ID A0A085M4Z2_9BILA Unreviewed; 397 AA.
AC A0A085M4Z2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN ORFNames=M513_06851 {ECO:0000313|EMBL:KFD52288.1}, M514_06851
GN {ECO:0000313|EMBL:KFD66749.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD52288.1, ECO:0000313|Proteomes:UP000030764};
RN [1] {ECO:0000313|EMBL:KFD52288.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD66749.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD52288.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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; KL363229; KFD52288.1; -; Genomic_DNA.
DR EMBL; KL367521; KFD66749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085M4Z2; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; 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:SF163; LIPASE; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..397
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010405241"
FT DOMAIN 36..94
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 341
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 370
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 397 AA; 45622 MW; 784A5278ED6E5F10 CRC64;
MTAASLNHIV AILAVLLLHT QQLRSQSGEE YMNTCDIIRL RGYECTEHTV ITKDKYILTM
HRLSPKQCGE MKKPGRPIIL QHGLLQSSIH WVINYANQSL GFLLANAGYD VWLGNIRGNI
YSKGHTSLSP YLKEYWNFTF DQMAEYDLPA MVEYVLQVTN HSSLDYVGHS QGTLIGFACF
SEKPDWARQK IRSFHAFAPV AYVGHTKTVL RLLRPFFQLV NWMLKHSHYE ILPNTDGVKW
VARKICKGKT VPICEKVLHK LGGYEPRNVN ATRLSIYLSH YPAGTSTLNI AHFGQLIKTN
KMQKFDYGTK GNLLRYNQTF PPQYHPERSR VPTALYWGAN DVLSVEKDVR RLINITHSEL
GLYRYENTEH VDFMWGLNMI DAAYAQLMRV LSKLPAR
//
