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Database: UniProt
Entry: A0A225B3L2_9EURO
LinkDB: A0A225B3L2_9EURO
Original site: A0A225B3L2_9EURO 
ID   A0A225B3L2_9EURO        Unreviewed;       487 AA.
AC   A0A225B3L2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=UA08_02278 {ECO:0000313|EMBL:OKL61876.1};
OS   Talaromyces atroroseus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Trachyspermi.
OX   NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL61876.1, ECO:0000313|Proteomes:UP000214365};
RN   [1] {ECO:0000313|EMBL:OKL61876.1, ECO:0000313|Proteomes:UP000214365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL61876.1,
RC   ECO:0000313|Proteomes:UP000214365};
RA   Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA   Mortensen U.H., Thrane U.;
RT   "Talaromyces atroroseus IBT 11181 draft genome.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC       {ECO:0000256|ARBA:ARBA00002169}.
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|ARBA:ARBA00000960,
CC         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:OKL61876.1}.
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DR   EMBL; LFMY01000003; OKL61876.1; -; Genomic_DNA.
DR   RefSeq; XP_020121997.1; XM_020264302.1.
DR   AlphaFoldDB; A0A225B3L2; -.
DR   STRING; 1441469.A0A225B3L2; -.
DR   GeneID; 31002033; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000214365; 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:UP000214365}.
FT   DOMAIN          1..487
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   487 AA;  52639 MW;  0AAC90130B4BCE71 CRC64;
     MKATMLLSPI ALGLLSYKYL IHHGVPSSLF YKSDTNDPGP ATIASPAANG VSRAVVVNPR
     ALPDAPNGYA PAFDNRTDGA TGKGQMGGLQ SATYVAALSG GSWALGSIFV NNFTSVAELQ
     ANFWNFSSES IFVGPGTMDP VQYWGDITAQ VKMKRAAGFV TSSPDFWGRM QGYYFFNASD
     GGVDLTWSSI AKTQAFQEGV MPLPLVVVDG QYFNQSDELP TPKQPVYEIS PWEFGTFDES
     IYGFAPLEYL GSRFVNGVVP ENETCVRGFD NAGFITGTSS DIYNENGRDI AVTLNDSISL
     LSSNTSEGSA MVELLSNDIQ QYLSAVSSNS SRTNGPAAYD PNPFYQYNQD SSPFAHDTRL
     TVVDGGEDEQ NIPLNPLIQR KRNVDIIFAV DSSANAHVIW PNGTAMIATY ERTLAGYAND
     TSFPSIPDAN TFVNLGLNNH PTFFGCNITY ISNVSEYVTS YNTTARDDMI LNGYNIVTQA
     NGTLDSN
//
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