ID A0A016UR66_9BILA Unreviewed; 381 AA.
AC A0A016UR66;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN Name=Acey_s0029.g1950 {ECO:0000313|EMBL:EYC17904.1};
GN Synonyms=Acey-lipl-8 {ECO:0000313|EMBL:EYC17904.1};
GN ORFNames=Y032_0029g1950 {ECO:0000313|EMBL:EYC17904.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC17904.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC17904.1}.
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DR EMBL; JARK01001365; EYC17904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016UR66; -.
DR STRING; 53326.A0A016UR66; -.
DR Proteomes; UP000024635; 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; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006693; AB_hydrolase_lipase.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005:SF90; LIPASE; 1.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 2.
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:UP000024635};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..381
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001492639"
FT DOMAIN 28..93
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 309
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 340
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 381 AA; 43892 MW; BE8BBAC31D3FD9AE CRC64;
MLLYYVLVFV SILNPAHPTR NEETFMKVPQ LISHFGYMFE EHYVTTEDGY ILTVHRIPVG
RDDRPAPHSS HRRPPVLLMH CLLCDSSVFV LNLPTQSLGF VLADAGFDVW MANTRGNEYG
KNHSYLSVGD KAFWNFTWYH HSRYDLKNTV EYVINATKQE DIYYVGHSQG TLIMFARLAE
DPHFNSKEMR MLSGVPLDVP HFLKKYFAGF CSVNVMSKVC NVFLTLVGMG TEQLTQFNNS
RWDVVAGHLP SASSALNLLH WAQVLRFHEL RKFDYGEARN IDVYGQKQPP LFNLTRITTP
MFMFWSSDDT LAPDTDVREH IIKKLGNALK GSFALAHFTH IDFILGLRAT EDVYKPIVRL
IYNDLAERAK TLHRLRTIIL K
//
