ID A0A0D2AC38_EXOME Unreviewed; 1864 AA.
AC A0A0D2AC38;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=PV10_00346 {ECO:0000313|EMBL:KIV96478.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV96478.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV96478.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV96478.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-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}.
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DR EMBL; KN847520; KIV96478.1; -; Genomic_DNA.
DR RefSeq; XP_016228052.1; XM_016364403.1.
DR STRING; 212818.A0A0D2AC38; -.
DR GeneID; 27318191; -.
DR VEuPathDB; FungiDB:PV10_00346; -.
DR HOGENOM; CLU_000690_0_0_1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000054302; 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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
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 SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000054302}.
FT DOMAIN 473..663
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 925..952
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1231..1258
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1864 AA; 210110 MW; B4CCC4D77D33D562 CRC64;
MAEMTWEKPA VSDNISSTRA LQTNLTRSKE NSPNRQHMGG PGPAVDLNGA LDDPAYRSEP
SKLSATQGPP SENVSPLSAV PNPTGGFKQP LGAPFAPLSI NSNHLDTSTS PGKEVPDADN
ALNGSGTAYG NGTPTAPRKS VQFSRDTEEI DIPILGQSTP PLDGSELDKP QSLYARLRAL
AIPQGFSHSR SASGLSTSAR SADGKDADAQ NNYFGRHDNA LAATLEEDSA EEADDDADGE
DSAAERREPQ PTSRTRRKRR IRRFDNIETA PSSPNSPMRP GLASVPQASD RPRPPVLVRR
VTDTDMPHNH KHQGLSEDEG HRNLSRETSA WTPRHPLRGL SYGGQRKPGD STPEGQKRPL
TLLNFAGITS SREAAPSDPT TPKTPSRRKI MSERGTSLSA AKWKQLKNSL RLLGQTRKKE
RTPDHEKSAE LLAELAAGTP AALMLASMFQ RDEHDNRRIP ILMEQLKLRI TDSEVDKDRY
KEADVSTPSD RHLIFRIELE YGNGINRMKW VVKRSLGDFI NLHAKYKLHY GSERLKGRGD
ASLDKFPKFP RSAFPYLKTW RGLDDETEED DDPANNPDDT AATDTEGRTP KLQSRPSFMP
SRRRSSVGGI QDPESGGLRR DLRFADRQRK KLELYLQLMI KFLLFRPESN RLCKFLEVSA
LGMRLAAEGS FHGKEGYLLI RSAKGLDFRR ALTPANITHR HTPKWFLVRH SYVVCVDSPE
EMHIYDVFLF DSDFRIQSKR RLKNHPRAKG LADAARESTG QHHRLKLINS ERRLKLLARG
ERQLHQFEES IRNMIEISPW VKINRFDSFA PIRPNCFAQW LVDGRDYMWV VSRAINQAKD
VIYIHDWWLS PELYMRRPPA ISQKWRLDRL LKRKAEQGVK IFVIVYRNIE SAIPIDSQYT
KFSLLDLHPN VFVQRSPNQF RQNTFFWAHH EKICIVDHTL AFVGGIDLCF GRWDTPQHTL
VDDKSTGFEA SDQPKDADHC QLWPGKDYSN PRIQDFYNLN KPYEEMYDRT RIARMPWHDI
SMQVVGQPAR DLTRHFVQRW NYILRQRKPT RPTPFLLPPP DFNPADLEAL GLDGTCEVQI
LRSAGPWSLG TPDKTEHSIM NAYVKMIEES EHFVYMENQF FITSCETEGA TVHNKIGDAL
VERITRASKN GEAWRAIIII PLIPGFQNTV EQEGGTSVRL IMQYQYRSIC RGESSIFGRL
KHAGVEPEDY IQFYSLRQWG RLGPNKTLVT EQLYIHAKCI IVDDRVALIG SANINERSML
GNRDSECAAI VRDTDLLWST MNGKPYQVGR FPHTLRMRLM REHLGLDVDK IMEDAQVMEA
EHQKSEIAGR STKSPSHGDE VASPQSEEED TLTPLGKRTA ELREELLKRS EELKSFNHDV
DWEQQDNPNL KSNRKLTEDS RVTGNANHRQ DVEGQGFDHM AEADAAGLIV GRDSAIAKGA
REVLIANLDT EGRATVQNPR RHGEAVRLPS YVAKQEVPNP PFPPRPTAER MNTEQLGLPM
LSILPALPPG DDTDIGGPPL EKLTSKDSVR TRHPLMNDLR RPMVDRDCMM DPIHDAFLYD
TWHAVAENNT KIYRSVFRCM PDNQVRTWED YRQYIAYEHR FNQLQGHDIP NDDKIPHPSK
SGPDTKSGPP GAGSHAPGAQ LKSIAKVPSD LEKHTGDIKD RVKEVFGGEG KEGQETSEKN
DLRAWAAEAN QAQADREGVS VAERQGIPTL HRQETLTEER SGLQTVIEGQ VISDEISGED
DEGSMEPPNS SPSTNTVVDK ETLSNGDTPT ISGSFVGYSE ATNVNSAQGA SATGKQRRRR
ATTRSSRREF SASDDILSVP EAEELLDCVQ GHLIIWPYDW LEKVEAGSNW LFPFDQISPI
EIYI
//
