ID   CHO2_ASPFN              Reviewed;         971 AA.
AC   B8N6H2;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=AFLA_014850;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(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; EQ963474; EED54233.1; -; Genomic_DNA.
DR   RefSeq; XP_002375505.1; XM_002375464.1.
DR   AlphaFoldDB; B8N6H2; -.
DR   SMR; B8N6H2; -.
DR   STRING; 5059.CADAFLAP00003370; -.
DR   EnsemblFungi; EED54233; EED54233; AFLA_014850.
DR   VEuPathDB; FungiDB:AFLA_014850; -.
DR   eggNOG; ENOG502QRGH; Eukaryota.
DR   HOGENOM; CLU_005987_0_0_1; -.
DR   OMA; DWVGLYM; -.
DR   UniPathway; UPA00753; -.
DR   Proteomes; UP000001875; 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   S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..971
FT                   /note="Phosphatidylethanolamine N-methyltransferase"
FT                   /id="PRO_0000405874"
FT   TOPO_DOM        1..85
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        107..109
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        131..195
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        217..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        245..277
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        299..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        322..389
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        390..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        412..417
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        418..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        442..473
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        474..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        495..496
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        497..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        518..575
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        576..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        597..971
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  109686 MW;  26891AE4748E542B CRC64;
     MDRGLSTSTR IDDEGLRERN VASQSTSTLS PEALTATGDV ELKDKTGKDC KTFGRTPDGT
     VFTVPQTHDM VSQLLSPSEP KNLSDVIVLA ILGAHILLLW QLPTGAKVPV FAIIYLFWRA
     AYNAGIGWLL HNQSHHKTLV RWAEKTKVFV NPATGKNPHP NVYNFFKREL ETKIPHDYSF
     DEAPIEYNTW LVFRRLVDLI LMCDFVSYCL FAIACSHHPV NESVLMTVLR WSAGIVLVLF
     NLWVKLDAHR VVKDFAWYWG DFFYLIDQEL TFDGVFEMAP HPMYSVGYAG YYGISLMAAS
     YKVLFISIIA HAAQFAFLVL VENPHIDKTY NPPPSRKRSA EQETGSVSSR TADSPIAPTP
     IDEQIPHAPT FSSSPPQSVH ELLGLHNLDL YRITDTSSVL IQFLVFALTV LTPSTPWYQF
     LFVANAAVWR LWFSIGVGYM LHRQSNHKAW TRHFVKYGET PQEAWNQWKG TYHLSMIMCY
     ASFIAAVWKM YNFPADWGYG LVLLRHVLGA GLISLQIWTS VSIYESLGEF GWFYGDFFFD
     GSSKLTYNGI YRFLNNPERV LGLAGVWGAV LITSSGAITF LALLSHILSL AFIQFIERPH
     MQKLYGQSLR QDAGLVKSLK KSLPPTLRQL HGSVDKIFDE SFEFIEEIIE TARPKLANGV
     NTFVKDTTAL FQSYPARVTI SRIDEDLAGY DSRDYSLEVE GTDSSSLAEH DQSTGREGAN
     ARMPLDRRGD LKNLVFEYGA PIRVKWTAPL NHSKKDWIGL YKVTDNTSRE VTRVSSQGRW
     IAVNEGAYDN LTCEKGIVKS DVVIKATQQQ DGDKRDLATG EVIFSGDKLF WTQGVFEFRY
     HHNAKHNVMA ISRPFEIRIG RYEEEDDHEL TQASVEKSLL PVIRSCFDRD PEIAPEAVDE
     PFGSLVERDG KFAKRVVFAV HQMFGVEFAP GVVQADGTVR NLAWRVCNAK RVLAPYSMSR
     NGASTPTERK E