ID C4XW41_CLAL4 Unreviewed; 701 AA.
AC C4XW41;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=CLUG_00164 {ECO:0000313|EMBL:EEQ36041.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ36041.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ36041.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ36041.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408076; EEQ36041.1; -; Genomic_DNA.
DR RefSeq; XP_002619005.1; XM_002618959.1.
DR AlphaFoldDB; C4XW41; -.
DR STRING; 306902.C4XW41; -.
DR GeneID; 8500304; -.
DR KEGG; clu:CLUG_00164; -.
DR VEuPathDB; FungiDB:CLUG_00164; -.
DR HOGENOM; CLU_014602_0_1_1; -.
DR InParanoid; C4XW41; -.
DR OMA; METYKRQ; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000007703; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 23..701
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005125138"
FT DOMAIN 55..608
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 634..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 77051 MW; C30A3E7711915D08 CRC64;
MKITVLAFVV CCLAIEWPWE DGEDSSSVQS SVTTVQSGSV EFTKTIRTYA PTSTKCPSGS
IVREASSLHS SEKDYMARRH EQTNENLAAF LSDRARLSNF DAQAFIEKTK NLHNITIGLA
FSGGGYRAMF SGAGELLALD DRYEYSNKSG LGGLLQSSSY ITGLSGGSWL VGTLVLNDWM
TVEEAISPDS GIWELENSIF NPSGINVFST LKYYQSLRTA VEGKANAGFE TSITDVWGRA
LSYQFFNPDT TYNGGENITW TSIRALSHFK NQSMPFPIIV ANGRSPGTLI VNENSTVFEF
TPYELGSWDP SLNSFVDLNF LGTTLDNGRP KNNTCYTNFD NAGFVMGTSS SLFNQALLRV
QSSSTLNWAV KKLLTLILSP FSENNVDIAT YKPNPFFNGE FGASETIASD ETLHLVDGGE
DMQNVPLYPL IQKERKVDVI FAYDNSADVH NWPNGSSLVY TYERQFSPQG KGTPFPYVPS
VEEFMTSDLF GKPVFFGCDA SNLTDLVGYH ESEGNSTDVP LVIYIPNSYH SFESNTSTYE
MSYSPKEIHK FIENGFEVSS RGNYSQDRKW PTCVGCAIIR RQQERLGEEQ SEECKDCFAN
YCWTGGLEDS PQRSIGPFKS ADLTSASSAA SKISSKSDSN FSSSSTDSTP DSSSGLSTSR
TANTNSQSSD SRSSSSRING SQGKRMGKYI YVLALFANMA M
//
