ID U4UUT0_DENPD Unreviewed; 1053 AA.
AC U4UUT0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE Flags: Fragment;
GN ORFNames=D910_11242 {ECO:0000313|EMBL:ERL93956.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL93956.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL93956.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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 -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
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DR EMBL; KB632375; ERL93956.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UUT0; -.
DR STRING; 77166.U4UUT0; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
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; 4.
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; 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; 2.
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};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742}.
FT DOMAIN 93..233
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 484..511
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 883..910
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1053
FT /evidence="ECO:0000313|EMBL:ERL93956.1"
SQ SEQUENCE 1053 AA; 119699 MW; C6401CA0581CE2B3 CRC64;
MYIRMERPSG SNDLSPTVSF PRTSIGSDAD YDDDLGVPTS IKVVDIGDGP VAIENSDDEL
EDETYEGGAP FSKLHNYVKF NSVNRNVFVP SEDIVVTLTG YERELTTHML NPNLYTIGIS
HAGFNWKINK RYKDIQSLHQ ELVLFRTGLN IPLPSKTHKN KRKTFKENVP KNKKGKRKAA
LPRFPNKPEI LVTYEKIPNR MKQIQDYLNN LVSIFIYRNH PDTLNFLEVS HVSFIKDLGS
KGKEGIVKKK SGSTHPGQSG CNFFGCYGCF CCLRWLKRWL FIKDTCFGYL NPETGKINCV
VLFDQGFEVA SAMYNMPLNT GWQVQTLSRS LTFKCKTKRK NREWIEALRE TTATTARLFV
QPNPHHSFAP IRCNTTATWF VDGSSYMSSL ADAIQNAKEE IFITDWWLSP EIYLKRPAIV
ADYWRLDKLL QRKAKDGVLI YILLYKEVEM ALGLNSFYSK QTLQDLHKNI KVLRHPDHAK
AGVFLWAHHE KTVVIDQTYA FLGGIDLCYG RWDDQIHRLT DLGSMTPALD LTTLRKRTSD
RPSGVVIYPI PVPYYKQVII PPVPPSDAQA DACVEPDLLP QLEPGDNLLL PNKCAVKPNT
PDMDRKNVFI DLTHKVKIKG KELINLVYAP TEDEGIKPNT PDINIDGTDE VGGKQDLQTP
EQIIETLDGS AKLWVGKDYV NFIVKDFTNL DLPFDDFIDR SSTPRMPWHD VGLCIHGEAA
RDVARHFIQR WNATKLEKAK GNAIYPYLLP KAYNDFKTMS INFPNSTHKV TCQVLRSIST
WSGGFLDPDY VEQSIHEAYI DSITRAQHYI YIENQFFITM PYHNPNIKNQ IGDALYKRII
RAYNGKDALL NRLKDAGIED PSEYVSFYGL RNHSRLNSEP ITELIYVHSK LMIVDDKIVI
CGSANINDRS LIGKRDSEIA VIIEDELFDD GIMNGNAYPC GKYAGTLRKC LFKEHLGLLD
NSACTAEFEV ADPIKLYEKV FHSLPSDSVE TFADIKKNNE TKPLWVEEFS RAEKMLESIQ
GHLVLLPLNF LSKENLTPAA ASVEGMLPTS LWT
//
