ID Q6VTE8_CRYGA Unreviewed; 517 AA.
AC Q6VTE8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
DE Flags: Fragment;
GN Name=PLB1 {ECO:0000313|EMBL:AAR01570.1};
OS Cryptococcus gattii (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=552467 {ECO:0000313|EMBL:AAR01570.1};
RN [1] {ECO:0000313|EMBL:AAR01570.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH312 {ECO:0000313|EMBL:AAR01570.1};
RX PubMed=14555486; DOI=10.1128/EC.2.5.1036-1045.2003;
RA Fraser J.A., Subaran R.L., Nichols C.B., Heitman J.;
RT "Recapitulation of the sexual cycle of the primary fungal pathogen
RT Cryptococcus neoformans var. gattii: implications for an outbreak on
RT Vancouver Island, Canada.";
RL Eukaryot. Cell 2:1036-1045(2003).
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; AY327615; AAR01570.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6VTE8; -.
DR VEuPathDB; FungiDB:I308_04865; -.
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|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..517
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012565226"
FT DOMAIN 42..517
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAR01570.1"
FT NON_TER 517
FT /evidence="ECO:0000313|EMBL:AAR01570.1"
SQ SEQUENCE 517 AA; 56053 MW; 67762F2461AC86F6 CRC64;
TTTFALSLFA ATALAIPPET PRIELQAERG LGDKSYAPWQ VDCPTNVTWI RNATTGLGSG
ERAYIEAREK LVQPAIEHIM AARGLETPPR TPVIGVALAG GGYRAMLTGL GGIMSMMNES
TEASESETGG WLEGVSYWSG LSGGSWATGT FMSNGGQLPT RLLENLWNID SNLIFPDDDK
VSFYAELYIE TNAKSDLGFP TQITDLWGLA IGSHVLPEQY QLSNNPNLTF SSLPSVVAAL
GNASLPMPII IAAEREAGEL IIAENATVWE FTPYKFGSWA FGSQYKSPGA FTPIEYLGTS
VNDGSPNGTC WKGFDQLSFV MGTSATLFNG AFLELNGTDS GLLTSLITAF LAELGEDQVD
ISRIPNTFSN YNSGENPIYN LTYITLVDAG ETNQNVPLEP LLIPARAVNA IVAFDASYDT
NYIWPNGTAL RTTYERARVL AEHENTRVLM PEVPSMNGFV NGGYNSRPTF FGCNDTTTPL
IIYVPSYPWS FAANTSTYQL SYETDEANQM LLNGMRS
//