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Database: UniProt
Entry: A0A1F7ZNY9_9EURO
LinkDB: A0A1F7ZNY9_9EURO
Original site: A0A1F7ZNY9_9EURO 
ID   A0A1F7ZNY9_9EURO        Unreviewed;       619 AA.
AC   A0A1F7ZNY9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=ABOM_009837 {ECO:0000313|EMBL:OGM41157.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM41157.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM41157.1, ECO:0000313|Proteomes:UP000179179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX   PubMed=27664179;
RA   Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT   "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT   bombycis.";
RL   Genome Biol. Evol. 0:0-0(2016).
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:OGM41157.1}.
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DR   EMBL; LYCR01000119; OGM41157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7ZNY9; -.
DR   STRING; 109264.A0A1F7ZNY9; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000179179; 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   CDD; cd07203; cPLA2_Fungal_PLB; 1.
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:UP000179179};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..619
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012768770"
FT   DOMAIN          37..579
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   619 AA;  66744 MW;  B6AAF31A4D56D00B CRC64;
     MKLNVLLLGA ALASATPDLH LRALPNAPDG YAPANVSCPA VKPAVRSASK LSQNETDWLD
     ARRKEVVSPL KNLLGRLNLT NFDASAYIDR VSANTSNLPT VGISVSGGGY RAMLNGAGAL
     KAFDSRTTNS TASGQLGGLL QSATYLSALS GGGWLVGSVF INNFTTISDL QTSENTWDLT
     NNILEGPSVK HFQLLNTVDY WTELVDTVKT KKEAGFNTSL TDYWGRALSY QFINASSGGP
     DYTWSSIALM ENFQRGQTPL PILVADGRNP GELVIGSNST VYEFNPWEFG TFDPAIYSFA
     PLEYLGSDFK GGQISSNGSC VRGFDNAGYV MGTSSSLFNQ GLLRLNGTKI PKIFKSAIAS
     ILEDLGQGND DIANYPNPFY EYTGATEAIA RRSHLSVVDG GEDGQNIPLH PLIQPERHVD
     VIFAVDSTAN IHSWPSGKSL VRTYERSLNS TISNGTVFPA VPDPNTFINL GLNKRPTFFG
     CDSKNLTGPA PLIVYLPNAP YTFLSNTSTF DLSYSYEDRD AMITNGYNVA TRGNGTEDAS
     WPSCVGCAIL SRSAERTGTT LPEVCSQCFK NYCWDGTINS TEPADYEPQL MIKTSLAPRK
     LPGYTAAIFP FALALAMML
//
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