CHO2_PHANO
ID CHO2_PHANO Reviewed; 932 AA.
AC Q0U2R3;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 64.
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=SNOG_13932;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445353; EAT78557.2; -; Genomic_DNA.
DR RefSeq; XP_001804132.1; XM_001804080.1.
DR AlphaFoldDB; Q0U2R3; -.
DR SMR; Q0U2R3; -.
DR STRING; 13684.SNOT_13932; -.
DR EnsemblFungi; SNOT_13932; SNOT_13932; SNOG_13932.
DR GeneID; 5981055; -.
DR KEGG; pno:SNOG_13932; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR InParanoid; Q0U2R3; -.
DR OrthoDB; 170424at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000001055; 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; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_03217; PEMT; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR Pfam; PF04191; PEMT; 1.
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..932
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405906"
FT TOPO_DOM 1..88
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 110..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 134..198
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 220..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..261
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 283..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 377
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 399..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 450..454
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 476..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 540..932
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 106574 MW; FA984C2DD3EFB4BC CRC64;
MADINHDGPK ADGSQMRERP SAKPLHLYNS EDAKKKVLEL NQEEEDNKHE EKRKTFGRTP
DGTVFIVPQT HDMVSQLLSP SQPKNLSDLA ILAVLASLIF TLYICPTSAR KPVFAAIFLF
WRAAYNAGIG WLLEGQSKHN RLVLWAKNSH IFENPETGNN PHPTIYKLIK REMETKIPKD
YKFEEAPLEY NTWLVFRRVV DLILMCDFVS YCLFAIACFN RPPESWLLFG LRWTTGIVLF
IFNVFVKLDA HRVVKDFAWY CYHVLFISIV AHAAQFAFLT LVEEPHIQKI YNPPPPRRMR
QNSEKFNPED RPATAHSDAT YTDTGVIYDS VRQPAPMHHI VGLQNTDFHR SIDVTVVLLC
FYMFCLATVT PNTIAVRLFL FVHAFVWRLW YALGLGYILD RQSKKKNWTR HFIKHGDTKE
EAWRQWKSLY HLSMTMCHAS FGAAVWKMYE LPSDWFLGLT LLRHVLGAGL LLLQLWTSTS
IYDSLGEFGW FCGDFFFDPP SSNLTYSGIY RFLNNPERVL GLAGVWGLAL ITWNPPIFYL
AATAHILNLA FLQFVERPHM QRLYGRKLRA ESGVSKTLRQ AMPSPVRNWQ SAADDYVNST
VEFIEDLLEH ARPKLAAGYE TIVKDTTALF KTYPARISIT RVPQDLAGLD PKQYKLEIEG
TPSAPTVEIQ KHGGREGELA RTPATRTSEF KTLTFEYGAP IRVRWQAPVN HHKKDWIGLY
MVTDNQSREV TRISSNGRWV ATNKGVYDST RAEDGILVSD RLVSVNSDED EGGDCYTGEV
EFRGDKLWWT TGVFEFRYHH GGKHHVMALS QAFEIRIARF DEDDVEVDAN GTVHRAVEQA
LLPVIQNCFD RDPEIAPSTP EESFGSLVER DGKFAKRVVF AVHQMFGIEF APEVVQADGN
ARNLAWRICN AKKILAPYSM SASRGRNTPT SR
