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Database: UniProt
Entry: A0A0V0U477_9BILA
LinkDB: A0A0V0U477_9BILA
Original site: A0A0V0U477_9BILA 
ID   A0A0V0U477_9BILA        Unreviewed;       868 AA.
AC   A0A0V0U477;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-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:KRX46029.1};
GN   ORFNames=T05_11058 {ECO:0000313|EMBL:KRX46029.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX46029.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX46029.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX46029.1};
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:KRX46029.1}.
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DR   EMBL; JYDJ01000065; KRX46029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0U477; -.
DR   Proteomes; UP000055048; 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; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR24139:SF35; PNPLA DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 2.
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}; Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT   REPEAT          211..243
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   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX46029.1"
SQ   SEQUENCE   868 AA;  98798 MW;  ACC3E502A07C7324 CRC64;
     LVGWMSLMQV ESSILKGRYW PFEIANNIFD GVFEVAKVVG NIILRKTWIT DISSEYSRGL
     YEICNDGGIL LLLSHCKKME RCICLRWERQ KMLCIFSSSN PSVALEMYHK LMNISSLIRA
     IHRHAVLGEL MTLVKEQPHW EDVHYAVFLG LDSYFEQELT NIDSARFWRN YMYIAELSAL
     FDAFFIDFRE EQLLEVSMCN MKVINLKSRP EGWTPLHLAV KAENFKLLEK LIHLGADIKA
     VDALDRNAFH LARKSNIIKL LANYLNPADL KVLVNESDVN FMTPLHYAVR EGTDAATQTL
     IQIGAKHSSS TPPFHLAIKM KNLSQIKCFL ENDPTVLEEK DTLTGNTALH TTYDLKILRL
     LLNYVKNEAT VNTLNNKAET PLLVQMQQSD ALSNIVALIA YGADVNASRD ADHFTALHLA
     VTKQQLSYVK ALFVFGADSS KVTKSGKTAL QIALELEKRN QSDISREIVS CIETYEKRYQ
     LENFEFLQSS SELMQFDDWC KFTRMLNVKN VIQRFTDDSV MTENLISFDG GGIRGLITIQ
     ILMLIEQAVG SDWFKNFQWV AGSSTGCIIA VGLCLGYSLG RMQKLYFQLK DTVFCGTKPY
     SEEGLESVLK QEFGTREMAS LMPRKLIVTA TNALTRPAKL KLFRSYPFPH SLQTAEEDMQ
     NDNPPLPIWK VIRSSCAAPY YFPPLDGIYI DGGLMSNNPS LELMTEMNRM NTVMNFQKRK
     ISNIGCFLSL GTGRTRTTEA YAPDFKSSWS IFDKFFHFKE FVTMLYTQCC QTDGCVVDRC
     RAWCESLGAA YFRLTPEIND LRLDETDDSR LIDACWETIR NHVLRLEMST FITELQCSRS
     CGVSSGHMTI KEPVHRSLKL LISVTKSS
//
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