P69520 (RIR2_HHV23) 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 38 kDa subunit Ribonucleotide reductase small subunit
Organism	Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2)
Taxonomic identifier	10313 [NCBI]
Taxonomic lineage	Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus › Human herpesvirus 2
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	337 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	Heterotetramer composed of a homodimer of the large subunit UL39 (R1) and a homodimer of the small subunit UL40 (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
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 – 337	337	Ribonucleoside-diphosphate reductase small chain		PRO_0000190505
Sites
	Active site	128	1	By similarity
	Metal binding	91	1	Iron 1 By similarity
	Metal binding	121	1	Iron 1 By similarity
	Metal binding	121	1	Iron 2 By similarity
	Metal binding	124	1	Iron 1 By similarity
	Metal binding	184	1	Iron 2 By similarity
	Metal binding	218	1	Iron 2 By similarity
	Metal binding	221	1	Iron 2 By similarity
Experimental info
	Sequence conflict	173	1	I → V in CAA24930. Ref.2
	Sequence conflict	235	1	G → D in CAA24930. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P69520 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 1E27E96599EE2120	FASTA	337	37,626
	10 20 30 40 50 60 MDPAVSPAST DPLDTHASGA GAAPIPVCPT PERYFYTSQC PDINHLRSLS ILNRWLETEL 70 80 90 100 110 120 VFVGDEEDVS KLSEGELGFY RFLFAFLSAA DDLVTENLGG LSGLFEQKDI LHYYVEQECI 130 140 150 160 170 180 EVVHSRVYNI IQLVLFHNND QARRAYVART INHPAIRVKV DWLEARVREC DSIPEKFILM 190 200 210 220 230 240 ILIEGVFFAA SFAAIAYLRT NNLLRVTCQS NDLISRDEAV HTTASCYIYN NYLGGHAKPE 250 260 270 280 290 300 AARVYRLFRE AVDIEIGFIR SQAPTDSSIL SPGALAAIEN YVRFSADRLL GLIHMQPLYS 310 320 330 APAPDASFPL SLMSTDKHTN FFECRSTSYA GAVVNDL

References

[1]	"Organization of the left-hand end of the herpes simplex virus type 2 BglII N fragment." Galloway D.A., Swain M.A. J. Virol. 49:724-730(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"DNA sequence homology between two co-linear loci on the HSV genome which have different transforming abilities." McLauchlan J., Clements J.B. EMBO J. 2:1953-1961(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Tinkering with a viral ribonucleotide reductase." Lembo D., Brune W. Trends Biochem. Sci. 34:25-32(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12700 Genomic DNA. Translation: AAA45807.1. X00048 Genomic DNA. Translation: CAA24930.1.
PIR	WMBE32. A00528. WMBEB2. A00529.
RefSeq	NP_044510.1. NC_001798.1.
3D structure databases
ProteinModelPortal	P69520.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1487327.
Phylogenomic databases
ProtClustDB	CLSP2509600.
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...
Other
BindingDB	P69520.
ChEMBL	CHEMBL2418.

Entry information

Entry name

RIR2_HHV23

Accession

Primary (citable) accession number: P69520
Secondary accession number(s): P03174

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program