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Database: UniProt
Entry: A0A0V1HH53_9BILA
LinkDB: A0A0V1HH53_9BILA
Original site: A0A0V1HH53_9BILA 
ID   A0A0V1HH53_9BILA        Unreviewed;       834 AA.
AC   A0A0V1HH53;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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:KRZ10158.1};
GN   ORFNames=T11_7574 {ECO:0000313|EMBL:KRZ10158.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ10158.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ10158.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ10158.1};
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:KRZ10158.1}.
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DR   EMBL; JYDP01000063; KRZ10158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1HH53; -.
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:SF34; 85_88 KDA CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR24139; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00248; ANK; 8.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
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|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          185..207
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          356..388
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          389..421
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          512..689
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ10158.1"
SQ   SEQUENCE   834 AA;  92715 MW;  984219EA953F1862 CRC64;
     LKRKRELMAN QPVHIYQDSK KINQVSKFVG NMVSAMREKV MGESWWLPSS CKTVVEIPTR
     SIRLLVEQER HEQFAIFRAN ENATGANQLY HVVLYWLDNK MLSLRRFSDS NEASNYYNML
     VHHSCLFQLI DNRKALDTLL DCIQAHSLWL PVHVAAKLGM KNYFEVIKSS ELSCKQQLSH
     VCQPEGCYPL HIAVESGNVD LVVYMIDCLQ ASLTVTDIRG QTPFHYAART SPTMIAALAC
     YDNEKSQINA LSKDGYTPLF LSISSCKPTC TAALLKQGAV LNIMCNGRSP IHMAMLQSGN
     KLNEMIKTLV EASPDCIYQA DKQTGNSALH VAGNKQALNA LLSVCPDINL NCRNNAGQTA
     LHLHTYLNNL SCVVALYYHG ADLNAKDTNG NTSLHIAVSA ENESMTKALL VLGADPNIVN
     DNGHSPRHTA ARLNVRGREL MRCLIIGGAI RCPVESSGCA ATCSYRNADE SDLSVQYTAL
     NYLETISVRK QEECIKKVVE MAATGKKFDV LLSLDGGGIR GVILILLYIE AALKKPLISY
     VTWLAGTSTG GFLAAGLAKG KSLRDCQKIY LRMKDCLFEG RIRPYQSDAF EQLIKANIGE
     TSKITDIVSP KLIITTVLAE KHPVQLHMFR NYTLPGDDNQ CCTQCSYIPD IPLWKVLRCS
     SAAPTYFDSV DNKFVDGGLI ANNPALDLLS EFERYKSCQE FSECNEEASV GCLLSIGTGR
     IPDMPIESLN LGFINVIDMV SAFKNLGYMI MDQVTAAEGR PVDRARSWCH CMGVPFFRFS
     TPMSKDFALD TKSDQDLIQM MWETLEYVVN QRNEIAMLVE LLNTLHSNSR FTEA
//
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