Q6R7K3 (RIR2_OSHVF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

ORF Names:

ORF20

Organism

Ostreid herpesvirus 1 (isolate France) (OsHV-1) (Pacific oyster herpesvirus) [Reference proteome]

Taxonomic identifier

654903 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Malacoherpesviridae › Ostreavirus › Ostreid herpesvirus 1

Virus host

Crassostrea gigas (Pacific oyster) (Crassostrea angulata) [TaxID: 29159]
Pecten maximus (King scallop) (Pilgrim's clam) [TaxID: 6579]

Protein attributes

Sequence length	579 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. 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.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family. Contains 1 fido domain.

Ontologies

Keywords
Biological process	DNA replication
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	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 – 579	579	Ribonucleoside-diphosphate reductase small chain		PRO_0000385024
Regions
	Domain	435 – 579	145	Fido
Sites
	Active site	167	1	By similarity
	Metal binding	130	1	Iron 1 By similarity
	Metal binding	160	1	Iron 1 By similarity
	Metal binding	160	1	Iron 2 By similarity
	Metal binding	163	1	Iron 1 By similarity
	Metal binding	225	1	Iron 2 By similarity
	Metal binding	258	1	Iron 2 By similarity
	Metal binding	261	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6R7K3 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: E7B90F9E49DF0791	FASTA	579	66,994
	10 20 30 40 50 60 MSQSTIKFDL GELTTTQCAR LLSKFIRKAT LTPEQFEILN TSYDELTEFD DHPLYGGATD 70 80 90 100 110 120 HHKDIVGKYD HALLKPAVYQ QLRDFATKME SSSWQQTEID AESDIPTWEQ ISENERDCVR 130 140 150 160 170 180 KVLAFFAVGD TLVKDRIAIF ADEFPLPECK DFIDWQTVNE GVHQRVYNNY LDALVKDKIY 190 200 210 220 230 240 LADLVNAYKD PEFAPIKKKV DWLGKIISVE NDSRGEMVVG QVCTEAIMFA ASFAILLKFR 250 260 270 280 290 300 APYMRALVLG NEFIRRDETL HFRFYAELLR LMPDRPSDER IAELLTEATE IELEFAEYVV 310 320 330 340 350 360 PEGVKYITKD RLIQHVKANT NQVCEMLDIN PIYFDQKGNV LLSPLLYMNT LESEQKINFF 370 380 390 400 410 420 EGKATEYNTK QYKVDFNNLF PPVKKMIEFA DEEEFIAAIV EGEGLSKDRN KDIVKQQLCL 430 440 450 460 470 480 AWDHLSSHDM EGLVDMTWTL KDVHRIAMNH VIFNNGEFSN GYKFTVIDSG KVMYPTYETV 490 500 510 520 530 540 EILESAVQGL IDDYNRDFSA LDKGVEKFDK DKIRVAARFI LDLLYIHPFS DGNGRTARLI 550 560 570 MAHLIGKMTT PINREEYLKS IYHYRQTGDV SVFVDQFYR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel class of herpesvirus with bivalve hosts." Davison A.J., Trus B.L., Cheng N., Steven A.C., Watson M.S., Cunningham C., Le Deuff R.M., Renault T. J. Gen. Virol. 86:41-53(2005) [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	AY509253 Genomic DNA. Translation: AAS00912.1.
RefSeq	YP_024565.1. NC_005881.1.
3D structure databases
HSSP	HSSP built from PDB template 1SMQ based on UniProtKB P09938.
ProteinModelPortal	Q6R7K3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2948202.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR003812. Fido. IPR012348. RNR-rel. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF02661. Fic. 1 hit. PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit. SSF140931. SSF140931. 1 hit.
PROSITE	PS51459. FIDO. 1 hit. PS00368. RIBORED_SMALL. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2_OSHVF

Accession

Primary (citable) accession number: Q6R7K3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program