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P10224

- RIR2_HHV11

UniProt

P10224 - RIR2_HHV11

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Protein
Ribonucleoside-diphosphate reductase small chain
Gene
UL40
Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Cofactori

Binds 2 iron ions per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Iron 1 By similarity
Metal bindingi124 – 1241Iron 1 By similarity
Metal bindingi124 – 1241Iron 2 By similarity
Metal bindingi127 – 1271Iron 1 By similarity
Active sitei131 – 1311 By similarity
Metal bindingi187 – 1871Iron 2 By similarity
Metal bindingi221 – 2211Iron 2 By similarity
Metal bindingi224 – 2241Iron 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
  2. deoxyribonucleoside diphosphate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase small chain (EC:1.17.4.1)
Short name:
R2
Alternative name(s):
Ribonucleotide reductase 38 kDa subunit
Ribonucleotide reductase small subunit
Gene namesi
ORF Names:UL40
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000009294: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei180 – 20021Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. host cell membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 340318Ribonucleoside-diphosphate reductase small chain
PRO_0000190503Add
BLAST

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

IntActiP10224. 2 interactions.
MINTiMINT-6732638.

Structurei

3D structure databases

ProteinModelPortaliP10224.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10224-1 [UniParc]FASTAAdd to Basket

« Hide

MDSAAPALSP ALTALTDQSA TADLAIQIPK CPDPERYFYT SQCPDINHLR    50
SLSILNRWLE TELVFVGDEE DVSKLSEGEL SFYRFLFAFL SAADDLVTEN 100
LGGLSGLFEQ KDILHYYVEQ ECIEVVHSRV YNIIQLVLFH NNDQARREYV 150
AGTINHPAIR AKVDWLEARV RECASVPEKF ILMILIEGIF FAASFAAIAY 200
LRTNNLLRVT CQSNDLISRD EAVHTTASCY IYNNYLGGHA KPPPDRVYGL 250
FRQAVEIEIG FIRSQAPTDS HILSPAALAA IENYVRFSAD RLLGLIHMKP 300
LFSAPPPDAS FPLSLMSTDK HTNFFECRST SYAGAVVNDL 340
Length:340
Mass (Da):38,019
Last modified:July 1, 1989 - v1
Checksum:i4B4ED994BF74FD3F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 184LTDQ → HTGH in strain: Nonneuroinvasive mutant HF10.
Natural varianti17 – 171D → G in strain: 17 syn+.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14112 Genomic DNA. Translation: CAA32303.1.
DQ889502 Genomic DNA. Translation: ABI63502.1.
FJ593289 Genomic DNA. Translation: ACM62263.1.
PIRiD30088. WMBES7.
RefSeqiNP_044642.1. NC_001806.1.

Genome annotation databases

GeneIDi2703364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14112 Genomic DNA. Translation: CAA32303.1 .
DQ889502 Genomic DNA. Translation: ABI63502.1 .
FJ593289 Genomic DNA. Translation: ACM62263.1 .
PIRi D30088. WMBES7.
RefSeqi NP_044642.1. NC_001806.1.

3D structure databases

ProteinModelPortali P10224.
ModBasei Search...

Protein-protein interaction databases

IntActi P10224. 2 interactions.
MINTi MINT-6732638.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2703364.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

Gene3Di 1.10.620.20. 1 hit.
InterProi IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view ]
PANTHERi PTHR23409. PTHR23409. 1 hit.
Pfami PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00368. RIBORED_SMALL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiRIR2_HHV11
AccessioniPrimary (citable) accession number: P10224
Secondary accession number(s): B9VQG8, Q09I93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 14, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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