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Database: UniProt
Entry: A0A0V1PJZ2_9BILA
LinkDB: A0A0V1PJZ2_9BILA
Original site: A0A0V1PJZ2_9BILA 
ID   A0A0V1PJZ2_9BILA        Unreviewed;       901 AA.
AC   A0A0V1PJZ2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
DE   Flags: Fragment;
GN   Name=Pla2g6 {ECO:0000313|EMBL:KRZ96554.1};
GN   ORFNames=T08_14643 {ECO:0000313|EMBL:KRZ96554.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96554.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ96554.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96554.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00023422};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000256|ARBA:ARBA00023422};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ96554.1}.
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DR   EMBL; JYDM01000007; KRZ96554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1PJZ2; -.
DR   STRING; 92180.A0A0V1PJZ2; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR047148; PLPL9.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR24139:SF34; 85/88 KDA CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR24139; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS51635; PNPLA; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01161};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW   ProRule:PRU01161}; Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          207..239
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          280..312
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          412..444
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          526..704
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   MOTIF           530..535
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           562..566
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           691..693
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        564
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        691
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   NON_TER         901
FT                   /evidence="ECO:0000313|EMBL:KRZ96554.1"
SQ   SEQUENCE   901 AA;  102418 MW;  49DF767183601244 CRC64;
     MLCKAKYCMD KLANPKTSNK KYYLELNSYL IRLAHMLVGW MSLMQVESSI LKGRYWPFEI
     ANNIFDGVFE VAKVVGNIIL RKTWITDISS EYSRGLYEIC NDGGILLLLS HCKKMERCIC
     LRWERQKIIF SSSNPSVALE MYHKLMNISS LIRAIHRHAV LGELMTLVKE QPHWEDVHYA
     VFLGLDSYFE QELTNIDRVI NLKSRPEGWT PLHLAVKAGN FKLLEKLIHL GADIKAVDAL
     DRNAFHLARK SNIIKVEGTL LANYLNPADL KVLVNQSDVN FMTPLHYAVR EGTDAATQTL
     IQIGAKHSSS TPPFHLAIKM KNLSQIKCFL ENDPSVLEEK DTLTGNTALH TTYDLKILRL
     LLNYVKNEAT VNTLNNKAET PLLVQMQQSD ALSNIVALIA YGADVNASRY VDHFTALHLA
     VTKQQLSYVK ALFVFGADSS KVTKSGKTAL QIALELEKRN QSDISREIVS CIETYEKRYQ
     LQNFEFLQSS SELMQFDDWC KFTRMLNVKN VIQRFTDDSV MTENLISFDG GGIRGLITIQ
     ILMLIEQAVG SDWFKNFQWV AGSSTGCIIA VGLCLGYSLG RMQKLYFQLK DTVFCGTKPY
     SEEGLESVLK QEFGTREMAS VMPRKLIVTA TNALTRPAKL KLFRSYPFPH SLQTAEEDMQ
     NDNPPLPIWK VIRSSCAAPY YFPPLDGIYI DGGLMSNNPS LELMTEMNRM NTVMNFQKRK
     ISNIGCFLSL GTGRTRTTEA YAPDFKSSWS IFDKFFHFKE FVTMLYTQCC QTDGCVVDRC
     RAWCESLGAA YFRLTPEIND LRLDETDDSR LIDACWETIR YFKENQEEIV TVCSFLKEVN
     ALEKNHVLRL EMSTFITELQ CSRSCGVSSG HMTIKEPLRS RVDYWDAGHD CLSSGGVSDK
     K
//
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