ID A0A0D0BZK2_9AGAR Unreviewed; 468 AA.
AC A0A0D0BZK2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GYMLUDRAFT_76587 {ECO:0000313|EMBL:KIK55369.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK55369.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK55369.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK55369.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; KN834807; KIK55369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0BZK2; -.
DR HOGENOM; CLU_026434_0_0_1; -.
DR OrthoDB; 142984at2759; -.
DR Proteomes; UP000053593; Unassembled WGS sequence.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
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; 1.
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:UP000053593};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 468 AA; 52620 MW; E332A385CD3D5FF3 CRC64;
MPATTTTHPC VRLTPPSSKS LQPSSIFSFG LSNPRSWLAS FARTSILSVL NDAISKGHLT
IIDSEGKHTY GRYQDGCNTV HLTVNNDQFW LRLMFSGDLG FSEAYMLGDI EVEDLKSCMD
LWLDNQAGME ETLSSSFARI SSAISGLYNS FLGQTKTQAR LNAIASYDQS NTLFKAFLSQ
EMMYSCALWD ESEGGVRGDL EMGPTPGDLE AAQRRKIHHV LRQARVKPGH RILEFGSGWG
GLAIEAARTF GCTVDTLTLS VEQKTLAEER IKAAGLEDKI RVHLMDYREI PAEFEKAFDA
FVSVEMLEHV GAKHYNTYFK LVDFALKSRD ATAVVTASTF PESRFSGYQP EDFMRRYMWP
NSCLPSATAL ITAAQAASNG RFTLEGVENH AAHYPRTLRE WGRRLEKNMT QEIIAKEYPA
LWDRANYEAF KKKWQYLFVY AGAGFAKGYI TCHMLTFIRQ NDCPEMCD
//