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P48592 (RIR2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 104. 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
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 small subunit
Gene names
Name:RnrS
ORF Names:CG8975
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length393 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Ribonucleoside-diphosphate reductase subunit M2
PRO_0000190454

Sites

Active site1801 By similarity
Metal binding1421Iron 1 By similarity
Metal binding1731Iron 1 By similarity
Metal binding1731Iron 2 By similarity
Metal binding1761Iron 1 By similarity
Metal binding2361Iron 2 By similarity
Metal binding2701Iron 2 By similarity
Metal binding2731Iron 2 By similarity

Amino acid modifications

Modified residue181Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P48592 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 0784173BCF1F6D9A

FASTA39345,115
        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

« Hide

References

« Hide '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. expand/collapse author list , 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: 10731132] [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. expand/collapse author list , 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: 12537572] [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: 12537569] [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: 8050359] [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: 18327897] [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.
RefSeqNP_525111.1. NM_080372.2.
UniGeneDm.569.

3D structure databases

ProteinModelPortalP48592.
SMRP48592. Positions 74-351.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-18112N.
IntActP48592. 3 interactions.
MINTMINT-336377.
STRINGP48592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088046; FBpp0087152; FBgn0011704.
GeneID36280.
KEGGdme:Dmel_CG8975.
NMPDRfig|7227.3.peg.4731.

Organism-specific databases

CTD36280.
FlyBaseFBgn0011704. RnrS.

Phylogenomic databases

eggNOGinNOG06274.
GeneTreeEMGT00050000008448.
InParanoidP48592.
OMAFNMYREV.
OrthoDBEOG47H45H.
PhylomeDBP48592.

Gene expression databases

ArrayExpressP48592.
BgeeP48592.
GermOnlineCG8975. Drosophila melanogaster.

Family and domain databases

InterProIPR009078. Ferritin/RR-like.
IPR012348. Ribncl_red-rel.
IPR000358. Ribonucl_redctse.
[Graphical view]
Gene3DG3DSA:1.10.620.20. Ribncl_red_rel. 1 hit.
KOK10808.
PANTHERPTHR23409. Ribonucl_redctse. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF47240. Ferritin/RR_like. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio797712.

Entry information

Entry nameRIR2_DROME
AccessionPrimary (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: January 25, 2012
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents