P32092 (DIPP_ASFB7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
mRNA-decapping protein g5R
EC=3.1.3.-

Alternative name(s):
Diphosphoinositol polyphosphate phosphohydrolase
Short name=DIPP
EC=3.6.1.52

Gene names

Ordered Locus Names:	Ba71V-102
ORF Names:	D250R

Organism

African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)

Taxonomic identifier

10498 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Asfarviridae › Asfivirus

Virus host

Ornithodoros (relapsing fever ticks) [TaxID: 6937]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Decapping enzyme required for the removal of the 5'-end m7GpppN cap tethered to viral and host mRNAs to allow their decay in cells. May therefore accelerate viral and cellular mRNA turnover to eliminate competing host mRNAs and allow stage-specific synthesis of viral proteins. Acceleration of the turnover of cellular transcripts may even promote the shutoff of host protein synthesis. In addition to the mRNA cap, g5R also efficiently hydrolyzes diphosphoinositol polyphosphates. Down-regulation of the level of PP-InsP5 (diphosphoinositol pentakisphosphate) may play a role in viral manipulation of the cellular secretory pathway, a step necessary for the formation of virions. Ref.4
Catalytic activity	Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
Cofactor	Magnesium or manganese.
Subcellular location	Host rough endoplasmic reticulum.
Sequence similarities	Belongs to the Nudix hydrolase family. DIPP subfamily. Contains 1 nudix hydrolase domain.
Biophysicochemical properties	Kinetic parameters: KM=1.2 µM for diphosphoinositol pentakisphosphate KM=0.67 mM for GTP KM=0.58 mM for p5A KM=0.92 mM for ATP KM=1.36 mM for p4A KM=1.70 mM for Gp4G KM=3.90 mM for Ap4A pH dependence: Optimum pH is 9.5.

Ontologies

Keywords
Cellular component	Host endoplasmic reticulum
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Cellular component	host cell rough endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	diphosphoinositol-polyphosphate diphosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 250	250	mRNA-decapping protein g5R		PRO_0000057089
Regions
	Domain	97 – 239	143	Nudix hydrolase
	Motif	132 – 153	22	Nudix box
Sites
	Active site	147	1	Nucleophile Probable
	Metal binding	138	1	Magnesium or manganese By similarity
	Metal binding	151	1	Magnesium or manganese Probable
	Metal binding	173	1	Magnesium or manganese By similarity
Experimental info
	Mutagenesis	147	1	E → Q: Complete loss of mRNA-decapping activity. Ref.4
	Mutagenesis	150 – 151	2	EE → QQ: Complete loss of mRNA-decapping activity.

Sequences

	Sequence		Length	Mass (Da)
	P32092 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 3EF2522180E42237	FASTA	250	29,875
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"African swine fever virus guanylyltransferase." Pena L., Yanez R.J., Revilla Y., Vinuela E., Salas M.L. Virology 193:319-328(1993) [PubMed: 8382399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the complete nucleotide sequence of African swine fever virus." Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., Rodriguez J.F., Vinuela E. Virology 208:249-278(1995) [PubMed: 11831707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The g5R (D250) gene of African swine fever virus encodes a Nudix hydrolase that preferentially degrades diphosphoinositol polyphosphates." Cartwright J.L., Safrany S.T., Dixon L.K., Darzynkiewicz E., Stepinski J., Burke R., McLennan A.G. J. Virol. 76:1415-1421(2002) [PubMed: 11773415] [Abstract] Cited for: CHARACTERIZATION.
[4]	"The African swine fever virus g5R protein possesses mRNA decapping activity." Parrish S., Hurchalla M., Liu S.-W., Moss B. Virology 393:177-182(2009) [PubMed: 19695654] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-147 AND 150-GLU-GLU-151.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07263 Genomic DNA. Translation: AAA42693.1. U18466 Genomic DNA. Translation: AAA65331.1.
PIR	B45391.
RefSeq	NP_042795.1. NC_001659.1.
3D structure databases
ProteinModelPortal	P32092.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1488866.
Phylogenomic databases
ProtClustDB	CLSP2510031.
Family and domain databases
InterPro	IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
SUPFAM	SSF55811. NUDIX_hydrolase. 1 hit.
PROSITE	PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DIPP_ASFB7

Accession

Primary (citable) accession number: P32092

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program