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NUD21_ARATH
ID   NUD21_ARATH             Reviewed;         198 AA.
AC   Q8VY81; Q9FX46;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Nudix hydrolase 21, chloroplastic;
DE            Short=AtNUDT21;
DE            EC=3.6.1.-;
DE   Flags: Precursor;
GN   Name=NUDT21; Synonyms=NUDX21; OrderedLocusNames=At1g73540;
GN   ORFNames=T9L24.30;
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
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).
RN   [4]
RP   NOMENCLATURE.
RX   PubMed=15878881; DOI=10.1074/jbc.m503536200;
RA   Ogawa T., Ueda Y., Yoshimura K., Shigeoka S.;
RT   "Comprehensive analysis of cytosolic nudix hydrolases in Arabidopsis
RT   thaliana.";
RL   J. Biol. Chem. 280:25277-25283(2005).
RN   [5]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=18815383; DOI=10.1104/pp.108.128413;
RA   Ogawa T., Yoshimura K., Miyake H., Ishikawa K., Ito D., Tanabe N.,
RA   Shigeoka S.;
RT   "Molecular characterization of organelle-type Nudix hydrolases in
RT   Arabidopsis.";
RL   Plant Physiol. 148:1412-1424(2008).
CC   -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC       diphosphate derivatives. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and
CC       inflorescences. {ECO:0000269|PubMed:18815383}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:18815383}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG30977.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC012396; AAG30977.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE35473.1; -; Genomic_DNA.
DR   EMBL; AY072369; AAL62361.1; -; mRNA.
DR   EMBL; BT002080; AAN72091.1; -; mRNA.
DR   PIR; B96762; B96762.
DR   RefSeq; NP_177495.2; NM_106012.6.
DR   AlphaFoldDB; Q8VY81; -.
DR   SMR; Q8VY81; -.
DR   STRING; 3702.AT1G73540.1; -.
DR   PaxDb; Q8VY81; -.
DR   PRIDE; Q8VY81; -.
DR   ProteomicsDB; 234939; -.
DR   EnsemblPlants; AT1G73540.1; AT1G73540.1; AT1G73540.
DR   GeneID; 843688; -.
DR   Gramene; AT1G73540.1; AT1G73540.1; AT1G73540.
DR   KEGG; ath:AT1G73540; -.
DR   Araport; AT1G73540; -.
DR   TAIR; locus:2206835; AT1G73540.
DR   eggNOG; KOG2839; Eukaryota.
DR   HOGENOM; CLU_037162_5_2_1; -.
DR   InParanoid; Q8VY81; -.
DR   OMA; EIWPECG; -.
DR   OrthoDB; 1324716at2759; -.
DR   PhylomeDB; Q8VY81; -.
DR   BioCyc; ARA:AT1G73540-MON; -.
DR   PRO; PR:Q8VY81; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8VY81; baseline and differential.
DR   Genevisible; Q8VY81; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Hydrolase; Magnesium; Manganese; Metal-binding; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..198
FT                   /note="Nudix hydrolase 21, chloroplastic"
FT                   /id="PRO_0000019963"
FT   DOMAIN          59..191
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           98..119
FT                   /note="Nudix box"
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  22636 MW;  BEB7EE8229210F59 CRC64;
     MISLFISNFS NLSNLSPTFD NMNMNIPSKK IVPVPTPSEK VVSLVSRTGR DLQRYNTAGY
     RQVVGCVPYR YKKHGGGEIE VLLISAQKKG KGMLLPKGGW EIDESIEEAA LRETIEEAGV
     TGQLEESLGK WQYKSKRHTM IHDGHMFPLL VSQQFEIWPE SEFRQRKWVS LSEAIELCQN
     SWMREALEAF INRKCQTQ
 
 
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