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UniProtKB/Swiss-Prot entry P32092


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DIPP_ASFB7
Primary accession number P32092
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 46)
Name and origin of the protein
Protein name Diphosphoinositol polyphosphate phosphohydrolase
Synonyms DIPP
EC 3.6.1.52
Gene name
OrderedLocusNames: Ba71V-102
ORFNames: D250R
From
African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV) [TaxID: 10498] 
Taxonomy Viruses; dsDNA viruses, no RNA stage; Asfarviridae; Asfivirus.
Virus hosts Ornithodoros (relapsing fever ticks) [TaxID: 6937]
Sus scrofa (Pig) [TaxID: 9823]
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/viro.1993.1128; PubMed=8382399 [NCBI, ExPASy, EBI, Israel, Japan]
Pena L., Yanez R.J., Revilla Y., Vinuela E., Salas M.L.;
"African swine fever virus guanylyltransferase.";
Virology 193:319-328(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1006/viro.1995.1149; PubMed=11831707 [NCBI, ExPASy, EBI, Israel, Japan]
Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., Rodriguez J.F., Vinuela E.;
"Analysis of the complete nucleotide sequence of African swine fever virus.";
Virology 208:249-278(1995).
[3]
CHARACTERIZATION.
PubMed=11773415 [NCBI, ExPASy, EBI, Israel, Japan]
Cartwright J.L., Safrany S.T., Dixon L.K., Darzynkiewicz E., Stepinski J., Burke R., McLennan A.G.;
"The g5R (D250) gene of African swine fever virus encodes a Nudix hydrolase that preferentially degrades diphosphoinositol polyphosphates.";
J. Virol. 76:1415-1421(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L07263; AAA42693.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18466; AAA65331.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B45391; B45391.
RefSeq NP_042795.1; -.
3D structure databases
ModBase P32092.
Ontologies
GO
GO:0005791; Cellular component: rough endoplasmic reticulum (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016787; Molecular function: hydrolase activity (inferred from electronic annotation from InterPro).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000086; NUDIX_hydrolase_core.
Graphical view of domain structure.
Gene3D G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
Pfam PF00293; NUDIX; 1.
Pfam graphical view of domain structure.
PRINTS PR00502; NUDIXFAMILY.
PROSITE PS00893; NUDIX; 1.
BLOCKS P32092.
ProtoNet P32092.
Genome annotation databases
GeneID 1488866; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   250  250     Diphosphoinositol polyphosphate phosphohydrolase. PRO_0000057089
DOMAIN   98   214  117     Nudix hydrolase. 
MOTIF   132   153  22     Nudix box. 
Sequence information
Length: 250 AA [This is the length of the unprocessed precursor] Molecular weight: 29875 Da [This is the MW of the unprocessed precursor] CRC64: 3EF2522180E42237 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDTAMQLKTS IGLITCRMNT QNNQIETILV QKRYSLAFSE FIHCHYSINA NQGHLIKMFN 

        70         80         90        100        110        120 
NMTINERLLV KTLDFDRMWY HIWIETPVYE LYHKKYQKFR KNWLLPDNGK KLISLINQAK 

       130        140        150        160        170        180 
GSGTLLWEIP KGKPKEDESD LTCAIREFEE ETGITREYYQ ILPEFKKSMS YFDGKTEYKH 

       190        200        210        220        230        240 
IYFLAMLCKS LEEPNMNLSL QYENRIAEIS KISWQNMEAV RFISKRQSFN LEPMIGPAFN 

       250 
FIKNYLRYKH 

P32092 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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