ID   A0A135UR18_9PEZI        Unreviewed;       648 AA.
AC   A0A135UR18;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=CSAL01_02702 {ECO:0000313|EMBL:KXH62797.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH62797.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH62797.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH62797.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-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:KXH62797.1}.
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DR   EMBL; JFFI01001150; KXH62797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135UR18; -.
DR   STRING; 1209931.A0A135UR18; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000070121; 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; cd07203; cPLA2_Fungal_PLB; 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:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           19..648
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5007747283"
FT   DOMAIN          53..604
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   648 AA;  69361 MW;  2964FCEAFD74124E CRC64;
     MMLPSLLAVA AAVAPVWAVD PVKPMAAGLI MEALDPRALP DSPSGGYAPA IVDCPSARPT
     IRSASALSPN ETAWLTRRRN VTVGPMREFL TRVSIPNFDA GAYIDRVKSS SSQLPNIALA
     VSGGGYRALM NGAGFLAAAD SRTPNSTSAG QIGGLLQSAT YVAGLSGGGW LVGSMFTNNF
     SSVVDLQRGS KGSAVWKFDR SIFSGPKESG LSILNTAEYW RDVAKQVDTK DQGFEVSITD
     YWGRALSYQL INATDGGPSY TFSSIADMPD FQSGQQPFPI LVSDGRAPNE RIISLNATVY
     EFNPFELGTW DNTAYGFAPL RYLASNFSAG RIPDNGSCVR GFDQAGFVMG TSSSLFNQFM
     LQNLSSAGLP DFIQSALTSI LNVLDQDNND IAQYVPNPFY GYNPRTNINA NQTQLSLVDG
     GEDLQNIPLH PLIQPNRAVD VIFAVDSSAD TNYNWPNGTA LRATYDRVAE PIANGTLFPP
     VPDANTFINL GLNRRPTFFG CNASNFTLSG NQRVPPLVVY LPNAPYVAHS NVSTFDPSYE
     LDQRDAIIQN GYDSATQGNA TLDANWPVCV ACAVLSRSMA RSRETVPDAC AQCFSRYCWN
     GTLDTRDVDY NPTFAIGNIE ANSPAARTGV SFAAGLLSAV AAMLVLAI
//