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Q196Z5 (RIR1_IIV3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase large subunit

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase large subunit
Gene names
ORF Names:IIV3-065R
OrganismInvertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus) [Reference proteome]
Taxonomic identifier345201 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageIridoviridaeChloriridovirus
Virus hostAedes vexans (Inland floodwater mosquito) (Culex vexans) [TaxID: 7163]
Culex territans [TaxID: 42431]
Culiseta annulata [TaxID: 332058]
Ochlerotatus sollicitans (eastern saltmarsh mosquito) [TaxID: 310513]
Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus) [TaxID: 329105]
Psorophora ferox [TaxID: 7183]

Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Enzyme regulation

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction 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 large chain family.

Ontologies

Keywords
   Biological processDNA replication
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 630630Ribonucleoside-diphosphate reductase large subunit
PRO_0000376950

Regions

Region82 – 832Substrate binding By similarity
Region317 – 3215Substrate binding By similarity
Region459 – 4635Substrate binding By similarity

Sites

Active site3171Proton acceptor By similarity
Active site3191Cysteine radical intermediate By similarity
Active site3211Proton acceptor By similarity
Binding site671Substrate By similarity
Binding site1111Substrate; via amide nitrogen By similarity
Site831Important for hydrogen atom transfer By similarity
Site901Allosteric effector binding By similarity
Site1191Allosteric effector binding By similarity
Site3341Important for hydrogen atom transfer By similarity
Site5971Important for electron transfer By similarity
Site5981Important for electron transfer By similarity
Site6251Interacts with thioredoxin/glutaredoxin By similarity
Site6281Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond83 ↔ 334Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q196Z5 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: B4F309D57AD92677

FASTA63071,757
        10         20         30         40         50         60 
MITIDESRNN LFDALGLQRL KDSYMKEDES SPQERFAFIA RQFCADDEPL AQRLYDYMSQ 

        70         80         90        100        110        120 
HWLSPSSPQL SFGRTKQGLP IACFLPYLHD TARGLIDTWA EVSELSMIGG GIGLGVGIRQ 

       130        140        150        160        170        180 
PDEKSVGIIP HLRTYDASCT AYKQGQTRRG SYAAYLDISH PEILSFLNTR RVGGDHNYKL 

       190        200        210        220        230        240 
LNLHNGVNVP DSFMKKIWIL STLAPFVKMD PCPTTETLFK KAVTTLKDSR YFGADDRWLG 

       250        260        270        280        290        300 
EVSFAALAEQ LDVVNRWDLI DPHTGKVKET IKATELWERI ILTRAETGEP YIHWIDTSNR 

       310        320        330        340        350        360 
ALPQFQKNLG LSIRQSNLCS EVVLPTDETR TAVCCLASLN LDYFDKWCNN EQFYLDVATY 

       370        380        390        400        410        420 
LDNVLQYFID HAPPTLKRAV HSARSERAIG IGALGFHSYL QSKMVDIESL PAYLINKKIF 

       430        440        450        460        470        480 
KTISSHLERV NLELGELRGE APDCVGTGRR FSHMTAIAPN ATSSIIMGNT SPSCEPFRAN 

       490        500        510        520        530        540 
IYKQDTISGS FVTYNKHLKR LLEERIPDNQ ARERVWSSIK MHDGSVQHLN QLTVQEKKVF 

       550        560        570        580        590        600 
KTWPEINQLS LVMLAADRQK WIDQSQSTSL FFNPDERISY VHKIHLKAWL HGLKTLYYFR 

       610        620        630 
SRKILTVDKV HHTTTTADPK TENDCTFCEG 

« Hide

References

[1]"Genome of invertebrate iridescent virus type 3 (mosquito iridescent virus)."
Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A., Kutish G.F., Rock D.L.
J. Virol. 80:8439-8449(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ643392 Genomic DNA. Translation: ABF82095.1.
RefSeqYP_654637.1. NC_008187.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4156315.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 2 hits.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIR1_IIV3
AccessionPrimary (citable) accession number: Q196Z5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways