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
//