ID A0A1U7LQR0_NEOID Unreviewed; 491 AA.
AC A0A1U7LQR0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Hormone-sensitive lipase {ECO:0000313|EMBL:OLL25010.1};
GN ORFNames=NEOLI_000116 {ECO:0000313|EMBL:OLL25010.1};
OS Neolecta irregularis (strain DAH-3).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Neolectales;
OC Neolectaceae; Neolecta.
OX NCBI_TaxID=1198029 {ECO:0000313|EMBL:OLL25010.1, ECO:0000313|Proteomes:UP000186594};
RN [1] {ECO:0000313|EMBL:OLL25010.1, ECO:0000313|Proteomes:UP000186594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAH-3 {ECO:0000313|EMBL:OLL25010.1,
RC ECO:0000313|Proteomes:UP000186594};
RA Cisse O., Nguyen A., Hewitt D.A., Jedd G., Stajich J.E.;
RT "Evolutionary innovation and constraint leading to complex multicellularity
RT in the Ascomycota.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OLL25010.1}.
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DR EMBL; LXFE01000515; OLL25010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7LQR0; -.
DR STRING; 1198029.A0A1U7LQR0; -.
DR OMA; FPEGWRY; -.
DR OrthoDB; 37251at2759; -.
DR Proteomes; UP000186594; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR23025:SF3; HORMONE-SENSITIVE LIPASE; 1.
DR PANTHER; PTHR23025; TRIACYLGLYCEROL LIPASE; 1.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 4: Predicted;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186594}.
FT DOMAIN 74..219
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 276..357
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ SEQUENCE 491 AA; 55994 MW; 8B4E85E42883D69F CRC64;
MLNLYQFTHR TAEQLRVSLA KVSSPYLKFF VGLSKPRLKI KRKIVIPRNS AEPSEVWIYF
NGSEEELKFQ RKLVFFIHGG GFISTNPECY EEVTFAWASE LNVPVVAINY KKAPEYPFPY
ALYECRDLYL EIVKTNGAII GFEHSQPLTI AFAGDSAGGN LATSLIILLL TEHLDIPIPA
GLVLVYPALD LNLTCWMTNE NMCLLRQESV RDVSDAVIDS KLNYEKRKSV LQPYSDNYSP
RKSLVKIFQT PPPKEAEKCF SPTPRMKNAR TKLAMTSRVS FFQDRILSPE MLRAMVLLYV
GPQNRPNFET DYLLCPLRAP TEVLAKFPKT YLLCGEKDAM VDDTVLLAGR IREAKRAALN
RRQNLQMTSL SSSENDWIEI VLLRGVSHGF FQMAFILPEA KKAISKCRGW LKEILDDQSF
ISPSFEDDDE PVEMKSSNSL LFPMGPTLPI SAMIPQNKEG HDTWERFVMQ ESDLLNRRRE
GVMRGLQFTE S
//