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Q6GZT8 (RIR1_FRG3G) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:
Putative ribonucleoside-diphosphate reductase large subunit

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase large subunit
Gene names
ORF Names:FV3-038R
OrganismFrog virus 3 (isolate Goorha) (FV-3) [Reference proteome]
Taxonomic identifier654924 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageIridoviridaeRanavirus
Virus hostAmbystoma (mole salamanders) [TaxID: 8295]
Hyla versicolor (chameleon treefrog) [TaxID: 30343]
Lithobates pipiens (Northern leopard frog) (Rana pipiens) [TaxID: 8404]
Notophthalmus viridescens (Eastern newt) (Triturus viridescens) [TaxID: 8316]
Rana sylvatica (Wood frog) [TaxID: 45438]

Protein attributes

Sequence length565 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
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionribonucleoside-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 – 565565Putative ribonucleoside-diphosphate reductase large subunit
PRO_0000410591

Regions

Region74 – 752Substrate binding By similarity
Region256 – 2605Substrate binding By similarity
Region400 – 4045Substrate binding By similarity

Sites

Active site2561Proton acceptor By similarity
Active site2581Cysteine radical intermediate By similarity
Active site2601Proton acceptor By similarity
Binding site601Substrate By similarity
Binding site1031Substrate; via amide nitrogen By similarity
Site751Important for hydrogen atom transfer By similarity
Site821Allosteric effector binding By similarity
Site1121Allosteric effector binding By similarity
Site2731Important for hydrogen atom transfer By similarity
Site5341Important for electron transfer By similarity
Site5351Important for electron transfer By similarity
Site5601Interacts with thioredoxin/glutaredoxin By similarity
Site5631Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond75 ↔ 273Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6GZT8 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 790187621FAFC2E7

FASTA56562,363
        10         20         30         40         50         60 
MTSAVSFPIT SQASDMLSKF YGSDLGSLYG TLAEKYSGGK PELAEKLRDY ACKGWFGYSS 

        70         80         90        100        110        120 
PILTSVTGSG LPISCFLLYV PDTIEGLVDH TSELRWLSVM GGGVAGHWDD VRGPSAKSCG 

       130        140        150        160        170        180 
TIPFLHTVDA DMSAYWQGKV RRGSYAAYMS ISHPDLIEFI TMRTPTGDVN RKNLNLHHGV 

       190        200        210        220        230        240 
NITDTFMRCV ERGENWDLVD PKSGAVAHTV SARELWERIL ETRFRTGEPY LNFIDTANRG 

       250        260        270        280        290        300 
LHPALKRKGL KIRGSNLCNE IHLPTAADRT AVCCLSSVNL ERYDEWRETD LVECLVEMLD 

       310        320        330        340        350        360 
NVIQTFVDEA PLKTPHTARA VRSAAGERSI GLGAMGWARY LQKHRIPFDS EEAVRLTGII 

       370        380        390        400        410        420 
FRGIKSAAVR ATRALAKERG EAPDLTGYGV RNAHLLAVAP NANSALLLGT SPSVEPEIGA 

       430        440        450        460        470        480 
AYVHRTRVGS HQAVNPYLKR DLESLGLDTE EVWDSIVSNK GSVQHIAALP DSLKKVYKTS 

       490        500        510        520        530        540 
FEMDQRVIVR QAAERQRHLC QGQSLNLFFP IGADKTNLSD VHRLAWKSGC KGLYYLRTCA 

       550        560 
GRTGHKIFEA KKNPEKTEEC TACQG 

« Hide

References

[1]"Comparative genomic analyses of frog virus 3, type species of the genus Ranavirus (family Iridoviridae)."
Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.
Virology 323:70-84(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY548484 Genomic DNA. Translation: AAT09697.1.
RefSeqYP_031616.1. NC_005946.1.

3D structure databases

ProteinModelPortalQ6GZT8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2947817.

Enzyme and pathway databases

UniPathwayUPA00326.

Family and domain databases

InterProIPR000788. RNR_lg_C.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
ProtoNetSearch...

Entry information

Entry nameRIR1_FRG3G
AccessionPrimary (citable) accession number: Q6GZT8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 40 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