P36603 (RIR2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	DNA replication
Cellular component	Cytoplasm Nucleus
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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_component	cytoplasm 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_function	metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 391	391	Ribonucleoside-diphosphate reductase small chain		PRO_0000190463
Sites
	Active site	173	1	By similarity
	Metal binding	135	1	Iron 1 By similarity
	Metal binding	166	1	Iron 1 By similarity
	Metal binding	166	1	Iron 2 By similarity
	Metal binding	169	1	Iron 1 By similarity
	Metal binding	229	1	Iron 2 By similarity
	Metal binding	263	1	Iron 2 By similarity
	Metal binding	266	1	Iron 2 By similarity
Experimental info
	Sequence conflict	285 – 288	4	VVEA → LLKP in CAA46231. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36603 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 740ECDBECC8D0170	FASTA	391	45,405
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	S34808. T39992.
RefSeq	NP_596546.1. NM_001022467.2.
3D structure databases
ProteinModelPortal	P36603.
SMR	P36603. Positions 60-349.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	276910. 3 interactions.
MINT	MINT-4688905.
STRING	4896.SPBC25D12.04-1.
Proteomic databases
MaxQB	P36603.
PaxDb	P36603.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC25D12.04.1; SPBC25D12.04.1:pep; SPBC25D12.04.
GeneID	2540381.
KEGG	spo:SPBC25D12.04.
Organism-specific databases
PomBase	SPBC25D12.04.
Phylogenomic databases
eggNOG	COG0208.
HOGENOM	HOG000255975.
KO	K10808.
OMA	DWAINWI.
OrthoDB	EOG7T1RMH.
PhylomeDB	P36603.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR012348. RNR-rel. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
SUPFAM	SSF47240. SSF47240. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801509.
PRO	P36603.

Entry information

Entry name

RIR2_SCHPO

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program