ID   A0A1E3HQV3_9TREE        Unreviewed;       645 AA.
AC   A0A1E3HQV3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=L202_04934 {ECO:0000313|EMBL:ODN77811.1};
OS   Cryptococcus amylolentus CBS 6039.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN77811.1, ECO:0000313|Proteomes:UP000094065};
RN   [1] {ECO:0000313|EMBL:ODN77811.1, ECO:0000313|Proteomes:UP000094065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN77811.1,
RC   ECO:0000313|Proteomes:UP000094065};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) 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:ODN77811.1}.
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DR   EMBL; AWGJ01000007; ODN77811.1; -; Genomic_DNA.
DR   RefSeq; XP_018993047.1; XM_019139104.1.
DR   AlphaFoldDB; A0A1E3HQV3; -.
DR   STRING; 1295533.A0A1E3HQV3; -.
DR   GeneID; 30156243; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000094065; 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:UP000094065};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           20..645
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5009027197"
FT   DOMAIN          46..569
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          596..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  68721 MW;  55D41DBC85AB8BAF CRC64;
     MTSVKTALTL SILSISALAA PPDISHAELV AERGLGDKSY APYKVDCPTN VTWVRNATTG
     LGDGEKAFQE ARQELVQPAI EKMMAARGLD NPPRTPIIGV ALAGGGYRAM LTGLGGVMGM
     MNESTEAQDS GTGGWLEGTS YWAGLSGGSW ATGSFMANGG QLPTDLLTNL WDMSSNLVFP
     DSGKLTFYPE LYQETNAKSD QGFPIQITDI WGLAVGKHVL PEEYQLSNNP NLTFSSLPSV
     VGALGNASLP MPIIIAAERE SGELVIAENA TVYEFTPYEF GSWAFGSDYK APGAFTPLEY
     LGSEVNNGSS NGTCWKGFDQ LSFIMGTSAT LFNSIFLSVN SSESSLLNSL CLSILGELGE
     DNLDISRIPN SFANYNSDEN PVSDFEYLTL IDAGETNQNV PLEPLIAPAR AVDAIVAFDS
     SYDTTYIWPN GTALRTTYER AQVLAEHENV KVRMPEIPSE AGMINGGYNT RPTFFGCNDT
     STPVIIYIPS YPWSYAANTS TYKLAYDNDV AEGVMLNAMR SLTLNNTVET WPTCFACALT
     DRAFDYTSSN RSSECQSCFD TWCWAGDDNT TDPGTYEPEI GSVPPWLLAQ GLSTGVADAP
     DTNSSSSSSS SDGDSGDAGS TSSGAEKLGA GLSLVLLASV VGFLL
//