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Reviewed, UniProtKB/Swiss-Prot Q01037 (RIR1_SHV21)

Last modified June 16, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activity

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

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterodimer of a large and a small chain.

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
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-diphosphate reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 767767Ribonucleoside-diphosphate reductase large subunit
PRO_0000187243

Sites

Active site1921Hydrogen atom transfer By similarity
Active site3921Proton acceptor By similarity
Active site3941Proton acceptor By similarity
Active site3961Proton acceptor By similarity
Active site4081Hydrogen atom transfer By similarity
Active site7091Electron transfer By similarity
Active site7101Electron transfer By similarity
Site2001Allosteric effector binding By similarity
Site7631Interacts with thioredoxin/glutaredoxin By similarity
Site7661Interacts with thioredoxin/glutaredoxin By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01037-1 [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: 1321287] [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: 1314457] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

X64346 Genomic DNA. Translation: CAA45684.1.
M86409 Genomic DNA. Translation: AAA46137.1.
RefSeqNP_040263.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1682460.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR013509. Ribncl_Rdtase_lsu_N.
IPR000788. Ribncl_red_lg_C.
[Graphical view]
PANTHERPTHR11573. Ribncl_red_lg_C. 1 hit.
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: June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents