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Q9LSD0 (RIR2C_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. 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 C

EC=1.17.4.1
Alternative name(s):
Ribonucleoside-diphosphate reductase TSO2 subunit
Ribonucleotide reductase small subunit C
Gene names
Name:TSO2
Ordered Locus Names:At3g27060
ORF Names:MOJ10.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Ref.4

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 chain By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in roots, cauline leaves, stems and flowers. Ref.4

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Ribonucleoside-diphosphate reductase small chain C
PRO_0000254195

Sites

Active site1141 By similarity
Metal binding761Iron 1 By similarity
Metal binding1071Iron 1 By similarity
Metal binding1071Iron 2 By similarity
Metal binding1101Iron 1 By similarity
Metal binding1691Iron 2 By similarity
Metal binding2031Iron 2 By similarity
Metal binding2061Iron 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LSD0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9EADC6E82B4DFCE1

FASTA33238,034
        10         20         30         40         50         60 
MPSMPEEPLL TPTPDRFCMF PIHYPQIWEM YKKAEASFWT AEEVDLSQDN RDWENSLNDG 

        70         80         90        100        110        120 
ERHFIKHVLA FFAASDGIVL ENLASRFMSD VQVSEARAFY GFQIAIENIH SEMYSLLLDT 

       130        140        150        160        170        180 
YIKDNKERDH LFRAIETIPC VAKKAQWAMK WIDGSQTFAE RIIAFACVEG IFFSGSFCSI 

       190        200        210        220        230        240 
FWLKKRGLMP GLTFSNELIS RDEGLHCDFA CLLYTLLKTK LSEERVKSIV CDAVEIEREF 

       250        260        270        280        290        300 
VCDALPCALV GMNRDLMSQY IEFVADRLLG ALGYGKVYGV TNPFDWMELI SLQGKTNFFE 

       310        320        330 
KRVGDYQKAS VMSSVNGNGA FDNHVFSLDE DF 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Arabidopsis ribonucleotide reductases are critical for cell cycle progression, DNA damage repair, and plant development."
Wang C., Liu Z.
Plant Cell 18:350-365(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB026649 Genomic DNA. Translation: BAB01087.1.
CP002686 Genomic DNA. Translation: AEE77261.1.
AY063837 mRNA. Translation: AAL36193.1.
AY117212 mRNA. Translation: AAM51287.1.
RefSeqNP_189342.1. NM_113620.3.
UniGeneAt.24911.
At.74191.

3D structure databases

ProteinModelPortalQ9LSD0.
SMRQ9LSD0. Positions 6-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid7654. 1 interaction.

Proteomic databases

PRIDEQ9LSD0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G27060.1; AT3G27060.1; AT3G27060.
GeneID822324.
KEGGath:AT3G27060.

Organism-specific databases

GeneFarm2091. 386.
TAIRAT3G27060.

Phylogenomic databases

InParanoidQ9LSD0.
KOK10808.
OMAGMPEIEY.
PhylomeDBQ9LSD0.
ProtClustDBPLN02492.

Enzyme and pathway databases

BioCycARA:AT3G27060-MONOMER.
UniPathwayUPA00326.

Gene expression databases

ArrayExpressQ9LSD0.
GenevestigatorQ9LSD0.

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...

Entry information

Entry nameRIR2C_ARATH
AccessionPrimary (citable) accession number: Q9LSD0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names