ID R7ULW0_CAPTE Unreviewed; 947 AA.
AC R7ULW0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=CAPTEDRAFT_168015 {ECO:0000313|EMBL:ELU04927.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELU04927.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELU04927.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELU04927.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP168015}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 EMBL; AMQN01008018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB301969; ELU04927.1; -; Genomic_DNA.
DR AlphaFoldDB; R7ULW0; -.
DR STRING; 283909.R7ULW0; -.
DR EnsemblMetazoa; CapteT168015; CapteP168015; CapteG168015.
DR HOGENOM; CLU_000690_2_0_1; -.
DR OMA; ILYWAHH; -.
DR Proteomes; UP000014760; 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 CDD; cd06895; PX_PLD; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
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; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX 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 Reference proteome {ECO:0000313|Proteomes:UP000014760}.
FT DOMAIN 51..183
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 429..456
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 763..790
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 113..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..130
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 109309 MW; 73AEFC422433F65B CRC64;
MTHLLITRNY FSLLFLSANI SVLSKIPFKT IHNPSLPFED STRRCFLPGR KINIEIKDVE
QADHSRLLNP NIYIVHIRHG PFFWTIKRRY KHFRHLHEQL MLLRAGAKLP IPTQKHRQRR
KSFARKKQSL PKFPKRPDPL IRTEEMDRRK QELQDYLQNV LRHPQFRNHP ETLKFLEVSH
LSFVNGLGSK WREGIVKKRS GGRKIRLHLC GECCGGCHST AHYQRRWLVL KDTFVAYVKP
ETGAVSDVLL MDREFEVKIG LMNTGIRHGM LISNYSRNLL VKCWTQHKSR QWEEQISKAA
AQTGKDFTQP NRYESFAPVR SRAYCNWFVD AATYMSAVAD GLESAKEEIF ITDWWLSPEL
HLKRPVTEGD KWRLDYLLKR KACQGVKIFV LLFKEIEAAL GINSYYSKQT LVGLHPTNIK
VMRDPDGLNL WSHHEKCVVI DQRIAFLGGI DLCYGRWDTR LHRLTDLGSD EGIVETDVDS
GQTQDEGDQG LVGEIKLWMG KDYVNFIFKD FVELDKPFTD MVDRSVTPRM PWHDIGAVCY
GHPARDVARH FIQRWNFTKL HKQKMNIDYP MLLPKSYENF SVPSWVPQQA FTCNCQITRS
SCEWSAGIKT IDCSIMNAYV DLIKNSKHYI YIENQFFISI EENPLIENAI GNALYERIMK
AHRDKETFRV YVVLPLLPAF EGELGTSKGT CIQAIIHWNY ASISRGGHSL LERLVQYGSP
IVLLLVVAFN VVFASLSVND PFEYISFYGL RTHEELIGNL TTELVYVHSK MMIVDDFSVI
IGSANINDRS LLGKRDSELA IIVQDTHTVP SRMNGKDFQA GTYASSLRKS LFREHLGIGP
TDTDIDVTDP VSTEFYKNVW LKQASINTTV YDKVFNCIPT EEVTSNHELR EYQKKPVLAQ
TDPDKARKEL KKVRGHLVLM PLQFLIQENL SPSPGTKEAF VPTIVWT
//
