ID   A0A1Z5TBT4_HORWE        Unreviewed;       507 AA.
AC   A0A1Z5TBT4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BTJ68_06503 {ECO:0000313|EMBL:OTA33505.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA33505.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA33505.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA33505.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC       {ECO:0000256|ARBA:ARBA00010815}.
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:OTA33505.1}.
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DR   EMBL; MUNK01000074; OTA33505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TBT4; -.
DR   STRING; 1157616.A0A1Z5TBT4; -.
DR   VEuPathDB; FungiDB:BTJ68_06503; -.
DR   InParanoid; A0A1Z5TBT4; -.
DR   OrthoDB; 142984at2759; -.
DR   Proteomes; UP000194280; 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; 1.
DR   PIRSF; PIRSF003085; CMAS; 3.
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:UP000194280};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          369..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  56209 MW;  E490EBCEF1371C83 CRC64;
     MTLLSPLTDR ATALATYAGS YAWPPLLSFS RAAILNLLKQ VQVGSLQITD TDGTLTVCGS
     PRRASAAPET EKSVYTTPHA ELRVLNDLFW VRLAIFADMG FAESYMLGEV ECPDLTAFFK
     VFITNRNYLA NGSTLTSTLS GKIAGFVRST NTLTNARLNI SAHYDISNDM FAAFLSPDMT
     YSCPIWLPKT DPASSQETLE QAQHRKLTRF LTNAHIKSSD HVLEIGTGWG SFAILAVQQT
     GCRVTSLTLS AEQKLLAEQR IAAAGLSDRI TVLLTDYRAL TPGRTEREKF DKVVSIEMLE
     AVGAEYLDTY FRCIDRLLKS EGGVAVFQCI TMPESRYEGY RTSDDFIRRY IFPGGHLPTV
     TQLLDAVRSG STPSKKDGGG KEQQQPQPQQ QQPRLIPESV ENIGPHYAKT LRLWRQAFMQ
     NFTSKIRPAL LHDHSSSTTS SAAGKGEEDG SNDNNKTMSE DEIETFRRKW EYYFAYCEAG
     FATKTLGDVI LTVGREGAVE MMEDVPL
//