ID F8QCQ4_SERL3 Unreviewed; 229 AA.
AC F8QCQ4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SERLA73DRAFT_189043 {ECO:0000313|EMBL:EGN93919.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GL945490; EGN93919.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QCQ4; -.
DR STRING; 936435.F8QCQ4; -.
DR eggNOG; ENOG502SNG8; Eukaryota.
DR HOGENOM; CLU_065200_6_0_1; -.
DR InParanoid; F8QCQ4; -.
DR OMA; HTEELYI; -.
DR OrthoDB; 1936220at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000008063; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.120.1630; -; 1.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR PANTHER; PTHR12714; PROTEIN-S ISOPRENYLCYSTEINE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR12714:SF27; SLR1182 PROTEIN; 1.
DR Pfam; PF04191; PEMT; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 229 AA; 25489 MW; 8936E1DE05CC792E CRC64;
MSLVVRALLV SVQAIGNQLA CTPPNATNVK TRYHTNEPYI LQMAPLMFKI HTTLLWLCAL
FEAISAINFY VPCLPVQVEP FFSSTTRPIS SITPLFMIGV LVSLSGVLIR LRCFRELGHL
FTFDLTFHPE HKLVTSGFYR YVRHPSYTGS LLLVAGLALS HCTRGSWARE CGPLGQMSAV
VLGTGWCIWA ISVCISRAYA EDGELRKNFG AEWDAYAARV PAWFFPGLL
//
