ID A0A182WAG9_9DIPT Unreviewed; 401 AA.
AC A0A182WAG9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN007347-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN007347-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN007347-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
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DR AlphaFoldDB; A0A182WAG9; -.
DR STRING; 112268.A0A182WAG9; -.
DR EnsemblMetazoa; AMIN007347-RA; AMIN007347-PA; AMIN007347.
DR VEuPathDB; VectorBase:AMIN007347; -.
DR OrthoDB; 3259424at2759; -.
DR Proteomes; UP000075920; 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:SF147; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..401
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008141024"
FT DOMAIN 36..95
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 377
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 401 AA; 45550 MW; 3D0FACFB97E15EB4 CRC64;
MALVTSSIRF LLMAWYIASS VGDIIFREED GFLTTPEITR KYGYTTEVHN IVTEDGYIVE
LHRIRGSPAS GPTDPTKLPV LLMHGLMGSS ADWILIGPEE ALPYLLADRG HDVWLGNARG
NRYSRNHTYL PLEEHEFWDF SFHEIGFYDL PAMVDHVLSR TGKTQLHYVG HSQGTTIFFV
LNSLRPEYNR KFRLMQALAP AVFLSHLQNP FLRFLAQHET VALQFVNSFG IYEMKPFPEE
INRLAKALCP DFYSRALCLD AMHTMTGNKY HHMSHLGFPM LMHHLPAGCS LKQVAHFGQE
VISGHFRPYD FGAVENRRRY TGNDVPPDYD LTKVTVPVVV FYGLDDQLTH PNDVRLLAGR
LPNLVALNQL PNATFNHMDF LLAGDVKDAL YDSIIGNVEQ T
//
