ID A0A0F7SAR1_9BASI Unreviewed; 995 AA.
AC A0A0F7SAR1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN Name=SSCI58790.1 {ECO:0000313|EMBL:CDW98599.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDW98599.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-2014) 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; CCFA01003538; CDW98599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7SAR1; -.
DR STRING; 49012.A0A0F7SAR1; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000242770; Unassembled WGS sequence.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
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; PF01648; ACPS; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 139..995
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 67..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 995 AA; 110056 MW; DE496CEE083979CF CRC64;
MPILTSLRQS PTYLYIKVYC LCALVTLSQA APVSSRIPKL GQTLQLNKYR LIRTRLGPRI
VPVEDAVPVS SRDTTTSSSQ ADDQAQPPNE VIISSDVLGP TEQLSTIRKL LRRWSSRPKD
LAQVKHLLRA DDTDLKAYPE LQWDATVRRS ASLHSEEVKF LRKRQLHLSS QGEDVLKQLL
ELPASEQVDP RDVPLVALGG SGGGYRAMYG FAGFIAAAKR SRLWDCLSWA AGVSGSCWTL
AAYYTIAYQD ADRLIRHYLS VASELAHPMS VHALDTVARS SRGVYFLLGP LMRKAQAGIV
GLGIMDLYAT LTTTYQFLSR EPRARLSRAS FQLSKVWSRS GISSAKEPLP VFTAVRVAPQ
DAPGVRPHTD SSLSKGQPPK RALTQHQSAA SKALTPNAAS STSNASSSVY TPVDDGKSDI
FALPAAKGYF QWFEATPLEV GSADIQGYIP TWAWGRPFVS GRSLDRRPEE SLSLLLGQCT
SAPAGPLTGY ISALLASLPK GTAMSRTLHF LNNFVRMKRW ERRWGNPIRA GDEPNPFYGL
NVAPVPKDTA KSVSSPSILG IGVDILHTPR LRHLLQRRTD RSRSPSADQT NGRRDENSTS
EPAALDKLAR RILCESERKQ FQDLAERHLE TSADRLRQLE QYLANRWSAK EAAYKALYPR
YVVSWKDLCV HKPGSLDDTL VDGVDLTRLE KQGFRTKKPI LSFSDEWRSR HSDVSSIPKL
HLSLSHDGDY VVANVLAEEF PSPSSRTPQQ APQEWNELSV SLSTQPANSD PLDATELELG
ASSSTHTSAQ TVKLHDVNPA ISASWESQGR IRLMDSGMSN NLPNHVLARK ERAADIIIAF
DASSDVQAGS AMRRIHNFAD DCSITLSDQT HLFPTPQPAR LSRHKQLDVE MEHKFLHQYA
RVLQGTRDED GSTFWLIYCP LLPNPTNAVY DPSTSSFSNS YNLVWTPAQV GTLLKTSQAN
LELYALQTVK HVMRKVYEDK KAARLGSISS STTSS
//
