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Database: UniProt
Entry: A0A0A2VDB2_BEABA
LinkDB: A0A0A2VDB2_BEABA
Original site: A0A0A2VDB2_BEABA 
ID   A0A0A2VDB2_BEABA        Unreviewed;      1071 AA.
AC   A0A0A2VDB2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN   ORFNames=BBAD15_g8857 {ECO:0000313|EMBL:KGQ05876.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05876.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ05876.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05876.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ05876.1}.
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DR   EMBL; ANFO01000907; KGQ05876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2VDB2; -.
DR   STRING; 1245745.A0A0A2VDB2; -.
DR   eggNOG; KOG2088; Eukaryota.
DR   HOGENOM; CLU_001871_0_0_1; -.
DR   Proteomes; UP000030106; 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:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_6G02710)-RELATED; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          752..918
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
FT   REGION          339..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1071 AA;  116494 MW;  BF670A9EC21F8264 CRC64;
     MASGKTPKHN PGPTLLPGPI ASTVSLATRS TSLAIRIGSV VGGYGLNAAR FTTLSSLELA
     RGLVEVVLTR AGKDTLDHAK SSLAAADAEN VLERSLEGLH YAVIQVAFWT SASFRLTGTT
     LSLASNTSQL LLSSLDKLLG STDSSRAVAS IITLMRREFR NPVTGFQGER VGVIDLTLAL
     SALAYLQQAC RKLPEEEARR NAFEEVIWDV VVLNDGDRVE FDDKIALQRG YAPAFNHEAS
     RRGSQDEEAL AQLESHITQS LPPEAKVTIS SYVTTVQTIT VEVEGCLPVL PTPPGAEIIE
     TTAPVSRSKR LSYPGHDNDG PYRVVYKIER DKFRVKNLQG GDDIETGSVL GEIESDKESP
     TPMQYNPATG TFLPVPAPSP PPKDVDDHES KSPPASPSSE ENDNIPKSIP TRKPEPTANQ
     KRQRQPAAAV SNKANAQNTI RISQKKKTDG IGRAVDKKPG LKQVLKEGSQ SISNMWNKDG
     IENGSRARQG NTASSRAESS QKVTALHNRP TKASQERSIA NRRSIATPEP LNRSSSRTSY
     LSLSDRRHSI AQSSYNAVTG GMKPPSPTLT KDSPFLQDST FRSRRGSLLG TTVPASPMRG
     HRRSGSHAPS IYSLATNDSQ TSLVLSSYYK KSTYSAADAL HTLRQEGFVD GTFPEGHLLP
     NITRYMRFSS ACYGSHFLKF LGISNNMPKM TSWDGIHQDV RHFAHHTESN TGNILLASFV
     DPQGGSDSTG ATGTGVPLVH YISLDHEAKA VVLACRGTLG FEDVMADMTC DYDDLVWKKR
     SYKVHKGVHA SARRLLYGGD GRVLVTLKEA LAEFPDYGLV LCGHSLGGGV TALLGVMLAE
     ANPNGPGFVT APEAAFKKML TDERSNSNVH NEVFIPAGRR IHVYAYGSPG VMSPKLRRIT
     RGLITTVVHG DDLVPHLSLG ILHDFQALTL AFKDKENATK ADMRKRMWAA IQGNLSYAWH
     GGSESRAVPG NDEHKWMLPA LAALRENFTC ERLVPPGEVF VIESYPALRR EAFLLNGEGL
     LGRPATRVIL KYVRDVETRF LEPRFGTSML TDHSPANYEN ALNKMRLGVV D
//
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