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P36603 (RIR2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 small chain

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase small subunit
Gene names
Name:suc22
ORF Names:SPBC25D12.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Nucleus. Cytoplasm. Note: Localization to the cytoplasm is CSN- and checkpoint-dependent and is required for an efficient DNA damage response. Ref.3

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentCytoplasm
Nucleus
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   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

purine deoxyribonucleoside triphosphate biosynthetic process

Inferred by curator. Source: PomBase

purine nucleoside metabolic process

Inferred by curator. Source: PomBase

pyrimidine deoxyribonucleoside triphosphate biosynthetic process

Inferred by curator. Source: PomBase

pyrimidine nucleoside metabolic process

Inferred by curator. Source: PomBase

regulation of DNA-dependent DNA replication

Traceable author statement PubMed 16252005. Source: PomBase

   Cellular_componentcytoplasm

Inferred from direct assay Ref.3. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

nucleus

Inferred from direct assay Ref.3PubMed 16823372. Source: PomBase

ribonucleoside-diphosphate reductase complex

Traceable author statement Ref.1. Source: PomBase

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.3. Source: PomBase

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 – 391391Ribonucleoside-diphosphate reductase small chain
PRO_0000190463

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

Experimental info

Sequence conflict285 – 2884VVEA → LLKP in CAA46231. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36603 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 740ECDBECC8D0170

FASTA39145,405
        10         20         30         40         50         60 
MGLEHLEEFS YPKEHGEEVE YDSEQGVRKI YVKSIKETFN FDNVSEEEKQ EGGDYYLGKK 

        70         80         90        100        110        120 
EDELDEVVLR PNPHRFVLFP IKYHEIWQFY KKAEASFWTA EEIDLSKDLV DWDNKLNADE 

       130        140        150        160        170        180 
RYFISTVLAY FAASDGIVNE NLLERFSSEV QIPEARCVYG FQIMIENIHS ETYSLLLDTY 

       190        200        210        220        230        240 
IREPKEKQRH FDAILTMGSI KAKAKWALRW INDEDSTYAI RLVAFAAVEG IFFSGSFASI 

       250        260        270        280        290        300 
FWLKKRGLMP GLTFSNELIC RDEGLHTDFA CLMFSHLKHR PGRKVVEAII VEAVDIEKEY 

       310        320        330        340        350        360 
FTDALPVSLL GMNKDLMCQY IEFVADRLLV ALGNDKYYNV TNPFDFMENI SLAGKTNFFE 

       370        380        390 
KKVSDYQIAG VMSGTKRAEK DDHTFTIDED F 

« Hide

References

« Hide 'large scale' references
[1]"The cell cycle genes cdc22+ and suc22+ of the fission yeast Schizosaccharomyces pombe encode the large and small subunits of ribonucleotide reductase."
Fernandez-Sarabia M.J., McInerny C., Harris P., Gordon C., Fantes P.
Mol. Gen. Genet. 238:241-251(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms."
Liu C., Powell K.A., Mundt K., Wu L., Carr A.M., Caspari T.
Genes Dev. 17:1130-1140(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65115 Genomic DNA. Translation: CAA46231.1.
CU329671 Genomic DNA. Translation: CAA20100.1.
PIRS34808.
T39992.
RefSeqNP_596546.1. NM_001022467.2.

3D structure databases

ProteinModelPortalP36603.
SMRP36603. Positions 60-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276910. 3 interactions.
MINTMINT-4688905.
STRING4896.SPBC25D12.04-1.

Proteomic databases

MaxQBP36603.
PaxDbP36603.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC25D12.04.1; SPBC25D12.04.1:pep; SPBC25D12.04.
GeneID2540381.
KEGGspo:SPBC25D12.04.

Organism-specific databases

PomBaseSPBC25D12.04.

Phylogenomic databases

eggNOGCOG0208.
HOGENOMHOG000255975.
KOK10808.
OMADWAINWI.
OrthoDBEOG7T1RMH.
PhylomeDBP36603.

Enzyme and pathway databases

UniPathwayUPA00326.

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

NextBio20801509.
PROP36603.

Entry information

Entry nameRIR2_SCHPO
AccessionPrimary (citable) accession number: P36603
Secondary accession number(s): O74355
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: June 11, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways