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Database: UniProt
Entry: Q6VTE8_CRYGA
LinkDB: Q6VTE8_CRYGA
Original site: Q6VTE8_CRYGA 
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
//
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