ID   A0A316ZKV1_9BASI        Unreviewed;       505 AA.
AC   A0A316ZKV1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:PWO01437.1};
GN   ORFNames=FA09DRAFT_327360 {ECO:0000313|EMBL:PWO01437.1};
OS   Tilletiopsis washingtonensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC   Tilletiopsis.
OX   NCBI_TaxID=58919 {ECO:0000313|EMBL:PWO01437.1, ECO:0000313|Proteomes:UP000245946};
RN   [1] {ECO:0000313|EMBL:PWO01437.1, ECO:0000313|Proteomes:UP000245946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4186 {ECO:0000313|EMBL:PWO01437.1,
RC   ECO:0000313|Proteomes:UP000245946};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC       {ECO:0000256|ARBA:ARBA00010815}.
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DR   EMBL; KZ819283; PWO01437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316ZKV1; -.
DR   STRING; 58919.A0A316ZKV1; -.
DR   OrthoDB; 142984at2759; -.
DR   Proteomes; UP000245946; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003333; CMAS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43667; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR   PANTHER; PTHR43667:SF2; TUBERCULOSTEARIC ACID METHYLTRANSFERASE UFAA1; 1.
DR   Pfam; PF02353; CMAS; 2.
DR   PIRSF; PIRSF003085; CMAS; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245946};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          191..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  55113 MW;  0BFA1EAE023838C0 CRC64;
     MSAAASRALA PLLSVAAPPL HGLARRVLLA YFARLTRGSL SITEHGQPDV RLGADAPQEG
     DAHAVLRVRH ARFWTRMLLG ADLGFAEAYM TGDVECDELG EVFRLFIHNR EALGNLEVGL
     LANASAWLQA QLNRRYANTR AGSLSNIGAH YDISNQMYEA FLSADMTYSC GVYPTLDADV
     GAARHASAKL AQLTNGAPRK PQGSGEFADD GPGGPTPPDA EARSDDGKAA KDELEAAQLT
     KLRLHIERAD IRKGHHVLEI GTGWGSFAME AVRRTGCTVE SLTLSVEQKA LAEARIAKAG
     MSGSIKVHLL DYRDMPASWN DSFDRVVSIE MLEAVGIEFL PTYFENVSRV LKAQGGAACF
     QCITMPESRF EAYAAGVDFI KKWIFPGGVL PSVTALIDAA TRGSKGTLQL DAALSIGPHY
     ARTLREWRQR FDAAFDEHVR PALLSDHKAI RELPAEAQAR EVEVFRKKWT YYFVYCEVGF
     TERVIGDHIL SFTREGNTSL PTCCG
//