ID   METL_ORYSJ              Reviewed;         371 AA.
AC   Q7XXD4; A0A0P0W730;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Probable inactive methyltransferase Os04g0175900;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=Os04g0175900, LOC_Os04g09654; ORFNames=OSJNBa0039G19.11;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22493492; DOI=10.1074/jbc.m112.351270;
RA   Shimizu T., Lin F., Hasegawa M., Okada K., Nojiri H., Yamane H.;
RT   "Purification and identification of naringenin 7-o-methyltransferase, a key
RT   enzyme in biosynthesis of flavonoid phytoalexin sakuranetin in rice.";
RL   J. Biol. Chem. 287:19315-19325(2012).
CC   -!- MISCELLANEOUS: Identified in a screen to identify naringenin 7-O-
CC       methyltransferase. However, it does not show such activity
CC       (PubMed:22493492). {ECO:0000305|PubMed:22493492}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
CC   -!- CAUTION: Lacks the typical His active site around position 277,
CC       suggesting it has no methyltransferase activity. {ECO:0000305}.
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DR   EMBL; AL731589; CAD39486.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF14076.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS87935.1; -; Genomic_DNA.
DR   EMBL; AK061551; BAG88000.1; -; mRNA.
DR   EMBL; AK104764; BAG96938.1; -; mRNA.
DR   AlphaFoldDB; Q7XXD4; -.
DR   SMR; Q7XXD4; -.
DR   STRING; 4530.OS04T0175900-01; -.
DR   PaxDb; Q7XXD4; -.
DR   PRIDE; Q7XXD4; -.
DR   EnsemblPlants; Os04t0175900-01; Os04t0175900-01; Os04g0175900.
DR   Gramene; Os04t0175900-01; Os04t0175900-01; Os04g0175900.
DR   eggNOG; KOG3178; Eukaryota.
DR   HOGENOM; CLU_005533_12_1_1; -.
DR   InParanoid; Q7XXD4; -.
DR   OMA; EATWLHA; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   Genevisible; Q7XXD4; OS.
DR   GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; PTHR11746; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..371
FT                   /note="Probable inactive methyltransferase Os04g0175900"
FT                   /id="PRO_0000418735"
FT   REGION          170..188
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   371 AA;  40048 MW;  1A56B060DC3703FB CRC64;
     MASGISRTPA TGVTAGGGDD EEAAWLHALE LISGFTVSMT LKAAIQLGLI DALTAAADGR
     ALTAGELVAQ LPAVDDAEAA TSVDRMLRLL ASFNVVRCST EAGPGGDPLR RYSPAPVCRW
     FTAGDNHQGS LAPRLMLDVD EDNLSTWHQM AAAVVSGGPS AFERAHGMPL FEYMGTNHRF
     NMLFNQAMSQ QSMMVMNKLL DRFHGFDGIS VLVDVGGGTG VTLKMIISRY KHITGVNFDL
     PHVISQAPSL PGVNHVAGNM FESVPKGDAI FLKSMLLRND EECIKILKNC HYALSDNGKV
     IVVDIVLPET PKPVPEAQNP LRMDVMMLNN LRGGKIRTEQ EYAKLAMDSG FSGSFRTTYI
     FANFMAIELC K