ID   A0A0D2G696_9EURO        Unreviewed;       809 AA.
AC   A0A0D2G696;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=Z517_12205 {ECO:0000313|EMBL:KIW74265.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW74265.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW74265.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW74265.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) 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|ARBA:ARBA00000960,
CC         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; KN846977; KIW74265.1; -; Genomic_DNA.
DR   RefSeq; XP_013278073.1; XM_013422619.1.
DR   AlphaFoldDB; A0A0D2G696; -.
DR   STRING; 1442368.A0A0D2G696; -.
DR   GeneID; 25311695; -.
DR   VEuPathDB; FungiDB:Z517_12205; -.
DR   HOGENOM; CLU_013227_1_0_1; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000053029; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053029};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           20..809
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005112984"
FT   DOMAIN          173..802
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          602..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  89841 MW;  EA749914D468A051 CRC64;
     MSAARLLFNS SSLQYTALAA LACAGVQSSA RRTKPVRLDS PSGIHTTQDA SLIAYARRVQ
     SHYAHAEDPN HATKRDDATI VDRTNDPDKY LPAFESDDEN AWASFSRNFH NVREGIARID
     WSTVGDKITD LVVPKWAKIL PDGFQKLQSE LSMQPGTLAD QIWQEAHDPY INPEIEWNAT
     VRVGDTLGSD ELEFRRKRKQ VVVKALAKYL GLDEKEIHPD DVPTIAICGS GGGLRAMVAG
     TSSYLSAQEA GLFDCVTYTA GVSGSCWLQT LFYSTLGKQD HRQLLKHIKS RIGTHIAFPP
     AALKLVTSAP TNKFILSGFV EKIKGDPGAT FGLVDVYSLL LAARLLVPHG ELDVNDQDLK
     LSNQRLYIEN GQLPMPIYTA VRHEIPVDEE EEELSKDNLA LKQKIKEKAR KEAWFQWIEM
     HPWEVWCEEF GAGIPTWSLG RPFKNGRNLL LDSGVALPEI RQSLLLGIWG SAFCATLAHY
     YKEIKPALIG MVGFDGVNQL VEEKNEDLIK IHPIDPATIP NFVYGMEGQL PSTCPDSVFK
     NDHLQLMDAG MSNNLPIYPL LRPGRDVDVL IAFDASADIQ KENWLSVVDG YAKQRGIKGW
     PVGAGWPRAS SKPQENVKAL EEAQATTPQE AATKLAAARE EDRENKAADK DNTTESPTTG
     SAPDTASVLG PCTVWVGSKA ERSSDEEPPP SKSLNWDASD NEDSASFHLM DPNAGIAVIY
     FPLLPHPDVP NIDPDKSDFM STWNFIYTPE QVDSVVELAK RNFAEGEEKV RETVRAVYER
     KKKVRLEKED KKTSKEWKGR IRRVGNTFV
//