ID   A0A162J5T0_9HYPO        Unreviewed;       804 AA.
AC   A0A162J5T0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=BBO_06364 {ECO:0000313|EMBL:OAA39838.1};
OS   Beauveria brongniartii RCEF 3172.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC   Beauveria brongniartii.
OX   NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA39838.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA39838.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA39838.1,
RC   ECO:0000313|Proteomes:UP000076863};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA39838.1}.
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DR   EMBL; AZHA01000021; OAA39838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162J5T0; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000076863; 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; 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}.
FT   DOMAIN          188..804
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   804 AA;  88507 MW;  F5255D3117604728 CRC64;
     MKHPGKILGQ LATNGLRPSV GRRRPAFSPL RLSNSLFTAA KQRRRASATT AIVAGGFLVW
     LLYPSEDFDR LSGKRAQATL VHPSAASKAD EGASSREGDQ EGGGGGGKKN ASTDETAWGS
     FTKGLEERSA AADKEWSAFS EKLVGFILPE WSRQIPSFIR KLQHELSDAP GSLAQELWAE
     AHNPSVHPEI QYTAKVRVSD ELCPDEKEFL ARRKKKTRAA LAKYLDIDEK DIHPDDIPTI
     AMCGSGGGLR ALIAGTGSLL AAAEDGLFDC ATYTAGVSGS CWLQLLYLAS FNKGSIPSLL
     EHLKARTSTH IAYPPVALQA FTSLPTSRPL LSGVIEKIRG DKNADFGLVD IYGLLLGARF
     LVPKGELGVN DWDFKISNQR GILRDGDRPL PIYTAVRHEI PGLEQGKDKT KSSEDVSTTK
     KQLEKVEKES WFQWFEITPY EVFCEEIGAG IPTWALGRRF KDGKDVPLAH GSHLPEIRAP
     LMMGIFGSAF CATLSHYYKE IQPIVKGLTG FGTIDQMISG QDSTLATVHP IDPAIIPNYA
     YQMYGKLAKT ATPSMYENEH IQLMDAGMSN NLPIYPLLRP GRGVDVLISF DASADIKTDN
     WLAVADGYAR QRGIKGWPVG VGWPQDEIKA VHEMKAAEAH STAQADAKIA QARSDQQQQQ
     HQEEHKSQKV SDLGYCTVWI GTTEERTTKE QAPATQPVSE AEHWRLSDPN AGLAVVYVPF
     LPNDKVPGVS PAESDFMSTW NFIYTPDNID DVVRLARANY DEGKAQIRNT VRAVYERKKQ
     LRMKREEKAQ ESRLRKLTNA VSLI
//