P69521 (RIR2_HHV2H) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase small chain
Short name=R2
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase 38 kDa subunit
Ribonucleotide reductase small subunit

Gene names

ORF Names:

UL40

Organism

Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2) [Reference proteome]

Taxonomic identifier

10315 [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.
Subcellular location	Host membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Host membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference 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
Cellular_component	host cell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW 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_0000190506
Regions
	Transmembrane	177 – 197	21	Helical; Potential
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

Sequences

	Sequence		Length	Mass (Da)
	P69521 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of herpes simplex virus type 2." Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J. J. Virol. 72:2010-2021(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z86099 Genomic DNA. Translation: CAB06726.1.
RefSeq	NP_044510.1. NC_001798.1.
3D structure databases
ProteinModelPortal	P69521.
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	P69521.

Entry information

Entry name

RIR2_HHV2H

Accession

Primary (citable) accession number: P69521
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 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program