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Database: UniProt
Entry: Q6BVG2_DEBHA
LinkDB: Q6BVG2_DEBHA
Original site: Q6BVG2_DEBHA 
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
//
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