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
//