ID   A0A026WLA4_OOCBI        Unreviewed;       415 AA.
AC   A0A026WLA4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN   ORFNames=X777_03061 {ECO:0000313|EMBL:EZA56441.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA56441.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA56441.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(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; KK107167; EZA56441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026WLA4; -.
DR   EnsemblMetazoa; XM_011337443.3; XP_011335745.1; LOC105278393.
DR   OMA; HIWTEDG; -.
DR   OrthoDB; 3259424at2759; -.
DR   Proteomes; UP000053097; 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; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR025483; Lipase_euk.
DR   PANTHER; PTHR11005:SF147; LIPASE-RELATED; 1.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000862};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR000862};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          91..217
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   ACT_SITE        184
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        360
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        391
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ   SEQUENCE   415 AA;  46749 MW;  261D7FD06B8E26A7 CRC64;
     MSGIGRQDEA HMATPELIEA HGYKAETHKI WTEDGYGLAV HRVLPSNDRV PSVPNIDSTI
     NTSTDCSVEC HNSSASVEAP ESRGSASSRL PVLLCHGLLS SSSDWVLLGP HEALSYVLCD
     SGYDVWLANC RGNTYSKYHK HYTRRDREFW NFSWHEIGYY DLPAMIDYIL KETGHSDLYY
     IGHSQGTTVF FVMGSERPEY NAKIKGMISL APAVFLSNQR SPLITFLVHI IDLLEWGSVI
     CNIHHLLPRN RWQSRILSTF TRNAPCTLTQ GLCNCWFSLI AGFGSNQLDK SIVPVIFGHF
     PAGSSTRQIF HFASIIHSGL FRKFDYGAKT NLALYGSTQP PKYSLERVKA PVALFYSDND
     LLIHHSDVQK LASTLPNVIE VKKVAYEKFN HIDYLWGRDA RTLLYNGVVA LLKKF
//