ID A0A1C7MW12_9FUNG Unreviewed; 396 AA.
AC A0A1C7MW12;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
DE Flags: Fragment;
GN Name=Pla2g4a {ECO:0000313|EMBL:OBZ80948.1};
GN ORFNames=A0J61_11003 {ECO:0000313|EMBL:OBZ80948.1};
OS Choanephora cucurbitarum.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Choanephora.
OX NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ80948.1, ECO:0000313|Proteomes:UP000093000};
RN [1] {ECO:0000313|EMBL:OBZ80948.1, ECO:0000313|Proteomes:UP000093000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ80948.1,
RC ECO:0000313|Proteomes:UP000093000};
RA Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT "Choanephora cucurbitarum.";
RL Submitted (MAR-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:OBZ80948.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LUGH01001581; OBZ80948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7MW12; -.
DR STRING; 101091.A0A1C7MW12; -.
DR InParanoid; A0A1C7MW12; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000093000; 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:SF40; LYSOPHOSPHOLIPASE; 1.
DR Pfam; PF01735; PLA2_B; 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|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Reference proteome {ECO:0000313|Proteomes:UP000093000}.
FT DOMAIN 123..396
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 369..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 396
FT /evidence="ECO:0000313|EMBL:OBZ80948.1"
SQ SEQUENCE 396 AA; 45829 MW; 7BB80BAA087E1C8E CRC64;
MFRQYRCFHK KAPLLKKLTM NKIPSKNPLW SIPFLKHEEN DQQKENALIS SLMTNKEWLK
HKLESIELPS VNAKMAELYP QFTEQFKQLS EGYGKMWDYL TMEDFRKIVE QLKKEENDPT
IHPELTKDGR VREGNTLSEE EQEFIKKRKR LQKEAFARLI DEDPNQIEEQ DIPVVGLASS
GGGYRAMIGL TGYIDAMKQS GIWDCIMYFS GISGSCWTMA LYYNQLTNAE PEKLKHHLEE
HVSTHWANIS NFMNVLLASP DNSKLLLQGA IQRYAQQKGD ISLVDIFGVL MGGTLLTKKP
SVSRPPEDRE AMEQAIQNDT MEHIDNSKVM HLTGQADYLS KGQEPMPIYC VVRHDISYGK
TFEERIQELK HSYQGKHKKE AESERETKDE VDHNKN
//
