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Conserved domains on  [gi|504056004|ref|WP_014289998|]
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MULTISPECIES: Lrp/AsnC family transcriptional regulator [Pyrobaculum]

Protein Classification

Lrp/AsnC family transcriptional regulator( domain architecture ID 11445815)

Lrp/AsnC (leucine-responsive regulatory protein/asparagine synthase C) family transcriptional regulator regulates many cellular processes such as amino acid metabolism, pili synthesis, and DNA repair and recombination

CATH:  3.30.70.920|1.10.10.10
Gene Ontology:  GO:0043565
PubMed:  16438681|21608015|27206730

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
2-74 3.16e-15

DNA-binding transcriptional regulator, Lrp family [Transcription];


:

Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 65.18  E-value: 3.16e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504056004   2 VEAFVFINTEIGAEDEVMDALVKMPEVKEAMIVYGPYDLVVKISTDTAESLRKLISEKIRKLPKIKSTTTLII 74
Cdd:COG1522   65 VTAFVEVKVPPHRLDEFAEALAAIPEVLECYLVTGDYDLLLKVVARDMEELERFLLERLAALPGVRRTETSFV 137
 
Name Accession Description Interval E-value
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
2-74 3.16e-15

DNA-binding transcriptional regulator, Lrp family [Transcription];


Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 65.18  E-value: 3.16e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504056004   2 VEAFVFINTEIGAEDEVMDALVKMPEVKEAMIVYGPYDLVVKISTDTAESLRKLISEKIRKLPKIKSTTTLII 74
Cdd:COG1522   65 VTAFVEVKVPPHRLDEFAEALAAIPEVLECYLVTGDYDLLLKVVARDMEELERFLLERLAALPGVRRTETSFV 137
AsnC_trans_reg pfam01037
Lrp/AsnC ligand binding domain; The l-leucine-responsive regulatory protein (Lrp/AsnC) family ...
 6-77 4.71e-13

Lrp/AsnC ligand binding domain; The l-leucine-responsive regulatory protein (Lrp/AsnC) family is a family of similar bacterial transcription regulatory proteins. The family is named after two E. coli proteins involved in regulating amino acid metabolism. This entry corresponds to the usually C-terminal regulatory ligand binding domain. Structurally this domain has a dimeric alpha/beta barrel fold. This domain binds almost exclusively amino acids but also 4-hydroxyphenylpyruvate and kynurenine (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426007  Cd Length: 73  Bit Score: 57.92  E-value: 4.71e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504056004   6 VFINTEIG-AEDEVMDALVKMPEVKEAMIVYGPYDLVVKISTDTAESLRKLISEKIRKLPKIKSTTTLIIAKS 77
Cdd:pfam01037  1 VEVKLEPGhALEEFAEALAAIPEVVECYRVTGDYDYLLKVVARDLEALERFLREKLRSLPGVARTETSIVLST 73
PRK11179 PRK11179
DNA-binding transcriptional regulator AsnC; Provisional
 18-73 4.36e-04

DNA-binding transcriptional regulator AsnC; Provisional


Pssm-ID: 183019 [Multi-domain]  Cd Length: 153  Bit Score: 36.23  E-value: 4.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504056004  18 VMDALVKMPEVKEAMIVYGPYDLVVKISTDTAESLRKLISEKIRKLPKIKSTTTLI 73
Cdd:PRK11179  86 ALAKLESLDEVVEAYYTTGHYSIFIKVMCRSIDALQHVLINKIQTIDEIQSTETLI 141
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 17-62 7.98e-03

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 33.08  E-value: 7.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504056004  17 EVMDALVKMPEVKEAMIVYGPYDL---VVK---ISTDTAESLRKLISEKIRK 62
Cdd:cd05972  342 EVESALLEHPAVAEAAVVGSPDPVrgeVVKafvVLTSGYEPSEELAEELQGH 393
 
Name Accession Description Interval E-value
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
2-74 3.16e-15

DNA-binding transcriptional regulator, Lrp family [Transcription];


Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 65.18  E-value: 3.16e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504056004   2 VEAFVFINTEIGAEDEVMDALVKMPEVKEAMIVYGPYDLVVKISTDTAESLRKLISEKIRKLPKIKSTTTLII 74
Cdd:COG1522   65 VTAFVEVKVPPHRLDEFAEALAAIPEVLECYLVTGDYDLLLKVVARDMEELERFLLERLAALPGVRRTETSFV 137
AsnC_trans_reg pfam01037
Lrp/AsnC ligand binding domain; The l-leucine-responsive regulatory protein (Lrp/AsnC) family ...
 6-77 4.71e-13

Lrp/AsnC ligand binding domain; The l-leucine-responsive regulatory protein (Lrp/AsnC) family is a family of similar bacterial transcription regulatory proteins. The family is named after two E. coli proteins involved in regulating amino acid metabolism. This entry corresponds to the usually C-terminal regulatory ligand binding domain. Structurally this domain has a dimeric alpha/beta barrel fold. This domain binds almost exclusively amino acids but also 4-hydroxyphenylpyruvate and kynurenine (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426007  Cd Length: 73  Bit Score: 57.92  E-value: 4.71e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504056004   6 VFINTEIG-AEDEVMDALVKMPEVKEAMIVYGPYDLVVKISTDTAESLRKLISEKIRKLPKIKSTTTLIIAKS 77
Cdd:pfam01037  1 VEVKLEPGhALEEFAEALAAIPEVVECYRVTGDYDYLLKVVARDLEALERFLREKLRSLPGVARTETSIVLST 73
PRK11179 PRK11179
DNA-binding transcriptional regulator AsnC; Provisional
 18-73 4.36e-04

DNA-binding transcriptional regulator AsnC; Provisional


Pssm-ID: 183019 [Multi-domain]  Cd Length: 153  Bit Score: 36.23  E-value: 4.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504056004  18 VMDALVKMPEVKEAMIVYGPYDLVVKISTDTAESLRKLISEKIRKLPKIKSTTTLI 73
Cdd:PRK11179  86 ALAKLESLDEVVEAYYTTGHYSIFIKVMCRSIDALQHVLINKIQTIDEIQSTETLI 141
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 17-62 7.98e-03

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 33.08  E-value: 7.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504056004  17 EVMDALVKMPEVKEAMIVYGPYDL---VVK---ISTDTAESLRKLISEKIRK 62
Cdd:cd05972  342 EVESALLEHPAVAEAAVVGSPDPVrgeVVKafvVLTSGYEPSEELAEELQGH 393
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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