A0A3V2G391 · A0A3V2G391_SALET

Function

function

mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Divalent metal cations. Mg2+ or Mn2+.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site69substrate
Binding site98Zn2+ (UniProtKB | ChEBI)
Binding site101Zn2+ (UniProtKB | ChEBI)
Binding site111substrate
Binding site116Zn2+ (UniProtKB | ChEBI)
Binding site119Zn2+ (UniProtKB | ChEBI)
Binding site124substrate
Binding site158a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site174a divalent metal cation 2 (UniProtKB | ChEBI)
Binding site174a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site178a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site178a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site192-199substrate
Binding site219a divalent metal cation 3 (UniProtKB | ChEBI)
Binding site219a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site241substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular FunctionNAD+ diphosphatase activity
Molecular FunctionNADH pyrophosphatase activity
Molecular Functionzinc ion binding
Biological ProcessNAD catabolic process
Biological ProcessNADH metabolic process
Biological ProcessNADP catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NAD-capped RNA hydrolase NudC
  • EC number
  • Short names
    DeNADding enzyme NudC
  • Alternative names
    • NADH pyrophosphatase
      (EC:3.6.1.22
      ) . EC:3.6.1.22 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      nudC
    • ORF names
      A4W49_22175
      , A4W57_21730
      , AIK92_23205
      , ASH82_22730
      , CB395_21560
      , D6J51_24240
      , D6K67_22940
      , DKU10_22665
      , DOJ23_20250
      , DP829_23345
      , DPJ44_23210
      , DPS10_23005
      , DQQ63_23625
      , DY868_23400
      , EUX26_22960
      , F9G64_22435
      , G0D76_24175
      , G3408_004539
      , G4B28_004472
      , G4B35_004476
      , G4I58_004438
      , G4I61_003023
      , G4L02_004628
      , G4Y23_004572
      , G9C15_004317
      , GCZ77_22575

Organism names

Accessions

  • Primary accession
    A0A3V2G391
  • Secondary accessions
    • A0A6C8XNX2

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain125-248Nudix hydrolase
Motif159-180Nudix box

Sequence similarities

Belongs to the Nudix hydrolase family. NudC subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    257
  • Mass (Da)
    29,607
  • Last updated
    2019-05-08 v1
  • MD5 Checksum
    DEA4CB3D9ED03BC3FC1A9D566691D543
MDRIIEKLESGWWIVSHEQKLWLPYGELPHGLAANFDLVGQRALRIGEWQGEPVWLVLQHRRHDMGSVRQVIDQDAGLFQLAGRGVQLAEFYRSHKFCGYCGHPMHPSKTEWAMLCSHCRERYYPQIAPCIIVAIRREDSILLAQHVRHRNGVHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPQSLMTAFMAEYDSGEIVIDPKELLEANWYRYDDLPILPPPGTVARRLIEDTVAMCRAEYD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAHCWL010000033
EMBL· GenBank· DDBJ
EBU6917470.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHFAS010000055
EMBL· GenBank· DDBJ
EBV3763838.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHGTQ010000048
EMBL· GenBank· DDBJ
EBV9203391.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHIGD010000028
EMBL· GenBank· DDBJ
EBW4106976.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHIXO010000026
EMBL· GenBank· DDBJ
EBW6734716.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHKXZ010000032
EMBL· GenBank· DDBJ
EBX3357689.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHOXC010000035
EMBL· GenBank· DDBJ
EBY7387599.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHPAD010000026
EMBL· GenBank· DDBJ
EBY7629244.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHWIJ010000027
EMBL· GenBank· DDBJ
ECB0525998.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKLND010000051
EMBL· GenBank· DDBJ
ECT0412963.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKPQX010000023
EMBL· GenBank· DDBJ
ECU3485579.1
EMBL· GenBank· DDBJ
Genomic DNA
AALIQJ010000054
EMBL· GenBank· DDBJ
EDA0177589.1
EMBL· GenBank· DDBJ
Genomic DNA
AALLSV010000028
EMBL· GenBank· DDBJ
EDA9404214.1
EMBL· GenBank· DDBJ
Genomic DNA
AALLTD010000029
EMBL· GenBank· DDBJ
EDA9439406.1
EMBL· GenBank· DDBJ
Genomic DNA
AAMGJL010000017
EMBL· GenBank· DDBJ
EDH0980933.1
EMBL· GenBank· DDBJ
Genomic DNA
AAMIHV010000035
EMBL· GenBank· DDBJ
EDH6431380.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAMJL010000017
EMBL· GenBank· DDBJ
HAC6918218.1
EMBL· GenBank· DDBJ
Genomic DNA
DAARLP010000016
EMBL· GenBank· DDBJ
HAE2915332.1
EMBL· GenBank· DDBJ
Genomic DNA
DAARUC010000054
EMBL· GenBank· DDBJ
HAE3942402.1
EMBL· GenBank· DDBJ
Genomic DNA
DAARUZ010000052
EMBL· GenBank· DDBJ
HAE4051278.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASLG010000020
EMBL· GenBank· DDBJ
HAE6002753.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASLQ010000045
EMBL· GenBank· DDBJ
HAE6032858.1
EMBL· GenBank· DDBJ
Genomic DNA
DAASRW010000019
EMBL· GenBank· DDBJ
HAE6748816.1
EMBL· GenBank· DDBJ
Genomic DNA
DAATPN010000020
EMBL· GenBank· DDBJ
HAE9563751.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAUAM010000072
EMBL· GenBank· DDBJ
HAF0865039.1
EMBL· GenBank· DDBJ
Genomic DNA
RSGD01000032
EMBL· GenBank· DDBJ
MID47794.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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