ID A0A3E2HPC6_SCYLI Unreviewed; 835 AA.
AC A0A3E2HPC6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
DE Flags: Fragment;
GN ORFNames=B7463_g1271 {ECO:0000313|EMBL:RFU35072.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU35072.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU35072.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU35072.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RFU35072.1}.
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DR EMBL; NCSJ02000013; RFU35072.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2HPC6; -.
DR OMA; FARYCWN; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR008253; Marvel.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR Pfam; PF01284; MARVEL; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Signal {ECO:0000256|RuleBase:RU362103};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 27..835
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5017495612"
FT TRANSMEM 651..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..582
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 801..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU35072.1"
FT NON_TER 835
FT /evidence="ECO:0000313|EMBL:RFU35072.1"
SQ SEQUENCE 835 AA; 90607 MW; 4B87962C495ED5B5 CRC64;
MFSLFFYLSA ITVALESSLF QQLVSADGVS NVGLAVIGAA QKRATIQAPN DYAPASVDCP
LNRPDVRQAT TLSDNETAWL EARGNNTISA MQDFLQRANI TGLDTNNYID DVVKNGSQMP
NIGIAFSGGG YRALMNGAGA LAAFDNRTTN STSQGQLGGI LQASTYLTGL SGGSWLVGSV
YVNNFTSVQD IIKMDYLWQF NNSIIEGPDT ISALDYYNSL LDTVRDKANA GFNTTITDYW
GRSLSFQLIN PVDGGPGYTF SSIANDPGFV AGNQPLPIII AIERQPGQLL ISANSSIYEF
NPWEIGTFNP STFAFAPLRY VGSNFTGGIL PQNAPCIAGF DNAGFIMGTS SSLFNQLYLT
TANTTSEAPS RTAISQIGQT XFFGYNNNTN MNAQSRSLAL VDGGEDLQNI PLDPLLQQSR
HVDVIFAVDS SADTANWPNG TAMVASFQRS LNSQGEGRTA FPSIPDQSTF VNLGLNRKPT
FFGCDINNMT GPGPLIVYLP NSPYEYNSNV STFQLSYNNT ERNTIILNGY NVATLGNSTL
DSQWPTCVGC AILSRSLNRT RTNIPQVCTQ CFERYCWNGT VNSTAPAPYE PTLAIQTSGN
CVSFSIMGAA SKTVSVVLRF WELACATIVA GLFGKYLHFL DEANVGGNGR IIYAVVIAGI
SILASLILMP PLKYSFYFFI LDFILFTCWM VAFGLTTNLT GTHGCHAHWY WTSWGYYWGG
WWRRMPLSAT TQSLVGTAAC AQWKTAIAFS FMGGWGWFVS GLLGIYVCSK PSDEQVVSGQ
MGTVSKTSNT VSRWYHKYTR TGHKTSSNDG LRTKETSYHG QETNGRGEPN VPATV
//
