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Conserved domains on  [gi|578811445|ref|XP_006715068|]
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decapping and exoribonuclease protein isoform X1 [Homo sapiens]

Protein Classification

DXO/RAI1 family decapping nuclease( domain architecture ID 10554558)

DXO/RAI1 family decapping nuclease similar to human decapping and exoribonuclease protein (also called 5'-3' exoribonuclease DXO) and Saccharomyces cerevisiae decapping nuclease RAI1, which are decapping enzymes for NAD-capped RNAs, specifically hydrolyzing the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RAI1 pfam08652
RAI1 like PD-(D/E)XK nuclease; RAI1 is homologous to Caenorhabditis elegans DOM-3 and human ...
 235-302 1.21e-27

RAI1 like PD-(D/E)XK nuclease; RAI1 is homologous to Caenorhabditis elegans DOM-3 and human DOM3Z and binds to a nuclear exoribonuclease. It is required for 5.8S rRNA processing. Profile-profile comparison tools demonstrate this to be a PD-(D/E)XK nuclease, with a full set of canonical active site signature motifs characteriztic to the PD-(D/E)XK nuclease superfamily.


:

Pssm-ID: 462550  Cd Length: 69  Bit Score: 103.75  E-value: 1.21e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811445  235 VDC--TDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRhKLLKWWAQSFLPGVPNVVAGFRNPDGFVSS 302
Cdd:pfam08652   1 VDCifSDFKPDDKDNLSHYVELKTSRVINNPRQQRKFEK-KLLKWWAQSFLVGVPRIIVGFRDDDGILRS 69
 
Name Accession Description Interval E-value
RAI1 pfam08652
RAI1 like PD-(D/E)XK nuclease; RAI1 is homologous to Caenorhabditis elegans DOM-3 and human ...
 235-302 1.21e-27

RAI1 like PD-(D/E)XK nuclease; RAI1 is homologous to Caenorhabditis elegans DOM-3 and human DOM3Z and binds to a nuclear exoribonuclease. It is required for 5.8S rRNA processing. Profile-profile comparison tools demonstrate this to be a PD-(D/E)XK nuclease, with a full set of canonical active site signature motifs characteriztic to the PD-(D/E)XK nuclease superfamily.


Pssm-ID: 462550  Cd Length: 69  Bit Score: 103.75  E-value: 1.21e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811445  235 VDC--TDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRhKLLKWWAQSFLPGVPNVVAGFRNPDGFVSS 302
Cdd:pfam08652   1 VDCifSDFKPDDKDNLSHYVELKTSRVINNPRQQRKFEK-KLLKWWAQSFLVGVPRIIVGFRDDDGILRS 69
 
Name Accession Description Interval E-value
RAI1 pfam08652
RAI1 like PD-(D/E)XK nuclease; RAI1 is homologous to Caenorhabditis elegans DOM-3 and human ...
 235-302 1.21e-27

RAI1 like PD-(D/E)XK nuclease; RAI1 is homologous to Caenorhabditis elegans DOM-3 and human DOM3Z and binds to a nuclear exoribonuclease. It is required for 5.8S rRNA processing. Profile-profile comparison tools demonstrate this to be a PD-(D/E)XK nuclease, with a full set of canonical active site signature motifs characteriztic to the PD-(D/E)XK nuclease superfamily.


Pssm-ID: 462550  Cd Length: 69  Bit Score: 103.75  E-value: 1.21e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578811445  235 VDC--TDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRhKLLKWWAQSFLPGVPNVVAGFRNPDGFVSS 302
Cdd:pfam08652   1 VDCifSDFKPDDKDNLSHYVELKTSRVINNPRQQRKFEK-KLLKWWAQSFLVGVPRIIVGFRDDDGILRS 69
 
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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