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P0C8H7 (RIR1_ASFK5) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 21. 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:Ken-057
OrganismAfrican swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV) [Complete proteome]
Taxonomic identifier561445 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
Virus hostOrnithodoros (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]

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

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, 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.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Ontologies

Keywords
   Biological processDNA replication
   Developmental stageEarly protein
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 779779Ribonucleoside-diphosphate reductase large subunit
PRO_0000355219

Regions

Region193 – 1942Substrate binding By similarity
Region420 – 4245Substrate binding By similarity
Region614 – 6185Substrate binding By similarity

Sites

Active site4201Proton acceptor By similarity
Active site4221Cysteine radical intermediate By similarity
Active site4241Proton acceptor By similarity
Binding site1781Substrate By similarity
Binding site2221Substrate; via amide nitrogen By similarity
Site1941Important for hydrogen atom transfer By similarity
Site2011Allosteric effector binding By similarity
Site2311Allosteric effector binding By similarity
Site4401Important for hydrogen atom transfer By similarity
Site7481Important for electron transfer By similarity
Site7491Important for electron transfer By similarity
Site7741Interacts with thioredoxin/glutaredoxin By similarity
Site7771Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond194 ↔ 440Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C8H7 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 7FF7134ECDC5C861

FASTA77987,767
        10         20         30         40         50         60 
MENFFIVKKL ASDTYGKALN VDLDRLLQAQ NKYTLQELIS YCSALTILHY DYSTLAARLS 

        70         80         90        100        110        120 
VYLLHQSTAS SFSEAVSLQA AQSCSRLSPQ FVDVVYKYKA IFDSYIDYSR DYKLTLLGIE 

       130        140        150        160        170        180 
TMKNSYLLKN KDGVIMERPQ DAYMRVAIMI YGMGRVVNMK MILLTYDLLS RHVITHASPT 

       190        200        210        220        230        240 
MFNAGTKKPQ LSSCFLLNVN DNLENLYDMV KTAGIISGGG GGIGLCLSGI RAKNSFISGS 

       250        260        270        280        290        300 
GLRSNGIQNY IVLQNASQCY ANQGGLRPGA YAVYLELWHQ DIFTFLQMPR LKGQMAEQRL 

       310        320        330        340        350        360 
NAPNLKYGLW VPDLFMEILE DQIHDRGDGT WYLFSPDQAP NLHKVFDLER SRHKNAHREF 

       370        380        390        400        410        420 
RKLYYQYVAE KRYTGVTTAK EIIKEWFKTV IQVGNPYIGF KDAINRKSNL SHVGTITNSN 

       430        440        450        460        470        480 
LCIEITIPCW EGSEAEQGVC NLAAVNLAAF IRENSYDYRG LIEAAGNVTE NLDNIIDNGY 

       490        500        510        520        530        540 
YPTEATRRSN MRHRPIGIGV FGLADVFASF KMKFGSPEAI AMDEAIHAAL YYGAMRRSVE 

       550        560        570        580        590        600 
LAKEKGSHPS FPGSAASKGL LQPDLWVRCD DLVFSWEERV AQTTQGVLTP KKWWQLRLAA 

       610        620        630        640        650        660 
MQGVRNGYLT ALMPTATSSN STGKNECFEP FTSNLYTRRT LSGEFIVLNK YLIDDLKEIN 

       670        680        690        700        710        720 
LWTEAIQQQL LNAGGSIQHI LDIPAEIRER YKTSREMNQK ILTKHAAARN PFVSQSMSLN 

       730        740        750        760        770 
YYFYEPELSQ VLTVLVLGWK KGLTTGSYYC HFSPGAGTQK KIIRNSEKAC SADCEACLL 

« Hide

References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY261360 Genomic DNA. No translation available.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP0C8H7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_ASFK5
AccessionPrimary (citable) accession number: P0C8H7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: October 16, 2013
This is version 21 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