ID   A0A3D8MVD8_9DELT        Unreviewed;       639 AA.
AC   A0A3D8MVD8;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=DV096_09925 {ECO:0000313|EMBL:RDV38123.1};
OS   Bradymonadaceae bacterium TMQ3.
OC   Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae.
OX   NCBI_TaxID=2283320 {ECO:0000313|EMBL:RDV38123.1, ECO:0000313|Proteomes:UP000256871};
RN   [1] {ECO:0000313|EMBL:RDV38123.1, ECO:0000313|Proteomes:UP000256871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMQ3 {ECO:0000313|EMBL:RDV38123.1,
RC   ECO:0000313|Proteomes:UP000256871};
RA   Wang S.;
RT   "Lujinxingia celare sp. nov., isolated from a marine island.";
RL   Submitted (AUG-2018) 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   -!- 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:RDV38123.1}.
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DR   EMBL; QRGZ01000003; RDV38123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8MVD8; -.
DR   OrthoDB; 9765044at2; -.
DR   Proteomes; UP000256871; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   Gene3D; 2.60.40.1260; Lamin Tail domain; 1.
DR   InterPro; IPR001322; Lamin_tail_dom.
DR   InterPro; IPR036415; Lamin_tail_dom_sf.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR   PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR   Pfam; PF00932; LTD; 1.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS51841; LTD; 1.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
FT   DOMAIN          148..175
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          341..372
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          427..592
FT                   /note="LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51841"
SQ   SEQUENCE   639 AA;  70878 MW;  A3E7406A5CCB1CF9 CRC64;
     METTTNVFEQ SGREHTMVIR GMASMARTLV LAALALSAAA CGLNDPGDLD TLDTPSVEVF
     FNSPGFKRGT EFNRKPSEFI TERIDAARVS VDAAVYGFNK QNIVDALVRA HYRGVRVRLV
     ADAGEYSRGS YGYDIMEQHK VPIQTGNQFH IMHDKFFVVD NRFVFVGTGN ISNSEFTYNN
     NNWVWFDNVA HAELYTAEFE QMFDGRFSAA KHPTTLPNVF QIGDTEVEVL FSPQDDAMGK
     ILEELKNVDT SIYFTIFAFT KDQVASEFIA RQREFEAYNE ANGFDTLPPL ERPKGVVGVL
     DRSQLHGNGQ YHQGYRLAAN GIPMRLDGNE NSGLPGDYQA GGGRLHAKTM ILDAGTPNAR
     VITGSFNWSS AATISNDEIL IILRGERITN QYLEEFYNIW NTGKDISTAM CTLMKDSDAL
     TCDDEVRPGD VVFSEVHFDG WNGERDPSDH NCGGGNDLDC RRRVTNDQFV ELYNTTDKPI
     NLSMWTLSNG QDVTMGFTPG TVIDPGEYFL VLDHNTVPLS ERDPQRGEHA FTNPDFVLNT
     ANDPRFRRLN LKSGSMQLQL RNTRQVVIDR AGDGSPAYFG GREGDTNYSM ERIIGADGNV
     GAGDARSSWK QCAAGQGGEN VNEAFRSFII ATPGEPNSP
//