ID   CHO2_TALMQ              Reviewed;         992 AA.
AC   B6QG32;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE            Short=PE methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE            Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE            Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE            EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217};
GN   Name=cho2; ORFNames=PMAA_084230;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- FUNCTION: Catalyzes the first step of the methylation pathway of
CC       phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC       phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine
CC       (PMME). {ECO:0000255|HAMAP-Rule:MF_03217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC         methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03217};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03217}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03217}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03217}.
CC   -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC       superfamily. CHO2 family. {ECO:0000255|HAMAP-Rule:MF_03217}.
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DR   EMBL; DS995901; EEA24417.1; -; Genomic_DNA.
DR   RefSeq; XP_002147928.1; XM_002147892.1.
DR   AlphaFoldDB; B6QG32; -.
DR   SMR; B6QG32; -.
DR   STRING; 441960.B6QG32; -.
DR   PRIDE; B6QG32; -.
DR   EnsemblFungi; EEA24417; EEA24417; PMAA_084230.
DR   GeneID; 7025551; -.
DR   KEGG; tmf:PMAA_084230; -.
DR   VEuPathDB; FungiDB:PMAA_084230; -.
DR   HOGENOM; CLU_005987_0_0_1; -.
DR   OrthoDB; 170424at2759; -.
DR   PhylomeDB; B6QG32; -.
DR   UniPathway; UPA00753; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03217; PEMT; 1.
DR   InterPro; IPR007318; Phopholipid_MeTrfase.
DR   InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR   Pfam; PF04191; PEMT; 2.
DR   PIRSF; PIRSF000383; PEAMT; 1.
DR   PROSITE; PS51598; SAM_CHO2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Methyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..992
FT                   /note="Phosphatidylethanolamine N-methyltransferase"
FT                   /id="PRO_0000405905"
FT   TOPO_DOM        1..84
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        106..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        133..197
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        219..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        247..279
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        301..302
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        324..403
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        425..426
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        448..477
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        478..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        498..524
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        525..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        546..581
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        582..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        603..992
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  112150 MW;  41437D374BDEEE21 CRC64;
     MDSASASGAQ RQDEGLRERM RPSPPVDIDA VDQALATAGY GVTTDNRTSD DKKTFGRTPD
     GTIFTVPQTH DMVSQLLSPT EPKNVSDLLV LAILAVHILI FWALSPQSRI PVFAAIYMFW
     RTSYNGGIGW LLHNQSHHNT MVRWATKSKI FVNPSTGKNP RPILYRLLKK DMETMIPKDY
     SFDEAPLEYN TWLVFRRFVD VILMCDFTSY CLFAIACGSR PENETTLMTA LRWAAGWVLV
     IFNLWVKLDA HRVVKDFAWY WGDFFFLIDQ ELTFDGVFEM APHPMYSVGY AGYYGISLMA
     ASYKVLFISI IAHAAQFAFL VLVENPHIDR VYNPPPPRKR SVQHDLKDLN GFNAQTSPIS
     DSFAATPAPN GIDDKASMQQ PPSSVHNLLG LHNLDLHRVT DSSVILIQLL VFALTVLTPS
     TPFYQYLFVA NAAIWRCWYS IGIGYILHRQ SKYKSWTRHF VKYGENTDEA WRQWKGSYHL
     SMTMCYASFV AATWKMYSMP SDWNHGLALL KHTLGFSLAA LQIWTSVSIY DSLGEFGWFF
     GDFFFDAQSK LTYSGIYRFL NNPERVLGLA GLWGAALITS KGAIIFLALI SHILTLAFIQ
     LVERPHMQKL YGRSLRKDAG LVKNLKRSLP PPLQQLGGSV DRIMDESFEF VEELLDSARP
     KLATGVNTFM KDAKSLFRQY PARITISRLD DEVAAGYNLE DYSLEIEGTE SSPSAQVERS
     SGKEGANARA PPERRGDLKS LIFEYGAPIR VKWTAPLNHS KKDWVGLYMV TDNTRREVTR
     ISSQGRWIAT NEGAYDSLTC EKGLVTSDIV ISASRRRDGE NRDLASGEMV FSGDKLFWTQ
     GVFEFRYHHN GKHNVMAISR PFEIRIGRFD EEDVVDMDNT TANSDGLIQA AIEEALLPVV
     RNCFDRNPEI APETYDEHFG SLVDRDGKYA KRVVFAVHQM FGVELAPEVV RADGNVRNMA
     WRICNAKKVL APYSMSRSRG TTTPTTQEKE LS