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P12848 (RIR1_VACCW) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 89. 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
Ordered Locus Names:VACWR073
ORF Names:I4L
OrganismVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) [Reference proteome]
Taxonomic identifier10254 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length771 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.

Catalytic activity

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

Cofactor

Mg2+. Maximal ribonucleotide reductase activity requires the presence of magnesium ions. Ref.4

Enzyme regulation

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, whereas dGTP favors ADP reduction and dTTP favors GDP reduction By similarity.

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.

Induction

Expressed early in the viral replicative cycle. Ref.1

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Contains 1 ATP-cone domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0 and above. Ref.4

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 771771Ribonucleoside-diphosphate reductase large subunit
PRO_0000187232

Regions

Domain1 – 9292ATP-cone
Region217 – 2182Substrate binding By similarity
Region427 – 4315Substrate binding By similarity
Region602 – 6065Substrate binding By similarity

Sites

Active site4271Proton acceptor By similarity
Active site4291Cysteine radical intermediate By similarity
Active site4311Proton acceptor By similarity
Binding site2021Substrate By similarity
Binding site2471Substrate; via amide nitrogen By similarity
Site2181Important for hydrogen atom transfer By similarity
Site2261Allosteric effector binding By similarity
Site2561Allosteric effector binding By similarity
Site4441Important for hydrogen atom transfer By similarity
Site7351Important for electron transfer By similarity
Site7361Important for electron transfer By similarity
Site7661Interacts with thioredoxin/glutaredoxin By similarity
Site7691Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond218 ↔ 444Redox-active 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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
[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] [Europe PMC] [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].
[4]"Vaccinia virus ribonucleotide reductase expression and isolation of the recombinant large subunit."
Slabaugh M.B., Davis R.E., Roseman N.A., Mathews C.K.
J. Biol. Chem. 268:17803-17810(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03399 Genomic DNA. Translation: AAB59806.1.
M20299 Genomic DNA. Translation: AAA48274.1.
AY243312 Genomic DNA. Translation: AAO89352.1.
PIRWZVZH4. A28611.
RefSeqYP_232955.1. NC_006998.1.

3D structure databases

ProteinModelPortalP12848.
SMRP12848. Positions 15-752.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-2158N.
IntActP12848. 1 interaction.
MINTMINT-131002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3707606.

Phylogenomic databases

ProtClustDBCLSP2509774.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
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: October 16, 2013
This is version 89 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