P50644 (RIR2_EHV4) 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
Organism	Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus)
Taxonomic identifier	10333 [NCBI]
Taxonomic lineage	Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus › Equid herpesvirus 4
Virus host	Equus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length	320 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, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. The N-terminal region confers antiapoptotic activity in differentiated cells such as neurons and is important for viral reactivation to increase neural survivability 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	Heterodimer of a large and a small chain.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA replication
Developmental stage	Early protein
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	ribonucleoside-diphosphate reductase complex 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 – 320	320	Ribonucleoside-diphosphate reductase small chain		PRO_0000190509
Sites
	Active site	114	1	By similarity
	Metal binding	77	1	Iron 1 By similarity
	Metal binding	107	1	Iron 1 By similarity
	Metal binding	107	1	Iron 2 By similarity
	Metal binding	110	1	Iron 1 By similarity
	Metal binding	170	1	Iron 2 By similarity
	Metal binding	204	1	Iron 2 By similarity
	Metal binding	207	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50644 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 7AF3511937730202	FASTA	320	36,172
	10 20 30 40 50 60 MALENSKKTD FADELLINAY FYTPECPDIE HLRLLSVANR WLDTDLPISD DLKDVAKLAP 70 80 90 100 110 120 AEREFYRFLF AFLSAADDLV NLNLGDLSAL FTQKDILHYY IEQESIEVTH SRVYSAIQLM 130 140 150 160 170 180 LFGNDATARA RYVASVVKDV AIDLKVSWLQ AKVRECKSVA EKYILMILIE GVFFASSFAS 190 200 210 220 230 240 IAYLRTHNLF VVTCQSNDLI SRDEAIHTNA SCCIYNNYLG GFEKPAPTRI YALFSEAVNI 250 260 270 280 290 300 ECEFLLSHAP KSSHLLDIEA IICYVRYSAD RLLGEIGLSP LFNAPKPPPS FPLAFMTVEK 310 320 HTNFFERRST AYSGTLINDL

References

[1]	"Sequences of the ribonucleotide reductase-encoding genes of equine herpesvirus 4." Riggio M.P., Onions D.E. Gene 143:217-222(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1942.
[2]	"Tinkering with a viral ribonucleotide reductase." Lembo D., Brune W. Trends Biochem. Sci. 34:25-32(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75354 Genomic DNA. Translation: CAA53101.1.
3D structure databases
ProteinModelPortal	P50644.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-6732622.
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_EHV4

Accession

Primary (citable) accession number: P50644

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program