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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

War-055

Organism
African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.

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, dGTP favors ADP reduction and dTTP favors GDP reduction (By similarity).By similarity

Pathwayi: DNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei177SubstrateBy similarity1
Sitei193Important for hydrogen atom transferBy similarity1
Sitei200Allosteric effector bindingBy similarity1
Binding sitei221Substrate; via amide nitrogenBy similarity1
Sitei230Allosteric effector bindingBy similarity1
Active sitei419Proton acceptorBy similarity1
Active sitei421Cysteine radical intermediateBy similarity1
Active sitei423Proton acceptorBy similarity1
Sitei439Important for hydrogen atom transferBy similarity1
Sitei747Important for electron transferBy similarity1
Sitei748Important for electron transferBy similarity1
Sitei773Interacts with thioredoxin/glutaredoxinBy similarity1
Sitei776Interacts with thioredoxin/glutaredoxinBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, 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:War-055
OrganismiAfrican swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV)
Taxonomic identifieri561444 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
Virus hostiOrnithodoros (relapsing fever ticks) [TaxID: 6937]
Phacochoerus aethiopicus (Warthog) [TaxID: 85517]
Phacochoerus africanus (Warthog) [TaxID: 41426]
Potamochoerus larvatus (Bushpig) [TaxID: 273792]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000000858 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003552211 – 778Ribonucleoside-diphosphate reductase large subunitAdd BLAST778

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi193 ↔ 439Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Expressioni

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 193Substrate bindingBy similarity2
Regioni419 – 423Substrate bindingBy similarity5
Regioni613 – 617Substrate bindingBy similarity5

Sequence similaritiesi

Family and domain databases

InterProiIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C8H9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METFCIETLA SDTYGKALNV DLDRLSQAQI KYTLQELISY CSALTILHYD
60 70 80 90 100
YSTLAARLSV YQLHQSTASS FSKAVRLQAA QSCSRLSPQF VDVVYKYKAI
110 120 130 140 150
FDSYIDYNRD YKLSLLGIET MKNSYLLKNK DGVIMERPQD AYMRVAIMIY
160 170 180 190 200
GMGKVVNIKM ILLTYDLLSQ HIITHASPTM FNAGTKKPQL SSCFLLNVND
210 220 230 240 250
NLENLYDMVK TAGIISGGGG GIGLCLSGIR AKNSFISGSG LRSNGIQNYI
260 270 280 290 300
MLQNASQCYA NQGGLRPGAY AVYLELWHQD IFTFLEMPRL KGQMAEQRLN
310 320 330 340 350
APNLKYGLWV PDLFMEILED QIHNRGDGRW YLFSPDQAPN LHKVFDLERS
360 370 380 390 400
QHENAHREFK KLYYQYVAEK RYTGVTTAKE IIKAWFKTVI QVGNPYIGFK
410 420 430 440 450
DAINRKSNLS HVGTITNSNL CIEVTIPCWE GDKAEQGVCN LAAVNLAAFI
460 470 480 490 500
RENGYDYRGL IEASGNVTEN LDNIIDNGYY PTEATRRSNM RHRPIGIGVF
510 520 530 540 550
GLADVFASLK IKFGSPEAIA MDEAIHAALY YGAMRRSIEL AKEKGSHPSF
560 570 580 590 600
PGSAASKGLL QPDLWVRCGD LIPSWEERVA QTTQGVLTRK SWRQLRLAAI
610 620 630 640 650
QGVRNGYLTA LMPTATSSNS TGKNECFEPF TSNLYTRRTL SGEFIVLNKY
660 670 680 690 700
LIDDLKEINL WTEAIQLQLL NAGGSIQHIL DIPAEIRDRY KTSREMNQKI
710 720 730 740 750
LTKHAAARNP FVSQSMSLNY YFYEPELSQV LTVLVLGWKK GLTTGSYYCH
760 770
FSPGAGTQKK IIRNSEKACN ADCEACLL
Length:778
Mass (Da):87,402
Last modified:November 25, 2008 - v1
Checksum:i5F0D50259308371F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY261366 Genomic DNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY261366 Genomic DNA. No translation available.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00326.

Family and domain databases

InterProiIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRIR1_ASFWA
AccessioniPrimary (citable) accession number: P0C8H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: January 7, 2015
This is version 23 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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.