ID A0A165L7R1_EXIGL Unreviewed; 436 AA.
AC A0A165L7R1;
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:KZV97474.1};
GN ORFNames=EXIGLDRAFT_764432 {ECO:0000313|EMBL:KZV97474.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV97474.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV97474.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV97474.1,
RC ECO:0000313|Proteomes:UP000077266};
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; KV425930; KZV97474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165L7R1; -.
DR STRING; 1314781.A0A165L7R1; -.
DR InParanoid; A0A165L7R1; -.
DR OrthoDB; 142984at2759; -.
DR Proteomes; UP000077266; 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:UP000077266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 436 AA; 49023 MW; 76E7D7DAE825D562 CRC64;
MGSSWSSARD AYARRFVDST LSAIRIGRLT VLLQVPDTAE EKLVYGQRTG DVDPEVDVTL
FVKSNNLWWR LCKNMDLGLS EAYLNGEVEC SDWVRLFTIY IRNRENFSTG AFALQVVPLI
QKLLSAGNTV SSAKRNAIEH YDSSNTLFEG FLSEDMNYSS PIWELGNDAE TLEAAQARKV
QALIQELSLE PSDHLLDIGC GWGNLAIEAV RASGCRVTGV TLSKEQKRLA EERIASAGFE
DKIRILLCDY REIPEVPGGY DKVVSVEMIE HVGRKHFPVF FGTISRLLNP QRGVMVLQAI
ICSNAQHDAK LNQPEGFIDK YIFPGGYLAS TPYILETIHT GSKGKLAVRT VRSIGPHYAK
ALRMWREKFL RNWDDQIKPK LMAEGKTNDA AMEFFKRRWE YYFSYCESGF RTGLIGDIIV
TASHDGAQEL LRGVPL
//
