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Database: UniProt
Entry: A0A1E4RXL5_CYBJN
LinkDB: A0A1E4RXL5_CYBJN
Original site: A0A1E4RXL5_CYBJN 
ID   A0A1E4RXL5_CYBJN        Unreviewed;       663 AA.
AC   A0A1E4RXL5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=CYBJADRAFT_28533 {ECO:0000313|EMBL:ODV71825.1};
OS   Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS   / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=983966 {ECO:0000313|EMBL:ODV71825.1, ECO:0000313|Proteomes:UP000094389};
RN   [1] {ECO:0000313|EMBL:ODV71825.1, ECO:0000313|Proteomes:UP000094389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC   NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV453938; ODV71825.1; -; Genomic_DNA.
DR   RefSeq; XP_020068864.1; XM_020217630.1.
DR   AlphaFoldDB; A0A1E4RXL5; -.
DR   STRING; 983966.A0A1E4RXL5; -.
DR   GeneID; 30992026; -.
DR   OMA; HANQSEL; -.
DR   OrthoDB; 1980513at2759; -.
DR   Proteomes; UP000094389; Unassembled WGS sequence.
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; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF56; MEIOTIC PHOSPHOLIPASE SPO1-RELATED; 1.
DR   Pfam; PF01735; PLA2_B; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094389}.
FT   DOMAIN          1..663
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   663 AA;  75543 MW;  7FF9AC579A43A6EB CRC64;
     MSLQKFLNRV KIPGLDVKRF TLSTSKPLNL AIAISGGGYR ASLTALGFLT ALDDRSSRSM
     DEGHLGGLLQ SASYISSISG GTWTLMSLSL SDFIPLVRLR NEWDINEPLL EGVPSLKMMD
     VSRNEIQVLP PEIRAVDDSE FYDKLNNNRN KRDFGTTGDE SFDDFYAYME LLPDLDESSH
     LVERDELKKD DTDWLETFKT FFRDMFKKKE DAKTVQNLLP DVEFAPVLSF KSMKKILNFY
     KNLHVEVRAK KAAGFPVSFT DYWGRALSRR VFPKSARAPN TTLSGVIDLP SFKRYQQPYP
     VIISNLREPG IETTSVNSSI FEFTPYEFGS WDSQMFVKMK YLGSSMYDGR PLIHINNRSV
     CYVGFDNAGF ITGTSSSLFN NVLIYIWNLA ASSTRDNFRA IKAVLNTFGL TSTQDTVDPK
     KHPDYALYSP NPFFRYGDAK LSPIYNSKHL FMVDGGEDGQ NIPYQPFLQP DRQVDVILSV
     DSTSDTEGWP NGTIVENTYL RYNDSGHTTT TITVNGMIKN INLFPEIPTP SEFVAQGLNK
     RPVFFGCHLE KYRQRYDSLP KSRYVNSFLP PIVGLFSNSE YSYSSNTSTF RVSYDDAEMS
     KMIQNAYNIA TYANSTIDRD YPRCIGCILI KREFDRKERS LSLLNNMTLP EFCYNCYSKY
     CYN
//
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