ID A0A2V1BU55_9HELO Unreviewed; 276 AA.
AC A0A2V1BU55;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=phosphoethanolamine N-methyltransferase {ECO:0000256|ARBA:ARBA00035674};
DE EC=2.1.1.103 {ECO:0000256|ARBA:ARBA00035674};
GN ORFNames=DL98DRAFT_517606 {ECO:0000313|EMBL:PVH76878.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH76878.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH76878.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH76878.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphoethanolamine + S-adenosyl-L-methionine = H(+) + N-
CC methylethanolamine phosphate + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:20365, ChEBI:CHEBI:15378, ChEBI:CHEBI:57781,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58190, ChEBI:CHEBI:59789;
CC EC=2.1.1.103; Evidence={ECO:0000256|ARBA:ARBA00035571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20366;
CC Evidence={ECO:0000256|ARBA:ARBA00035571};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004969}.
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DR EMBL; KZ804182; PVH76878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1BU55; -.
DR STRING; 1485229.A0A2V1BU55; -.
DR Proteomes; UP000244409; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR44307:SF20; METHYLTRANSF_25 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44307; PHOSPHOETHANOLAMINE METHYLTRANSFERASE; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:PVH76878.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PVH76878.1}.
FT DOMAIN 81..170
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
SQ SEQUENCE 276 AA; 30467 MW; CAF88875AD4AC6CC CRC64;
MQYFRSNLTQ VKTSLKLQAS FTNNRNLATG IAFPMSTQGS LAGLKVFEAL NIEYENAYAD
NEIKKSCITH AISLLPPFSK VLDVGCGTGI PVSSMLSKAS LFVIGFDISP KMIALAKSRV
KGDFSVSDML SYTPTGKFAG VFMIFAHMRL SYRDFHAAVF KFASVLQPGG ILVLGQVPSD
SYVKNESVEM NSYVEGYDVP FMGDMVPIMM MSAEGQRHFL TSMGLEIVWE RIDTFQPKNE
KCKPEEQQYI IARKPNTNVL QPRPLPDTDL LGSGGI
//
