ID A0A815T327_9BILA Unreviewed; 1098 AA.
AC A0A815T327;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 05-FEB-2025, entry version 15.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=NZN594_LOCUS42899 {ECO:0000313|EMBL:CAF1500960.1};
OS Rotaria sp. Silwood1.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Rotaria.
OX NCBI_TaxID=2762511 {ECO:0000313|EMBL:CAF1500960.1, ECO:0000313|Proteomes:UP000663835};
RN [1] {ECO:0000313|EMBL:CAF1500960.1}
RP NUCLEOTIDE SEQUENCE.
RA Nowell W R.;
RL Submitted (FEB-2021) 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:CAF1500960.1}.
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DR EMBL; CAJNOP010000363; CAF1500960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A815T327; -.
DR Proteomes; UP000663835; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
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:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:TreeGrafter.
DR CDD; cd01254; PH_PLD; 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; 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; 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; 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:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000663835}.
FT DOMAIN 79..223
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 476..503
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 914..941
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1098 AA; 128288 MW; 4C4D21D57B55E273 CRC64;
MANHGDSGGV RALVRHTAAM AELAIHAGHP DRKHNEYLPY PDDNFDEIDD ERFERTGKFT
IEHIHNRRGE TFVPNARVHI KSIVADRTYA AFTEFLNPYL YCITTRYGPF EWSVYKRYRH
FHDLHKALAH FVEIETKRSL SDLEKKTLEM YRITLTYLTG LQDENNEYPC FPTRNDRMAF
INDAIIQERC EILAEYLNKV LKHPKFRRHP ATCEFFEVSC LSFIYGISIS RKEGYLLKRS
HDDYRGQHTF FRLPFFCDVC KRHHDRKWFI IKDSYITYIR PNTHELRFPM LVDRGFHILT
GIRHVRTYRG IKIKNLQRTL VIKCRTTRDS DEWTQHLAEL IEQAKGFVDK TASRFNSYAP
IREKQLAYWF INGKSYMEAV AKGLLTAKEE VFITDWWLSP EVMLVRPTED EEFRLDNILG
RIADAGVRVY VMVFKEMSFA VGLNSSYTKR ILTSKSKRGF IKVIRHPDHH PNGGVLLWSH
HEKMVVIDQK IAFVGGIDLC YGRWDDDFMR LVDLGAENDT TLKSPYDIVV ENAAAGGTET
VESAQKATTQ MAEQAGEKPI KSSDRLRTVF SAPNKASEDI KFGEPTHEHK IEFRRKALTK
KYIPTTSDRR MFEDDEKVAR RPDKYARKWR KLAQKAKKGS DDSDNEEVVE EPQAVISLSL
EIDRRQKLFI GKDYSNVYEK DFETLEKYSE DFIDRKIVPR MPWHDEALVV FGQTARDVAR
HFIQRWNIHK CEKYLNNDNY PFLLPKSYDD EEDLTVKNWK DFLESRPLKV DAQCVRSVGP
WSAGTKTIES SIQNAYIQMI DAAKHYIYIE NQFFITIAQD PDVRNLLGDT LFRRIERAHK
LQEKFRIYVV LPLLPGFDSI NAVQAVLYFI MRSITKGDSS LFKRLERAGI PPNDYISFFG
MRTHDILMGR LVTEIIYVHS KLMIIDDRMA ICGSANINDR SLLGQRDSEF CIVINDREEE
QGRFNGQPYR IGKFCSSWRR KLFAMLLGIQ FENSKNIDIT DPVSEEFYNY FRAIARKNTL
IYEEVFATMP SDHVRKFDQI SGYNGMAKMA DTDPIQAQQK LKDIQGLVVE YPLYFLDEED
YLPSINTPEG IVPTVTWT
//
