ID A0A2H3C1X0_9AGAR Unreviewed; 695 AA.
AC A0A2H3C1X0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=ARMSODRAFT_720835 {ECO:0000313|EMBL:PBK73212.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK73212.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:28868; EC=3.1.1.116;
CC Evidence={ECO:0000256|ARBA:ARBA00024531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC Evidence={ECO:0000256|ARBA:ARBA00024531};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KZ293421; PBK73212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3C1X0; -.
DR OrthoDB; 373802at2759; -.
DR Proteomes; UP000218334; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR PANTHER; PTHR45792:SF8; DIACYLGLYCEROL LIPASE-ALPHA; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000218334};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 389..557
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 695 AA; 75807 MW; 718D2F7C50B1C197 CRC64;
MTIMENWDSY GRNTLDLASS AAALGFSVVK AGTRLGFSVT RNVASAAVKV TTSVVDNTLF
GGSDVTQPVV GGAVSSVISF AEQITLAPIF LTEYITSTSI IAAHSSINVF SVIFPGSSET
SFSLVAVLAL LKREWKELGY AGNLPEKQYG LTQIARGVIA WVALQGVTRE WQEKRFFKSL
REIHVRDPPR STESLHARRG SRVRVTSDII FPGNRAQIIA ADIGEAPPRA QSVAHHRYKA
ARTKVSPQVF VEPKRLSNAA LKATLRRLSK MVLAGYGGPT LLFFGVPLTP AGSLPAGSSQ
ARSEEAQLAR AINASEAEAS GDLSEREVPS PLPDSYSWWD VMLGKHDQDI FSQFAKSPNE
LIQADVVIGQ EHLMPRFWVL TDHGRQQVVL VIRGTMSLNE IAVDLTCDPE DFAPSRTTTS
EQDETPIPGQ FTFPTPSVEP PSPKYQVHSG ILRMAKAMGD VGKPVQIAVQ EALHRNPGYD
LVICGHSLGA GVAALLGLMW ADVRTCLTVR SSGLPVKRRV SVYCFAPPAT TDVPLAKLSE
NLIVSFVYSH DIVSRLSIGT VKDLRNAAMW LCDANVAGGA LRESGYAAVT ERANKWKAGM
GSQDDPDWFI AMRKTLEANM QQPKKMFPPG RLLWALRDSD LHPTHRSEES SSGPDKLRLF
EVLDVEKSFS QILFAKDMLS AHLPHKYDSV LHDLL
//
