
Cdd:PRK11432 114 KQRVKEALelvdlAGFE------DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRE 177
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
340-481 |
2.18e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 39.86 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 340 ILGPNGAGKSTLLTLLAGELLPTAGERRVD--------PALQVGYFAqHQ---------REQLDLEAsplvHLQRQDPRA 402
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDggdiddpdVAEACHYLG-HRnamkpaltvAENLEFWA----AFLGGEELD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 403 EEQRLRNF-LGGMgfpgdkADGPVGQCSGGERVRLVLA-LLIWQAPsLLLLDEPTNHLDLDMREALAEALENY--AGGLV 478
Cdd:PRK13539 108 IAAALEAVgLAPL------AHLPFGYLSAGQKRRVALArLLVSNRP-IWILDEPTAALDAAAVALFAELIRAHlaQGGIV 180
|
...
gi 648648866 479 VVA 481
Cdd:PRK13539 181 IAA 183
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
146-209 |
2.19e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARY----PGTVIVIAHDRRFLDSV 209
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYL 138
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-178 |
2.29e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.50 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIEQPPEWVVAHLPQEVPGSDRRAVDYV-------LDGDAELRD 93
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVfqfpesqLFEETVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 94 LQrrLEQANDGAEQARlyaaleaidgwsAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDLLLLDEP 173
Cdd:PRK13649 107 VA--FGPQNFGVSQEE------------AEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
....*
gi 648648866 174 TNHLD 178
Cdd:PRK13649 173 TAGLD 177
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
146-221 |
2.31e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.21 E-value: 2.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 146 DFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWLARYPG--TVIVIAHDRRFLDSVCTHVAHIERGTI 221
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
427-483 |
2.58e-03 |
|
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: 39.55 E-value: 2.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 427 QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLD----LDMREALAEALENYAGGLVVVAHD 483
Cdd:cd03301 130 QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-201 |
2.59e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 2.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 145 RDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDV-------ETILWLEDWLARypgTVIVIAH 201
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseklieKTIVDIKDKADK---TIITIAH 1417
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-208 |
2.63e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 30 VGLTGANGSGKSSLLAALQGELALDAGEIeqppewvvahlpqevpgsdrravdYVLDGDAELRDLQRRLEQANDGAEQAR 109
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV------------------------IYIDGEDILEEVLDQLLLIIVGGKKAS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 110 LYAALeaidgwsaeararrllaglgfapadaerpmrdfsggwRMRLGLARTLMTRSDLLLLDEPTNHLDVET-------- 181
Cdd:smart00382 61 GSGEL-------------------------------------RLRLALALARKLKPDVLILDEITSLLDAEQeallllle 103
|
170 180
....*....|....*....|....*...
gi 648648866 182 -ILWLEDWLARYPGTVIVIAHDRRFLDS 208
Cdd:smart00382 104 eLRLLLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
330-502 |
2.69e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 40.10 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 330 LRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGERRVDPAL---------------QVGYFAQHQREQL-------DL 387
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPESQLfeetvlkDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 388 EASPL---VHLQRQDPRAEEQrlrnfLGGMGFPGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMR- 463
Cdd:PRK13643 107 AFGPQnfgIPKEKAEKIAAEK-----LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARi 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648648866 464 --EALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:PRK13643 182 emMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
391-501 |
2.74e-03 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 39.98 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 391 PLVHLQRQdPRAE-EQRLRNFLG--GMGfpgDKADGPVGQCSGGE--RVRLVLALliwqA--PSLLLLDEPTNHLD---- 459
Cdd:COG1126 101 APIKVKKM-SKAEaEERAMELLErvGLA---DKADAYPAQLSGGQqqRVAIARAL----AmePKVMLFDEPTSALDpelv 172
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 648648866 460 ---LD-MREaLAEalenyaGGL--VVVAHDRELLARVCDRFWTVEAGR 501
Cdd:COG1126 173 gevLDvMRD-LAK------EGMtmVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
418-490 |
2.84e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 418 GDKADGPVGQCSGGERV------RLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--------LVVVAHD 483
Cdd:TIGR00606 1190 GDTALDMRGRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSrsqqrnfqLLVITHD 1269
|
....*..
gi 648648866 484 RELLARV 490
Cdd:TIGR00606 1270 EDFVELL 1276
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
148-201 |
2.98e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 39.76 E-value: 2.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDV-------ETILWLEDwlaRYpgTVIVIAH 201
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPisagkieETLLGLKD---DY--TMLLVTR 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
338-488 |
3.53e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.51 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 338 IGILGPNGAGKSTLltllagellptagerrvdpALQVGYFAQhqreqldleaSPLVHLQRQDPRAEEQRLRNFLGGMGFP 417
Cdd:smart00382 5 ILIVGPPGSGKTTL-------------------ARALARELG----------PPGGGVIYIDGEDILEEVLDQLLLIIVG 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648648866 418 GDKADGpvgqcSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGGLVVVAHDRELLA 488
Cdd:smart00382 56 GKKASG-----SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL 121
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-59 |
4.28e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.78 E-value: 4.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 648648866 14 QILLQHASLTVHAGWRVGLTGANGSGKSSLLAALQGELALDAGEIE 59
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL 59
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-179 |
4.46e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.91 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 20 ASLTVHAGWRVGLTGANGSGKSSLLAAL--------QGELALDAGEIE-QPPEWVVAHLPQEVPgSDRRAVDYVLDGDA- 89
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLfgaypgrwEGEIFIDGKPVKiRNPQQAIAQGIAMVP-EDRKRDGIVPVMGVg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 90 ---ELRDLQRrleqandgaeqarlYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSD 166
Cdd:PRK13549 360 kniTLAALDR--------------FTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPK 425
|
170
....*....|...
