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P12848

- RIR1_VACCW

UniProt

P12848 - RIR1_VACCW

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Protein
Ribonucleoside-diphosphate reductase large subunit
Gene
VACWR073, I4L
Organism
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Mg2+. Maximal ribonucleotide reductase activity requires the presence of magnesium ions.1 Publication

Enzyme regulationi

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.

pH dependencei

Optimum pH is 8.0 and above.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei202 – 2021Substrate By similarity
Sitei218 – 2181Important for hydrogen atom transfer By similarity
Sitei226 – 2261Allosteric effector binding By similarity
Binding sitei247 – 2471Substrate; via amide nitrogen By similarity
Sitei256 – 2561Allosteric effector binding By similarity
Active sitei427 – 4271Proton acceptor By similarity
Active sitei429 – 4291Cysteine radical intermediate By similarity
Active sitei431 – 4311Proton acceptor By similarity
Sitei444 – 4441Important for hydrogen atom transfer By similarity
Sitei735 – 7351Important for electron transfer By similarity
Sitei736 – 7361Important for electron transfer By similarity
Sitei766 – 7661Interacts with thioredoxin/glutaredoxin By similarity
Sitei769 – 7691Interacts with thioredoxin/glutaredoxin By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase large subunit
Gene namesi
Ordered Locus Names:VACWR073
ORF Names:I4L
OrganismiVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Taxonomic identifieri10254 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000000344: Genome

Subcellular locationi

GO - Cellular componenti

  1. ribonucleoside-diphosphate reductase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 771771Ribonucleoside-diphosphate reductase large subunit
PRO_0000187232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi218 ↔ 444Redox-active By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Expressed early in the viral replicative cycle.1 Publication

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

DIPiDIP-2158N.
IntActiP12848. 1 interaction.
MINTiMINT-131002.

Structurei

3D structure databases

ProteinModelPortaliP12848.
SMRiP12848. Positions 15-752.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-cone
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni217 – 2182Substrate binding By similarity
Regioni427 – 4315Substrate binding By similarity
Regioni602 – 6065Substrate binding By similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.

Family and domain databases

InterProiIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12848-1 [UniParc]FASTAAdd to Basket

« Hide

MFVIKRNGYK ENVMFDKITS RIRKLCYGLN TDHIDPIKIA MKVIQGIYNG    50
VTTVELDTLA AEIAATCTTQ HPDYAILAAR IAVSNLHKET KKLFSEVMED 100
LFNYVNPKNG KHSPIISSIT MDIVNKYKDK LNSVIIYERD FSYNYFGFKT 150
LEKSYLLKIN NKIVERPQHM LMRVAVGIHQ WDIDSAIETY NLLSEKWFTH 200
ASPTLFNAGT SRHQMSSCFL LNMIDDSIEG IYDTLKRCAL ISKMAGGIGL 250
SISNIRASGS YISGTNGISN GIIPMLRVYN NTARYIDQGG NKRPGVMAIY 300
LEPWHSDIMA FLDLKKNTGN EEHRTRDLFI ALWIPDLFMK RVKDDGEWSL 350
MCPDECPGLD NVWGDEFERL YTLYERERRY KSIIKARVVW KAIIESQIET 400
GTPFILYKDA CNKKSNQQNL GTIKCSNLCT EIIQYADANE VAVCNLASVA 450
LNMFVIDGRF DFLKLKDVVK VIVRNLNKII DINYYPIPEA EISNKRHRPI 500
GIGVQGLADA FILLNYPFDS LEAQDLNKKI FETIYYGALE ASCELAEKEG 550
PYDTYVGSYA SNGILQYDLW NVVPSDLWNW EPLKDKIRTY GLRNSLLVAP 600
MPTASTAQIL GNNESVEPYT SNIYTRRVLS GEFQVVNPHL LRVLTERKLW 650
NDEIKNRIMA DGGSIQNTNL PEDIKRVYKT IWEIPQKTII KMAADRGAFI 700
DQSQSMNIHI ADPSYSKLTS MHFYGWSLGL KTGMYYLRTK PASAPIQFTL 750
DKDKIKPPVV CDSEICTSCS G 771
Length:771
Mass (Da):87,738
Last modified:October 1, 1989 - v1
Checksum:i6CA07F0C58F6A8F9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti447 – 4471A → G in AAA48274. 1 Publication
Sequence conflicti467 – 4671D → V in AAA48274. 1 Publication
Sequence conflicti526 – 5261L → I in AAA48274. 1 Publication
Sequence conflicti601 – 6066MPTAST → LPLHQH in AAA48274. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03399 Genomic DNA. Translation: AAB59806.1.
M20299 Genomic DNA. Translation: AAA48274.1.
AY243312 Genomic DNA. Translation: AAO89352.1.
PIRiA28611. WZVZH4.
RefSeqiYP_232955.1. NC_006998.1.

Genome annotation databases

GeneIDi3707606.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03399 Genomic DNA. Translation: AAB59806.1 .
M20299 Genomic DNA. Translation: AAA48274.1 .
AY243312 Genomic DNA. Translation: AAO89352.1 .
PIRi A28611. WZVZH4.
RefSeqi YP_232955.1. NC_006998.1.

3D structure databases

ProteinModelPortali P12848.
SMRi P12848. Positions 15-752.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-2158N.
IntActi P12848. 1 interaction.
MINTi MINT-131002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3707606.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

InterProi IPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiRIR1_VACCW
AccessioniPrimary (citable) accession number: P12848
Secondary accession number(s): Q76ZU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 14, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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