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P09853 (RIR1_HHV23) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 83. 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 136 kDa subunit
Ribonucleotide reductase large subunit
OrganismHuman herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2)
Taxonomic identifier10313 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1144 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.

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
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 – 11441144Ribonucleoside-diphosphate reductase large subunit
PRO_0000187237

Regions

Region588 – 5892Substrate binding By similarity
Region798 – 8025Substrate binding By similarity
Region975 – 9795Substrate binding By similarity
Compositional bias151 – 1599Poly-Pro
Compositional bias224 – 2318Poly-Asp

Sites

Active site7981Proton acceptor By similarity
Active site8001Cysteine radical intermediate By similarity
Active site8021Proton acceptor By similarity
Binding site5731Substrate By similarity
Binding site6191Substrate; via amide nitrogen By similarity
Site5891Important for hydrogen atom transfer By similarity
Site8151Important for hydrogen atom transfer By similarity
Site11181Important for electron transfer By similarity
Site11191Important for electron transfer By similarity
Site11391Interacts with thioredoxin/glutaredoxin By similarity
Site11421Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond589 ↔ 815Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P09853 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 4771481C3103FC78

FASTA1,144125,093
        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 DEDTGSGSET LSRSSSIWAA GATDDDDSDS DSRSDDSVQP 

       250        260        270        280        290        300 
DVVVRRRWSD GPAPVAFPKP RRPGDSPGNP GLGAGTGPGS ATDPRASADS DSAAHAAAPQ 

       310        320        330        340        350        360 
ADVAPVLDSQ PTVGTDPGYP VPLELTPENA EAVARFLGDA VDREPALMLE YFCRCAREES 

       370        380        390        400        410        420 
KRVPPRTFGS APRLTEDDFG LLNYALAEMR RLCLDLPPVP PNAYTPYHLR EYATRLVNGF 

       430        440        450        460        470        480 
KPLVRRSARL YRILGILVHL RIRTREASFE EWMRSKEVDL DFGLTERLRE HEAQLMILAQ 

       490        500        510        520        530        540 
ALNPYDCLIH STPNTLVERG LQSALKYEEF YLKRFGGHYM ESVFQMYTRI AGFLACRATR 

       550        560        570        580        590        600 
GMRHIALGRQ GSWWEMFKFF FHRLYDHQIV PSTPAMLNLG TRNYYTSSCY LVNPQATTNQ 

       610        620        630        640        650        660 
ATLRAITGNV SAILARNGGI GLCMQAFNDA SPGTASIMPA LKVLDSLVAA HNKQSTRPTG 

       670        680        690        700        710        720 
ACVYLEPWHS DVRAVLRMKG VLAGEEAQRC DNIFSALWMP DLFFKRLIRH LDGEKNVTWS 

       730        740        750        760        770        780 
LFDRDTSMSL ADFHGEEFEK LYEHLEAMGF GETIPIQDLA YAIVRSAATT GSPFIMFKDA 

       790        800        810        820        830        840 
VNRHYIYDTQ GAAIAGSNLC TEIVHPSSKR SSGVCNLGSV NLARCVSRRT FDFGMLRDAV 

       850        860        870        880        890        900 
QACVLMVNIM IDSTLQPTPQ CARGHDNLRS MGIGMQGLHT ACLKMGLDLE SAEFRDLNTH 

       910        920        930        940        950        960 
IAEVMLLAAM KTSNALCVRG ARPFSHFKRS MYRAGRFHWE RFSNASPRYE GEWEMLRQSM 

       970        980        990       1000       1010       1020 
MKHGLRNSQF IALMPTAASA QISDVSEGFA PLFTNLFSKV TRDGETLRPN TLLLKELERT 

      1030       1040       1050       1060       1070       1080 
FGGKRLLDAM DGLEAKQWSV AQALPCLDPA HPLRRFKTAF DYDQELLIDL CADRAPYVDH 

      1090       1100       1110       1120       1130       1140 
SQSMTLYVTE KADGTLPAST LVRLLVHAYK RGLKTGMYYC KVRKATNSGV FAGDDNIVCT 


SCAL 

« Hide

References

[1]"Herpes simplex virus specifies two subunits of ribonucleotide reductase encoded by 3'-coterminal transcripts."
Swain M.A., Galloway D.A.
J. Virol. 57:802-808(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Organization of the left-hand end of the herpes simplex virus type 2 BglII N fragment."
Galloway D.A., Swain M.A.
J. Virol. 49:724-730(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 981-1144.
[3]"DNA sequence homology between two co-linear loci on the HSV genome which have different transforming abilities."
McLauchlan J., Clements J.B.
EMBO J. 2:1953-1961(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1036-1144.
[4]"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
M12700 Genomic DNA. Translation: AAA45806.1.
X00048 Genomic DNA. Translation: CAA24929.1.

3D structure databases

ProteinModelPortalP09853.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP09853.

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_HHV23
AccessionPrimary (citable) accession number: P09853
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: December 11, 2013
This is version 83 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