ID F0ZMM9_DICPU Unreviewed; 403 AA.
AC F0ZMM9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN ORFNames=DICPUDRAFT_152935 {ECO:0000313|EMBL:EGC34804.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC34804.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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; GL871082; EGC34804.1; -; Genomic_DNA.
DR RefSeq; XP_003288661.1; XM_003288613.1.
DR AlphaFoldDB; F0ZMM9; -.
DR STRING; 5786.F0ZMM9; -.
DR ESTHER; dicpu-f0zmm9; Acidic_Lipase.
DR EnsemblProtists; EGC34804; EGC34804; DICPUDRAFT_152935.
DR GeneID; 10499115; -.
DR KEGG; dpp:DICPUDRAFT_152935; -.
DR eggNOG; KOG2624; Eukaryota.
DR InParanoid; F0ZMM9; -.
DR OMA; DGEHVDC; -.
DR OrthoDB; 5474043at2759; -.
DR Proteomes; UP000001064; 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; IPR022742; Hydrolase_4.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005:SF165; LIPASE; 1.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR Pfam; PF12146; Hydrolase_4; 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:UP000001064};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..403
FT /note="Lipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003265236"
FT DOMAIN 38..103
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT DOMAIN 105..214
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
FT ACT_SITE 180
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 376
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 403 AA; 44778 MW; C9B15E288DA76A2C CRC64;
MKLLYLYLLV AVLFSIANSS LFASSSSSSS NPDLVRNISE IIQARGYPVE NHQAITPDGY
ILSVQRIPAG RYQNNPNPYG SNGKPAVILQ HGVEDLGITW VLQENVYQSL GFILADNGFD
VWINNVRGTT YSNSNINYSS DSKEFWAFSF DEMAQYDLPT VVDYVLETTG NKKVGYVGHS
QGTTMAFIGM TNQTVADKIN LFVALAPVVR VTHCESDLLN ILSDFNVDIL FAALGFNAFL
PDTPFLQKYL PVICKNAPSI CENSLALIMG WDEASINTTR LPVYMAHEPG GTSVQNVIHW
SQATKDGYQK FDYGVVGNLA HYGQATPPQY NIRDFNVPVV VYSGGQDYLA DPTDVQWLID
RLSSLVNWKS LPSYSHLDFV WGENAYIDVY GEVTQYLLKY ANA
//