P10224 (RIR2_HHV11) 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 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]

Taxonomic identifier

10299 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus › Human herpesvirus 1

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Signal 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
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 340	318	Ribonucleoside-diphosphate reductase small chain		PRO_0000190503
Regions
	Transmembrane	180 – 200	21	Helical; Potential
Sites
	Active site	131	1	By similarity
	Metal binding	94	1	Iron 1 By similarity
	Metal binding	124	1	Iron 1 By similarity
	Metal binding	124	1	Iron 2 By similarity
	Metal binding	127	1	Iron 1 By similarity
	Metal binding	187	1	Iron 2 By similarity
	Metal binding	221	1	Iron 2 By similarity
	Metal binding	224	1	Iron 2 By similarity
Natural variations
	Natural variant	15 – 18	4	LTDQ → HTGH in strain: Nonneuroinvasive mutant HF10.
	Natural variant	17	1	D → G in strain: 17 syn+.

Sequences

	Sequence		Length	Mass (Da)
	P10224 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 4B4ED994BF74FD3F	FASTA	340	38,019
	10 20 30 40 50 60 MDSAAPALSP ALTALTDQSA TADLAIQIPK CPDPERYFYT SQCPDINHLR SLSILNRWLE 70 80 90 100 110 120 TELVFVGDEE DVSKLSEGEL SFYRFLFAFL SAADDLVTEN LGGLSGLFEQ KDILHYYVEQ 130 140 150 160 170 180 ECIEVVHSRV YNIIQLVLFH NNDQARREYV AGTINHPAIR AKVDWLEARV RECASVPEKF 190 200 210 220 230 240 ILMILIEGIF FAASFAAIAY LRTNNLLRVT CQSNDLISRD EAVHTTASCY IYNNYLGGHA 250 260 270 280 290 300 KPPPDRVYGL FRQAVEIEIG FIRSQAPTDS HILSPAALAA IENYVRFSAD RLLGLIHMKP 310 320 330 340 LFSAPPPDAS FPLSLMSTDK HTNFFECRST SYAGAVVNDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1." McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P. J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus." Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y. Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nonneuroinvasive mutant HF10.
[3]	"Herpes simplex virus type 1 bacterial artificial chromosome." Cunningham C., Davison A.J. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 17 syn+.
[4]	"Tinkering with a viral ribonucleotide reductase." Lembo D., Brune W. Trends Biochem. Sci. 34:25-32(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14112 Genomic DNA. Translation: CAA32303.1. DQ889502 Genomic DNA. Translation: ABI63502.1. FJ593289 Genomic DNA. Translation: ACM62263.1.
PIR	WMBES7. D30088.
RefSeq	NP_044642.1. NC_001806.1.
3D structure databases
ProteinModelPortal	P10224.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-6732638.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2703364.
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_HHV11

Accession

Primary (citable) accession number: P10224
Secondary accession number(s): B9VQG8, Q09I93

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program