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Database: UniProt
Entry: A0A0V1MVD9_9BILA
LinkDB: A0A0V1MVD9_9BILA
Original site: A0A0V1MVD9_9BILA 
ID   A0A0V1MVD9_9BILA        Unreviewed;       904 AA.
AC   A0A0V1MVD9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:KRZ75583.1};
GN   ORFNames=T10_12213 {ECO:0000313|EMBL:KRZ75583.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ75583.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ75583.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ75583.1};
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:KRZ75583.1}.
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DR   EMBL; JYDO01000036; KRZ75583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1MVD9; -.
DR   Proteomes; UP000054843; 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   PRINTS; PR01415; ANKYRIN.
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:UP000054843};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          177..209
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          246..278
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          378..410
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          504..682
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   MOTIF           508..513
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           540..544
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   MOTIF           669..671
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        542
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        669
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ75583.1"
SQ   SEQUENCE   904 AA;  102990 MW;  13944B0E5F18C549 CRC64;
     LNFRLVGWMS LMQVESSILK GRYWPFEIAN NIFDGVFEVA KVVGNIILRK TWITDISSEY
     SRGLYEICHD SGILLLLSHC KKMERCICVR WERQKMLCIF SSSNHSVAYE MYHKLMNISS
     LIRVIHRDAV LGELMTLVKE QPQWEDIHYA VSLGLDSYFE QELTNIDRVI NLKSRPEGWT
     PLHLAVKAGN LKLLEKLIHL GADIKAVDTS ARNVFHLARK TKIIKILANY LNPADLKVLV
     NQSDVNFMTP LHYAVREGTD AAVQALIQIG AKHSSSTPPF HLAIKMKNLS QIKCFLENDP
     SVLEEKDTLT GNTALHTTYD LKILRLLLNY VKNEATVNTL NNKNETPLLV QMQQSDALSN
     IVALIAHGAD VNASRYADHF TALHLAVTKQ QLAYVKALFV FGADSSKVTK SGKTALQIAL
     ELEKRNQSDI SREIVSCIKT YEKRYRLQNF EFLQSSSESM QFDGNDQFIF FFSFEDWCKF
     SRMLNVKKVI QQFTDDSVMT ENLISFDGGG IRGLITIQML MLIEQAVGSD WFKNFQWVAG
     SSTGCIIAVG LCLGYSLDRM QRLYFQLKDT VFCGTKPYSE EGLENFLKQE FGTREIASVM
     PRKLIVTATN ALTRPAKLKL FRSYPFPHSL QTADEDMQND NPPLPIWKVI RSSCAAPFYF
     PPLDGIYIDG GLMSNNPSLE LMTEINRMNT VMNFKKRKNS NIGCFLSLGT GRTRTTEAYA
     PDFKSSWSIF HKLFHFKEFL TMLYTQCCQT DGCVVDRCRA WCESLGAAYF RLTPEINDLC
     LDETDDSRLI DACWETIQYF KENQEEIVTV CSFLKEVNTL NKNHVLRLEM SIFITELQCS
     RSRGVSPVRM TIKEPVHHNS FPSFKAAKLS YEVELTTGMR NAIACLLGRD YILPIFLITS
     SRSI
//
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