ID A0A0M4ELY7_DROBS Unreviewed; 1411 AA.
AC A0A0M4ELY7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE Flags: Fragment;
GN ORFNames=Dbus_chr2Rg2259 {ECO:0000313|EMBL:ALC42680.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC42680.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC42680.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC42680.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-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 -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
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; CP012524; ALC42680.1; -; Genomic_DNA.
DR STRING; 30019.A0A0M4ELY7; -.
DR OMA; EPQNYIS; -.
DR Proteomes; UP000494163; Chromosome 2r 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; 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; 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};
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:UP000494163}.
FT DOMAIN 265..494
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 756..783
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1223..1250
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 350..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ALC42680.1"
SQ SEQUENCE 1411 AA; 159305 MW; A3B73AEE153D6C89 CRC64;
WRNVFATRTV GARVRLWIAL RSVSVAGGRA RYAKRECICV LVNMLQSTET PATNVEASNP
NEAAGDAAAA AAATTTNTQW RRHRRSISQL MASLADDAYR PTHLDGYVNH GYDDLDSSYL
FAQYEAMAAS ANGAPLPPYT RSADTQSGEE CEGVGDDDVF KDCADDAAAE EHDLAHQSRC
LPEFQFSMID SEYDETLAFD DSVTILSNVG DKPVLVERKD TDEDDDEFDD ENSVQLRQEL
PYLSIYGPSV KFNSFQRKVF IPGCEIHVRI VDTERSVTTH LLNPNLYTIE LTHGPFKWTI
KRRYKHFSSL HQQLSFFRTS LNIPFPSRAH KEKRTTLKAA ACQMADESTL KDLPAHTKVK
HTSTPAKDHN RSSTANQSRT NNNKNTSGCS AAAADAAAAT PGGGGSGGGT VATIANATHT
SLLMSLAPRR IQRKRKKKKR KLPRFPNRPE SLITVEHLPV RIKQLEDYLY NLLNISLYRY
HHETLNFVEV SNVSFVSGLG IKGKEGGILK RTGSTRPGQA GCNFFGCFQR NCCVRCNYFC
SDVVCGTWRN RWFFVKETCF GYVRPTDGSI RAVILFDQGF DVSTGIYQTG MRKGLQVLTN
CRHIVLKCWT RRKCKEWMQY LKNTAHTYAR DFTCPNPHMS YAPMRANTQA IWYVDGAQYM
AAVADALEAA SEEIYIADWW LSPEIYMKRP ALDGDYWRLD KILLRKAMQG VRVFVLLYKE
VEMALGINSY YSKSTLAKHE NIKVMRHPDH ARGGVLLWAH HEKIVVIDQA YAYIGGIDLC
YGRWDDRSHR LTDLGSISTA SASGSTRYTP SVYFNKDEVD SAFGSRKSSR NASHETPVKE
ANTSVGVELR RLKPGDRLLI PEMLTSTPTA DSPIEGMKLN TPEMERKNVL DRLKNNAMKG
ARIGKDFVQR LTANESFATD KCNDNELEDT GESNAAEQTG GSSCTQQDAC HISSEFYGQA
KYWFGKDYSN FILKDWMNLN APFADIIDRT TTPRMPWHDV GICVVGASAR DVARHFIQRW
NAMKLEKLRD NPRFPYLMPK SYHQIKLNAQ LQQLQQRRQQ RVTCQLLRSV SAWSCGFIEA
DLVEQSIHDA YIETITKAQH YIYIENQFFI TMQLGMGVSG AHNNVRNQIG ETLFKRIVRA
FKERKRFRVY VIMPLLPGFE GDVGGNTGIA VRAITHWNYA SISRGRTAIL TRLQEAGVVE
PQNYISFHSL RNHSYLNNTP ITELIYVHSK LLIADDRVVI CGSANINDRS MIGKRDSEIA
AIIMDEEFED GRMNGNKYPS GIFAGRLRKY LFKEHLGLLD GDSSSRCDLD ISDPVCDRFW
HGTWRYISTK NTDIYDEVFK CIPTDYVKTF ASLKKYQEEP PLSKSDPEMA AKRATEIQGH
LVNLPLEFLN KEVLTPPGTS KEGLIPTSVW T
//
