P50645 (RIR2_SUHVK) 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

Name:	RR2
Synonyms:	UL40

Organism

Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain Kaplan))

Taxonomic identifier

33703 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus › Suid herpesvirus 1

Virus host

Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	303 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 (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
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
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 – 303	303	Ribonucleoside-diphosphate reductase small chain		PRO_0000190511
Sites
	Active site	97	1	By similarity
	Metal binding	60	1	Iron 1 By similarity
	Metal binding	90	1	Iron 1 By similarity
	Metal binding	90	1	Iron 2 By similarity
	Metal binding	93	1	Iron 1 By similarity
	Metal binding	153	1	Iron 2 By similarity
	Metal binding	187	1	Iron 2 By similarity
	Metal binding	190	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50645 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 560F19FDE6C7A9C3	FASTA	303	34,375
	10 20 30 40 50 60 MEYFYTSQCP DMDHLRSLSV ANRWLETDLP LGDDAKDVAA LSEPELEFYR FLFAFLSAAD 70 80 90 100 110 120 DLVNVNLGSL SELFTQKDIL HYYIEQECIE VVHSRVYSAI QLMLFRGDAA ARERYVRAAL 130 140 150 160 170 180 RDEAIRRKVE WLDSRVAECA SVAEKYLLMI LIEGIFFASS FASISYLRTH NLFVVTCQSN 190 200 210 220 230 240 DFISRDEAIH TSASCCIYNN YLGDAPRPDE ARIHQLFAEA VEIECEFLRA RAPRDSLLLD 250 260 270 280 290 300 LPAIISYVRY SADRLLQAIG ASPLFGAPAP AADFPMALMV AEKHTNFFER RSTNYTGTVV NDL

References

[1]	"Large and small subunits of the Aujeszky's disease virus ribonucleotide reductase: nucleotide sequence and putative structure." Kaliman A., Boldogkoi Z., Fodor I. Biochim. Biophys. Acta 1219:151-156(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [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	X72087 Genomic DNA. Translation: CAA50977.1. X80797 Genomic DNA. Translation: CAA56776.1.
PIR	S47526.
RefSeq	YP_068343.1. NC_006151.1.
3D structure databases
ProteinModelPortal	P50645.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2952536.
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...

Entry information

Entry name

RIR2_SUHVK

Accession

Primary (citable) accession number: P50645

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program