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OMTL2_ORYSJ
ID   OMTL2_ORYSJ             Reviewed;         354 AA.
AC   Q7XXI9;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Caffeate O-methyltransferase-like protein 2 {ECO:0000305};
DE            Short=OsCOMTL2 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000305};
GN   Name=COMTL2 {ECO:0000305};
GN   OrderedLocusNames=Os04g0104900 {ECO:0000312|EMBL:BAF13918.1},
GN   LOC_Os04g01470 {ECO:0000305};
GN   ORFNames=OSJNBa0094O15.13 {ECO:0000312|EMBL:CAD39344.2};
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   INDUCTION BY UV-C.
RX   PubMed=24035516; DOI=10.1016/j.phytochem.2013.08.012;
RA   Park H.L., Lee S.W., Jung K.H., Hahn T.R., Cho M.H.;
RT   "Transcriptomic analysis of UV-treated rice leaves reveals UV-induced
RT   phytoalexin biosynthetic pathways and their regulatory networks in rice.";
RL   Phytochemistry 96:57-71(2013).
CC   -!- INDUCTION: Induced by UV-C. {ECO:0000269|PubMed:24035516}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL662935; CAD39344.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF13918.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS87525.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7XXI9; -.
DR   SMR; Q7XXI9; -.
DR   STRING; 4530.OS04T0104900-01; -.
DR   PaxDb; Q7XXI9; -.
DR   PRIDE; Q7XXI9; -.
DR   EnsemblPlants; Os04t0104900-01; Os04t0104900-01; Os04g0104900.
DR   Gramene; Os04t0104900-01; Os04t0104900-01; Os04g0104900.
DR   eggNOG; KOG3178; Eukaryota.
DR   HOGENOM; CLU_005533_12_1_1; -.
DR   InParanoid; Q7XXI9; -.
DR   OMA; EMITCRY; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
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   2: Evidence at transcript level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..354
FT                   /note="Caffeate O-methyltransferase-like protein 2"
FT                   /id="PRO_0000437950"
FT   ACT_SITE        259
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT   ACT_SITE        319
FT                   /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT   BINDING         198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002"
FT   BINDING         221
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002"
FT   BINDING         255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P28002"
SQ   SEQUENCE   354 AA;  38376 MW;  DFB8CE73BC1D352A CRC64;
     MTPAADGDDD ETTCIRALEL IFTFVVPMTL KATIKLGLLD ALTGGGHALT ADELAAAAQL
     PAEAASSVDR MLRLLASLDV VKCAPTDTGG EAAVRRYTPA PVCRWFAGER SLAPLAMFLL
     DDDYLSTWNQ LPAAVAGGDG QVAFEKARGM PMFEYMGTNR RLNTLFNQAM VQQSTVVIGK
     LLERFQGFDG VSVLVDVGGG TGATLEMITS RYKNITGVNF DLPHVIAQAP SLPGVKHIAG
     NMFESVPNGD AIFLKSMLHL HNDEDCIKIL KKCHQALTHN GKVIAVEILL PAIPEPVPTA
     QNPFRMDMIM LNNHWGGKER TEPEFAKLAV ECGYTGVFQA TYIFANYWAL EFSK
 
 
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