ID Q6BVG2_DEBHA Unreviewed; 1819 AA.
AC Q6BVG2;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN OrderedLocusNames=DEHA2C02926g {ECO:0000313|EMBL:CAG85847.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG85847.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG85847.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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};
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DR EMBL; CR382135; CAG85847.2; -; Genomic_DNA.
DR RefSeq; XP_457807.2; XM_457807.1.
DR STRING; 284592.Q6BVG2; -.
DR GeneID; 2900269; -.
DR KEGG; dha:DEHA2C02926g; -.
DR VEuPathDB; FungiDB:DEHA2C02926g; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_3_0_1; -.
DR InParanoid; Q6BVG2; -.
DR OMA; DSLWTKH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000000599; Chromosome C.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
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 InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
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 SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
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:UP000000599};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 803..830
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1113..1140
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1591..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1689..1704
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1819 AA; 208516 MW; 2E0AA2D0AD707A17 CRC64;
MLSGITSVSN EPSSTEENKY GMKYNSRRIS LPRFTSNDDV FDEDNTEETN DATNKENIPN
GNGVPPGLRE NEDPEEIYRI VSGGSKRGNE EQIEQTPIKP QKSRMANFND SPRIVGNSWS
FFNRNEDKQE LRYDNEDDEG RSTTPYTSQQ AKEDDQQPNG DIEPDLPSGD VESPGQISPQ
HIDESYREED TNQADVTQVS NEQAALPPQP TRGQSFTNFL PAKFGGRSNQ NTGAKRKFQF
FSRKNKNKDR ESRRGTTVPA PDEDEADRAT GERAQLLVGT LIIGSPAINL LASCLLEDEK
GISRSPLLLT LIGFKITDIS STINTKNRKF RIDLEYGVGP QRLKWSVERN AKDLLYLHSR
FKFDSWKKEV VRSKNSDLPK YPMPPLRTRG NNEQNRKKSG ANQINPGRSN QTSLDINDEM
AGVDGMLEAP ENDNASIATG RTFTDRLRAH LSNISSVSTE LQSPEQLRTK IVKNKDYINQ
VTNYLNELIK LVALKPQSNK IFQFFEISPI SSLLSYETGF LGKQGVVHIG GTAKSQGWRV
GHFKANDLKG MIDRRSEKWL LVRGSYVMYV ADINATSPLE VFLVDSKFRI HYHGDDDKSF
LSARYDEESD YDDSSLIHNV LGRSEDANSE DAHKNVFKHL NIVLENSERK LVLIPKSFKE
KKLWIKSLTD MKASTIWSEP HRFGSFAPIR TNCFAQWFVD GRDYFWAVSS ALEMAKDVIF
IHDWWLSPEL YLRRPANGNQ QWRIDRILQR KAQQGVKIFV IVYRNVGSTV STDSLYTKHS
LLSLNEDNIH VIRSPNQLLQ NTYFWAHHEK LCIIDQTVAF LGGIDLCYGR FDTPDHVLVD
DSKMDFNSLD SEFSVTPEEY IRFQTFPGKD YSNPRVKDFM ELDKPYESMY NRNEVPRMPW
HDVHMVTSGK VARDLSRHFV QRWNYLIRQK RPSRYTPLLT PPPDFSDEEA AEMGLDGTCE
VQLLRSSGNW SLGLKEHEQS IQNAYLKLIE TSEHFVYIEN QFFVTSCVID GNEIQNRIGD
ALVDRIIRAY NEGTNWRAII VIPLMPGFES QVDEPDGSSV RVIMQCQFMS ISRQPTSIFA
KLRKYGIDPD DYIQFFSLRK WGIIGPDRTL VTEQLYIHAK TMIVDDRAAI IGSANINERS
MRGSRDSEVA AVVRDTNTVK SRMNGEEYLA GKFAYSLRMR LMREHLGVSV DVLDIVERRF
NRFEEFAHTS QGLKARTSKF RNKENTILSA MVELASRDIL DEPNGTYRWQ NYQRVNQVDD
SIDQVPLDDV EEDEKGQNIP SPLSLPISFS NRTGTNEANK GIRDSKKHSY DARVQHNENH
KKDVFGDGPD KYKSKLAKRA RLNSARFLRE LASKAMEENP VGIFLPDSNV VKEFLESDDC
EMIDEMDEES ENIITERNRE RWQLLKKVSY LQRVAARTKD QTEDESKKRV AAGMELFSQD
PLPQNTKQEN KTVEPIDSID NPNQKIISSL DPSNYKSPAS TNEKKSFDPS SSSADYSDDI
PIVSLDEEGV RQTVQTVNSK GIENFSTFVD PYGFEDPLDE DFYEDMWYEH ARRNTELFRM
IFHTQPDDEV SSWKEYKNHS KLQRAFLLSQ QHEAKSRKQN KYFNGGQDDM SFSDSETDNN
TEYRKPDMNK RNSQATINVK KLEDVGLLGE VPSSSSSSSS SSASNMRNEP RSRFRRNNAK
SNTIPELDEN ESDTFEDAEE HMDYDEESDS RSPESENNQK HSAQNGSIPQ LNVNGETYKQ
NDVDDSPAPK KTRRGRKTFS ARRKAILGER IFERDTAERI LREIQGHLVI FPADWLMREL
EGGNWFYNTD RIPPIDIYD
//