ID   A0A0F8WXB2_9EURO        Unreviewed;       641 AA.
AC   A0A0F8WXB2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=ARAM_007146 {ECO:0000313|EMBL:KKK16007.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK16007.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK16007.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK16007.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-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:KKK16007.1}.
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DR   EMBL; JZBS01003128; KKK16007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8WXB2; -.
DR   STRING; 308745.A0A0F8WXB2; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000034291; 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: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:UP000034291};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           20..641
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005117507"
FT   DOMAIN          50..573
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          43..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  69287 MW;  E8EC3121183BD9CD CRC64;
     MKATTTVLAL AGLLSGAGAT AIPTSADVEV SLIERALPNA PDGYTPRSVS CPANRPTVRT
     ASSLSPNETS WLETRRAKTE SALKDFFGHV SIQNFDAVSY LNRIATNTSN LPNVGIAVSG
     GGYRALMNGA GAIKAFDSRT ANSTSSGKLG GLLQSATYLA GLTTGDGEVW QFQNSIFEGP
     HDGSIQLLDS TSYYKDIYDE VQGKKDAGYE TSITDYWGRA LSYQLINATH GGPSYTWSSI
     ALTEQFQQGN MPMPLLVADG RYPGELLIDG NATVYEFNPW EFGTFDPTIY GFVPLEYLGS
     RFVGGSIPSN ESCVRGFDNA GYVMGTSSTL FNQFFLQINS TDLPSFLTHA LSDILAKIDK
     DDDDIAVYSP NPFYQWRNES SPYASQADLD IVDGGEDLQN IPLHPLLQPE RKLDVIFAVD
     SSADTTYNWP NGTALVATYE RSLNSSGIAN GTEFPAVPDQ NTFVNLGLNT RPTFFGCNSS
     NTSAPLVVYI PNYPYSFLSN FSTFDPSYKE AQRDDAIMNG YNVATMANST RDSDWSACVG
     CAILSRSFDR TNTQVPDLCT TCFNRYCWNG TTNSTDPSGY EPSEVLVESK SAASGVFPAV
     LSTVVVASVT IFTMLFEELA EFYGGCDATF SGSMREKLTG T
//