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Database: UniProt
Entry: A0A176WPY3_MARPO
LinkDB: A0A176WPY3_MARPO
Original site: A0A176WPY3_MARPO 
ID   A0A176WPY3_MARPO        Unreviewed;       355 AA.
AC   A0A176WPY3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=(S)-coclaurine N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AXG93_4461s1590 {ECO:0000313|EMBL:OAE35178.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE35178.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE35178.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE35178.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC       {ECO:0000256|ARBA:ARBA00010815}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAE35178.1}.
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DR   EMBL; LVLJ01000253; OAE35178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WPY3; -.
DR   OrthoDB; 33942at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43832; -; 1.
DR   PANTHER; PTHR43832:SF1; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF02353; CMAS; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
SQ   SEQUENCE   355 AA;  41127 MW;  6F87CBA3574800E3 CRC64;
     MASVLALPTE YAAKLGLRTL HSNVIPDFLV RMGTRTLLAS RLKEIYKSSG EEQQSELMRF
     VQSLKQMPIA VNTRDANEQH YEVPTEFYKL VLGKHLKYSS ALFLKPTNTL EEAEEAMLSL
     YCERAHLEDG QSVLDVGCGW GSLSLFIAQK YPKSRVTGVS NSETQKAFID DEAQKRGLTN
     LKIVTCDINT FEAEERFERV LSIEMFEHMK NYQKLLKKIS SWMEPSGLLF IHTFTHKLAA
     YHFENEDETD WMTRNFFSGG TMAADSLLLY FQDDVSIENH WKVNGRNYAQ TSEEWLKRMD
     ANIKQIRSIF AATYGEKEVT MWIVNWRTFF MAVAELFAYN NGEEWGVSHY LFRKR
//
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