A0A261Y136 · A0A261Y136_9FUNG

  • Protein
    Inosine triphosphate pyrophosphatase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.

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

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 divalent metal cation per subunit; can use either Mg2+ or Mn2+.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site758-763ITP (UniProtKB | ChEBI)
Binding site786Mg2+ (UniProtKB | ChEBI)
Binding site798ITP (UniProtKB | ChEBI)
Binding site880-883ITP (UniProtKB | ChEBI)
Binding site903ITP (UniProtKB | ChEBI)
Binding site908-909ITP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentextracellular region
Cellular Componentmembrane
Cellular Componentnucleus
Molecular Functioncellulase activity
Molecular Functioncellulose binding
Molecular FunctiondITP diphosphatase activity
Molecular FunctionITP diphosphatase activity
Molecular Functionmetal ion binding
Molecular Functionmonoatomic cation transmembrane transporter activity
Molecular Functionnucleotide binding
Molecular FunctionXTP diphosphatase activity
Biological Processcellulose catabolic process
Biological Processdeoxyribonucleoside triphosphate catabolic process
Biological Processinorganic ion homeostasis
Biological Processintracellular monoatomic cation homeostasis
Biological Processnucleotide metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inosine triphosphate pyrophosphatase
  • EC number
  • Short names
    ITPase
    ; Inosine triphosphatase
  • Alternative names
    • Non-canonical purine NTP pyrophosphatase
    • Non-standard purine NTP pyrophosphatase
    • Nucleoside-triphosphate diphosphatase
    • Nucleoside-triphosphate pyrophosphatase
      (NTPase
      )

Gene names

    • ORF names
      BZG36_02578

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • AZ0501
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Endogonomycetes > Endogonales > Endogonales incertae sedis > Bifiguratus

Accessions

  • Primary accession
    A0A261Y136

Proteomes

Subcellular Location

Cytoplasm
Nucleus
Membrane
; Multi-pass membrane protein

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_501231161619-926Inosine triphosphate pyrophosphatase

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region229-256Disordered
Compositional bias230-256Polar residues
Domain262-299CBM1
Compositional bias361-380Polar residues
Region361-399Disordered

Sequence similarities

Belongs to the HAM1 NTPase family.
Belongs to the glycosyl hydrolase 45 (cellulase K) family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    926
  • Mass (Da)
    99,012
  • Last updated
    2017-11-22 v1
  • Checksum
    6DE1BBC6EF9E65DB
MVKILLTVVALSIAAVHADNLSPGGTATRYWDCCKPSGGISGKAAVNRPVFSCAQDGVTHVDPSTNSACAGGTAYTCTNYQPFVSSCNPNLSYAFGARAQSNDESTFECACYQVTFAQLPGKTLIVQATNDGGDVPATNFDIQIPGGGVGLFDACTAEYNAPPGGWGAQYGGISSQTQCSQLPASLQKGCNWRFTWFADNPTISSISRVKCPSQLTDLSGCIRNDDASQPAPSVGCNGPQPSTSNMSTSTSKASSTPKPTATCAALYAQCGGQGYTGPTCCISSTCQYQNPSEFADKDLVLDTFAFMLRFTSTLGHSTMFVCRRTCHPQSGLFQGSSGTISPRARLVTGGLFVRQGRFLSTLRPDNPQDKTSSTPSSHPDSHSHSHSHGHAHGHEGHSHAHLVDALETTSSRGWRITVVGLVANVGLCVTKGVAGWVMNSASLVADAAHSLSDMISDFVTLYTYRVSRRPPDELHPYGYGKYETVGSLAVSSILIVGALGIGYHSYELLLQVLPETFTGALNSNALPDAAVASAPTSHASVDAGIAAAKEAHEGASLSNLLPFHSHAHEHHDTLLNPNAAWFALASVIIKEWLYQATIKVGKDERSDVLIANAWHHRSDAFSSIVALAAIAGSHFGVPILDPLGGILVSGMILKTGVEIMLGSLKELVDANVDDDVLQQVQQAITRLQKTQPDLIDFHSIRGRKAGPFILVDLILQVNPTLTVEKAHRVEDAVRRARSNLRIDNYRESMGKHQLVFVTGNKNKLAEVQAILGDTVDLVNRSLDLPEIQGTPEEVARAKCIAAAEQDHVSPKIPVSALTLFKGYPVHTWHEGLNKLLAGYEDKSAYALCIFALSKGPGEVPILFEGRTDGRIVPARGPNNFGWDPIFEPTGFDETYAEMPKSTKNTISHRFRALEKLSAYLSHYPPQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias230-256Polar residues
Compositional bias361-380Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MVBO01000046
EMBL· GenBank· DDBJ
OZJ04288.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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