P48592 (RIR2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase subunit M2
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase small subunit

Gene names

Name:	RnrS
ORF Names:	CG8975

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	DNA replication
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype PubMed 17310982. Source: FlyBase deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro neurogenesis Inferred from mutant phenotype PubMed 21549331. Source: FlyBase
Cellular_component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	Ribonucleoside-diphosphate reductase subunit M2		PRO_0000190454
Sites
	Active site	180	1	By similarity
	Metal binding	142	1	Iron 1 By similarity
	Metal binding	173	1	Iron 1 By similarity
	Metal binding	173	1	Iron 2 By similarity
	Metal binding	176	1	Iron 1 By similarity
	Metal binding	236	1	Iron 2 By similarity
	Metal binding	270	1	Iron 2 By similarity
	Metal binding	273	1	Iron 2 By similarity
Amino acid modifications
	Modified residue	18	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P48592 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 0784173BCF1F6D9A	FASTA	393	45,115
	10 20 30 40 50 60 MASKENIADN MEKFSLKSPS KKILTDSTNN VRKMSIGHEA NGQLAKESST VNGIGKSANS 70 80 90 100 110 120 LMEKSVTPFD PSLEPLLREN PRRFVIFPIQ YHDIWQMYKK AEASFWTVEE VDLSKDLTDW 130 140 150 160 170 180 HRLKDDERHF ISHVLAFFAA SDGIVNENLV ERFSQEVQIT EARCFYGFQI AMENVHSEMY 190 200 210 220 230 240 SVLIDTYIRD PHQREYLFNA IETMPAVKRK ADWALSWISS KSANFGERII AFAAVEGIFF 250 260 270 280 290 300 SGSFASIFWL KKRGLMPGLT FSNELISRDE GLHCDFAVLM FQHLVQRPKR ERIIEIIRDA 310 320 330 340 350 360 VAIEQEFLTD ALPVNLIGMN CDLMSQYIEF VADRLLVELG VGKIYNTKNP FNFMEMISLD 370 380 390 GKTNFFEKKV GEYQRMGVVS NPLDNVFTLD ADF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Developmental control of a G1-S transcriptional program in Drosophila." Duronio R.J., O'Farrell P.H. Development 120:1503-1515(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-362. Strain: Oregon-R.
[5]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013599 Genomic DNA. Translation: AAF58599.2. AY051936 mRNA. Translation: AAK93360.1. U09370 Genomic DNA. Translation: AAA56996.1.
RefSeq	NP_525111.1. NM_080372.3.
UniGene	Dm.569.
3D structure databases
ProteinModelPortal	P48592.
SMR	P48592. Positions 74-351.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-18112N.
IntAct	P48592. 3 interactions.
MINT	MINT-336377.
STRING	7227.FBpp0087152.
Proteomic databases
PaxDb	P48592.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0088046; FBpp0087152; FBgn0011704.
GeneID	36280.
KEGG	dme:Dmel_CG8975.
Organism-specific databases
CTD	36280.
FlyBase	FBgn0011704. RnrS.
Phylogenomic databases
eggNOG	COG0208.
GeneTree	ENSGT00390000013305.
InParanoid	P48592.
KO	K10808.
OMA	ICNRRCQ.
OrthoDB	EOG47H45H.
PhylomeDB	P48592.
Enzyme and pathway databases
UniPathway	UPA00326.
Gene expression databases
Bgee	P48592.
GermOnline	CG8975. Drosophila melanogaster.
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. Ferritin/RR_like. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RnrS. drosophila.
GenomeRNAi	36280.
NextBio	797712.

Entry information

Entry name

RIR2_DROME

Accession

Primary (citable) accession number: P48592
Secondary accession number(s): Q9V640

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project