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Database: UniProt
Entry: A0A1B7TC40_9ASCO
LinkDB: A0A1B7TC40_9ASCO
Original site: A0A1B7TC40_9ASCO 
ID   A0A1B7TC40_9ASCO        Unreviewed;       571 AA.
AC   A0A1B7TC40;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, 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=HANVADRAFT_53267 {ECO:0000313|EMBL:OBA26290.1};
OS   Hanseniaspora valbyensis NRRL Y-1626.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=766949 {ECO:0000313|EMBL:OBA26290.1, ECO:0000313|Proteomes:UP000092321};
RN   [1] {ECO:0000313|Proteomes:UP000092321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-1626 {ECO:0000313|Proteomes:UP000092321};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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:OBA26290.1}.
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DR   EMBL; LXPE01000020; OBA26290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7TC40; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000092321; 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:UP000092321};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           22..571
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5008447692"
FT   DOMAIN          32..571
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   571 AA;  62375 MW;  7A8D4BF69B390D52 CRC64;
     MQYSSSLITA LLLLASNSVS AATSAYQPEV VSCPSNSSSL VRTSGGLSTD ETEWVTKRDA
     ITEPILKSYL SSQLNSTSTL DKIFSDDNDQ KPKIAFAVSG GSYRAMLSGA GMLSAFDNRT
     DDNTGSGKLG GLLQASTYLA GLSGGNWLTT SLAFNDWISV QEVVDQVKNS NGSSLWNITN
     SILAPFGAEE PMNDLLRWAK IRTDIQNKED AGFPVSIVDL WGLALSYQFF ENGAENLIWS
     SLQKSDVFAN AEMPFIISTA EQYNAVETIN TTIFEFNPFE FGSWEHEKFA NIEYLGTSFK
     DGSPVNSTQC VNNFDNAGYI LGTSAGLFNL VAEKIDSLGL TGTTKEILEI LISSWASENG
     IPAAYPNPFY GLEAESNDFG SNITYLEDLY LVDGGEDGET LPFVPLLQEE REIDAIFAFD
     IDANTDELWP SGLSLYATYA RQAQPIGADI AFPFVPNTTV FVEESLNEKT VFFGCNATLL
     SELAYIPPLV VYIPNKEYTF ASNTSTFQLS YTDKEKLGMI ENGYAAAYQN NTDSDYATCI
     SCAVILRAQQ RLDITPSAEC QSCFDNYCWS P
//
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