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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei177 – 1771SubstrateBy similarity
Sitei193 – 1931Important for hydrogen atom transferBy similarity
Sitei200 – 2001Allosteric effector bindingBy similarity
Binding sitei221 – 2211Substrate; via amide nitrogenBy similarity
Sitei230 – 2301Allosteric effector bindingBy similarity
Active sitei419 – 4191Proton acceptorBy similarity
Active sitei421 – 4211Cysteine radical intermediateBy similarity
Active sitei423 – 4231Proton acceptorBy similarity
Sitei439 – 4391Important for hydrogen atom transferBy similarity
Sitei747 – 7471Important for electron transferBy similarity
Sitei748 – 7481Important for electron transferBy similarity
Sitei773 – 7731Interacts with thioredoxin/glutaredoxinBy similarity
Sitei776 – 7761Interacts 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, 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]
ProteomesiUP000000858: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 778778Ribonucleoside-diphosphate reductase large subunitPRO_0000355221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 1932Substrate bindingBy similarity
Regioni419 – 4235Substrate bindingBy similarity
Regioni613 – 6175Substrate bindingBy similarity

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...

Publicationsi

  1. "African swine fever virus genomes."
    Kutish G.F., Rock D.L.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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

External Data

Dasty 3

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 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.