ID A0A0D1ZXY8_9PEZI Unreviewed; 662 AA.
AC A0A0D1ZXY8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=PV09_08996 {ECO:0000313|EMBL:KIV99337.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV99337.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIV99337.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV99337.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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; KN847579; KIV99337.1; -; Genomic_DNA.
DR RefSeq; XP_016209207.1; XM_016362982.1.
DR AlphaFoldDB; A0A0D1ZXY8; -.
DR STRING; 253628.A0A0D1ZXY8; -.
DR GeneID; 27316969; -.
DR VEuPathDB; FungiDB:PV09_08996; -.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; A0A0D1ZXY8; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW Signal {ECO:0000256|RuleBase:RU362103};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 22..662
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005112367"
FT TRANSMEM 638..661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..613
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 662 AA; 70084 MW; 5E14C5BE3A54906A CRC64;
MSIKVVLGAL SVAGVLWHAQ GLYITEPNSG RNLVDTVTAR KRGSPDAPNG YVPTEVDCPT
TRPSIRSAHE LSQSEVDWLK TRRPKTVDPL KDLLGRLNIT GLDTNAYIDN HSSNISNIPN
IAIAASGGGW RALLNGAGLI AAFDSRTTNS TNPGHLGGLL QSSTYLSGLS GGSWLVGSIY
MNNFSTVPTL LDSNAEKSAS GFLWGFQESI LAGPPASGTI DNVVDTADYF TTIYDQVQGK
EDAGYNTTLT DYWGRALAYT LINATDGGPA YTWSSIAKDA AFQQGDWPLP VVVADGRAPG
ELLVSLNATN YEFNPWEMGS WDPTVYGFAP VQYVGSEFDN GVLPTSKSCV AGFDSASFVM
GTSSSLFNQL LLNLNSTSLP GVVKAGFEAL LSRLDKAEED IADWAPNPFR GWNEGSNPSA
GDVTLTLVDG GEDLQNIPLT PLIQPSRAVD VIFAIDSSAD TVAPGAANWP NGTAMVASYE
RSLHAIANGT AFPAVPAQNT FVNLGLNNRP TFFGCDAANT SAPTPLIVYL PNAPYVYASN
VSTFQLEYTK AQQLAIVQNG YDVATMGNAS RDARWPACVG CAILSRSFDR TATPVPDICR
SCFADYCWNG TLANQPPARP YEPELILPDR AINATKKGAA AVLPAPTALA LAAAISLSLL
LA
//
