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P50642 (RIR1_EHV4) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 60. 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
OrganismEquine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus)
Taxonomic identifier10333 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeVaricellovirus
Virus hostEquus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length789 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, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.

Catalytic activity

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

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
   Developmental stageEarly protein
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 – 789789Ribonucleoside-diphosphate reductase large subunit
PRO_0000187242

Regions

Region222 – 2232Substrate binding By similarity
Region435 – 4395Substrate binding By similarity
Region620 – 6245Substrate binding By similarity

Sites

Active site4351Proton acceptor By similarity
Active site4371Cysteine radical intermediate By similarity
Active site4391Proton acceptor By similarity
Binding site2071Substrate By similarity
Binding site2531Substrate; via amide nitrogen By similarity
Site2231Important for hydrogen atom transfer By similarity
Site4521Important for hydrogen atom transfer By similarity
Site7641Important for electron transfer By similarity
Site7651Important for electron transfer By similarity
Site7841Interacts with thioredoxin/glutaredoxin By similarity
Site7871Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond223 ↔ 452Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P50642 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 7CD9A24F3147988B

FASTA78988,047
        10         20         30         40         50         60 
MALDFLSTDC PLGIVSDIIS NVNTIKEYGY SSELSTTLAP RPSREQVLEY ITRVVDKLKP 

        70         80         90        100        110        120 
LCRVDERLYI ACGELVHLRI KARNTDLKYW LKSSEIDLSD VVEQAILEHI DFVQKTLNSF 

       130        140        150        160        170        180 
ETSEYRDLCS LGLQSALKYE EMYLAKMRGG RLESMGQFFL RLATTATHYT MEQPAMARVL 

       190        200        210        220        230        240 
VSGEVGWTYI FRAFFTALAG QVVIPATPIM LFGGRDCGSM ASCYLLNPRV TDMNSAIPAL 

       250        260        270        280        290        300 
MEEVGPILCN RGGIGLSLQR FNTPPTEGCS RGVMALLKLL DSMTMAINSD GERPTGVCVY 

       310        320        330        340        350        360 
FEPWHADIRA ILNMRGMLAR DETVRCDNIF ACMWTPDLFF DRYQRYVDGE SGIMWTLFDD 

       370        380        390        400        410        420 
TASHLCHMYG NDFTREYERL ERCGFGIDAI PIQDMAFIIV RSAVMTGSPF LMFKDACNRH 

       430        440        450        460        470        480 
YHFDMRQRGA IMGSNLCTEI IQHADETQNG VCNLASINLP KCLALPPPNI AGVPYFDFAA 

       490        500        510        520        530        540 
LGRAAATATI FVNAMMCAST YPTVKSQKGV EENRSLGLGI QGLHTTFLML DLDMASPEAH 

       550        560        570        580        590        600 
QLNKQIAERL LLNSMKASAT LCKLGMQPFK GFEDSKYSRG ELPFDAYPNV TLTNRNAWRR 

       610        620        630        640        650        660 
LRTDIKQYGL YNSQFVAYMP TVSSSQVTES SEGFSPVYTN LFSKVTATGE VLRPNVLLMR 

       670        680        690        700        710        720 
TIRSIFPQEC ARLQALSTLE AAKWSVVGAF GDLPVGHPLS KFKTAFEYDQ TMLINMCADR 

       730        740        750        760        770        780 
AAFVDQSQSM SLFITEPADG KLPASRIMNL LVHAYKRGLK TGMYYCKIKK ATNNGVFVGG 


DLVCTSCSL 

« Hide

References

[1]"Sequences of the ribonucleotide reductase-encoding genes of equine herpesvirus 4."
Riggio M.P., Onions D.E.
Gene 143:217-222(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75354 Genomic DNA. Translation: CAA53100.1.

3D structure databases

ProteinModelPortalP50642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP50642. 2 interactions.
MINTMINT-6732615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_EHV4
AccessionPrimary (citable) accession number: P50642
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 60 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