ID   MTR3_THECC              Reviewed;         349 AA.
AC   A0A061DM17;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Probable methyltransferase TCM_000336 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
GN   ORFNames=TCM_000336 {ECO:0000312|EMBL:EOX91023.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6;
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Livingstone D. III,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; CM001879; EOX91023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061DM17; -.
DR   SMR; A0A061DM17; -.
DR   STRING; 3641.EOX91023; -.
DR   EnsemblPlants; EOX91023; EOX91023; TCM_000336.
DR   Gramene; EOX91023; EOX91023; TCM_000336.
DR   eggNOG; ENOG502QQAF; Eukaryota.
DR   HOGENOM; CLU_019628_2_0_1; -.
DR   OMA; SHKIMHH; -.
DR   OrthoDB; 689338at2759; -.
DR   Proteomes; UP000026915; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IBA:GO_Central.
DR   Gene3D; 1.10.1200.270; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR005299; MeTrfase_7.
DR   InterPro; IPR042086; MeTrfase_capping.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR31009; PTHR31009; 1.
DR   Pfam; PF03492; Methyltransf_7; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..349
FT                   /note="Probable methyltransferase TCM_000336"
FT                   /id="PRO_0000451805"
FT   BINDING         18
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE70"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE70"
FT   BINDING         21..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         58..59
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT   BINDING         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         59
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT   BINDING         64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE70"
FT   BINDING         94..97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         135..137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         152..154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         153..157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT   SITE            222
FT                   /note="Involved in substrate discrimination"
FT                   /evidence="ECO:0000250|UniProtKB:Q2HXI6"
SQ   SEQUENCE   349 AA;  39384 MW;  412B98C74AEF533E CRC64;
     MDVEKVFHMT GGVGKTSYAQ NSSLQKKASD MVKHITMETI EELYYSIAPK SLGIADLGCS
     SGPNSLSLIK DIVEVVEETS HKLFHPLPEF RVYLNDLPTN DFNSVFKSLP DFYRDLKKDR
     NEGGPAIFIA GYPGSFYGRL FPNNCLHFIY SSYSLHWLSK VPPALYDEHG KSTNKGNVYI
     SESSPPSVSQ AYWNQFQEDF SLFLKSRSVE VVTGGRMVLI LLGRIGQDHV DRGNSFFWEI
     LSRSLAISVS QGQIDREKLD SYEVHFYAPS TNEIEDEVGR EGSFEVDRLE MFEIDREAKD
     GESYGTAVAM TVRAIQESMI CNHFGDGIDL DTLFNNYGKM VDEEMAKQN