ID A0A178B0N7_9PLEO Unreviewed; 824 AA.
AC A0A178B0N7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=IQ06DRAFT_246086 {ECO:0000313|EMBL:OAL03153.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL03153.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL03153.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL03153.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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}.
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DR EMBL; KV441709; OAL03153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178B0N7; -.
DR STRING; 765868.A0A178B0N7; -.
DR InParanoid; A0A178B0N7; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000077206; 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; cd00147; cPLA2_like; 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:SF40; LYSOPHOSPHOLIPASE; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000077206}.
FT DOMAIN 206..810
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 78..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 770..797
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 78..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 92491 MW; 5F8ECD21D5439E70 CRC64;
MALIRGSRDL GQLWLRRTRR GLHTQRQTSR TSHFVATSLR YGPPCLIATA AIGYLSTASP
LLSSRPIQLD APSSWSQWMP GFSRGSQQRN ASTSAEGAEN QNTEQDEEKS GEQEAPPQTR
VVKGYSEEDS SGGDKSTWQT IRNSFPSPPD LKSASTIGDT IIDYVIPGWV KMMPGFIRKL
QNELSMAPGS LAEEIWYEAN NPEANPEIIW DASVRISNEL CKEEKAFREK RTHFTKKALA
RYLDIPEATI NPDDIPIIAM CGSGGGLRAL VAGTSSYLST KEHGLFDCVT YTAGVSGSCW
LQTLYYSDIT QRSHARLIRH LKNRLGVHIA FPPDALELLV SAPTNKYLLS ALVEKAKGVP
DAEFGIVDIY GALLAARLLV PKGELSVSEY DFKVSNQRRF TDDGSHPLPI YTAVRHEIPL
AEQSDMVDRI EAEAKARREA WFQWFEFTPY EMWCEELSAG IPTWAMGRQF DKGRTVWRDN
GLALPEVRVP LLMGIWGSAF CATLSHYYKE IRPVLVGLTG FSSLDAMISE RDEDLVKVHP
IDPASIPNFA LGLREFLPPS CPESIFEQKN FQFMDAGMSN NLPIYPLLRP GRDVDILVAF
DASADVRTDN WLKVADGYAR QRGIKGWPVG AGWPSEDETM EEVQESLDAA QAKTEEEAQA
HISKAQSDDA AAQKSSKKKD LGFCNVWVGT TEERVSDTSP PESKLVEEDW ELMHPESGIT
VIYYPFLANP KVPGVDPKTS DFMSTWNFVY TPEQIDNVVE LARTNFAEGA DRTKRTVRAV
YERKKKLREQ REKDERERRW RWKLKQGRVR GIRVGESEQG DQFS
//
