ID   A0A0D2D9Z6_9EURO        Unreviewed;       741 AA.
AC   A0A0D2D9Z6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=PV05_03587 {ECO:0000313|EMBL:KIW59112.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW59112.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW59112.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW59112.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) 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|ARBA:ARBA00000960,
CC         ECO:0000256|RuleBase:RU362103};
CC   -!- SIMILARITY: Belongs to the lysophospholipase family.
CC       {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN847318; KIW59112.1; -; Genomic_DNA.
DR   RefSeq; XP_013319696.1; XM_013464242.1.
DR   AlphaFoldDB; A0A0D2D9Z6; -.
DR   STRING; 348802.A0A0D2D9Z6; -.
DR   GeneID; 25325495; -.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000054342; 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   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF62; LYSOPHOSPHOLIPASE; 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:UP000054342}.
FT   DOMAIN          146..685
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          140..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  79764 MW;  47F24650969FCC81 CRC64;
     MAAKNSLPSI HRYITTHSAS GISRFDKTIP SKALWRHVPE ASFFLAYTTK SFPVTIGDDA
     DLDDYTNAFA SPPKVTVSGG TVLRVMDIGP GVSSPMHRTV SLDYSIVLEG SRSYGFAESV
     SIEVSNAVAR RALPNAPNGY APEGSACPSP EPVIRSGSTL SPDETSWLAK RRNQTQAAMI
     DLFSRINVKD FDAPGFLNNQ AKNVSALPNI GIAVSGGGYR AMMNGAGAVA AYDSRTANST
     GVGHLGGLLQ ATTYISGLSG GSWLLGSLYM NNFTTVPALL SDNTGTLWDL DYSVLEGPAT
     ISNYWRTLVN DITDKEDAGF NTSITDYWGR SLSYQFINTT DGGLSYTWSS IALQPEFIEG
     QMPLPLVIAV ERTPDQLAIA SNTPIYEFNP WELGTFDPRS YGFVPLMYLG SNFSAGKLQQ
     NTLCVRGFDN AGFVMGTSSS LFNQGFLVLN GSNQSSILTE AITQILEEIG EDNNDISLYS
     PNPFHQYNVE TNPSAESTTL VLVDGGEDLQ NIPFHPLLQS SREVDVIFAI DSSADVETRW
     PNGTSIVATY RRSLISTDNG TAAFPSIPDQ STFVNLGLNS KPTFFGCDSK NMTGVGPLIV
     YLPNSPYSYF SNVSTFDLEY NDTERDGIVQ NGYNVATMAN GTVDEEWQTC VGCAILSRSL
     ERTGVAIPAT CQHCFSTYCW NGTINDTFPG LYDPQLVETP QNATSSGGSN ATTSGGIKSY
     GAANFLAVSF IFGVCAVQIW I
//