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P79733 (RIR2_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 114. 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 subunit M2

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase protein R2 class I
Ribonucleotide reductase small chain
Ribonucleotide reductase small subunit
Gene names
Name:rrm2
Synonyms:r2
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activity

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

Cofactor

Binds 2 iron ions per subunit By similarity.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterodimer of a large and a small subunit.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

deoxyribonucleoside diphosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion 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 – 386386Ribonucleoside-diphosphate reductase subunit M2
PRO_0000190452

Sites

Active site1731 By similarity
Metal binding1351Iron 1 By similarity
Metal binding1661Iron 1 By similarity
Metal binding1661Iron 2 By similarity
Metal binding1691Iron 1 By similarity
Metal binding2291Iron 2 By similarity
Metal binding2631Iron 2 By similarity
Metal binding2661Iron 2 By similarity

Amino acid modifications

Modified residue61Phosphoserine Ref.4
Modified residue311Phosphothreonine Ref.4

Experimental info

Sequence conflict2791N → S in AAH75746. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P79733 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: C168846FB57F9F4E

FASTA38644,594
        10         20         30         40         50         60 
MSSTRSPLKT KNENTISTKM NNMSFVDKEN TPPSLSSTRI LASKTARKIF DESEGQSKAK 

        70         80         90        100        110        120 
KGAVEEEPLL KENPHRFVIF PIQYHDIWQM YKKAEASFWT AEEVDLSKDL QHWDSLKDEE 

       130        140        150        160        170        180 
RYFISHVLAF FAASDGIVNE NLVERFTQEV QVTEARCFYG FQIAMENIHS EMYSLLIDTY 

       190        200        210        220        230        240 
IKDSKEREFL FNAIETMPCV KKKADWALNW IGDKNARYGE RVVAFAAVEG IFFSGSFASI 

       250        260        270        280        290        300 
FWLKKRGLMP GLTFSNELIS RDEGLHCDFA CLMFKHLINK PSEETVKKII MNAVEIEQEF 

       310        320        330        340        350        360 
LTDALPVKLI GMNCDLMKQY IEFVADRLLL ELGFDKVYRV ENPFDFMENI SLEGKTNFFE 

       370        380 
KRVGEYQRMG VMSGTTDNTF TLDADF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of cDNAs encoding ribonucleotide reductase from zebrafish Danio rerio."
Mathews C.Z., Sjoeberg B.-M., Karlsson M.
Mol. Mar. Biol. Biotechnol. 5:284-287(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[3]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: AB.
Tissue: Embryo.
[4]"Online automated in vivo zebrafish phosphoproteomics: from large-scale analysis down to a single embryo."
Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J., Slijper M., Heck A.J.R.
J. Proteome Res. 7:1555-1564(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND THR-31, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57965 mRNA. Translation: AAB37103.1.
BX248136 Genomic DNA. Translation: CAI21240.1.
BC044355 mRNA. Translation: AAH44355.1.
BC075746 mRNA. Translation: AAH75746.1.
RefSeqNP_571525.1. NM_131450.2.
XP_002665783.1. XM_002665737.2.
XP_005170223.1. XM_005170166.1.
UniGeneDr.75098.

3D structure databases

ProteinModelPortalP79733.
SMRP79733. Positions 26-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000008907.

Proteomic databases

PRIDEP79733.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000027851; ENSDARP00000008907; ENSDARG00000020711.
ENSDART00000112155; ENSDARP00000103553; ENSDARG00000078069.
GeneID100330864.
30733.
KEGGdre:100330864.
dre:30733.

Organism-specific databases

CTD6241.
ZFINZDB-GENE-990415-25. rrm2.

Phylogenomic databases

eggNOGCOG0208.
GeneTreeENSGT00390000013305.
HOGENOMHOG000255975.
HOVERGENHBG001647.
InParanoidP79733.
KOK10808.
OMAGVMNSTK.
OrthoDBEOG7VMP5N.
PhylomeDBP79733.
TreeFamTF300465.

Enzyme and pathway databases

UniPathwayUPA00326.

Gene expression databases

BgeeP79733.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20807081.
PROP79733.

Entry information

Entry nameRIR2_DANRE
AccessionPrimary (citable) accession number: P79733
Secondary accession number(s): Q6DI44
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: May 14, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways