ID   A0A3B0KDP3_DROGU        Unreviewed;       443 AA.
AC   A0A3B0KDP3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Blast:Lipase 1 {ECO:0000313|EMBL:SPP81778.1};
GN   ORFNames=DGUA_6G013516 {ECO:0000313|EMBL:SPP81778.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP81778.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701}.
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DR   EMBL; OUUW01000006; SPP81778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0KDP3; -.
DR   OMA; ELNMTMF; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR006693; AB_hydrolase_lipase.
DR   InterPro; IPR025483; Lipase_euk.
DR   PANTHER; PTHR11005:SF144; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   Pfam; PF04083; Abhydro_lipase; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..443
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017412866"
FT   DOMAIN          43..94
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   REGION          403..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..443
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        335
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        364
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ   SEQUENCE   443 AA;  50250 MW;  4DBF43087BD61815 CRC64;
     MPHAKWMRCL LWLTLQCMWV DGGYLEDNFP ASVIEDAHLS TLQLLQKYKY PAEGHQVTTE
     DNYILTVHRI PRPGAQPVLL VHGLEDTSST WIVMGPQSGL GYFLYGHGYD VWMGNVRGNR
     YSRGHRQLNA NTDRAYWSFS WHEIGVYDLP AMIDGVLAKT GYAKLSYFGH SQGTTSFFVL
     ASSRPEYNAK IHLMSALAPV AFMAHAKAPL LGIARVGINM LGESFELFPH SYMYLNQCLQ
     SAGMLKTCLR FLWQVVGKNR EEFNMTMLPV VLGHIPGGCN VKQPVHYMQL RSSGRFCQYD
     HEAKENQKIY GRSSPPDYRL ERITAPIALY YGSNDYLSAV EDVQRLAKLL PNVVENHLYK
     KWNHVDMIWA ISARHSIQPK MLEAMRYWES AVGGSKHAEA TTSYVVEEEI AEPVSEAATE
     SPDDETEVEE QTGKEREGAR DED
//