gi 648648866 167 LLLLDEPTNHLDV 179
Cdd:PRK13549 426 ILILDEPTRGIDV 438
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
148-202 |
4.78e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.38 E-value: 4.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 648648866 148 SGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETILWLEDWL----ARYpgTVIVIAHD 202
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMhelkEQY--TIIIVTHN 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
308-500 |
4.95e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.77 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 308 PLLALDHAEVCTGERVRLQPTTLRLRPEDRIGILGPNGAGKSTLLTLLAGELLPTAGE--------RRVDPAL--QVGYF 377
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTitinninyNKLDHKLaaQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 378 AQHQREQLDLEAS------------------PLVHLQRQDPRAEEQRLRnflggMGFPGDkADGPVGQCSGGERVRLVLA 439
Cdd:PRK09700 84 IIYQELSVIDELTvlenlyigrhltkkvcgvNIIDWREMRVRAAMMLLR-----VGLKVD-LDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648648866 440 LLIWQAPSLLLLDEPTNHL---DLDMREALAEALENYAGGLVVVAHDRELLARVCDRFWTVEAG 500
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
335-502 |
5.28e-03 |
|
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: 40.00 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 335 EDRI-GILGPNGAGKSTLLTLLAGELLPTAG---------ERRVDPALQ-VGYFAQHQ--REQLDLEASPLVHLQRQDPR 401
Cdd:TIGR01257 955 ENQItAFLGHNGAGKTTTLSILTGLLPPTSGtvlvggkdiETNLDAVRQsLGMCPQHNilFHHLTVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 402 AEEQRL--RNFLGGMGFpGDKADGPVGQCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--L 477
Cdd:TIGR01257 1035 WEEAQLemEAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGrtI 1113
|
170 180
....*....|....*....|....*
gi 648648866 478 VVVAHDRELLARVCDRFWTVEAGRL 502
Cdd:TIGR01257 1114 IMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
427-502 |
5.62e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 39.94 E-value: 5.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648648866 427 QCSGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAGG--LVVVAHdRELLARVCDRFWTVEAGRL 502
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGrtTFIIAH-RLSTVRNADRILVFDNGRV 547
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
372-483 |
5.96e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 372 LQVGYFAQHQREQLDLEASPLVHLQRQDP--RAEEQRLRNFLGgmgfpgdkaDGPVGQCSGGERVRLVLALLIwqapsLL 449
Cdd:COG0419 110 LGLEIYEELKERLKELEEALESALEELAElqKLKQEILAQLSG---------LDPIETLSGGERLRLALADLL-----SL 175
|
90 100 110
....*....|....*....|....*....|....
gi 648648866 450 LLDepTNHLDLDMREALAEALENyaggLVVVAHD 483
Cdd:COG0419 176 ILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-200 |
6.18e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 39.42 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 21 SLTVHAGWRVGLTGANGSGKSSLLAAL--------QGELALDAGEIE-QPPEWVVAHLPQEVPgSDRRAVDYVLD----G 87
Cdd:TIGR02633 280 SFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfEGNVFINGKPVDiRNPAQAIRAGIAMVP-EDRKRHGIVPIlgvgK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 88 DAELRDLQRrleqandgaeqarlYAALEAIDGWSAEARARRLLAGLGFAPADAERPMRDFSGGWRMRLGLARTLMTRSDL 167
Cdd:TIGR02633 359 NITLSVLKS--------------FCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190
....*....|....*....|....*....|....*.
gi 648648866 168 LLLDEPTNHLDVET---ILWLEDWLARYPGTVIVIA 200
Cdd:TIGR02633 425 LILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVS 460
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
145-183 |
6.38e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 38.40 E-value: 6.38e-03
10 20 30
....*....|....*....|....*....|....*....
gi 648648866 145 RDFSGGWRMRLGLARTLMTRSDLLLLDEPTNHLDVETIL 183
Cdd:cd03233 117 RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
425-501 |
8.00e-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: 38.93 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 425 VGQCSGGERVRLVL--ALLIwqAPSLLLLDEPTNHLDLDMREALAEALENYAGGL----VVVAHDRELLARVCDRFWTVE 498
Cdd:COG4148 131 PATLSGGERQRVAIgrALLS--SPRLLLMDEPLAALDLARKAEILPYLERLRDELdipiLYVSHSLDEVARLADHVVLLE 208
|
...
gi 648648866 499 AGR 501
Cdd:COG4148 209 QGR 211
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
429-497 |
9.43e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 39.09 E-value: 9.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648648866 429 SGGERVRLVLALLIWQAPSLLLLDEPTNHLDLDMREALAEALENYAG-GLVVVAHDRELLARVCDRFWTV 497
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSSRVYQMFDSV 277
|
|
| |
