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P08543

- RIR1_HHV11

UniProt

P08543 - RIR1_HHV11

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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene
UL39
Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei566 – 5661Substrate By similarity
Sitei582 – 5821Important for hydrogen atom transfer By similarity
Binding sitei612 – 6121Substrate; via amide nitrogen By similarity
Active sitei791 – 7911Proton acceptor By similarity
Active sitei793 – 7931Cysteine radical intermediate By similarity
Active sitei795 – 7951Proton acceptor By similarity
Sitei808 – 8081Important for hydrogen atom transfer By similarity
Sitei1111 – 11111Important for electron transfer By similarity
Sitei1112 – 11121Important for electron transfer By similarity
Sitei1132 – 11321Interacts with thioredoxin/glutaredoxin By similarity
Sitei1135 – 11351Interacts with thioredoxin/glutaredoxin By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
  2. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication, Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Short name:
R1
Alternative name(s):
ICP6
Ribonucleotide reductase 136 kDa subunit
Ribonucleotide reductase large subunit
Gene namesi
ORF Names:UL39
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000009294: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11371137Ribonucleoside-diphosphate reductase large subunitPRO_0000187236Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi582 ↔ 808Redox-active By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

IntActiP08543. 2 interactions.
MINTiMINT-6732628.

Structurei

3D structure databases

ProteinModelPortaliP08543.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 393107alpha-crystallin domain By similarityAdd
BLAST
Regioni581 – 5822Substrate binding By similarity
Regioni791 – 7955Substrate binding By similarity
Regioni968 – 9725Substrate binding By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi150 – 1545Poly-Pro
Compositional biasi190 – 23950Asp/Ser-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Family and domain databases

InterProiIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08543-1 [UniParc]FASTAAdd to Basket

« Hide

MASRPAASSP VEARAPVGGQ EAGGPSAATQ GEAAGAPLAH GHHVYCQRVN     50
GVMVLSDKTP GSASYRISDN NFVQCGSNCT MIIDGDVVRG RPQDPGAAAS 100
PAPFVAVTNI GAGSDGGTAV VAFGGTPRRS AGTSTGTQTA DVPTEALGGP 150
PPPPRFTLGG GCCSCRDTRR RSAVFGGEGD PVGPAEFVSD DRSSDSDSDD 200
SEDTDSETLS HASSDVSGGA TYDDALDSDS SSDDSLQIDG PVCRPWSNDT 250
APLDVCPGTP GPGADAGGPS AVDPHAPTPE AGAGLAADPA VARDDAEGLS 300
DPRPRLGTGT AYPVPLELTP ENAEAVARFL GDAVNREPAL MLEYFCRCAR 350
EETKRVPPRT FGSPPRLTED DFGLLNYALV EMQRLCLDVP PVPPNAYMPY 400
YLREYVTRLV NGFKPLVSRS ARLYRILGVL VHLRIRTREA SFEEWLRSKE 450
VALDFGLTER LREHEAQLVI LAQALDHYDC LIHSTPHTLV ERGLQSALKY 500
EEFYLKRFGG HYMESVFQMY TRIAGFLACR ATRGMRHIAL GREGSWWEMF 550
KFFFHRLYDH QIVPSTPAML NLGTRNYYTS SCYLVNPQAT TNKATLRAIT 600
SNVSAILARN GGIGLCVQAF NDSGPGTASV MPALKVLDSL VAAHNKESAR 650
PTGACVYLEP WHTDVRAVLR MKGVLAGEEA QRCDNIFSAL WMPDLFFKRL 700
IRHLDGEKNV TWTLFDRDTS MSLADFHGEE FEKLYQHLEV MGFGEQIPIQ 750
ELAYGIVRSA ATTGSPFVMF KDAVNRHYIY DTQGAAIAGS NLCTEIVHPA 800
SKRSSGVCNL GSVNLARCVS RQTFDFGRLR DAVQACVLMV NIMIDSTLQP 850
TPQCTRGNDN LRSMGIGMQG LHTACLKLGL DLESAEFQDL NKHIAEVMLL 900
SAMKTSNALC VRGARPFNHF KRSMYRAGRF HWERFPDARP RYEGEWEMLR 950
QSMMKHGLRN SQFVALMPTA ASAQISDVSE GFAPLFTNLF SKVTRDGETL 1000
RPNTLLLKEL ERTFSGKRLL EVMDSLDAKQ WSVAQALPCL EPTHPLRRFK 1050
TAFDYDQKLL IDLCADRAPY VDHSQSMTLY VTEKADGTLP ASTLVRLLVH 1100
AYKRGLKTGM YYCKVRKATN SGVFGGDDNI VCMSCAL 1137
Length:1,137
Mass (Da):124,051
Last modified:July 1, 1989 - v2
Checksum:i8A3777F4C22D8F85
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701N → S in strain: Nonneuroinvasive mutant HF10, 17 syn+ and Isolate pYN1.
Natural varianti1133 – 11331M → T in strain: Nonneuroinvasive mutant HF10.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1034 – 10341A → P in AAA45805. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14112 Genomic DNA. Translation: CAA32314.1.
M18410 Genomic DNA. Translation: AAA45805.1.
DQ889502 Genomic DNA. Translation: ABI63501.1.
FJ593289 Genomic DNA. Translation: ACM62262.1.
PIRiA26536. WMBEB1.
RefSeqiNP_044641.1. NC_001806.1.

Genome annotation databases

GeneIDi2703361.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14112 Genomic DNA. Translation: CAA32314.1 .
M18410 Genomic DNA. Translation: AAA45805.1 .
DQ889502 Genomic DNA. Translation: ABI63501.1 .
FJ593289 Genomic DNA. Translation: ACM62262.1 .
PIRi A26536. WMBEB1.
RefSeqi NP_044641.1. NC_001806.1.

3D structure databases

ProteinModelPortali P08543.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P08543. 2 interactions.
MINTi MINT-6732628.

Chemistry

BindingDBi P08543.
ChEMBLi CHEMBL3840.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2703361.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

InterProi IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
[Graphical view ]
Pfami PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiRIR1_HHV11
AccessioniPrimary (citable) accession number: P08543
Secondary accession number(s): B9VQG7, Q09I94
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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