CHO2_PYRTR
ID CHO2_PYRTR Reviewed; 896 AA.
AC B2WFD4;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 54.
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=PTRG_09202;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231624; EDU42253.1; -; Genomic_DNA.
DR RefSeq; XP_001939534.1; XM_001939499.1.
DR AlphaFoldDB; B2WFD4; -.
DR SMR; B2WFD4; -.
DR STRING; 45151.EDU42253; -.
DR EnsemblFungi; EDU42253; EDU42253; PTRG_09202.
DR GeneID; 6347491; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_0_1; -.
DR InParanoid; B2WFD4; -.
DR OMA; DWVGLYM; -.
DR OrthoDB; 170424at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000001471; 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..896
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000405911"
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..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..256
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 278..279
FT /note="Cytoplasmic"
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..304
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 326..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 363..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..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 449..481
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT TOPO_DOM 503..896
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 102284 MW; FF7E4443621F36D3 CRC64;
MADVGDLKAD GSQLRERPSA KPLHLNNSDD AKQKVLKLND QEDKDHKNDE SKKRTYGRTP
DGTVFIVPQT HDMVSQLLSP SQPKNLSDIA VLAVLASLIL TFYALPKSAR VPIFAIIFLF
WRAGYNAGIG WLLDGQSKHN RLVLWAKQSH IFEKPETGKN PNPALYKLLK RELETKIPKD
YKFEEAPLEY NTWLVFRRVV DLILMCDFVS YCLFALACFN RPQESWFLWA LRWTTGIILF
LFNLWVKLDA HRVVKDFAWY WGDFFYLIDQ SLTFDGVFEM APHPMYSVGY AGYYGIALMM
ASYKVLAISI IAHAAQFAFL ILVESRHIDK LYNPPPPRLK TFLFVNAFAW RLWYTLGLGY
ILDRQSKKKN WTKHFIKYGD TKEEAWRQWK SLYHLSMTMS HASFVALAWK MYSLPPDGLT
GLTLFRHVLG AGMIALQVWT AMSIYESLGE FGWFCGDFFF DPPSKSLTYN GIYRFLNNPE
RVLGLAGVWG IAIITWSPAV FYVATTAHIL NLAFLQFVEK PHVIKLYGEN LREMSGVSKT
VRQALPDPVR QWQSAADQYI NTTVESIEAM LDRARSKFAG SVDTFVNDTT SLFKSYPARI
PISRHHSEDL SGLNLKQYKL EIEGTTLPPA VEQQKNGGRE GELARTPAIR TNDFKTLCLE
YGAPIRVRWQ APLNHSKKDW IGLYMVTDNQ SRKVTRISSN GRWVATNPDA FDSTRADDGI
LVSDKLLPAN DNDEESTDCY TGEVEFHGDK LWWTTGVFEF RYHHGGRHHV MALSQAFEIR
IPKFDETDVE VDDNGTIHRA VEETLLPIIQ NCFDRDPEIA PSTSEEPFGS LVERDGKFAR
RVVFAVHQMF GIEFAPEVVQ ADGTVRNLAW RICNAKKVLA PYSMSATHGR NTPTMG
