ID   A0A183IV23_9BILA        Unreviewed;       404 AA.
AC   A0A183IV23;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN   ORFNames=SBAD_LOCUS7470 {ECO:0000313|EMBL:VDP13231.1};
OS   Soboliphyme baturini.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX   NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000775101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SBAD_0000775101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP13231.1, ECO:0000313|Proteomes:UP000270296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
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DR   EMBL; UZAM01010656; VDP13231.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183IV23; -.
DR   WBParaSite; SBAD_0000775101-mRNA-1; SBAD_0000775101-mRNA-1; SBAD_0000775101.
DR   Proteomes; UP000050793; Unplaced.
DR   Proteomes; UP000270296; 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:SF100; 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.
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:UP000270296};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..404
FT                   /note="Lipase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035045646"
FT   DOMAIN          32..95
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        343
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        372
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ   SEQUENCE   404 AA;  46085 MW;  4065323E54D3CEF3 CRC64;
     MFTFYGFASL IFVGVYTEGI TARDPEILMN CSQLIGYWEY PMEEHRVVTE DGYILKIYRI
     PHGHSRNVMY DFTPKPVVFI QHGLLSSCAD WISNLRNESL AFVFADAGFD VWLGNFRGNT
     YGREHIRLNT TSHEFWQFSW DQMAEYDLPA MVNMALNVSG AEHLYYIGHS EGAMTVFAKL
     SNDQEFAKKL KLVFALGPVT TVAHIKGVLS FLAKLTPQIA KITELFGIDE FLPDNKFVDF
     MKELFCKKHV AVELCKNILF LIAGPDSHQL NTTRVPVYIS HTSAGTSVRN IVHFAQLARN
     GHYEMYDYGS AAKNIFYYGQ ATPPVYDVRN ITVPVSLFWG AEDWLADPQD VVDGLLSKLK
     TVTSHFLKGF NHLDFLWGLR ATKMVYDVIR DEIYKDLVID NLKS
//