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P26713 (RIR2_ASFM2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismAfrican swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV) [Complete proteome]
Taxonomic identifier10500 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
Virus hostOrnithodoros (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 length327 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Ribonucleoside-diphosphate reductase small chain
PRO_0000190492

Sites

Active site1081 By similarity
Metal binding701Iron 1 By similarity
Metal binding1011Iron 1 By similarity
Metal binding1011Iron 2 By similarity
Metal binding1041Iron 1 By similarity
Metal binding1641Iron 2 By similarity
Metal binding1981Iron 2 By similarity
Metal binding2011Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P26713 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: E78508DB1978F4B0

FASTA32738,966
        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 

« Hide

References

« Hide '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.
PIRRDVZAS. B40568.

3D structure databases

ProteinModelPortalP26713.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR2_ASFM2
AccessionPrimary (citable) accession number: P26713
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: December 11, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways