ID B9W9G0_CANDC Unreviewed; 1710 AA.
AC B9W9G0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN OrderedLocusNames=Cd36_10880 {ECO:0000313|CGD:CAL0000165106};
GN ORFNames=CD36_10880 {ECO:0000313|EMBL:CAX45442.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX45442.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX45442.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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 ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; FM992688; CAX45442.1; -; Genomic_DNA.
DR RefSeq; XP_002417730.1; XM_002417685.1.
DR GeneID; 8045278; -.
DR KEGG; cdu:CD36_10880; -.
DR CGD; CAL0000165106; Cd36_10880.
DR VEuPathDB; FungiDB:CD36_10880; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_3_2_1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000002605; Chromosome 1.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
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 InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376}.
FT DOMAIN 750..777
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1060..1087
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1710 AA; 196193 MW; 05D79634DB5DC2BC CRC64;
MSPTVEQPIS PLDENPLNGN DNKSKSKGFF GNEKEGDRHD LNEVQENGTI DSNDAIRQSS
DIDRIFRSVH NGPILPDHRS PSPNTRDDSS QVIGNPLSFY YSNDDKEYRY DTDRHQQQSH
TKGKHLEDEQ QNSNRFELVN DEDVDKYPSR KESSRPTHTR SATLSGFMQS RILGRSVSTN
QETSPTEPEF ANLHDALHPK EDTTKSGRLK KTLRRFNRRK TKDKRQSTMT AEFDELNDES
ENATMERAEK LLAGMSTGAP AINLMASCLL EDEHGITRAP LLLSVLGFRL TDVTPKETSR
NRRFRIDLEY GIDKHRMKWS IERNATDLAY LAYKLERTRI VSRVVGNKSQ PLPRLPIPPI
RKLDNKRSKK TKSVLSDSRV KDDHILAPDN NDNHSLSPVP SALSRVRSRL GSITSVGSLE
KYPELLELRR KKNVQFMKDV ENYLKELIEI TELKTSANIL FTFFELSPLS SLLSYESGYT
GKQGPVHIGG TAKAQGWRVG HFKVNDLKGI YERRVEKWML VRNSYVTYVS DINSTTPLDV
FLVDSDFKIS ARNLEIANRD DDDSLFDNSS VAQQQMHENE NKFFPHLKIT LENRERKLVM
SPKSQREHSL WIDSLRTMQN STIWSQNKRF DSFAPVRENC FAQWFVDARD YFWAVSTALE
MAKDTIMIHD WWLSPELYLR RPANGNQQYR IDRLLQRKAK EGVKIFVIIY RNVGSTVATD
SLYTKHSILS LDEENIHVIR SPNQLLQNTF FWAHHEKLCI VDHTYAFLGG IDLCYGRYDT
PDHALTDDSG VDFSNIAQDD RITAENFANF QVFVGKDYSN PRVKDFSELE KPYESMYNRN
IVPRMPWHDV HMYTCGQTAR DLARHFVQRW NYLIRQKRPS RLTPLLLPPS DLTEEEVLAH
GLDGTCEVQL LRSSGNWSLG LKEHEQSIQN AYLKLIETSE HFVYIENQFF VTACFIDGIE
IKNRIGDALV DRIIRAHREG TNWKAIIVIP LMPGFEAQVD EAEGSSVRVI MQCQYMSISR
GETSIFAKLR KKGIDPDQYI QFFSLRKWGR IGSNRTLVTE QLYIHAKTMI VDDRSVIIGS
ANINERSMRG VRDSEVAAVI RDKEMVKSKM NGKPYLAAKF AHTLRMRLMR EHLGVNIDIV
DVVERRFKRF ENFAASEEGK KFATNKFRNP ENRTLSAMVE IASRDILQQP EGTRRWKEFI
HVSKYDAEIA EVNFEEEDTT LPPPLFLPIS FNNRTGPFEA NKGVRDSKKH SYDNRVQNSE
SHKKDVYGEG LDKYKSKLAK RARVSSGKFL NELSLLAMET NPTGSFLPDF DSVRNFLESD
DCHMSGEMDD ESEDMIAERN KERWMLLKKI SYLQRLAARE KSMNDTENQR RAKLGLPVLS
KSDNAGDGSD SQGLPVSGTL PTSEGIDTDF SLDKEFPTVS LSESAARDII NNLTTPNAAV
SNFVDPYEFE DPIDPDFYEA RWNEFARRNT DIYRMVFHCQ PDDVVGRWSE YTHFTKLQSM
FMKAQDRDTD QGQLAENYSD EKAEVGDNQE PRRANNSRLE QVDEASEDEY GLLGKAPPER
GHENQNKSEQ ETNLRAKLSR RVSTFAGVAE NRDKHASDKT AHKSEGNIQG AEKTSTEGEE
SEESGTPTDK PSATAGTVPA SKTRKRARTY LARRKIQSGD VVYDKNSAER LLNAVQGHLV
YFPAEWLSVE LRNNNWFYNT DRLPPMEIYD
//
