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

P50643 (RIR1_SUHVK) 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
Gene names
Name:RR1
Synonyms:UL39
OrganismSuid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain Kaplan))
Taxonomic identifier33703 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeVaricellovirus
Virus hostSus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length835 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
   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 – 835835Ribonucleoside-diphosphate reductase large subunit
PRO_0000187244

Regions

Region277 – 2782Substrate binding By similarity
Region489 – 4935Substrate binding By similarity
Region666 – 6705Substrate binding By similarity

Sites

Active site4891Proton acceptor By similarity
Active site4911Cysteine radical intermediate By similarity
Active site4931Proton acceptor By similarity
Binding site2621Substrate By similarity
Binding site3081Substrate; via amide nitrogen By similarity
Site2781Important for hydrogen atom transfer By similarity
Site5061Important for hydrogen atom transfer By similarity
Site8101Important for electron transfer By similarity
Site8111Important for electron transfer By similarity
Site8301Interacts with thioredoxin/glutaredoxin By similarity
Site8331Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond278 ↔ 506Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P50643 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 20D4AF7366667EBA

FASTA83591,060
        10         20         30         40         50         60 
MPPRAPRPAG AVSPPFPPLA GPPLKARAPR ARDSPLTSPC RAHAAMASVV APAASSSAAA 

        70         80         90        100        110        120 
PGADAFLDAA CPEDVARALA AELEALRALG HDVGAPAPGA SRREAALFIT RAVDGLKAFS 

       130        140        150        160        170        180 
RVDERVYVAC GKLVHLRVRS READLDAWLA SPELALIPAV AAAVRRHRAR VEAALRWFWR 

       190        200        210        220        230        240 
EAYPALYARG LQSALKYEEM YLARLEHGRC EAMDQFFVRL AAAAATATRR PMALVLCGSD 

       250        260        270        280        290        300 
AWPEVFDAYF RALATQAIVP ATPLMLFAGR ARGSLASCYL LNPLPRTTEE AVRAITDEVA 

       310        320        330        340        350        360 
PILLRRGGVG LSLQSFNRTP SGDCTRGIMA VLKALDSMTA AINSDSERPT GVCVYVEPWH 

       370        380        390        400        410        420 
ADVRAVLNMR GMLAADESLR CDNIFSCLWT PDLFFQRYQR HLDGERAVKW TLFDDRASHL 

       430        440        450        460        470        480 
ASLHGPDFAR EYERLERLGL GVESLPIQDM AFLIVRSAVM TGSPFLMMKD ACNRHFHTDT 

       490        500        510        520        530        540 
RGAALATSNL CTEIVQRATP GENGVCNLAS VNLPACLAGG AFDFAALRRA ARVAAVFVNA 

       550        560        570        580        590        600 
MMRIGNYPTG ASVEGVRRSR SLGIGLQGLH TTVLALDMDM ADPAARRLNA AIAEELLYGV 

       610        620        630        640        650        660 
MDASVELCER GLRPFDGFEH SRYARGVMPF DAYERVSLRE PMRWDALRVR IAEHGVYNAQ 

       670        680        690        700        710        720 
FVALMPTVSS SQVTESSEGF SPTFTNMFSK VTISGELLRP NLPLMETLRR LFPRECARRD 

       730        740        750        760        770        780 
AVARLERAQW SVAAAFGELP AGHPLAKFKT AFEYDQELLI DMCADRAPFV DHSQSMSLFL 

       790        800        810        820        830 
TEPADGKLHA SRVMGLLMRA YNLGLKTGMY YCKIRKATNN GVFTGGDLVC TSCHL 

« Hide

References

[1]"Large and small subunits of the Aujeszky's disease virus ribonucleotide reductase: nucleotide sequence and putative structure."
Kaliman A., Boldogkoi Z., Fodor I.
Biochim. Biophys. Acta 1219:151-156(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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72087 Genomic DNA. Translation: CAA50976.1.
X80797 Genomic DNA. Translation: CAA56775.1.
PIRS40140. S47345.

3D structure databases

ProteinModelPortalP50643.
ModBaseSearch...
MobiDBSearch...

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_SUHVK
AccessionPrimary (citable) accession number: P50643
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