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Q6Y657 (RIR2B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:
Putative ribonucleoside-diphosphate reductase small chain B

EC=1.17.4.1
Alternative name(s):
Ribonucleoside-diphosphate reductase R2B subunit
Ribonucleotide reductase small subunit B
Gene names
Name:RNR2B
Ordered Locus Names:At5g40942
ORF Names:MMG1.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceUncertain

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Ref.1

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, rosette leaves, stems and flowers. Ref.1

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Caution

Could be the product of a pseudogene in cv. Columbia. The N-terminus is shortened due to a frameshift in position 140. The resulting sequence lacks the conserved features of the family.

Sequence caution

The sequence AAO42187.1 differs from that shown. Reason: Frameshift at position 140.

The sequence AB023040 differs from that shown. Reason: Frameshift at position 140.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentCytoplasm
   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

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 – 333333Putative ribonucleoside-diphosphate reductase small chain B
PRO_0000254194

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

Experimental info

Sequence conflict2211L → F Ref.2
Sequence conflict2211L → F in AAO42187. Ref.3
Sequence conflict2461P → S Ref.2
Sequence conflict2461P → S in AAO42187. Ref.3
Sequence conflict2751A → G Ref.2
Sequence conflict2751A → G in AAO42187. Ref.3
Sequence conflict2811S → T Ref.2
Sequence conflict2811S → T in AAO42187. Ref.3
Sequence conflict3111I → V Ref.2
Sequence conflict3111I → V in AAO42187. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q6Y657 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: CA20B044F92DB922

FASTA33338,331
        10         20         30         40         50         60 
MPSMPEEPIL TPTPDRFCMF PIQYPQIWEM YKKAEASFWT AEEVDLSQDN RDWENSLTND 

        70         80         90        100        110        120 
ERHFIKHVLA FFAASDGIVL ENLSTRFMSD VQISEARAFY GFQIAIENIH SEMYSLLLDT 

       130        140        150        160        170        180 
YIKDNKERDH LFRAIETIPC VTKKAEWAMK WINGSQSFAE RIVAFACVEG IFFSGSFCSI 

       190        200        210        220        230        240 
FWLKKRGLMP GLTFSNELIS RDEGLHCDFA CLIYSLLRTK LDEDRLKAIV CDAVEIEREF 

       250        260        270        280        290        300 
VCDALPCALV GMNRELMSQY IEFVADRLLA ALGCAKVYGV SNPFDWMELI SLQGKTNFFE 

       310        320        330 
KRVGEYQKAS IMSSVHGNAA FNDDHVFKLD EDF 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
Strain: cv. Landsberg erecta.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. XI."
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY178109 mRNA. Translation: AAO62422.1.
AB023040 Genomic DNA. No translation available.
BT004167 mRNA. Translation: AAO42187.1. Frameshift.

3D structure databases

ProteinModelPortalQ6Y657.
SMRQ6Y657. Positions 6-287.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ6Y657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GeneFarm2199. 386.
TAIRAT5G40942.

Phylogenomic databases

eggNOGCOG0208.
HOGENOMHOG000255975.

Enzyme and pathway databases

BRENDA1.17.4.2. 399.
UniPathwayUPA00326.

Gene expression databases

ArrayExpressQ6Y657.
GenevestigatorQ6Y657.

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 nameRIR2B_ARATH
AccessionPrimary (citable) accession number: Q6Y657
Secondary accession number(s): Q84W71
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 70 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