P28847 (RIR2_EHV1B) 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:

20

Organism

Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus) [Complete proteome]

Taxonomic identifier

31520 [NCBI]

Taxonomic lineage

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

Virus host

Equus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length	321 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 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
Technical term	Complete 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	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 – 321	321	Ribonucleoside-diphosphate reductase small chain		PRO_0000190508
Sites
	Active site	115	1	By similarity
	Metal binding	78	1	Iron 1 By similarity
	Metal binding	108	1	Iron 1 By similarity
	Metal binding	108	1	Iron 2 By similarity
	Metal binding	111	1	Iron 1 By similarity
	Metal binding	171	1	Iron 2 By similarity
	Metal binding	205	1	Iron 2 By similarity
	Metal binding	208	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P28847 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 81E1FF57B12B84A4	FASTA	321	36,017
	10 20 30 40 50 60 MSIENSKEAA LTAELSLAGA FFYTPECPDI EHLRSLSVAN RWLDTDLPIS DDLKDVAKLT 70 80 90 100 110 120 PAEREFYRFL FAFLSAADDL VNLNLGDLSA LFTQKDILHY YIEQESIEVT HSRVYSAIQL 130 140 150 160 170 180 MLFGNDAAAR ARYVASIIGD AAIGRKVAWL QAKVRECGSV AEKYILMILI EGLFFASSFA 190 200 210 220 230 240 SIAYLRTHNL FVVTCQSNDL ISRDEAIHTR ASCCIYNNYL GGFEKPEPKR IYELFSEAVN 250 260 270 280 290 300 IECEFLLSHA PQYSHLLDIG AIISYVRYSA DRLLGEIGLS PLFNAPKPSP SFPLAFMTVE 310 320 KHTNFFERRS TAYSGTLIND L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence of equine herpesvirus-1." Telford E.A.R., Watson M.S., McBride K., Davison A.J. Virology 189:304-316(1992) [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	AY665713 Genomic DNA. Translation: AAT67277.1.
PIR	WMBEA1. C36797.
RefSeq	YP_053065.1. NC_001491.2.
3D structure databases
ProteinModelPortal	P28847.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1487524.
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_EHV1B

Accession

Primary (citable) accession number: P28847

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program