ID A0A0D2J043_9EURO Unreviewed; 1841 AA.
AC A0A0D2J043;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 44.
DE RecName: Full=Phospholipase D1 {ECO:0000256|ARBA:ARBA00074658};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE AltName: Full=Choline phosphatase 1 {ECO:0000256|ARBA:ARBA00042228};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1 {ECO:0000256|ARBA:ARBA00079280};
GN ORFNames=Z520_01207 {ECO:0000313|EMBL:KIY02742.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY02742.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY02742.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY02742.1,
RC ECO:0000313|Proteomes:UP000053411};
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 Fonsecaea multimorphosa CBS 102226.";
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; KN848063; KIY02742.1; -; Genomic_DNA.
DR RefSeq; XP_016636864.1; XM_016771725.1.
DR STRING; 1442371.A0A0D2J043; -.
DR GeneID; 27706953; -.
DR VEuPathDB; FungiDB:Z520_01207; -.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000053411; 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-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
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 FunFam; 3.30.870.10:FF:000011; Phospholipase; 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 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:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 475..665
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 929..956
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1235..1262
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..580
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1841 AA; 206285 MW; 660BD1AC2E948D23 CRC64;
MAETDETKQH PVALGAATDQ ERLSARGAQL QPAFQPAFKA TGEPGPALLS NSRSTNTSAG
GPTPSGSTPR DASPDKLTPF STTSRASSAL KKTYGSGSNL ARSATNEHSV SGREPADLEN
AVQSNGTPTV GRKSVQFSRD TQEISPHSNG HTTPPAGRAD GSEQDKPHSL YARLRALAIP
QGYSFSHARS PSGLSASGRS VEGKDVDNQP STQSGRNEIG LAATLEEDSG AEADADAEES
SAAENSTSQW ASRKRRRKIQ RFDDIETAPS SPHSLMRPGF ASAPINSDTD IERPRALVRR
ATDTDMINSP QGVSEDEGRK QLTNGTGWTP RHPLRGLSYG GQRKPGDTTP EGPRRPLTLL
NFANITSSRE AGSSEAQTPK TPSRRKQLAE RSSTLSAAKW RQLKNTLKTF GQGRKKPPTP
EIQRSAALLA ELAAGAPAAL MLASMFQRDE HNHRRVPVLL EQLKVQVTDS EVDQHKSKDD
KAIKETDEDK VLRHLIFKIE CEYGNGANRM KWVIKRSLGD FSKMHIRYKT AYNAGRLRLK
SDGRKKMPKF PLEVFPYLKS LRLFADEGDD EEADACDDTD PGTATDTERP TPRSQTRSAI
TPKRRKSSVA GFNDPVTPGS TRREMFAERQ RKTLEKYLQA MIQFMLFRPE SNRLCRFLEI
SALGVRLAAE GSEHGKEGLL LIRSAKGLDF RALNALEFKK RHTPKWFLVR HSYVVCVDSA
EQMHIYDVFL FDSDFKIQSR RSRKSDQRSA KELAEAAKES AKHPQHHRLK LVNSERKLKL
ISNNERQLQQ FEESIREMVA GSPWAKINRF ESFAPVRPNC FAQWLVDGRD HMWVVSRALN
QAKDVIYIHD WWLSPELYMR RPPAISQKWR LDRLLKRKAE EGVKIFVIVY RNIDAAIPID
SQYTKFSLLD LHPNIFVQRS PNQFRQNTFF WAHHEKICIV DHTVAFVGGI DLCFGRWDTP
QHTLVDDKPT GFEPSDEPKD ADHCQLWPGK DYSNPRIQDF YALNKPYEEM YDRSRVARMP
WHDISMQVVG QPARDLTRHF VQRWNYILRQ RKPTRPTPFL LPPPDFNPAD LEALGLDGTC
EVQICRSAGP WSLGTPDKTE HSIMNAYIKL IEESEHFVYI ENQFFISSCE TEGATVHNKI
GDALVERITR ASKHQEAWKA VVIIPLIPGF QNTVEEEGGT SVRLIMQYQY RSICRGESSI
FGRLKAVGID PEEYIQFYSL RQWGRIGPRK TLVTEQLYIH AKCMVVDDRV ALIGSANINE
RSMLGNRDSE CAAIVRDTDM VWSWMNGKPY QVGRFPHTLR MRLMREHLGL DVDKIMEDAQ
VMEAEHNKMR SSGKSVRSES PDDAFGSPLS EAGDVLSPLQ GQDTELHEEL LQRTEEFRSF
NHDVDWEQQG NPNLKSKRAG VTQDPRVTGD PHHKEDVEGH GYDRMAEIAA EGLGDGRDST
LVKGTKEVLL SMIDPEGKAA LEEPRKHGEQ LRMPSYVVKM ETPNPPLPPK PGLRRMDTVQ
LGLPMLSQLP PLPAGDDSDI GGPTLVKVSS KDSMGPRHPL MDELRRPLVD RDSMTDPIHD
AFLYDTWHAV AENNTKIYRT VFRCMPDNQV RNWDEYHQYV AYEQRFNQLQ GNDLPKEDKV
SDPSRAGSVA KSGPPGAGSR HPAAEIKAVT HVPTDIEKAT ADVKEKIKNV LGEKSAHSHE
DAEKAKLRRW AAETNQAQAE RLGMPTLHRQ ETLTEEKSGL QTVPEGQTIV DEGSGTGEDD
DFSTERPISS LSSTAAEKEK SASNGTPSTA NGHFVGYSDA VNQNAAQSTA NIAGSGRRRR
RATTRSSRRD FSASDDILTI EEAEELLGCV QGHLVVWPYD W
//
