ID A0A2N5T304_9BASI Unreviewed; 575 AA.
AC A0A2N5T304;
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_05920 {ECO:0000313|EMBL:PLW54883.1}, PCANC_09264
GN {ECO:0000313|EMBL:PLW19858.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW19858.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW19858.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW19858.1};
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:PLW19858.1}.
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DR EMBL; PGCJ01000806; PLW19858.1; -; Genomic_DNA.
DR EMBL; PGCJ01000039; PLW54883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5T304; -.
DR STRING; 200324.A0A2N5T304; -.
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..32
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 33..575
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5015019232"
FT DOMAIN 51..575
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 575 AA; 63882 MW; 2D460277F567F92A CRC64;
MLHLRQRIPL QYLHSLLLSL WIGASILLKA ECSDFQLPHS PSGNYEPSRV RCPPGLRVRV
ADQYPWPISP GEYNYTSGKA KKSILQWESY LRQLRLQDFN ITQFLESAVR EGGAPGETLP
NIAFATSGGG DRALLFSASM LDAFDLRNKE AVEARTGGIL QLANYVTGLS AGAWLLTSWA
TANFERMPKL NSTVWGLNQQ KGYLSWKLLR VLPKHILEAL RKKMAGFDIS FVDVWGRILS
TQYIDDPEDG KGILFSAIKE TPSYKAREFP LPILTSLSRR SSGELITLQS PIYEMTPEDF
SVWHPGLNAS IPMEYLGSQM SFGKGEAISC VKGFDNAGFL MGVSSNVFSF QDGSNQNPNL
GEKFANALIK GKFYEALIPN PFYGQNSGLP SGSGGFVDSN SETLLLADGA MAQENLPLFP
LLQPSRKVDV ILAFDATVNG FAFDAPNVDG YPNGTALYKT YLKVQDPEFR NYPFPKIPNS
LTNKFVAGGY NKRPTFFGCD KEDGPLIVYL PNYFASHRTD MRTMKTDFTG DEIDGFFKNS
FLIATQKNRT TNNKRDQTIQ EHLNAFDASR SIAAD
//
