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Database: UniProt
Entry: A0A091LSN9_9GRUI
LinkDB: A0A091LSN9_9GRUI
Original site: A0A091LSN9_9GRUI 
ID   A0A091LSN9_9GRUI        Unreviewed;       409 AA.
AC   A0A091LSN9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Lipase member M {ECO:0000313|EMBL:KFP45801.1};
DE   Flags: Fragment;
GN   ORFNames=N324_05000 {ECO:0000313|EMBL:KFP45801.1};
OS   Chlamydotis macqueenii (Macqueen's bustard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX   NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP45801.1, ECO:0000313|Proteomes:UP000053330};
RN   [1] {ECO:0000313|EMBL:KFP45801.1, ECO:0000313|Proteomes:UP000053330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP45801.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701}.
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DR   EMBL; KK764014; KFP45801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091LSN9; -.
DR   Proteomes; UP000053330; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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:SF168; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053330};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..409
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001876486"
FT   TRANSMEM        283..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..107
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   ACT_SITE        182
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        355
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        384
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP45801.1"
FT   NON_TER         409
FT                   /evidence="ECO:0000313|EMBL:KFP45801.1"
SQ   SEQUENCE   409 AA;  46653 MW;  2213111185ED28ED CRC64;
     TMMWLFVSIA CLMCTSEKSD GSPEVSMDVG EIVRYHGYPY EEHEVMTDDG YYLTVQRIPH
     GRDNSASTSI SHKAEAQGSS MFCPTPKPAV LLQHGLVLEG SNWVTNLPNS SLGFILADAG
     YDVWIGNSRG NSWSRKHKEF EFHHKEYSAY SFHEMAMYDL PATINYILQK TGQEQLYYVA
     YSQGTTTGFI AFSSIPELDH KIKMFFALAP ITTNSNMKSP LVRLFDLPEV LVKLILGRTV
     VFDKGELLQQ VISSLCSYTI FKRFCSLVLY LPGGFTNSLN VVLFFPIISI VFLMVPSNAW
     VINTVLLLFQ VYQTGEFKYY DYGSDNMLHY NQITPPFYEL ENMKAPLAAW YGGKDWISAP
     EDVNITLPRI TNVAYQKYIP EFVHFDFLWG VQAYEQVYKE ILELMEKSA
//
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