ID G0MPT7_CAEBE Unreviewed; 1416 AA.
AC G0MPT7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=Cbn-pld-1 {ECO:0000313|EMBL:EGT40793.1};
GN ORFNames=CAEBREN_19655 {ECO:0000313|EMBL:EGT40793.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL379806; EGT40793.1; -; Genomic_DNA.
DR STRING; 135651.G0MPT7; -.
DR EnsemblMetazoa; CBN19655.1; CBN19655.1; WBGene00158380.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_0_1; -.
DR InParanoid; G0MPT7; -.
DR OMA; INNAQHY; -.
DR Proteomes; UP000008068; 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; 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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT DOMAIN 157..387
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 636..663
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1225..1252
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1416 AA; 162589 MW; 3357B5B0FABEA0CF CRC64;
MESEDEESRR PRTTSSGHLE PVDTTAHNSV DSSVMHDRGI PGLLPATQAS EKQKKAVIRF
RDHEGRADSP PSNLNVRRNS RTVHIDEVAS PQSLEYDDDS DSSDDDEIQY CDCVAAALQQ
SLPGTPGRKG IIPYMSIYDT QQQARRRGYW IPGVPVNAKI VKVERNPDRG IHFINTLLYT
IELEHGHFRW SVIRNYKDFT LLNNRLMAHR AREQFMAPIK RTQERFDNYL EHMGIDIIPD
HKPDCPYSNQ SSKRKRHPKL EVLKRDSDGI EESKNTSAPL ASAETPGDIE EAQKKEVAMQ
EAVQSGILQE EPDASATSEG TPKRQRRQQR KKDRHTLPRF PMMPDSMVTN LEHRKELLEN
WLQMVLHIPI NRNHHETAEF LEVSRYSFVN ELGGKHTEGF VKKRPGGSRA FLGWKQCCVR
YFLPWSKRWL MVRDSFVAYM DHRSEQIRTV LLMDRDFKVA AGGKETEGIP TGLIITNTQH
ELHLKCRRIQ DTATWKAIIE QSMAGIGNIW LQPHRFSSSF PVRENCHAKW FVDAKTYMEY
AADMMELARE EIYITDWWLS PEIYMKRPAL EGNYWRLDEI LKRKAEQGVK IFILLYKEME
MALGLNSIYT KRTLQNLHEN IKVMRHPDHY PSTGTFFWAH HEKLLVIDQL ISFVGGVDLC
FGRWDDHRHV LTDLGSVQYS GAHLVGTNMA SGLRSLMTAP LTLSPLGLEE HEQVTPRNEN
GVKHVAVKEV EEPQDVTERT QETEIDDDEE VSENPDVKKM MEETVFTDKE TGGVVVRTLN
RFPVDETMRH SSPPDPQKNF KETKTTVVES SSTTGGITTK TTTTTTTTKV VKDNTLEKEK
NKKDLRRAVT SLDRQRKHVP IEVLDRAGPA PSMMEKSVKS GMNMAEAAEK YKEYVESGAV
QKEKHRAQTP PNRRKAKKDS KITRAVGNWK SNRAKRKWKQ MLESDEATMG YELDWLRLRE
MDEKGDGDDQ IDGGVKLWYG KDYVNYIAKD FVEVDMPFHD FIDRGTTPRM PWHDIHSVTF
GAPARDVARH FIQRWNATKT EKLKDDNNYP YLLPKSYENV RVPRVFKTAN ASEMVNVQVL
RSLSKWSGLI NQTEDSIQMA YLSLIANSKH YIYIENQFFV SMIDSIEVTN EVCKVLYNRI
VRAYKEKENF RVYIMIPLLP GFEGDVGAPG GSSLQAVLHW TYRSLSQGPN SLIQRLKAVM
PDPFKYIHVG SLRTYDQLGQ KLVSELVYIH CKLLIVDDET VIIGSANIND RSQCGNRDSE
VCCVYTDVVK ERSVMDGKPY EAGRFAKSLR MQCMREHLGL LPDSRRKAKF PYAVSCDDPV
ADSFYVDVWQ SVAKSNAQIY EEVFRSYPTD FVETFDEFQK WTSQIPMSEY SPQQAEERVR
DLKGVLVDFP LNFLCKAVLT PGITSKEGLV PSAVFT
//
