Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P28846 (RIR1_EHV1B) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 71. 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
Name:21
OrganismEquine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus) [Complete proteome]
Taxonomic identifier31520 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeVaricellovirus
Virus hostEquus caballus (Horse) [TaxID: 9796]

Protein attributes

Sequence length790 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
   Technical termComplete proteome
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 – 790790Ribonucleoside-diphosphate reductase large subunit
PRO_0000187241

Regions

Region223 – 2242Substrate binding By similarity
Region436 – 4405Substrate binding By similarity
Region621 – 6255Substrate binding By similarity

Sites

Active site4361Proton acceptor By similarity
Active site4381Cysteine radical intermediate By similarity
Active site4401Proton acceptor By similarity
Binding site2081Substrate By similarity
Binding site2541Substrate; via amide nitrogen By similarity
Site2241Important for hydrogen atom transfer By similarity
Site4531Important for hydrogen atom transfer By similarity
Site7651Important for electron transfer By similarity
Site7661Important for electron transfer By similarity
Site7851Interacts with thioredoxin/glutaredoxin By similarity
Site7881Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond224 ↔ 453Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P28846 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: D8A21677716F5844

FASTA79088,399
        10         20         30         40         50         60 
MALNFLQSDC PLAIIQDVIS RVDAISDYGY ANELSTTLPP RPSRSQVLEY ITRVVDTLKP 

        70         80         90        100        110        120 
RCRVDERLYV VCGELVHLRI RTRNVEDLKY WLNSTEIALN EIVEKDILDH LDFIQRTLHA 

       130        140        150        160        170        180 
FESSEYRELC ALGLQSALKY EEMYLAKMRG GRIESMGQFF LRLATTATHY TMEEPAMARV 

       190        200        210        220        230        240 
LVSGEVGWTY IFKAYFTALA GQVLIPATPI MLFGGRDCGS LASCYLLNPR VTDMNSAMLA 

       250        260        270        280        290        300 
LMEEAGPILC NRGGIGLSLQ RFNTPPKEGC SRGVMALLKL IDSMTMAINS DGERPTGVCV 

       310        320        330        340        350        360 
YFEPWHADIR AILNMRGMLA RDETVRCDNI FACMWTPDLF FDRYQRYLDG ESGVMWTLFD 

       370        380        390        400        410        420 
DTASHLCHMY GKEFEEEYER LEQCGFGVDS IPIQDMAFII VRSAVMTGSP FLMFKDACNK 

       430        440        450        460        470        480 
HYHFDLRRKG AIMGSNLCTE IIQHADETQN GVCNLASINL PKCLAIPPPH TAGVPYFDFA 

       490        500        510        520        530        540 
ALGRAAATAT IFVNSMMRAG TYPTVKSQRG VDENRSLGLG IQGLHTAFLM LDLDMASPEA 

       550        560        570        580        590        600 
RQLNKQIAER LLLNSMKASA TLCRLGMKPF KGFEDSKYSL GELPFDSYPG VTLANRNAWR 

       610        620        630        640        650        660 
RLRTEIKQHG LYNSQFVAYM PTVSSSQVTE SSEGFSPVYT NLFSKVTATG EVLRPNLLLM 

       670        680        690        700        710        720 
RTIRSIFPRE CARLQALSTL EMAQWSVVGA FGDLPVGHPL SKFKTAFEYD QRTLIDMCAD 

       730        740        750        760        770        780 
RAPFVDQSQS MSLFITEPAD GKLPASKIMS LLVHAYKRGL KTGMYYCKIK KATNNGVFVG 

       790 
GDLVCTSCSL 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence of equine herpesvirus-1."
Telford E.A.R., Watson M.S., McBride K., Davison A.J.
Virology 189:304-316(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY665713 Genomic DNA. Translation: AAT67278.1.
PIRWMBEA2. D36797.
RefSeqYP_053066.1. NC_001491.2.

3D structure databases

ProteinModelPortalP28846.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP28846.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1487540.

Phylogenomic databases

ProtClustDBCLSP2509601.

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_EHV1B
AccessionPrimary (citable) accession number: P28846
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 16, 2013
This is version 71 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