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Conserved domains on  [gi|74750917|sp|Q8N268|]
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RecName: Full=Putative uncharacterized protein encoded by LINC02910

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III super family cl00261
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 68-111 3.14e-03

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.


The actual alignment was detected with superfamily member PRK03646:

Pssm-ID: 469695 [Multi-domain]  Cd Length: 355  Bit Score: 35.86  E-value: 3.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74750917   68 RSKGLK-----IEGLLQSRELG-----NSWTVTMCIWVLKALQSSAPNKPLD-WL 111
Cdd:PRK03646  67 RERGWKgpilmLEGFFHAQDLElydqhRLTTCVHSNWQLKALQNARLKAPLDiYL 121
 
Name Accession Description Interval E-value
dadX PRK03646
catabolic alanine racemase;
68-111 3.14e-03

catabolic alanine racemase;


Pssm-ID: 179622 [Multi-domain]  Cd Length: 355  Bit Score: 35.86  E-value: 3.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74750917   68 RSKGLK-----IEGLLQSRELG-----NSWTVTMCIWVLKALQSSAPNKPLD-WL 111
Cdd:PRK03646  67 RERGWKgpilmLEGFFHAQDLElydqhRLTTCVHSNWQLKALQNARLKAPLDiYL 121
 
Name Accession Description Interval E-value
dadX PRK03646
catabolic alanine racemase;
68-111 3.14e-03

catabolic alanine racemase;


Pssm-ID: 179622 [Multi-domain]  Cd Length: 355  Bit Score: 35.86  E-value: 3.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74750917   68 RSKGLK-----IEGLLQSRELG-----NSWTVTMCIWVLKALQSSAPNKPLD-WL 111
Cdd:PRK03646  67 RERGWKgpilmLEGFFHAQDLElydqhRLTTCVHSNWQLKALQNARLKAPLDiYL 121
 
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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