ID A0A164WZP7_9AGAM Unreviewed; 455 AA.
AC A0A164WZP7;
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:KZS95510.1};
GN ORFNames=SISNIDRAFT_483741 {ECO:0000313|EMBL:KZS95510.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS95510.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS95510.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS95510.1,
RC ECO:0000313|Proteomes:UP000076722};
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; KV419401; KZS95510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164WZP7; -.
DR STRING; 1314777.A0A164WZP7; -.
DR OrthoDB; 142984at2759; -.
DR Proteomes; UP000076722; 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:UP000076722};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 455 AA; 51519 MW; 23DA73944F787949 CRC64;
MTKSSVSPWS PSFISRLEFT RALHSWLINF ARSTLTEACQ KGILIGHLTI IDSQGTYSFG
NNDKQTEPQV TIEVVNDAFW TRVLFGGDLG FGEAYLVGDL KTDDLKGAFE IWLENRSSLE
SLSAFASRAI SSLSAISSAL IGQTQMKSRL NAIASYDTSN ALFECFLSKE MQYSCALWDT
PEDGLNPFLL DQTDAPEVSL ESAQDRKLHH VLRAARVKPG DRILEFGSGW GALAITAAKY
YKCTVDTITL SIEQKKLAEE RIRSEGLENL ITVHLCDYRD LPRSFEKAFD AFVSIEMIEH
VGPRYYQTYF KLVDWALKSQ NATAVVTTST CPEGRWTVYQ TEDFCRKYIW PNGTLPSPTI
LITSAAKATK SRLQLECVEN HSAHYPRTLR TWALNLATRL PQYREKIIKD QPASNLEDPA
VMEVFLRKWM YLFGYAEAGF EKGYIGCHMF TWRRL
//
