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P06474

- RIR2_HHV1K

UniProt

P06474 - RIR2_HHV1K

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Protein

Ribonucleoside-diphosphate reductase small chain

Gene

UL40

Organism
Human herpesvirus 1 (strain KOS) (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.By similarity

Catalytic activityi

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

Cofactori

Binds 2 iron ions per subunit.By similarity

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  2. DNA replication Source: UniProtKB-UniPathway
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)
Alternative name(s):
Ribonucleotide reductase 38 kDa subunit
Ribonucleotide reductase small subunit
Gene namesi
Name:UL40
OrganismiHuman herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10306 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Ribonucleoside-diphosphate reductase small chainPRO_0000190504Add
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.By similarity

Structurei

3D structure databases

ProteinModelPortaliP06474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

P06474-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSAAPALSP ALTAHTGHSA TADLAIQIPK CPDPERYFYT SQCPDINHLR
60 70 80 90 100
SLSILNRWLE TELVFVGDEE DVSKLSEGEL SFYRFLFAFL SAADDLVTEN
110 120 130 140 150
LGGLSGLFEQ KDILHYYVEQ ECIEVAHSRV YNIIQLVLFH NNDQARREYV
160 170 180 190 200
AGTINHPAIR AKVDWLEARV RECASVPEKF ILMILIEGIF FAASFAAIAY
210 220 230 240 250
LRTNNLLRVT CQSNDLISRD EAVHTTASCY IYNNYLGGHA KPPPDRVYGL
260 270 280 290 300
FRQAVEIEIG FIRSQAPTDS HILSPAALAA IENYVRFSAD RLLGLIHMKP
310 320 330 340
LFSAPPPDAS FPLSLMSTDK HTNFFECRST SYAGAVVNDL
Length:340
Mass (Da):37,966
Last modified:November 1, 1995 - v2
Checksum:i921DC04B9D278DE5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02212 Genomic DNA. Translation: AAA66436.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02212 Genomic DNA. Translation: AAA66436.1 .

3D structure databases

ProteinModelPortali P06474.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P06474.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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

  1. "Detailed characterization of an apparently unspliced beta herpes simplex virus type 1 gene mapping in the interior of another."
    Draper K.G., Frink R.J., Wagner E.K.
    J. Virol. 43:1123-1128(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Wagner E.K.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "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_HHV1K
AccessioniPrimary (citable) accession number: P06474
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3