ID   A0A094D391_9PEZI        Unreviewed;       817 AA.
AC   A0A094D391;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=V497_03339 {ECO:0000313|EMBL:KFY60856.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY60856.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY60856.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFY60856.1}.
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DR   EMBL; JPJZ01000776; KFY60856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094D391; -.
DR   STRING; 1420910.A0A094D391; -.
DR   HOGENOM; CLU_013227_1_0_1; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000029268; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
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   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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          154..714
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          589..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..663
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   817 AA;  90295 MW;  A3E1C95756055C94 CRC64;
     MESNGTVAKA TTIVLVAGLA YILYENDFLQ PLPPTKTRER LTVERVAREK LEEKVEKDAN
     ENVEELSKLP FAKAAAPDKN ADDSSWGRFA SGFESLSSLK DVEWSTVQAN ITGYILPEWA
     KNIQEGLSKL QLEMSMAPGS LADEIWKDAQ DPENNPEIVR KASVRVSQEL CDEEKEFLKK
     RKVVTTAALA KYLGIPEEEV HPDDVPTIAM VSSGGGLRAL VAGTGSLLAA NEDGLFQCVT
     YTAGVSGSCW MQTIYHSSLS HRRFDYMVNH LRARLGTHIA YPPDALTALN SAPTNKFLLS
     GFVEKLKGDP GADFGVVDLY GLLLAARLLV PKGELGVDNR NLKISNQRES LKNGEHPMPI
     YTAVRHEIPI LEESTDKEKE TNKPSAATKA LAKKESWFQW FEISPYEMFC EEFSAGIPTW
     AMGRQFKDGE DVPQENGLRV PEMKLPLLMG VFGSAMCATL SHYAKEVKPI MKGILPVGFS
     TIRDIIEENN DDLSKVHPID PASIPNFCVG MKDRLPETAP DSIFETDHIE LMDAGMSNNL
     PIYSCLRPGR DVDILIAFDA SADIKTENWL QVTEGYALQR GIKGWPLGAG WPKQEDSSEQ
     AAAQLEDAQV ASAAEADARL NEAKAEAKAD HKAHDKDARA DASKDKADKS DAGKDKEAAD
     SDNNTADNGD LGHCNVWVGS TQEREHTDQS HAPQSKSEEP ESKAELEEWQ LMKPDAGIAV
     VYFPLIPNKK LEGVEPETSP YMSTWNFIYT PEDVDNVVGL AKANFDEGKE RTRRVVRAVY
     ERKKRAREER EGKEREAVFK RNMKLGAVGE DGGQEHD
//