ID   RI2BC_ARATH             Reviewed;         158 AA.
AC   P0DKH2; Q6Y657; Q84W71;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Putative ribonucleoside-diphosphate reductase small chain B;
DE   AltName: Full=Ribonucleoside-diphosphate reductase R2B subunit;
DE   AltName: Full=Ribonucleotide reductase small subunit B;
GN   Name=RNR2B; Synonyms=RNR2B-1; OrderedLocusNames=At5g40942; ORFNames=MMG1.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION AS A
RP   PSEUDOGENE.
RC   STRAIN=cv. Columbia;
RX   PubMed=16399800; DOI=10.1105/tpc.105.037044;
RA   Wang C., Liu Z.;
RT   "Arabidopsis ribonucleotide reductases are critical for cell cycle
RT   progression, DNA damage repair, and plant development.";
RL   Plant Cell 18:350-365(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. In strain cv. Columbia,
CC       a frameshift at position 140 results in a truncated RNR2B protein. The
CC       resulting sequence lacks the conserved features of the family. A second
CC       start codon could potentially direct the translational initiation of a
CC       second peptide homologous with TSO2 (AC Q9LSD0) at residues 141 to 332.
CC       A complete sequence for a functional RNR2B can be found in strain cv.
CC       Landsberg erecta (AC P0DKH3). {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO42187.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR   EMBL; AB023040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BT004167; AAO42187.1; ALT_SEQ; mRNA.
DR   AlphaFoldDB; P0DKH2; -.
DR   SMR; P0DKH2; -.
DR   PeptideAtlas; P0DKH2; -.
DR   PRIDE; P0DKH2; -.
DR   Araport; AT5G40942; -.
DR   BRENDA; 1.17.4.1; 399.
DR   BRENDA; 1.17.4.2; 399.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P0DKH2; baseline and differential.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR030475; RNR_small_AS.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; PTHR23409; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
PE   5: Uncertain;
KW   Reference proteome.
FT   CHAIN           1..158
FT                   /note="Putative ribonucleoside-diphosphate reductase small
FT                   chain B"
FT                   /id="PRO_0000254194"
SQ   SEQUENCE   158 AA;  18715 MW;  4436AA30D489682A CRC64;
     MPSMPEEPIL TPTPDRFCMF PIQYPQIWEM YKKAEASFWT AEEVDLSQDN RDWENSLTND
     ERHFIKHVLA FFAASDGIVL ENLSTRFMSD VQISEARAFY GFQIAIENIH SEMYSLLLDT
     YIKDNKERDH LFRAIETIPC DEKSRMGYEM DQRISKLR