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Database: UniProt
Entry: A0A0V0X173_9BILA
LinkDB: A0A0V0X173_9BILA
Original site: A0A0V0X173_9BILA 
ID   A0A0V0X173_9BILA        Unreviewed;       393 AA.
AC   A0A0V0X173;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN   Name=LIPF {ECO:0000313|EMBL:KRX81661.1};
GN   ORFNames=T06_11854 {ECO:0000313|EMBL:KRX81661.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81661.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX81661.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX81661.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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}.
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:KRX81661.1}.
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DR   EMBL; JYDK01000029; KRX81661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0X173; -.
DR   STRING; 92179.A0A0V0X173; -.
DR   Proteomes; UP000054673; 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:UP000054673}.
FT   DOMAIN          37..93
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        341
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        369
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ   SEQUENCE   393 AA;  45274 MW;  6365335801A67F8E CRC64;
     MKFCPSCVLC HEVGDSSGNT VEDCGRRHLP EVDLQAKEII EYHGYTAEEH DVTTVDGYII
     RLHRIPVSIE NAGNTAVLLL HGLAASSTSF ITNEPKQCLA FLLADRGYDV WLGNVRGNLF
     CQQHRSLTSE DPKFWRFSWD EMAAYDFPAT VDYILEKTEK ETLRFVGYSQ GALIGFAALS
     LLPDLRQKIC CFVALAPAVT LAYFKSPLRH VNRCVPLMER LFRRCGESQH GDATKVSKYM
     KPFLKNDPFD QLSQNIIFRM IGPDSRKYID KDRIPVYLSH NPAGTSYQNM VHYLQMMNSK
     QLRHFDYGLV KNFLKYGQAR PPIYPLENVD VPLYIIWSEK DVYANKKDIE LLFSRVRHAK
     ELKITDYSHL DFLWANNVGE TVYSRVIEFL EQF
//
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