ID E6R8X4_CRYGW Unreviewed; 1051 AA.
AC E6R8X4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000256|RuleBase:RU361122};
DE Short=PEAMT {ECO:0000256|RuleBase:RU361122};
DE EC=2.1.1.17 {ECO:0000256|RuleBase:RU361122};
GN OrderedLocusNames=CGB_G0480W {ECO:0000313|EMBL:ADV23251.1};
OS Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV23251.1, ECO:0000313|Proteomes:UP000007805};
RN [1] {ECO:0000313|EMBL:ADV23251.1, ECO:0000313|Proteomes:UP000007805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WM276;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwong-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 0:0-0(2011).
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:0000256|RuleBase:RU361122}.
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:0000256|RuleBase:RU361122};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000256|RuleBase:RU361122}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU361122}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361122}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. CHO2 family. {ECO:0000256|RuleBase:RU361122}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361122}.
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DR EMBL; CP000292; ADV23251.1; -; Genomic_DNA.
DR RefSeq; XP_003195038.1; XM_003194990.1.
DR AlphaFoldDB; E6R8X4; -.
DR GeneID; 10190815; -.
DR KEGG; cgi:CGB_G0480W; -.
DR VEuPathDB; FungiDB:CGB_G0480W; -.
DR eggNOG; ENOG502QRGH; Eukaryota.
DR HOGENOM; CLU_005987_0_1_1; -.
DR OrthoDB; 1561at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000007805; Chromosome G.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 1.20.120.1630; -; 1.
DR Gene3D; 2.60.40.2840; -; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR PANTHER; PTHR32138; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR32138:SF0; PHOSPHATIDYLETHANOLAMINE N-METHYLTRANSFERASE; 1.
DR Pfam; PF04191; PEMT; 2.
DR PIRSF; PIRSF000383; PEAMT; 3.
DR PROSITE; PS51598; SAM_CHO2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU361122};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU361122};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361122};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361122};
KW Methyltransferase {ECO:0000256|RuleBase:RU361122};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|RuleBase:RU361122};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264,
KW ECO:0000256|RuleBase:RU361122};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU361122};
KW Transferase {ECO:0000256|RuleBase:RU361122};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361122};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361122}.
FT TRANSMEM 113..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 264..282
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 302..331
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 391..412
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 487..505
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 525..544
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT TRANSMEM 583..611
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361122"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1051 AA; 118732 MW; 70F62C2B49E04660 CRC64;
MAELAPSQEG KLADSSNQDS QSTLRLRKTL PHNNTESISS VGDEKSADTE DKSQDQVTWG
KTSTGAVFRV PNTHSFVHTL LTTTHRSSLT RLTLFSLVAQ PVLFYLLRNH RLLRSVFFLL
YFAFWRGCYD WGFAWVLRKQ SEKKWVVKLL RNWGWLDVNS EQGGEQGRAW AKWWKRELEM
KMDDGYKWES VPQEFNAWLM FRQLVDVVLL NDFVSYACFA WANLHFPPNH SVFMHIFRWV
LGWSLILFNL WVKMDAHRVV KDYAWYWGDA FWLMVMQHDL VFDGVYEIAP HPMYSVGYAG
YYGLSMVVGS YAVLFVSLAA HAAQFAFLLW FENPHIERTY GGGKKPLASR VPLAWERTEH
EQEQLEGSSS TIVEGSEAPT PSATEGRSTD FALVLLVIYA LSSLIPSLSL NVSLAGHFLH
VLLWRLFHSF GLGLILRAQS KSKWLVRHYL KHYHYPEDAH VDDEDESDIK ESVVKRATEE
SFGNWQVMYN ISLVMTYVSF VGLAWKTYHL PSDWTVSGTM LRHVLGLSLI ALHIWSAVSS
YEVLGDFGWL YSDFFLIEQI PSQLAYTGIY RFLNNPERSM GGAAFFGLWL ISNSKLVFAL
ALASHLSHWW FLTFVEGPHM QRLYGKRLRK DGGLTKTLKN VAGKTIATKT GKHAHDIQRV
VQEVRGSIEK VEEKVTEAVE EFLDHARPMF TDMVNDTRVL LQQSRERMII TRVANDISAY
DTSRYGLHIA TSSSAPTPRF HVGQPIRVSW TAPSNHSRKD WIGIYRLGSC KSQLVTRVSS
VGKWMPIYEE EWNGNDPVDP AERERKGDSG EVVFRGDQLP WQPGEYELRY HHDGKHNVMS
RLAPVEIVVD KPKSSSVKAI HQTLLNIVCV SLDSDPNLVP KSARKKTTPA AIPASHVSEV
SLREDLPAIQ ESDGKETEEG AADRIEHNQK ELSEDHADDG DTPSLNTPIV SGVPTPSTHP
PSSPIPPFSS SDHGTPPSSS AHSFASSNDP DYTVGHGGDD DFVIMTENQA KRIAHLAEMA
FGVELSPDVV VAEANVGSLA RRIVGARSLI K
//
