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P08543 (RIR1_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. 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

Short name=R1
EC=1.17.4.1
Alternative name(s):
ICP6
Ribonucleotide reductase 136 kDa subunit
Ribonucleotide reductase large subunit
Gene names
ORF Names:UL39
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1137 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. 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.

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 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.

Domain

Contains an alpha-crystallin domain homologous to small heat-shock proteins By similarity.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Ontologies

Keywords
   Biological processDNA replication
Host-virus interaction
   Developmental stageEarly protein
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 11371137Ribonucleoside-diphosphate reductase large subunit
PRO_0000187236

Regions

Region287 – 393107alpha-crystallin domain By similarity
Region581 – 5822Substrate binding By similarity
Region791 – 7955Substrate binding By similarity
Region968 – 9725Substrate binding By similarity
Compositional bias150 – 1545Poly-Pro
Compositional bias190 – 23950Asp/Ser-rich

Sites

Active site7911Proton acceptor By similarity
Active site7931Cysteine radical intermediate By similarity
Active site7951Proton acceptor By similarity
Binding site5661Substrate By similarity
Binding site6121Substrate; via amide nitrogen By similarity
Site5821Important for hydrogen atom transfer By similarity
Site8081Important for hydrogen atom transfer By similarity
Site11111Important for electron transfer By similarity
Site11121Important for electron transfer By similarity
Site11321Interacts with thioredoxin/glutaredoxin By similarity
Site11351Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond582 ↔ 808Redox-active By similarity

Natural variations

Natural variant701N → S in strain: Nonneuroinvasive mutant HF10, 17 syn+ and Isolate pYN1.
Natural variant11331M → T in strain: Nonneuroinvasive mutant HF10.

Experimental info

Sequence conflict10341A → P in AAA45805. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08543 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 8A3777F4C22D8F85

FASTA1,137124,051
        10         20         30         40         50         60 
MASRPAASSP VEARAPVGGQ EAGGPSAATQ GEAAGAPLAH GHHVYCQRVN GVMVLSDKTP 

        70         80         90        100        110        120 
GSASYRISDN NFVQCGSNCT MIIDGDVVRG RPQDPGAAAS PAPFVAVTNI GAGSDGGTAV 

       130        140        150        160        170        180 
VAFGGTPRRS AGTSTGTQTA DVPTEALGGP PPPPRFTLGG GCCSCRDTRR RSAVFGGEGD 

       190        200        210        220        230        240 
PVGPAEFVSD DRSSDSDSDD SEDTDSETLS HASSDVSGGA TYDDALDSDS SSDDSLQIDG 

       250        260        270        280        290        300 
PVCRPWSNDT APLDVCPGTP GPGADAGGPS AVDPHAPTPE AGAGLAADPA VARDDAEGLS 

       310        320        330        340        350        360 
DPRPRLGTGT AYPVPLELTP ENAEAVARFL GDAVNREPAL MLEYFCRCAR EETKRVPPRT 

       370        380        390        400        410        420 
FGSPPRLTED DFGLLNYALV EMQRLCLDVP PVPPNAYMPY YLREYVTRLV NGFKPLVSRS 

       430        440        450        460        470        480 
ARLYRILGVL VHLRIRTREA SFEEWLRSKE VALDFGLTER LREHEAQLVI LAQALDHYDC 

       490        500        510        520        530        540 
LIHSTPHTLV ERGLQSALKY EEFYLKRFGG HYMESVFQMY TRIAGFLACR ATRGMRHIAL 

       550        560        570        580        590        600 
GREGSWWEMF KFFFHRLYDH QIVPSTPAML NLGTRNYYTS SCYLVNPQAT TNKATLRAIT 

       610        620        630        640        650        660 
SNVSAILARN GGIGLCVQAF NDSGPGTASV MPALKVLDSL VAAHNKESAR PTGACVYLEP 

       670        680        690        700        710        720 
WHTDVRAVLR MKGVLAGEEA QRCDNIFSAL WMPDLFFKRL IRHLDGEKNV TWTLFDRDTS 

       730        740        750        760        770        780 
MSLADFHGEE FEKLYQHLEV MGFGEQIPIQ ELAYGIVRSA ATTGSPFVMF KDAVNRHYIY 

       790        800        810        820        830        840 
DTQGAAIAGS NLCTEIVHPA SKRSSGVCNL GSVNLARCVS RQTFDFGRLR DAVQACVLMV 

       850        860        870        880        890        900 
NIMIDSTLQP TPQCTRGNDN LRSMGIGMQG LHTACLKLGL DLESAEFQDL NKHIAEVMLL 

       910        920        930        940        950        960 
SAMKTSNALC VRGARPFNHF KRSMYRAGRF HWERFPDARP RYEGEWEMLR QSMMKHGLRN 

       970        980        990       1000       1010       1020 
SQFVALMPTA ASAQISDVSE GFAPLFTNLF SKVTRDGETL RPNTLLLKEL ERTFSGKRLL 

      1030       1040       1050       1060       1070       1080 
EVMDSLDAKQ WSVAQALPCL EPTHPLRRFK TAFDYDQKLL IDLCADRAPY VDHSQSMTLY 

      1090       1100       1110       1120       1130 
VTEKADGTLP ASTLVRLLVH AYKRGLKTGM YYCKVRKATN SGVFGGDDNI VCMSCAL 

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Structural features of ribonucleotide reductase."
Nikas I., McLauchlan J., Davison A.J., Taylor W.R., Clements J.B.
Proteins 1:376-384(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Isolate pYN1.
[3]"Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nonneuroinvasive mutant HF10.
[4]"Herpes simplex virus type 1 bacterial artificial chromosome."
Cunningham C., Davison A.J.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 17 syn+.
[5]"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
X14112 Genomic DNA. Translation: CAA32314.1.
M18410 Genomic DNA. Translation: AAA45805.1.
DQ889502 Genomic DNA. Translation: ABI63501.1.
FJ593289 Genomic DNA. Translation: ACM62262.1.
PIRWMBEB1. A26536.
RefSeqNP_044641.1. NC_001806.1.

3D structure databases

ProteinModelPortalP08543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08543. 2 interactions.
MINTMINT-6732628.

Chemistry

BindingDBP08543.
ChEMBLCHEMBL3840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703361.

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_HHV11
AccessionPrimary (citable) accession number: P08543
Secondary accession number(s): B9VQG7, Q09I94
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 1, 1989
Last modified: May 14, 2014
This is version 95 of the entry and version 2 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