ID A0A0N4ZBS9_PARTI Unreviewed; 1247 AA.
AC A0A0N4ZBS9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000498800.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000498800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR AlphaFoldDB; A0A0N4ZBS9; -.
DR STRING; 131310.A0A0N4ZBS9; -.
DR WBParaSite; PTRK_0000498800.1; PTRK_0000498800.1; PTRK_0000498800.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR Gene3D; 3.30.1520.10; Phox-like domain; 2.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 3.
DR SUPFAM; SSF64268; PX domain; 2.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376}.
FT DOMAIN 63..266
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 514..541
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1059..1086
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 698..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1247 AA; 144450 MW; 6B9F82B59C3E230B CRC64;
MTTEENSPIA EESLFELCDC LLDCNSSILK QRNLKGYIPY ASVYDSLDDV RKRGYFIPGK
PVTAKIIDVS RDEQSHVHVI NAYLYTIQLS HGKYVWTVTK RFSDFLNLHR RLIAHRAVEM
VKQPIFHKSS KFEDVLKVVA ANNYHHHDCP LYKLFNEQAN NVQTLAYTGD NITENNRLKK
GTNLNENKSP TLASPENVDS PEIMKALIST NFSLPKIPKV PEIALSEESI QERREQLEKW
IQAVLATPIN RNYHETAEFL EVSRYSFINQ MGKYKEGEMR KRPGGSRVFL GWKQTCVRYF
LRWSHRWLIV KDTYVCYMHP RSSRIRLVLL LDDAFSINCP NLEIAYKPKD LVISNKQHIL
HMKCSSVDEV EWWKSEIRKI MEGPGNIWLK IHPHKSSFPL RNDCFSKWFV DGKEYWEYAA
DMIELAQEEI FIADWWLCPH VYMKRPMNEG NKWRLDVMLK RKAEQGVKIF ILVYKEVEVA
LNLNSLWMKK TIQDIHPNIM VMRHPDHYPG TGTFFWAHHE KLLVIDQIIA FVGGLDLCYG
RWDDNVHRLT DLGSIQKSSC MSGNNNETDY NLISGMRQVA GLSASLCPSG KVCETLMNDD
NPISNEVIAE GLEEVKDEDE VDGNQSGKSK LIQKKNSKMA SIVTKFKPTR KGKESFSRMK
PQIQSHVDVK MNDVTGKQEL TIPVKEQSKY KIEIEYERKN RKSKSLSRSR SKSPSPNDDI
IECNNDNIKE GEEHKLSTKD KKVWGKVTRN IKDQTRSKVG RIVSHWGTNK MKNRWRDVLN
EDSALGQYEL NWLKLKSSNE EETSKLQGGS KLWPGKDYVN YNKKDFIEVE EPFKDFIDRT
RIARMPWHDI HSVTFGTAAR DVARHFIQRW NATKTEKLKD EKKYPYILPK SYDSVRIPRI
FFPISIPTNV QVLRSVATWS TLVNETEESI QNAYIELIST SKSYIYIENQ FFVSMVGSRD
VSNKICKALV DRITLAHENK ETFRVYILIP LLPGFEGGLR SDAPTTSLHT VLHWTMVSID
NSEMSLYHCL RNRAINPDDY VSFCSLRTHS ELWGKMVTEL VYIHCKCMII DDEKVIIGSA
NINDRSQVGN RDSEVCLLIT DNEFTNSTIN GRPCKAGKFA KSLRVQLMEE HLGMLKDSPS
KTQLKINLDD PVGEKFWDQW NFIAKNNTEI FEKVFRCFPT DKTETIDELD KWNVQMSLAE
LDPKEAKELL KKLSGNLVVY PRKFLRRQNL QPSIVSKEGI IPCSVFT
//
