ID A0A0V1PDL1_9BILA Unreviewed; 1211 AA.
AC A0A0V1PDL1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=PLD1 {ECO:0000313|EMBL:KRZ94351.1};
GN ORFNames=T08_13379 {ECO:0000313|EMBL:KRZ94351.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ94351.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ94351.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ94351.1};
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 1,2-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}.
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:KRZ94351.1}.
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DR EMBL; JYDM01000019; KRZ94351.1; -; Genomic_DNA.
DR Proteomes; UP000054924; 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; 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; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
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 InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 2.
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; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT DOMAIN 59..274
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 281..387
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 526..553
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1024..1051
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 129..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 138715 MW; 056C614981D5FB2F CRC64;
MSELDCSSST STSDDEKCDC SILEESSSPS EDGKLMFSSL YDKQTSQDCY LANTPITAEI
TEVAEDGGTT RIFNAFHSRV YKIELQHGKY RWTIFRRYKD FFSLHNRILL YRAKRSLIPT
TRRRRQLQLS LEYDSRGGGG EGGNTEVATP SAQPGDASRD GKIIKIKQLS PVLLKYGYEN
RSQIAAVDQP TGDNGTAVMH TASLKYNKSD GTVEKSLKRK KKHCRLPSFP IWPLHNRADN
RKERLEKYLS AVLHVPAYRN LQETREFIEV SRFSFVSGLG GKNKEGYLKK RPGGRLTYGG
VVRCCAELMA SWQYRWVFLK DSYLAYVKPE GEDLRAVMLL DPGFHFKLEM HQKPRLIIEN
LNRTLVLKSK TKENAIEWKD ALENAIEVSG KQWLQNHDFG SSFPKRRNVY GRWFVDGKSY
MENLANMLEL AKEQIFITGW WLSPEIYLKR PAAAGRRWRL DEILKRKXXX XXXXXEEGIR
VYVLLYKEVE LALGINSAYS KRILQQLHAN IKVMRHPDHL PGSGVFLWAH HEKLVIIDQN
IAFVGGIDLC YGRWDDPKHR LTDFGSVSFG SARDASLTEE KSLMSAMRSM SKMLPVVQMC
NAGLVSQQIA ENPPEQSSAV VVKHCAELEI EPEVVAGEER ERRIVRFLRS SSRFGLPNFA
NLLMKHKSRM QRNNAADCKQ RGSQVLSADD GETVDDATKR RKSLFAVFFF YLHTCLIHGG
LCSVFQRIAP WMKLRRAVEE GDLKCENVDD AAMCYEEKLT CLQMEDDTDP GLYGCGKLWI
GKDYANFIYK DFTEINLPYN DFIDRRQTPR MPWHDIAAVV YCSVARDLAR HFIERWNACK
TEKAKHNQRI PYLIPKSYEK VEMPHIFHKI AYKCHIQVIR SCSQWSFGSN MVEDSIHRAY
VHLIKNAKHY IYIENQFFVS LLNSHDVHNS IAKALYDRIL QAYNDKETFR VYVMMPLLPG
FEGQLGTTGG SALQAVLHWT YCSLCKGPNS LLFNLAQHIE DPSEYIVFCS LRTHATLMEK
LVSEIIYIHS KLMIVDDLFT IIGSANINDR SMLGKRDSEV AIYVEDCEFS RSSMNGQLYQ
AGRFAFSLRT DLFAEHLGLS DTSAKRKSQL DVRDPVSTEF FTTWKQIAAR NADIFEKVFG
CIPSNSVKNF VELKQYKKRL CLGEFDLLRA RTLLEQLNGN LVLFPMKFLC QSDLSPSPIT
KEGLAPSSLF T
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