P26713 (RIR2_ASFM2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase small chain
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase small subunit

Gene names

Ordered Locus Names:

Mal-052

Organism

African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV) [Complete proteome]

Taxonomic identifier

10500 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Asfarviridae › Asfivirus › African swine fever virus

Virus host

Ornithodoros (relapsing fever ticks) [TaxID: 6937]
Phacochoerus aethiopicus (Warthog) [TaxID: 85517]
Phacochoerus africanus (Warthog) [TaxID: 41426]
Potamochoerus larvatus (Bushpig) [TaxID: 273792]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Cofactor	Binds 2 iron ions per subunit By similarity.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterotetramer composed of a homodimer of the large subunit (R1) and a homodimer of the small subunit (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n By similarity.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA replication
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 327	327	Ribonucleoside-diphosphate reductase small chain		PRO_0000190492
Sites
	Active site	108	1	By similarity
	Metal binding	70	1	Iron 1 By similarity
	Metal binding	101	1	Iron 1 By similarity
	Metal binding	101	1	Iron 2 By similarity
	Metal binding	104	1	Iron 1 By similarity
	Metal binding	164	1	Iron 2 By similarity
	Metal binding	198	1	Iron 2 By similarity
	Metal binding	201	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26713 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: E78508DB1978F4B0	FASTA	327	38,966
	10 20 30 40 50 60 MEELLIENSQ RFTIFPIQHP ECWNWYKKLE SMTWTAQEVD MCKDIDDWEA MPKPQREFYK 70 80 90 100 110 120 QILAFFVVAD EIVIENLLTN FMREIKVKEV LYFYTMQAAQ ECVHSEAYSI QVKTLIPDEK 130 140 150 160 170 180 EQQRIFSGIE KHPIIKKMAQ WVRQWMDPAR NSLGERLVGF AAVEGILFQN HFVAIQFLKE 190 200 210 220 230 240 QNIMPGLVSY NEFISRDEGM HCSFACFLIS NYVYNIPEEK IIHKILKEAV ELVDEFINYA 250 260 270 280 290 300 FDKARGRVPG FSKEMLFQYI RYFTDNLCFM MQCKSIYNVG NPFPQMTKFF LNEVEKTNFF 310 320 ELRPTQYQNC VKDDAFAFKL FLDDDDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequences of the ribonucleotide reductase genes from African swine fever virus show considerable homology with those of the orthopoxvirus, vaccinia virus." Boursnell M., Shaw K., Yanez R.J., Vinuela E., Dixon L. Virology 184:411-416(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"African swine fever virus genomes." Kutish G.F., Rock D.L. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64728 Genomic DNA. No translation available. AY261361 Genomic DNA. No translation available.
PIR	RDVZAS. B40568.
3D structure databases
ProteinModelPortal	P26713.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR012348. RNR-rel. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2_ASFM2

Accession

Primary (citable) accession number: P26713

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program