ID   A0A0P1B7N1_9BASI        Unreviewed;      1003 AA.
AC   A0A0P1B7N1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH11934.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH11934.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCYA01000065; CEH11934.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1B7N1; -.
DR   STRING; 401625.A0A0P1B7N1; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF40; LYSOPHOSPHOLIPASE; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          112..731
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   DOMAIN          887..996
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          613..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..739
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1003 AA;  112282 MW;  C664460180A49730 CRC64;
     MPLARRIRTS PGYLYLKLYL LCSLVSFFQA RPITPLIKAF RRAESTLTHT NAASLAKFYA
     SMLNRPRGMG ERIASVLAEA ARLPRRWFDR AKDLAEIRGR IQEEEIDVKR WPELQWDSHV
     RISRQMHPIE SRFLRQRRRA IAQSGSLSRL LDLPKDEIVH PKDVPLVSVD CLWRCPVRCV
     HAALLTAALD FVPLGQIGIG GSGGGYRAKF GFTAGLFALQ RGGVWDCAAW SAGVSGSCWT
     LAALYTIASH DAQKLLAHYT AVASEGIHPL SRQALDVVAR SKRGTYFLLA PLLAKARSGV
     VGLGLMDLYA TMTTSYQFLS RSPQARPRLS RSTFQWSRVF SRSALHDGAQ PMPILTAVRR
     DLAVQTPPYQ WWEATPIEIG SPEKGAWIPS WSFGRIFERG ECKRRLPEMS LALLLGYCTS
     APAGPLSGYI SALLATLPEE TLARNLLSRL NAFVQRQRFE KMWGNPIRAA DEPNPLWRGR
     APKLDAVTHI GQSAATGLES APRLKLMDSG LANNLPSHIF TMPSRLADVI VAMDYSSDVQ
     TGASLARLSL FGVERGLHLV KRPGLAAKTE EELEETRHAK ASLDASSTST DFARSFKGKY
     AQIVDAWPAN EQHPAGLHEA PSDTSRAALP GKDKQSHTIV YCPLLPHACQ PLFDPANSEF
     SNSYNLVWTA EQVGTLARTA QACVEEEVIG AVRAIVREHY ERRKAARLEL AEQRSGHQNA
     MRHHEGHEAE QERQPSKRAR TDQVAAASTK MTKAGDGRDQ EPVANVDVRN RTAGYMAPVT
     RRDFIEAHRV SGLEDSEVYY MARWISRDQA EKWRKELDDL PQWYRPTLKV YGREIKQSRA
     IAAFSREAGL PLKYSGHEVE MHCPFPPLLD EIAKRLCTKE ILGEEVQFNH AMLNRYDDGS
     VYIGKHSDNL ENQVIVTVSL GAERTFTFEE KKARGVKSTV DKARQSRKRS LVLESGSVLV
     MQGDVQKRFT HEIARESKKS PIYSQPRTSI TFRQLVYEKR TVI
//