A0A5N9E0H8 · A0A5N9E0H8_9CHLR

Function

function

Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.

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

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site329S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site358S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site379S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site422S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site449
Active site449Nucleophile
Site531Important for substrate specificity
Active site588Proton acceptor
Site589Important for substrate specificity
Site673Important for substrate specificity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctiondTTP diphosphatase activity
Molecular FunctionrRNA (uridine-C5-)-methyltransferase activity
Molecular FunctionUTP diphosphatase activity
Biological Processnucleotide metabolic process
Biological ProcessrRNA base methylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    dTTP/UTP pyrophosphatase
  • EC number
  • Short names
    dTTPase/UTPase
  • Alternative names
    • Nucleoside triphosphate pyrophosphatase
    • Nucleotide pyrophosphatase
      (Nucleotide PPase
      )

Gene names

    • Name
      rlmD
    • ORF names
      FI722_09030

Organism names

Accessions

  • Primary accession
    A0A5N9E0H8

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain101-159TRAM
Region494-525Disordered
Compositional bias497-511Polar residues

Sequence similarities

Belongs to the Maf family. YhdE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    738
  • Mass (Da)
    80,367
  • Last updated
    2020-04-22 v1
  • Checksum
    09F5B23BC2B6F5E4
MLVAWLGFIRTKSKLDPKNQEPRPPTHQFNVRTHQGQPVEVLINPGTRPTRMGIPMPGQTPSFSGFSARLGLSLRPNATLLGFSPTLNYSIYEFMEIAKRITQQGDRVTLSLTSWGRLGEAMAEFDGHNVFVAGGIPGEKVVAEVVKVHRKYVSAKVVAVLEASPDRVEPPCPYYDECTGCQWQHLSYDAQLKTKREKVTDALQRVGDFSNPPVSEVKPSPNEYGYRNHARFTINREGALGYVNRETRQFVRIDKCLLMHDGVNKLLEELQDNCGETTQLSIRASKYSGDFLVQPYMVHPDIRVTTGQKKYTESVDGHEFLVSSPSFFQVNVDQAAAAAGIVRDRLHLTQDDVLLDAYTGVGTFAILLASSVKQVIAVEESSAAVADAKQNAGGLPNLEFVLGRTEDVLRRLPVTPAVVVLDPPRSGCQPRALESLIEMAPSRVAYVSCDAETLGRDLKILCAGGYRLDEVAPLDMFPQTHHVECVALLSRGEQPNEPMAGTITSRAPEPTLETEPESADPPITLASASPRRRELMDILGLEFAVMPADLAEEPIPGETPVDMVRRLSAEKALAVAATVQSGLVIGADSTVAFEGQAVGKPVDDDDARRMLHQLSGTTHHVSTGITVVDAASGRAISDAMTSEITLRHLSDQEIDASIASGVPRDKAGAYAVQDTELRPAADWQGCYNNIVGLPICRLLEMLQELGYQMPDGWTVPDEIACGEDCPTIINAGQEEKAP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias497-511Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VFHF01000218
EMBL· GenBank· DDBJ
MQG42024.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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