ID   A0A084QET0_STAC4        Unreviewed;       832 AA.
AC   A0A084QET0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN   ORFNames=S40285_05847 {ECO:0000313|EMBL:KFA62465.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA62465.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA62465.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA62465.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000256|RuleBase:RU362103};
CC   -!- SIMILARITY: Belongs to the lysophospholipase family.
CC       {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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DR   EMBL; KL660795; KFA62465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QET0; -.
DR   STRING; 1283841.A0A084QET0; -.
DR   HOGENOM; CLU_013227_1_0_1; -.
DR   InParanoid; A0A084QET0; -.
DR   OMA; WALGRRF; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   CDD; cd00147; cPLA2_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF40; LYSOPHOSPHOLIPASE; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU00555};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT   DOMAIN          190..602
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          30..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          783..814
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        30..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   832 AA;  92834 MW;  BE61FA0E113B2EA8 CRC64;
     MFRSAKPLKS LSLLQARTRI CPSLVCRRAP PLSSQSQRPL FSWSKTRRES QRGRTPSRIP
     LAIATGGLVI WLLYPSDDFA ELSDKGSGRK SRRRNDASQD DADQDDQEAE GQEALLYPAF
     ANFARRFESY SLKTDIEWLA LSDKLVDLIL PEWSKLIPVY IRKLQRELSM SPGSLADEIW
     REAQNPDINP EIRYRAIVRV SNDLCDEEKE YLARRRRVTR AALAKYLGLE EKDIHPDDIP
     TIAMCGSGGG LRALVAGASS MLATEEDGLF DCVTYTSGVS GSCWLQALYL TSFNRGNLGS
     LLEHLKSRAS VHIAYPPVAF NSLVSLPTSK YILSGLVEKL KGDPNADFGL VDIYGLLLAA
     RYLVPKGELG VNERDFKLSN QREYIKYGQL PLPIYTAVRH EIPELEVAAS QPTTDEAAVA
     KHIEQSADKE AWFQWYEITP YEFFCEEFGA GIPTWALGRR FKSGRDVPLD HGFHLPEIRL
     PLLMGIFGSA FCATLSHYYR EIRPVVRKIS GLDTIDHVIS GRDDDLSKVH PIDPASIPNF
     AYQMHGRLPA TTPPSILENE YIQLMDAGMS NNLPIYPLLR PGRDVDVVVA FDASADVKTD
     NWLSVVDGYT QQRGIKGWPV GIGWPKPGES VSQVSKELES AEAQSTREAE DKLSEAKREQ
     DTLRKEAIQQ GEDVKSGKGP SKFVPGNQEA GDLGYCTVWV GTTQQRTSDA PPPTKAITDS
     DSWKLMEPDA GIAVIYLPFV SNPKAPGISP GTSDYLSTWN FCYTADQIDQ VVQLARANYD
     EGREQIRSTV RAVYERKKKL REEAEKQLRL AKYRDIASRG EAVLLGEGDQ FS
//