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Database: UniProt
Entry: E4ZNX8_LEPMJ
LinkDB: E4ZNX8_LEPMJ
Original site: E4ZNX8_LEPMJ 
ID   E4ZNX8_LEPMJ            Unreviewed;       237 AA.
AC   E4ZNX8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Similar to O-methyltransferase family 3 {ECO:0000313|EMBL:CBX93347.1};
GN   ORFNames=LEMA_P042480.1 {ECO:0000313|EMBL:CBX93347.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00023453}.
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DR   EMBL; FP929105; CBX93347.1; -; Genomic_DNA.
DR   RefSeq; XP_003836712.1; XM_003836664.1.
DR   AlphaFoldDB; E4ZNX8; -.
DR   STRING; 985895.E4ZNX8; -.
DR   EnsemblFungi; CBX93347; CBX93347; LEMA_P042480.1.
DR   GeneID; 13282717; -.
DR   eggNOG; KOG1663; Eukaryota.
DR   HOGENOM; CLU_067676_8_0_1; -.
DR   InParanoid; E4ZNX8; -.
DR   OMA; PAYFEWA; -.
DR   OrthoDB; 5473331at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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   InterPro; IPR002935; SAM_O-MeTrfase.
DR   PANTHER; PTHR10509:SF14; CATECHOL O-METHYLTRANSFERASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR10509; O-METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:CBX93347.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBX93347.1}.
SQ   SEQUENCE   237 AA;  25483 MW;  7B45B00053C8EF79 CRC64;
     MNDPTLTKHD PRWTDVDTYT VSHLHSSPTA IPPPSTLAAT LAHQQASGLP DIAVSPSQGK
     YLQLTARATR SRHILEVGTL GGYSTLWLAS SHPDARITSV EISADNAAVA RANLERAGVS
     DRVDVVVGAG VEVLPRLADE VKRGVREKFQ FVFIDADKEN NWNYVDVALG MCEAGAVVIV
     DNVVRGGHLA DASTQDSMVL GARRVVENIG RDDRLDGCVL QVVGEKSYDG FLMAVVR
//
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