ID A0A366RTA8_9HYPO Unreviewed; 654 AA.
AC A0A366RTA8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=FIESC28_05277 {ECO:0000313|EMBL:RBR20313.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR20313.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR20313.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR20313.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-2018) 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:RBR20313.1}.
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DR EMBL; QKXC01000107; RBR20313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366RTA8; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000253153; 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}; Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 18..654
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5016482704"
FT DOMAIN 53..606
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 654 AA; 71121 MW; EC43753536094F99 CRC64;
MLGPLAFTLW LSSTAIAVSD STGLAPVPDI NKSLSIRALP DSPSGDYAPK VVDCPSTRPK
VRLADGLSDD EESWVRLRRN NTIDPLKDLL SRVNISGFDA EKWIDQNKNN ATALPNIAIA
ASGGGYRALM NGAGFISAAD SRNNKSGPIS GLLQSSTYLA GLSGGGWLVG SIFANNFTTV
PELQKGDKGS DIWAFDRSIF KGPEKSGFSI LNTAKYWDDI KDAVDEKDKG WNTTLTDWWG
RALSYQLIDA AEGGPSYTFS SIADTSNFKN ADTPFPILVA DGRAPGQRIV SLNATVYEFN
PFEFGTWDPT TYGFAPIEYL ASNFTNGTIN KTGECVRGFD QFGFVMGTSS SLFNQFLLNN
ITKIGEENDI PSIVVKAIQG VLLALDESDE DIADYTPNPF YKWDPTGKSY NADVTQLTLV
DGGEDLQNIP LHPLIQPSRE VDVIFAIDSS ADTENNWPNG TALRATYDRV GSSIGNGTKF
PSVPSAETFI NEKLNQRPTL FGCDANNFTL SDGELPPPLI FYIPNAPYTF MSNVSTFDLS
YSIPERDSII LNALNGATQG NGTLDEQWPT CVTCAIMSRS WWKANETVPK ECSACFDKYC
WNGKSNNTEV KNYQPTFIIA NETAQAEDNA AISSFTPGWY MTAAVGTAMF LAIL
//