ID A0A229WWV4_9EURO Unreviewed; 544 AA.
AC A0A229WWV4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CDV55_104077 {ECO:0000313|EMBL:RHZ67855.1}, CFD26_106879
GN {ECO:0000313|EMBL:RLL97674.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL97674.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL97674.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ67855.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RLL97674.1}.
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DR EMBL; NKHV02000050; RHZ67855.1; -; Genomic_DNA.
DR EMBL; NIDN02000071; RLL97674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229WWV4; -.
DR STRING; 1245748.A0A229WWV4; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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:UP000215289};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 23..544
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5011807140"
FT DOMAIN 30..544
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 544 AA; 58173 MW; 044C96CEE8765DF6 CRC64;
MSVPTTLTLL LWGSAFWLGI EAGYAPIHTT CPDIPLVRPA SGLSSAESAY RQQRKQIADQ
NLAAWLTKTD SGFQTNGSLP TLALTTSGGG YRSALVGAGV IQGLDARDSD ISTSGLYQAL
TYQSGLSGGA WLLSSIAGNN YPTISYLKET LWEQAFQDSL LVPGNLLVAE AYGKIVADIT
AKGAAGFPPT LTDPWGRLLS YQFLQGPDGG VDTTLSSVSG LSNFTSHAVP YPVILTLGVK
TWDGQCLPGP NATIWEFSPY EFGSWDSDVS AFTPTHYLGT SLSGGQPTVQ GSCVINYDNL
GYVLGSSSNL FNEACSSVPT ATNSTTSLTE DLAEMVAQVH QLSTSDEYAV LPNPFYEYNS
STAVANPANP VWEQPTLHLV DGGEALQNNP IWPFLQPARA VDVMIVNDNS ADTSNNFPNG
SEILTTYVQS QSAGLTRMPY IPSVETFLSQ GLNRRPTVFG CNTTAITIVY LPNVNITYPS
NTSTEQVQYS VPETEGMISN GVAMAEQPGE IDWPLCLACV IMMKTNTTLP ASCAPCWAKY
CYYQ
//