ID   A0A2N5SZE5_9BASI        Unreviewed;       550 AA.
AC   A0A2N5SZE5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=PCANC_09197 {ECO:0000313|EMBL:PLW18607.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW18607.1, ECO:0000313|Proteomes:UP000235388};
RN   [1] {ECO:0000313|EMBL:PLW18607.1, ECO:0000313|Proteomes:UP000235388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW18607.1};
RA   Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA   Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA   Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT   "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT   Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL   Submitted (NOV-2017) 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:PLW18607.1}.
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DR   EMBL; PGCJ01000828; PLW18607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5SZE5; -.
DR   STRING; 200324.A0A2N5SZE5; -.
DR   Proteomes; UP000235388; 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   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:UP000235388};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           21..550
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5014490648"
FT   DOMAIN          53..550
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   550 AA;  61374 MW;  5499BC335D8DBEC3 CRC64;
     MPSWFYIVIT LLLCFQYISA VPTFQEIDNP NLRRRDPALA TSPSGGYVPV HIDCPQNPFV
     RSPFDKDNGH AQLGRGESTY IKEKAAQSIP LWQKYLENVR LEKFKIDEFL KPAKEKGGVA
     ALTLPNIGFA VSGGSVRALL YGTSILDSFD SRNDKANEAK VGGILQLANY AVGVSGASWL
     IGGWATSNFP VLSTLVPTWR LSQDNELWKW NVAKHYGSHH KMVKKKHKAG FPVSLVENEP
     GKKKQQIGKA VLWSSIREGS LYKKREAPFV MAVATSRPDK GKPFTPESPT YEFSAEEFGL
     YHPYLNVSIP IEHLGSTYTA TRPESQRCVA GFDNAGFIMG MSSNIFSVGD APKEDKKPKY
     IRVAQKFVHD HTDFEGKVPN PFKGLGKKSD PSGGDFQDTD RDLILMADSG LIEENIPIRP
     LIQPERKLDV VFALDSSAAG QDPRDPSLYR YPNGAQLYGI YSKTKLPVYG GYHMPNIPNA
     SDGTFTKLGY TKRPTFFGCD DLRGPLIIYM PNYHATEDTN AATEKLTFKL LKMLDQHRIR
     TGQFAWHVPW
//