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
//