ID   A0A1U7LL32_NEOID        Unreviewed;       514 AA.
AC   A0A1U7LL32;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=NEOLI_004073 {ECO:0000313|EMBL:OLL23348.1};
OS   Neolecta irregularis (strain DAH-3).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Neolectales;
OC   Neolectaceae; Neolecta.
OX   NCBI_TaxID=1198029 {ECO:0000313|EMBL:OLL23348.1, ECO:0000313|Proteomes:UP000186594};
RN   [1] {ECO:0000313|EMBL:OLL23348.1, ECO:0000313|Proteomes:UP000186594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAH-3 {ECO:0000313|EMBL:OLL23348.1,
RC   ECO:0000313|Proteomes:UP000186594};
RA   Cisse O., Nguyen A., Hewitt D.A., Jedd G., Stajich J.E.;
RT   "Evolutionary innovation and constraint leading to complex multicellularity
RT   in the Ascomycota.";
RL   Submitted (APR-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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:OLL23348.1}.
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DR   EMBL; LXFE01001786; OLL23348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7LL32; -.
DR   STRING; 1198029.A0A1U7LL32; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000186594; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:UP000186594};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           18..514
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5010398154"
FT   DOMAIN          30..514
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   514 AA;  56546 MW;  0797EE7709BF3BCE CRC64;
     MRDLALFAFL WAPLVIAVRI HVPFVPVEGK CPSSYIVNAQ TLNPEEVDWL SKMSSINEAS
     FRSYLSSYPD INISSVPNIG IALSGGGYRS MLTSLGVLQA LDETPGFAGL LRTSRYITSL
     SGGAFAGASL ATLGYPKIEG SLWNLSSSVF LPFGHSTVKN IHFWRDIFHQ IKLKRDLGFH
     VSLTDYWGLA LSKQLKIEGD LWSRTNATGP FPIIVTYNRP GDIRARPEQA NATHFDISPS
     EIGSWQLNSL AQTKYLGSTA NKCVEDFDDA GYQSWKPHSY SFDRFIVGVS SSVFHYVLVK
     AIEFLGLNDD LFGKLLEEAG RDYLVAQIPN PFAGIKGNPF CQESVIPLVD GALDGQGIPL
     GPLLRPQRKV DVIIAVDSAD DKNDLPNGTS LGFTARYASS VGLPFPVIPD TDTFLSQNLT
     SRPTLFGCHS QEGPLIVYIA NMPYSFDSAV TSAKLAFSDN DRDAMIENGR KVMTKDDDEV
     WAKCLACAIS KRTAEREGKT LEGCEECWKE YCWN
//