ID A0A232EYB6_9HYME Unreviewed; 432 AA.
AC A0A232EYB6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN ORFNames=TSAR_002182 {ECO:0000313|EMBL:OXU23412.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU23412.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU23412.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU23412.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU23412.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
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:OXU23412.1}.
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DR EMBL; NNAY01001620; OXU23412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232EYB6; -.
DR STRING; 543379.A0A232EYB6; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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:SF147; LIPASE-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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000862};
KW Lipid degradation {ECO:0000256|PIRNR:PIRNR000862};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000862};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..432
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012714621"
FT DOMAIN 62..119
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT ACT_SITE 196
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 369
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 432 AA; 48648 MW; E5BC012D388DF851 CRC64;
MMRESFICSV LLLSGLVGCG SSGLAQGFNF FDYISPLSIK REKSLGRSDG VEKIPVLDFI
GLVKRHDYPA EEHKITTLDG YLLRLHRIPG SQKSPSASDK PVVFLQHGIL ASSDQFVIAG
PERDLAFILA DAGYDVWLGN IRGNTYSRSH VQLSPDRNPE FWQFSMHEMG LYDASAAIDH
ILQITGQQSI IYVGHSMGTS IVLILLSCKP EYNDKIRLVI NMASVGYWIR PRNFIKLLKD
NGEVLQRFLL AARITEVFPQ TLANGEILNG TCRAGSPFQH LCMDFIQYVS GYSPELFDTR
LVAESFSYFP AGGSTQTLLH FYQNIKAGKM QMYDHGLVGN FARYNQRTPP VYNLENIVTP
VVLIYGRSDA VATPEDSMDL LNRLRNARAE SVPYDNFNHL DFIWGKDTKR LLQNRIMQII
ENFMRNGSLS VL
//
