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P89462 (RIR1_HHV2H) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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):
ICP10
Ribonucleotide reductase 136 kDa subunit
Ribonucleotide reductase large subunit
Gene names
ORF Names:UL39
OrganismHuman herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2) [Reference proteome]
Taxonomic identifier10315 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1142 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. Ref.3

Catalytic activity

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

ATP + a protein = ADP + a phosphoprotein.

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.

Subcellular location

Host cell membrane. Host endosome membrane. Note: Associates with the host cytoskeleton Potential. Ref.2

Domain

Contains an alpha-crystallin domain homologous to small heat-shock proteins. Ref.4

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11421142Ribonucleoside-diphosphate reductase large subunit
PRO_0000385162

Regions

Region294 – 400107alpha-crystallin domain
Region586 – 5872Substrate binding By similarity
Region796 – 8005Substrate binding By similarity
Region973 – 9775Substrate binding By similarity
Compositional bias151 – 1599Poly-Pro
Compositional bias186 – 23954Asp/Ser-rich

Sites

Active site7961Proton acceptor By similarity
Active site7981Cysteine radical intermediate By similarity
Active site8001Proton acceptor By similarity
Binding site5711Substrate By similarity
Binding site6171Substrate; via amide nitrogen By similarity
Site5871Important for hydrogen atom transfer By similarity
Site8131Important for hydrogen atom transfer By similarity
Site11161Important for electron transfer By similarity
Site11171Important for electron transfer By similarity
Site11371Interacts with thioredoxin/glutaredoxin By similarity
Site11401Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond587 ↔ 813Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P89462 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 5A46D3985338BB21

FASTA1,142124,923
        10         20         30         40         50         60 
MANRPAASAL AGARSPSERQ EPREPEVAPP GGDHVFCRKV SGVMVLSSDP PGPAAYRISD 

        70         80         90        100        110        120 
SSFVQCGSNC SMIIDGDVAR GHLRDLEGAT STGAFVAISN VAAGGDGRTA VVALGGTSGP 

       130        140        150        160        170        180 
SATTSVGTQT SGEFLHGNPR TPEPQGPQAV PPPPPPPFPW GHECCARRDA RGGAEKDVGA 

       190        200        210        220        230        240 
AESWSDGPSS DSETEDSDSS DEDTGSETLS RSSSIWAAGA TDDDDSDSDS RSDDSVQPDV 

       250        260        270        280        290        300 
VVRRRWSDGP APVAFPKPRR PGDSPGNPGL GAGTGPGSAT DPRASADSDS AAHAAAPQAD 

       310        320        330        340        350        360 
VAPVLDSQPT VGTDPGYPVP LELTPENAEA VARFLGDAVD REPALMLEYF CRCAREESKR 

       370        380        390        400        410        420 
VPPRTFGSAP RLTEDDFGLL NYALAEMRRL CLDLPPVPPN AYTPYHLREY ATRLVNGFKP 

       430        440        450        460        470        480 
LVRRSARLYR ILGVLVHLRI RTREASFEEW MRSKEVDLDF GLTERLREHE AQLMILAQAL 

       490        500        510        520        530        540 
NPYDCLIHST PNTLVERGLQ SALKYEEFYL KRFGGHYMES VFQMYTRIAG FLACRATRGM 

       550        560        570        580        590        600 
RHIALGRQGS WWEMFKFFFH RLYDHQIVPS TPAMLNLGTR NYYTSSCYLV NPQATTNQAT 

       610        620        630        640        650        660 
LRAITGNVSA ILARNGGIGL CMQAFNDASP GTASIMPALK VLDSLVAAHN KQSTRPTGAC 

       670        680        690        700        710        720 
VYLEPWHSDV RAVLRMKGVL AGEEAQRCDN IFSALWMPDL FFKRLIRHLD GEKNVTWSLF 

       730        740        750        760        770        780 
DRDTSMSLAD FHGEEFEKLY EHLEAMGFGE TIPIQDLAYA IVRSAATTGS PFIMFKDAVN 

       790        800        810        820        830        840 
RHYIYDTQGA AIAGSNLCTE IVHPASKRSS GVCNLGSVNL ARCVSRQTFD FGRLRDAVQA 

       850        860        870        880        890        900 
CVLMVNIMID STLQPTPQCT RGNDNLRSMG IGMQGLHTAC LKMGLDLESA EFRDLNTHIA 

       910        920        930        940        950        960 
EVMLLAAMKT SNALCVRGAR PFSHFKRSMY RAGRFHWERF SNASPRYEGE WEMLRQSMMK 

       970        980        990       1000       1010       1020 
HGLRNSQFIA LMPTAASAQI SDVSEGFAPL FTNLFSKVTR DGETLRPNTL LLKELERTFG 

      1030       1040       1050       1060       1070       1080 
GKRLLDAMDG LEAKQWSVAQ ALPCLDPAHP LRRFKTAFDY DQELLIDLCA DRAPYVDHSQ 

      1090       1100       1110       1120       1130       1140 
SMTLYVTEKA DGTLPASTLV RLLVHAYKRG LKTGMYYCKV RKATNSGVFA GDDNIVCTSC 


AL 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of herpes simplex virus type 2."
Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.
J. Virol. 72:2010-2021(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Intracellular internalization and signaling pathways triggered by the large subunit of HSV-2 ribonucleotide reductase (ICP10)."
Hunter J.C., Smith C.C., Bose D., Kulka M., Broderick R., Aurelian L.
Virology 210:345-360(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway."
Perkins D., Pereira E.F., Gober M., Yarowsky P.J., Aurelian L.
J. Virol. 76:1435-1449(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27."
Chabaud S., Lambert H., Sasseville A.M., Lavoie H., Guilbault C., Massie B., Landry J., Langelier Y.
FEBS Lett. 545:213-218(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALPHA-CRYSTALLIN DOMAIN.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z86099 Genomic DNA. Translation: CAB06725.1.
PIRA05247.
RefSeqNP_044509.1. NC_001798.1.

3D structure databases

ProteinModelPortalP89462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1677930. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1487325.

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_HHV2H
AccessionPrimary (citable) accession number: P89462
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 81 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