ID V9DL07_9EURO Unreviewed; 1858 AA.
AC V9DL07;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=G647_10388 {ECO:0000313|EMBL:ETI26627.1};
OS Cladophialophora carrionii CBS 160.54.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI26627.1, ECO:0000313|Proteomes:UP000030678};
RN [1] {ECO:0000313|EMBL:ETI26627.1, ECO:0000313|Proteomes:UP000030678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI26627.1,
RC ECO:0000313|Proteomes:UP000030678};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL Submitted (MAR-2013) 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; KB822702; ETI26627.1; -; Genomic_DNA.
DR RefSeq; XP_008724601.1; XM_008726379.1.
DR GeneID; 19988881; -.
DR VEuPathDB; FungiDB:G647_10388; -.
DR HOGENOM; CLU_000690_0_0_1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000030678; 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}.
FT DOMAIN 469..660
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 924..951
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1230..1257
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1662..1681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1858 AA; 208188 MW; BB0BEDDA700F7C49 CRC64;
MAEAIGRIQA GAGLPAEKAN DKRNGVAMKT TPSYRNGTVN GEPGPAVTTN ERPTYPSASS
PTPPATSPRD VSPDILTAFS TSSRTNSAVR NPYGSGSNLV RSATNEPTLG GKELGGTDTA
LHGTGTPTAG RKSVQFSRDT EEIGSQNNPQ ATPNDGSEHE KPHSLYARLR ALAIPQGYSF
SHTRSPSGLS ASARSAEGKD LDSQFVVPGR HETGLSATLE EDSGAEADAD ADESSAAENY
TSRATARRRR RKLQRFDDIE TAPSSPHSPI RTGFASAPTN SDSERPRVLT RRATDTDMVS
FPQGVSEDEG RKQLSKDTSW KPRHPLRGLS YGGSQRRTGD TTPEGSQRRP LTLLSFANIG
SSREGASSAE QTPKTPSRRK LLAERSSTLG AAKWSQLKNS IRTLGQRKKK VPTPENVRSA
ALLAELAAGA PAALMLASMF QRDERNQRRV PVLLEQLKVQ IVDSEVDHNK IRDDKALKES
DEDRVLRHLI FKIECEYGNG ANRMKWVIKR SLGDFSRLHI KYKGAYNAGR LRLRSDGRKK
LPHFPLDVFP YLKSLRLFAD EPEVNDEPDA GYETEPGTAT DTERPTPQSQ TRPAVTPNRR
KSSIAGLPDP TTAAGTRREA FAERQRKSLE RYLREMIQFL LFRPESNRLC RFLEISALGM
RLAAEGSEHG KEGLLLIRSA KGLDFRALNA GEFKKRHSPK WFLVRHSYVV CVDSAEQMHI
YDVFLFDSDF QIQPRRLRST EQRSAKELAS LAKESAKHPQ HHRLKLINSE RKLKLLSDNE
RQLQQFEDSI RELVAASPWA KVNRFDSFAP VRPNCFAQWL VDGRDHMWVV SRALNQAKDV
IYIHDWWLSP ELYMRRPPAI SQKWRLDRLL KRKAEEGVKI FVIVYRNIDA AIPIDSQYTK
FSLLDLHPNV FVQRSPNQFR QNTFFWAHHE KVCIVDHTVA FVGGIDLCFG RWDTPQHTLI
DDKPTGFEPS EEPRDADHCQ LWPGKDYSNP RIQDFYALNK PYEEMYDRQR VARMPWHDIS
MQVVGQPARD LTRHFVQRWN YILRQRKPTR PTPFLLPPPD FNPADLEALG LDGTCEVQIC
RSAGPWSLGT PDKTEHSIMN AYIKMIEESE HFVYIENQFF ISSCETESTV VHNKIGDALV
ERITRASKND EAWKAVVVIP LIPGFQNTVE EEGGTSVRLI MQYQYRSICR GESSIFGRLK
AVGINPEDYI QFYALRQWGR IGPRKTLVTE QLYIHAKCMV VDDRVAIIGS ANINERSMLG
NRDSECAAVV RDTDMVWSRM NGKPYQVGRF PHTLRMRLMR EHLGLDVDKI MEEAQVMEAD
RHKTHSSGKS LRSESPDDTF HSPSSEADDV LGPLDDGRGA ESHEDVLQRV EEFRSFNHDV
DWEQEGNPNL KSKRAGVTQD PRVTGDPHHK DDVKGFGHDR MAAITAVGLG NGRDTTIVRG
NKEVLVSDLD SEGRATLTEP RRRGEHARLT SYVAKMEMPN PPLPPKPTLE RMSTHQLGLP
MISQLPPLPA SDDSDIGGPV LAKATSKDSV RAHHPLINEL RRPLIDRDCM VDPVHDAFFF
DTWHTVAENN TKIYRSVFRC MPDNQVRNWE DYHQYLAYEQ RFNQLQGNDM PAEQKVTDPS
RGGEVSSGPP GVGARYPVAE IKAVAHVPSD IEKRTNEIKG KLKNALGERS KDEKTDPEKE
KLRIWAAEAN RAQAEKEGKP NLHRQETLAT ERAGLQTVPE GQTIADEGSA TGDDDEVSTD
PPNSSPSSTA AEKEKSTING TPPTATGPFV GYSEGVNQNA TQTTANSGGG SRRRRRATTR
SSRGNFSASD DLLSIEEAEE LLGCVQGHLV VWPYDWLEKV EAGGNWLFPF DQISPIEI
//
