ID A0A1I7W2A8_LOALO Unreviewed; 1197 AA.
AC A0A1I7W2A8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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 Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_8893};
RN [1] {ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_8893}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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; A0A1I7W2A8; -.
DR STRING; 7209.A0A1I7W2A8; -.
DR WBParaSite; EN70_8893; EN70_8893; EN70_8893.
DR eggNOG; KOG1329; Eukaryota.
DR Proteomes; UP000095285; Unassembled WGS sequence.
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; cd01254; PH_PLD; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 2.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
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; 2.
DR PROSITE; PS50035; PLD; 2.
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};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000095285}.
FT DOMAIN 487..514
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1007..1034
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 607..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1197 AA; 136759 MW; 9EABB47590F78105 CRC64;
MADGNDNGDF NGFACDCIVS QLYEALPGSP SYKIGIVPYL STYDTQDQAR HRGYWIPGVP
VEARITDVKR DQKFGLHLIN AYLYVIELEH GPFRWTVVKQ NKDFAVLAAR LLTHRAAERI
RAPVRRAQEA LDDALESIGI DIIPDHTDDC PYRKTTEDQK VHDLNRCDDL DNMRQSGTTE
KEISVKQQPV LTDPTGTAAV PIPNVLPLTK ENSLERKNVR LSEIKSHQLP SLGFVPDAVI
DPNERRQRLE KWLRAVLHIP VNRNHHETAE FLEVSRFSFI NELGGKYCEG FVKKRPGGGR
VFIGWKQCCV RYCLRWSKRW LILKDSSVCY MNPRTEQIRF VLLFDRDFDV SAGSSETDGM
PNGLVISNQQ HILALKCRTP LDAIQWKEAI LESMNGIGRI WLENHPYGST FPVRRAQSVQ
WFVDGRSFME HAANMMELAR EEIFIAGWWL SPEIFMKRPP VEGNRWRLDE ILKVLRHPDH
YLSSGTFFWA HHEKLIVIDQ LIAFVGGVDL CFGRWDDCRH KLADCGSVKI SEQQNICAGG
NFSVAKSVRQ IVKAAGILSP IGLEEDEEVV KKTDGYDEIN RSNNLVNQEI GNDKKTKTKI
IQRRSTTFAK RKQHKKSQQN EGDIEAPRKL TEHGHVFLSV VKHTQTVIRK PKSTVEIPPI
EMLNMSAERM DIHDAMDKYK AYVHSGKAEE AKHNAEKKST PPPQRKILSK VAHSLKPSSA
KKHWQKVKQE TTRYDLRYME LRDQNEKIRA IEECMTGAGK LWVGKDYANF IHKDFVELDM
PFHDFIDRNM TPRMPWHDIH ACTYGSAARD IARHFIQRWN ATKTEKSKEL KEYPFLLPKC
YDTIKVPRVI ETYSNLADVQ ILRSVSKWSS LTNATEDSIQ QAYLSLIANA QHYVYIENQF
FVSIIDSADV GNEICKVLCE RIKRAYREKA KFRVYIMLPL LPGFEGDIGA PGGSALQAVL
HWTYKSLSRG PDSLIESLKK FMPDPMEYIH IGSLRTYEIL SGKLLTELIY IHCKLMIVDD
RYVIIGSANI NDRSQVGNRD SEVCILVKDC ENVPSRMDGK PYNAGKFAFS LRKALMMEHL
GLLPEQKRKP PKREIDVDDP VADSFFVGTW GAIAKKNTEI FEKVFNVIPT DKLRDFVEVQ
MHVAKIPLSE TVPQVAEEYL RDLIGNLVEF PLNFLANANL APGFASKEGI VPSSVFT
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