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Database: UniProt
Entry: G8BUE1_TETPH
LinkDB: G8BUE1_TETPH
Original site: G8BUE1_TETPH 
ID   G8BUE1_TETPH            Unreviewed;       673 AA.
AC   G8BUE1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   Name=TPHA0F02460 {ECO:0000313|EMBL:CCE63727.1};
GN   OrderedLocusNames=TPHA_0F02460 {ECO:0000313|EMBL:CCE63727.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63727.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE63727.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE612861; CCE63727.1; -; Genomic_DNA.
DR   RefSeq; XP_003686161.1; XM_003686113.1.
DR   AlphaFoldDB; G8BUE1; -.
DR   STRING; 1071381.G8BUE1; -.
DR   GeneID; 11535656; -.
DR   KEGG; tpf:TPHA_0F02460; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   OMA; PENETCV; -.
DR   OrthoDB; 1826981at2759; -.
DR   Proteomes; UP000005666; Chromosome 6.
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:UP000005666};
KW   Signal {ECO:0000256|RuleBase:RU362103}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT   CHAIN           22..673
FT                   /note="Lysophospholipase"
FT                   /evidence="ECO:0000256|RuleBase:RU362103"
FT                   /id="PRO_5005132969"
FT   DOMAIN          34..586
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          617..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  71615 MW;  ED0A42A7A5A6A29F CRC64;
     MQLFSFLVTA PLLASILEVQ AWSPHNSYTP ANVTCPNDFN LIREGASSLS SNETEWLSRR
     DEITKAALKE FLQRATSNFT DSSIVNEIFG ASNSSNSSNS TVSKLRVGIA ASGGGYRAML
     SGAGMVAAFD NRTIGANAYG FGGLLQGSTY LSGLSGGNWL TGTLAWNNWT SVQDIIDNTY
     TDNSIWDITD GLVSGTANNT LMWETIFAEV AGKSAAGYNT SLADYWGRGL AYNFFPNLPN
     GGSGYTWSTL RDSNVFLNAE MPFPITVTDA RDPNTTISYV NSTIVEFNPF EMGSWDPSLN
     SFADVKYIGS AVNNGSPIVD GVCAAGFDNA GFIIGTSSTL FTPAMSSAVG TLLGNSSSTV
     GTFLVNEIAV DTNDVANFGP NPFYGSSFGI SNIGNKDILT LADGGEDNIE LPLIALIQKQ
     RDLDVVFALD NSADTAENWP DGNGLISAYR RQFYPQGSNI SFPYVPDAET FVSEGLNKRP
     TFFGCDAANL TNLAYVPPLI VYLPNYEVSY ASNTSTLQLA YNETERLSMI QNGFEAVTRG
     NFTEDSKFLG CVACAVMRRS QESLGLDLPS ECQSCFDTYC WDGSLSDSAA LDSAANSTST
     ISSTSASNST TMSISMTTST SASSSNNNGT SASSNSTPSR SSTSSHNGAT SLDVTTKITL
     VTVFIFNFLL GNF
//
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