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Q01037 (RIR1_SHV21) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:61
Synonyms:EELF2
OrganismSaimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri) [Reference proteome]
Taxonomic identifier10383 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeRhadinovirus
Virus hostSaimiri sciureus (Common squirrel monkey) [TaxID: 9521]

Protein attributes

Sequence length767 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
   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

   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 – 767767Ribonucleoside-diphosphate reductase large subunit
PRO_0000187243

Regions

Region191 – 1922Substrate binding By similarity
Region392 – 3965Substrate binding By similarity
Region578 – 5825Substrate binding By similarity

Sites

Active site3921Proton acceptor By similarity
Active site3941Cysteine radical intermediate By similarity
Active site3961Proton acceptor By similarity
Binding site1761Substrate By similarity
Binding site2221Substrate; via amide nitrogen By similarity
Site1921Important for hydrogen atom transfer By similarity
Site4081Important for hydrogen atom transfer By similarity
Site7091Important for electron transfer By similarity
Site7101Important for electron transfer By similarity
Site7631Interacts with thioredoxin/glutaredoxin By similarity
Site7661Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond192 ↔ 408Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01037 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: FE5922B11FFCA6DF

FASTA76787,216
        10         20         30         40         50         60 
MSQETIISNL IDMLKVSAGW DREANEISGR LFHKLMDMSS TETISQYMSL FGPLLEPHIL 

        70         80         90        100        110        120 
EFIQNYEQEI DEVCLEYRAS YDFMCLRNCG ILPAKRFYDT YVLPPRTEMN GKYESIPHFF 

       130        140        150        160        170        180 
ARIAAYCAWN CIMCEPLKDT LVYVQKRDWN VEIKTDMQIF KYFYKVISSQ LVCCATPVMR 

       190        200        210        220        230        240 
SAGVAGENLS SCFIIAPTLD TEKSTISSIF GELAPLLASR SGVGVDVTKF SFGGKNIHSC 

       250        260        270        280        290        300 
LKLINAQVEF FNDKSVRPVS VATYIEVWHC QIHEFLSAKL PENPDRCNSI FQGVCVPSLF 

       310        320        330        340        350        360 
FKMYESDPNG LWYLFDPQDA PNLTRLYGLE FEEEYLRLVS EKKYKQSVTL KSLMFSLINT 

       370        380        390        400        410        420 
IIKTGSPYVI SKEAMNKHHW YETQGEAINC SNLCAEIVQQ PKQFTSTCNL ANVCLPKCLN 

       430        440        450        460        470        480 
SSNFPYTCSN TAQFDFSKLE YAVQAAVFII NACILSPSPT SSATVGQRER SMGIGCHGLA 

       490        500        510        520        530        540 
DVFSEMGYGY LDLESECLDR DIFETMYYTA VKTSSEICSV GKGQPFAGFR KSKLAHGVFH 

       550        560        570        580        590        600 
WATWDAMPQR VPMKQWIHLQ DNIKKFGVFN SQFIALMPTA GTSQLTGYTD SFYPYFANMS 

       610        620        630        640        650        660 
SKVSNKEEIM KPNITFLKNV KPQDLCTVRF YGGDVSMMPE DVSTRYKHFL TAFDYCPEAQ 

       670        680        690        700        710        720 
MRRASIRAPY VDQSQSLTLF LTEENVQSAK YLKDLLLLGF RLGLKTIMYY CRVKKTTKLL 

       730        740        750        760 
QLECLKLDEH TKKDAQIVLA DLARELPDSH KTEDACPLDQ SECIACQ 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the herpesvirus saimiri genome."
Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B., Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B., Honess R.W.
J. Virol. 66:5047-5058(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus saimiri (HVS) L-DNA: general conservation of genetic organization between HVS and Epstein-Barr virus."
Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.
Virology 188:296-310(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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
X64346 Genomic DNA. Translation: CAA45684.1.
M86409 Genomic DNA. Translation: AAA46137.1.
RefSeqNP_040263.1. NC_001350.1.

3D structure databases

ProteinModelPortalQ01037.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1682460.

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_SHV21
AccessionPrimary (citable) accession number: Q01037
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: May 14, 2014
This is version 75 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