ID   A0A5N5T851_9CRUS        Unreviewed;       936 AA.
AC   A0A5N5T851;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   18-JUN-2025, entry version 25.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   Name=PLDBETA2 {ECO:0000313|EMBL:KAB7502349.1};
GN   ORFNames=Anas_09889 {ECO:0000313|EMBL:KAB7502349.1};
OS   Armadillidium nasatum.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Peracarida; Isopoda; Oniscidea; Crinocheta;
OC   Armadillidiidae; Armadillidium.
OX   NCBI_TaxID=96803 {ECO:0000313|EMBL:KAB7502349.1, ECO:0000313|Proteomes:UP000326759};
RN   [1] {ECO:0000313|EMBL:KAB7502349.1, ECO:0000313|Proteomes:UP000326759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANa2 {ECO:0000313|EMBL:KAB7502349.1};
RC   TISSUE=Whole body excluding digestive tract and cuticle
RC   {ECO:0000313|EMBL:KAB7502349.1};
RX   PubMed=31600190; DOI=.1371/journal.pbio.3000438;
RA   Becking T., Chebbi M.A., Giraud I., Moumen B., Laverre T., Caubet Y.,
RA   Peccoud J., Gilbert C., Cordaux R.;
RT   "Sex chromosomes control vertical transmission of feminizing Wolbachia
RT   symbionts in an isopod.";
RL   PLoS Biol. 17:e3000438-e3000438(2019).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC       {ECO:0000256|ARBA:ARBA00010683}.
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:KAB7502349.1}.
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DR   EMBL; SEYY01007791; KAB7502349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5T851; -.
DR   OrthoDB; 14911at2759; -.
DR   Proteomes; UP000326759; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR   CDD; cd00030; C2; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR024632; PLipase_D_C.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF60; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF12357; PLD_C; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000326759}.
FT   DOMAIN          1..114
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          164..291
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          474..511
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          782..809
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   936 AA;  106723 MW;  E24663D6B4FF25E1 CRC64;
     MVYLTGRIEV VVVEAYDLLN LDQSFFNSDD KSDPYCIVSA DGINGSRRIG KTCTIDDCLN
     PKWNYKMVAD LNQDVTGLRF VVKDKDLITS ELIGSCFVDT MSFVTSDRPY ENLLQLSTAH
     GKRAGSIRVQ IMYTGTGSST AIESTVADRM KLKTEDMMAR ISYSSNQNEP HSGKKSVVLH
     GLLEVYIGHA LNLPNLDKSL FSLRAGDVSD PFIEVIVEDP FNEKWKVATT SVIDNNLNPE
     WDESFYINIC HDIVTLNFVV KDKDVLSADL IGTVAFQAED LIIAPEIKGE FDLFKNGKPL
     KGAKLSLRLC YKSSNELSNS LEVPGCFFRM RELNRVTLYQ DAHCVGMHPI RRNDGTYYKQ
     PRAWKDLYNA IMEAKEFIYI VGWSVNTRIS MLRWQNEDDR SIGEILLQKA NEGVQVLIMI
     WDELTSTDFN KEGAMGTSDE ATAEFFKNTP VTVVLVSRER KTKDISTKQR FTNFCYTHHQ
     KCVIMDGEIP DSPNRRQTVA FLGGLDLTNG RFDIPEHPLF VTLDNDHKDD FYNSLYVGKT
     QYGPREPWHD IHCRLEGPVT QDLFSNFIER WNKQGIPKKN VPINANLENK KFIYRIPERW
     NVQIFRSINS DSATFESCTK PKGLSVKKER IFDNSIQRAY IHHIRRAKKY IYMENQYFMG
     SSHEWLECRE AHVENLVPLE IAAHIEGKIR KGERFTAYIL VPMFPEGKPA DKVIQEMLHW
     QFRTIEMMYY RVANAINHAG IDAHPQDYLL FLCLGKKEGT NPEPVPTELT GHAAGAFKHR
     RLMIYVHSKM AIFDDEYIIV GSANINDRSL NGNRDTEIAM GTFQAEHLSS HVRLADGEIS
     MFRKSLWLEH MGDKAPLNDN PADLNCIRKV KDLAEEGFLS FIDESNRKGI RHLLIYPLNV
     GYDGSVTTRD ECPTFPDTVA SIIGKKSGYF PSSLTS
//