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Reviewed, UniProtKB/Swiss-Prot P12848 (RIR1_VACCW)

Last modified June 16, 2009. Version 66. 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
Ordered Locus Names: VACWR073
ORF Names: I4L
OrganismVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Taxonomic identifier10254 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length771 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.

Contains 1 ATP-cone domain.

Ontologies

Keywords
   Biological processDNA replication
   Developmental stageEarly protein
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   Technical termAllosteric enzyme
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

protein binding

Inferred from electronic annotation. Source: InterPro

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 – 771771Ribonucleoside-diphosphate reductase large subunit
PRO_0000187232

Regions

Domain1 – 9292ATP-cone

Sites

Active site2181Hydrogen atom transfer By similarity
Active site4271Proton acceptor By similarity
Active site4291Proton acceptor By similarity
Active site4311Proton acceptor By similarity
Active site4441Hydrogen atom transfer By similarity
Active site7351Electron transfer By similarity
Active site7361Electron transfer By similarity
Site2261Allosteric effector binding By similarity
Site2561Allosteric effector binding By similarity
Site7661Interacts with thioredoxin/glutaredoxin By similarity
Site7691Interacts with thioredoxin/glutaredoxin By similarity

Experimental info

Sequence conflict4471A → G in AAA48274. Ref.2
Sequence conflict4671D → V in AAA48274. Ref.2
Sequence conflict5261L → I in AAA48274. Ref.2
Sequence conflict601 – 6066MPTAST → LPLHQH in AAA48274. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P12848-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 6CA07F0C58F6A8F9

FASTA77187,738
        10         20         30         40         50         60 
MFVIKRNGYK ENVMFDKITS RIRKLCYGLN TDHIDPIKIA MKVIQGIYNG VTTVELDTLA 

        70         80         90        100        110        120 
AEIAATCTTQ HPDYAILAAR IAVSNLHKET KKLFSEVMED LFNYVNPKNG KHSPIISSIT 

       130        140        150        160        170        180 
MDIVNKYKDK LNSVIIYERD FSYNYFGFKT LEKSYLLKIN NKIVERPQHM LMRVAVGIHQ 

       190        200        210        220        230        240 
WDIDSAIETY NLLSEKWFTH ASPTLFNAGT SRHQMSSCFL LNMIDDSIEG IYDTLKRCAL 

       250        260        270        280        290        300 
ISKMAGGIGL SISNIRASGS YISGTNGISN GIIPMLRVYN NTARYIDQGG NKRPGVMAIY 

       310        320        330        340        350        360 
LEPWHSDIMA FLDLKKNTGN EEHRTRDLFI ALWIPDLFMK RVKDDGEWSL MCPDECPGLD 

       370        380        390        400        410        420 
NVWGDEFERL YTLYERERRY KSIIKARVVW KAIIESQIET GTPFILYKDA CNKKSNQQNL 

       430        440        450        460        470        480 
GTIKCSNLCT EIIQYADANE VAVCNLASVA LNMFVIDGRF DFLKLKDVVK VIVRNLNKII 

       490        500        510        520        530        540 
DINYYPIPEA EISNKRHRPI GIGVQGLADA FILLNYPFDS LEAQDLNKKI FETIYYGALE 

       550        560        570        580        590        600 
ASCELAEKEG PYDTYVGSYA SNGILQYDLW NVVPSDLWNW EPLKDKIRTY GLRNSLLVAP 

       610        620        630        640        650        660 
MPTASTAQIL GNNESVEPYT SNIYTRRVLS GEFQVVNPHL LRVLTERKLW NDEIKNRIMA 

       670        680        690        700        710        720 
DGGSIQNTNL PEDIKRVYKT IWEIPQKTII KMAADRGAFI DQSQSMNIHI ADPSYSKLTS 

       730        740        750        760        770 
MHFYGWSLGL KTGMYYLRTK PASAPIQFTL DKDKIKPPVV CDSEICTSCS G 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and transcriptional analysis of the vaccinia virus HindIII I fragment."
Schmitt J.F.C., Stunnenberg H.G.
J. Virol. 62:1889-1897(1988) [PubMed: 2835495] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence and molecular genetic analysis of the large subunit of ribonucleotide reductase encoded by vaccinia virus."
Tengelsen L.A., Slabaugh M.B., Bibler J.K., Hruby D.E.
Virology 164:121-131(1988) [PubMed: 3284177] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."
Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

J03399 Genomic DNA. Translation: AAB59806.1.
M20299 Genomic DNA. Translation: AAA48274.1.
AY243312 Genomic DNA. Translation: AAO89352.1.
PIRWZVZH4. A28611.
RefSeqYP_232955.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2158N.

Genome annotation databases

GeneID3707606.

Family and domain databases

InterProIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR013509. Ribncl_Rdtase_lsu_N.
IPR000788. Ribncl_red_lg_C.
[Graphical view]
PANTHERPTHR11573. Ribncl_red_lg_C. 1 hit.
PfamPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_VACCW
AccessionPrimary (citable) accession number: P12848
Secondary accession number(s): Q76ZU9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 16, 2009
This is version 66 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