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Database: UniProt
Entry: A0A0V1H492_9BILA
LinkDB: A0A0V1H492_9BILA
Original site: A0A0V1H492_9BILA 
ID   A0A0V1H492_9BILA        Unreviewed;       901 AA.
AC   A0A0V1H492;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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:KRZ05302.1};
GN   ORFNames=T11_3398 {ECO:0000313|EMBL:KRZ05302.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ05302.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ05302.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ05302.1};
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:KRZ05302.1}.
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DR   EMBL; JYDP01000142; KRZ05302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1H492; -.
DR   STRING; 268475.A0A0V1H492; -.
DR   Proteomes; UP000055024; 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; PF00023; Ank; 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}; Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024}.
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          492..677
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ05302.1"
SQ   SEQUENCE   901 AA;  102312 MW;  6DF6C3E6A8FD9FBB CRC64;
     LNFRFVGWMS LMQVESSILK GRYWPFEIAN NIFDGVFEVA KVVGNIILRK TWITDISSEY
     SRGLYEICHD SGILILLSHC KKMERSICVR WERQKMLCIF SSSNHSVAYE MYHKLMNISS
     LIRAIHRDAV LGELMTLVKE QPQWEDIHYA VSLGLDSYFE QELTNNDRVI NLKSRPEGWT
     PLHLAVKAGN LKLLEKLIHL GADIKAVDTS ARNVFHLARK TNIIKILANY LNPADLKVLI
     NQSDVNFMTP LHYAVREGTD ATIQALIQIG AKHSSSTPPF HLAIKMKNLS QIKCFLENDP
     SVLEEKDTLT GNTALHTTYD LKILRLLLNY VKNEATVNTL NNKNETPLLV QMQQSDALSN
     IVALIAHGAD VNASRYADHF TALHLAVTKQ QLAYVKALFV FGADSSKVTK SGKTALQIAL
     ELEKRNQSDI SREIVSCIET YEKRYRLQNF EFLQSSSESM QFDDWCKFSR MLNVKKVIQQ
     FTDDSVMTEN LISFDGGGIR GLITIQMLML IEQAVGSDWF KNFQWVAGSS TGCIIAVGLC
     LGYSLDRMQR LYFQLKDTVF CGTKPYSEEG LENFLKQEFG TKEIASVMPR KVDFPAVRLI
     VTATNALTRP AKLKLFRSYP FPHSLQTADE DMQNDNPPLP IWKVIRSSCA APFYFSPLDG
     IYIDGGLMSN NPSLELMTEI NRMNTVMNFK KRKNSNIGCF LSLGTGRTRT TEAYAPDFKS
     SWSIFHKIFH FKEFVTMLYT QCCQTDGCVV DRCRAWCESL GAAYFRLTPE INDLCLDETD
     DSRLIDACWE TIQYFKENQE EIVTVCSFLK EINTLNKNHV LRLEMSTFIT ELQCSRSRGV
     SPGCMTIKEP VHHNSSPSFK AAKLSYEVEL TTGMRNAIAC LLGVGATKWL GTTELYLAYF
     F
//
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