ID V2XUV4_MONRO Unreviewed; 244 AA.
AC V2XUV4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Protein-S-isoprenylcysteine O-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Moror_14986 {ECO:0000313|EMBL:ESK83164.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK83164.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK83164.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK83164.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK83164.1}.
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DR EMBL; AWSO01001642; ESK83164.1; -; Genomic_DNA.
DR RefSeq; XP_007857528.1; XM_007859337.1.
DR AlphaFoldDB; V2XUV4; -.
DR KEGG; mrr:Moror_14986; -.
DR HOGENOM; CLU_065200_6_0_1; -.
DR OrthoDB; 1603024at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000017559; 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:SF9; PROTEIN-S-ISOPRENYLCYSTEINE O-METHYLTRANSFERASE; 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:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..244
FT /note="Protein-S-isoprenylcysteine O-methyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004711921"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 244 AA; 26929 MW; 3A3D8F30DE40D50F CRC64;
MVTLDSLALA KAFLVFSSAV SFGVSFTPPN GGPKSLPPTP SLKRGFTADM REWILVFLIK
YALPIEVKMY YLVSVNEVIH VLSSIFPTLP VQPYFPSLVS NTELSPVLLL GALLSISGCI
FRIFCYRALS EGFTFELVPA GKLSNNPTLV KSPKLITHGP YSIVRHPSYA ACWINFTGSV
MVHLWILGTG ARLLACGWLI GVGGGITVLL MRMDDEDNLM RKQFGSEWEA WSKVVRYKLC
PGMY
//
