ID A0A165FC72_9BASI Unreviewed; 465 AA.
AC A0A165FC72;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:KZT56536.1};
GN ORFNames=CALCODRAFT_483894 {ECO:0000313|EMBL:KZT56536.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT56536.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT56536.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT56536.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; KV423976; KZT56536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165FC72; -.
DR STRING; 1353952.A0A165FC72; -.
DR InParanoid; A0A165FC72; -.
DR OrthoDB; 142984at2759; -.
DR Proteomes; UP000076842; 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; 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:UP000076842};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 465 AA; 52410 MW; 1B5803F328E8A744 CRC64;
MRPMDSFAES FVVGYLGGIS RGRLRIVTPA AIYNFPTDEM KEKPQLGSTD VVGDASDIHA
TITVRRDSFW LRVLTTADLG FAEAYMTGEI DVDDLTSLFM LFIYNRESLS SVSSFKSCLS
YVPTFGSRKL LDLTASLATL NNAKANVSAH YDMSNRMFEA FLSSDMTYSC GLFESLDEDL
VECQKGSELL GLDPLELAQL RKLRHICNKA DIRDGHRVLE IGTGWGSFSM LAASLFKCTI
DTVTLSEQQA ALARERIAKA GLSDRIRVHV VDYRSLPAEW EGQFDRFVSI EMMEHVGAEY
MDTYWRMVDW ALKKSGAGVI QVSTIPDARM KVYAKDVDFI RKWIFPGGFL PSASMLLSTL
NSGSDGRLVV ESVGNIGPHY SRTLREWQRR FSKSFESVVV PELREQYDIS RVECETFKRK
WNYYFSYCEA GFSTRTLGVH IISFTREGNV ELGCDVRLDG EDTTQ
//