O57175 (RIR2_VACCA) 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

Ordered Locus Names:

MVA032L, ACAM3000_MVA_032

Organism

Vaccinia virus (strain Ankara) (VACV)

Taxonomic identifier

126794 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus › Vaccinia virus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. 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	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.
Induction	Expressed early in the viral replicative cycle.
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 – 319	319	Ribonucleoside-diphosphate reductase small chain		PRO_0000190495
Sites
	Active site	108	1	By similarity
	Metal binding	70	1	Iron 1 By similarity
	Metal binding	101	1	Iron 1 By similarity
	Metal binding	101	1	Iron 2 By similarity
	Metal binding	104	1	Iron 1 By similarity
	Metal binding	163	1	Iron 2 By similarity
	Metal binding	197	1	Iron 2 By similarity
	Metal binding	200	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	O57175 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 0444D6A80EA0AD51	FASTA	319	36,947
	10 20 30 40 50 60 MEPILAPNPN RFVIFPIQYH DIWNMYKKAE ASFWTVEEVD ISKDINDWNK LTPDEKYFIK 70 80 90 100 110 120 HVLAFFAASD GIVNENLAER FCTEVQITEA RCFYGFQMAI ENIHSEMYSL LIDTYVKDSN 130 140 150 160 170 180 EKNYLFNAIE TMPCVKKKAD WAQKWIHDSA GYGERLIAFA AVEGIFFSGS FASIFWLKKR 190 200 210 220 230 240 GLMPGLTFSN ELISRDEGLH CDFACLMFKH LLHPPSEETV RSIITDAVSI EQEFLTAALP 250 260 270 280 290 300 VKLIGMNCEM MKTYIEFVAD RLISELGFKK IYNVTNPFDF MENISLEGKT NFFEKRVGEY 310 QKMGVMSQED NHFSLDVDF

References

[1]	"The complete genomic sequence of the modified vaccinia Ankara strain: comparison with other orthopoxviruses." Antoine G., Scheiflinger F., Dorner F., Falkner F.G. Virology 244:365-396(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J., Khristova M., Wohlhueter R.M. Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Isolate Acambis 3000.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U94848 Genomic DNA. Translation: AAB96415.1. AY603355 Genomic DNA. Translation: AAT10430.1.
PIR	T30782.
3D structure databases
ProteinModelPortal	O57175.
SMR	O57175. Positions 2-282.
ModBase	Search...
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_VACCA

Accession

Primary (citable) accession number: O57175

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program