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P12848

- RIR1_VACCW

UniProt

P12848 - RIR1_VACCW

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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

VACWR073

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).By similarity

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Maximal ribonucleotide reductase activity requires the presence of Mg(2+) 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).By similarity

pH dependencei

Optimum pH is 8.0 and above.1 Publication

Pathwayi

Sites

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 771771Ribonucleoside-diphosphate reductase large subunitPRO_0000187232Add
BLAST

Amino acid modifications

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP12848.
SMRiP12848. Positions 15-752.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-conePROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MFVIKRNGYK ENVMFDKITS RIRKLCYGLN TDHIDPIKIA MKVIQGIYNG
60 70 80 90 100
VTTVELDTLA AEIAATCTTQ HPDYAILAAR IAVSNLHKET KKLFSEVMED
110 120 130 140 150
LFNYVNPKNG KHSPIISSIT MDIVNKYKDK LNSVIIYERD FSYNYFGFKT
160 170 180 190 200
LEKSYLLKIN NKIVERPQHM LMRVAVGIHQ WDIDSAIETY NLLSEKWFTH
210 220 230 240 250
ASPTLFNAGT SRHQMSSCFL LNMIDDSIEG IYDTLKRCAL ISKMAGGIGL
260 270 280 290 300
SISNIRASGS YISGTNGISN GIIPMLRVYN NTARYIDQGG NKRPGVMAIY
310 320 330 340 350
LEPWHSDIMA FLDLKKNTGN EEHRTRDLFI ALWIPDLFMK RVKDDGEWSL
360 370 380 390 400
MCPDECPGLD NVWGDEFERL YTLYERERRY KSIIKARVVW KAIIESQIET
410 420 430 440 450
GTPFILYKDA CNKKSNQQNL GTIKCSNLCT EIIQYADANE VAVCNLASVA
460 470 480 490 500
LNMFVIDGRF DFLKLKDVVK VIVRNLNKII DINYYPIPEA EISNKRHRPI
510 520 530 540 550
GIGVQGLADA FILLNYPFDS LEAQDLNKKI FETIYYGALE ASCELAEKEG
560 570 580 590 600
PYDTYVGSYA SNGILQYDLW NVVPSDLWNW EPLKDKIRTY GLRNSLLVAP
610 620 630 640 650
MPTASTAQIL GNNESVEPYT SNIYTRRVLS GEFQVVNPHL LRVLTERKLW
660 670 680 690 700
NDEIKNRIMA DGGSIQNTNL PEDIKRVYKT IWEIPQKTII KMAADRGAFI
710 720 730 740 750
DQSQSMNIHI ADPSYSKLTS MHFYGWSLGL KTGMYYLRTK PASAPIQFTL
760 770
DKDKIKPPVV CDSEICTSCS G
Length:771
Mass (Da):87,738
Last modified:October 1, 1989 - v1
Checksum:i6CA07F0C58F6A8F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti447 – 4471A → G in AAA48274. (PubMed:3284177)Curated
Sequence conflicti467 – 4671D → V in AAA48274. (PubMed:3284177)Curated
Sequence conflicti526 – 5261L → I in AAA48274. (PubMed:3284177)Curated
Sequence conflicti601 – 6066MPTAST → LPLHQH in AAA48274. (PubMed:3284177)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 93 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