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Q8SS24 (ITPA_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Inosine triphosphate pyrophosphatase
Short name=ITPase
Short name=Inosine triphosphatase
EC=3.6.1.19
Alternative name(s):
Non-canonical purine NTP pyrophosphatase
Non-standard purine NTP pyrophosphatase
Nucleoside-triphosphate diphosphatase
Nucleoside-triphosphate pyrophosphatase
Short name=NTPase
Gene names
Ordered Locus Names:ECU04_1180
OrganismEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]
Taxonomic identifier284813 [NCBI]
Taxonomic lineageEukaryota › Fungi › Microsporidia › Unikaryonidae › Encephalitozoon ›

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_03148

Catalytic activity

A nucleoside triphosphate + H2O = a nucleotide + diphosphate. HAMAP-Rule MF_03148

Cofactor

Binds 1 divalent metal cation ion per subunit; can use either magnesium or manganese By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the HAM1 NTPase family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
Nucleus
   LigandMagnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphate diphosphatase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192Inosine triphosphate pyrophosphatase HAMAP-Rule MF_03148
PRO_0000413139

Regions

Region8 – 136Substrate binding By similarity
Region64 – 652Substrate binding By similarity
Region169 – 1702Substrate binding By similarity

Sites

Metal binding341Magnesium or manganese By similarity
Metal binding641Magnesium or manganese By similarity
Binding site461Substrate By similarity
Binding site1641Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8SS24 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: F6BA42A8B3B40F82

FASTA19221,149
        10         20         30         40         50         60 
MGRIYFATTN LKKLKEIRSL FEADIVHMNI PMVEIQASLE RIVDHKLNQV VPCIGEGDAV 

        70         80         90        100        110        120 
IVDDTAVAFE GLYGFPGVYI KDFLRIGSRK ISEIVGKIGN SNATAFCCLG IAHYRDGRVV 

       130        140        150        160        170        180 
KKVFFGELEG SIVESKEDGL EGFDYIFLPS GSSMCLGDMP VDEKNRISHR RIASKKLADY 

       190 
MASVGIIKAH GS

« Hide

References

[1]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL590444 Genomic DNA. Translation: CAD25306.1.
RefSeqNP_584802.1. NM_001041152.1.

3D structure databases

HSSPHSSP built from PDB template 1B78 based on UniProtKB Q57679.
ProteinModelPortalQ8SS24.
ModBaseSearch...

Protein-protein interaction databases

STRING6035.ECU04_1180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID858950.
KEGGecu:ECU04_1180.

Phylogenomic databases

eggNOGCOG0127.
HOGENOMHOG000293320.
OMAHRRIALE.

Family and domain databases

HAMAPMF_03148. HAM1_NTPase.
InterProIPR002637. Ham1p-like.
[Graphical view]
PANTHERPTHR11067. PTHR11067. 1 hit.
PfamPF01725. Ham1p_like. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameITPA_ENCCU
AccessionPrimary (citable) accession number: Q8SS24
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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