ID   A0A2N5VLW1_9BASI        Unreviewed;       626 AA.
AC   A0A2N5VLW1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=PCANC_08140 {ECO:0000313|EMBL:PLW50981.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW50981.1, ECO:0000313|Proteomes:UP000235388};
RN   [1] {ECO:0000313|EMBL:PLW50981.1, ECO:0000313|Proteomes:UP000235388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW50981.1};
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:PLW50981.1}.
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DR   EMBL; PGCJ01000087; PLW50981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5VLW1; -.
DR   STRING; 200324.A0A2N5VLW1; -.
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..29
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           30..626
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5014494431"
FT   DOMAIN          35..626
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   626 AA;  68564 MW;  964068BCC325063E CRC64;
     MAHAHQSLFT RLFAALVLLS FSLAQRASAT PHFVTCPSTS KSLIRSSISK DFKQRLCSQE
     ARYIASRRAN VARPAYANFL GNVQRALRTH SPTTTLPIYV SQIMAGENFA TLPRTGFAVS
     GGGMRALQFS IGVLSAFEAK NEQSIRVGTG GLLNAADYIS GLSGGSMTVL ALTYGAYDLA
     SVNSPKALDH ILPQFDMFSP GNFSKIPGST ADQLNQKYLT EAFVKMSGKR QAGFRVTLAD
     LWGLFIRFHT LGQTTVSNFY DFSLPHGADE SFSGIRNLPK FRKFLQPYPI ITALGLSSPD
     QYASRKEPSA FVPITSNQYE FTPFETGSWD SNLASFIPTE YLGTRLRAGI PLDRTKCVNK
     FDQAHFLSGI SSDIFPSLNT SQEFFFEKSA IKSLVKAINT TFGSSQPGIS IDTASVPNPF
     FQSGTDRYSD RNSFDLRLLD GGLDGAVTPY YPLLAPARQL DVIIGIDSVS LDNDGGGDYS
     TGASLKATFS RASLEAKRRF PKIPDDPKSY LTLRSHPNFF GCEEPDTPLV IWIPNSPPLD
     GSRGITNSSI NRVQYDLAES VKIISAASEI GYRGFPSQQL IAKKQYRDPL WSACLACAVA
     DRSRFRMGAP REGVCADCFN RYCWKS
//