ID   ZRP4_MAIZE              Reviewed;         364 AA.
AC   P47917;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=O-methyltransferase ZRP4;
DE            Short=OMT;
DE            EC=2.1.1.-;
GN   Name=ZRP4;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. NKH31; TISSUE=Root;
RX   PubMed=8278520; DOI=10.1104/pp.102.3.1001;
RA   Held B.M., Wang H., John I., Wurtele E.S., Colbert J.T.;
RT   "An mRNA putatively coding for an O-methyltransferase accumulates
RT   preferentially in maize roots and is located predominantly in the region of
RT   the endodermis.";
RL   Plant Physiol. 102:1001-1008(1993).
CC   -!- FUNCTION: May be involved in the O-methylation of suberin
CC       phenylpropanoid precursors.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Accumulates preferentially in the roots and is
CC       located predominantly in the region of the endodermis, low levels are
CC       seen in the leaves, stems and other shoot organs.
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}.
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DR   EMBL; L14063; AAA18532.1; -; mRNA.
DR   PIR; JQ2268; JQ2268.
DR   RefSeq; NP_001105689.1; NM_001112219.1.
DR   AlphaFoldDB; P47917; -.
DR   SMR; P47917; -.
DR   STRING; 4577.GRMZM2G017557_P01; -.
DR   PaxDb; P47917; -.
DR   PRIDE; P47917; -.
DR   GeneID; 542706; -.
DR   KEGG; zma:542706; -.
DR   MaizeGDB; 65328; -.
DR   eggNOG; KOG3178; Eukaryota.
DR   OrthoDB; 817726at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P47917; baseline and differential.
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..364
FT                   /note="O-methyltransferase ZRP4"
FT                   /id="PRO_0000204440"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         231
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         252
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         265
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   364 AA;  39583 MW;  FB8AD93AD5A6611D CRC64;
     MELSPNNSTD QSLLDAQLEL WHTTFAFMKS MALKSAIHLR IADAIHLHGG AASLSQILSK
     VHLHPSRVSS LRRLMRVLTT TNVFGTQPLG GGSDDDSEPV YTLTPVSRLL IGSQSSQLAQ
     TPLAAMVLDP TIVSPFSELG AWFQHELPDP CIFKHTHGRG IWELTKDDAT FDALVNDGLA
     SDSQLIVDVA IKQSAEVFQG ISSLVDVGGG IGAAAQAISK AFPHVKCSVL DLAHVVAKAP
     THTDVQFIAG DMFESIPPAD AVLLKSVLHD WDHDDCVKIL KNCKKAIPPR EAGGKVIIIN
     MVVGAGPSDM KHKEMQAIFD VYIMFINGME RDEQEWSKIF SEAGYSDYRI IPVLGVRSII
     EVYP