ID A5DRD7_PICGU Unreviewed; 1735 AA.
AC A5DRD7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=PGUG_05838 {ECO:0000313|EMBL:EDK41740.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK41740.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK41740.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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};
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DR EMBL; CH408162; EDK41740.2; -; Genomic_DNA.
DR RefSeq; XP_001482075.1; XM_001482025.1.
DR SMR; A5DRD7; -.
DR STRING; 294746.A5DRD7; -.
DR GeneID; 5123926; -.
DR KEGG; pgu:PGUG_05838; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_3_0_1; -.
DR InParanoid; A5DRD7; -.
DR OMA; DSLWTKH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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:UP000001997}.
FT DOMAIN 757..784
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1067..1094
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1642
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1735 AA; 197405 MW; 0017BB4A0FA3F68E CRC64;
MTQSEDENID PRNTASEING QEHIEGDNKA EKISEKAGQG ATNEHHSDDE GGPLSGTTSP
GSPRSPKKER DSSFFPSSST IMANPWSLFG FKNADRQESR YNSESEEERD RMPFSDAEYE
QSGSPEEPEG TNDPPVPAKD YDTETNGDEL QRPRPSTGHQ RSSFAFIPSI LRNDSSMPSN
HQDTNEDKGR KRKFQFFSRK GKKDRDRKAS TAVPQDDADV ATGERAQSLI ASLIVGAPSI
NLVASCLLED ERGIARAPLL LSLLGFQIID ISPSVGTKNR RFSIDLEYGV GPQRLKWSVE
KNAKDLLYLH SRFKFGSWRT DGRKDLPRYP LPPLRFREND GKSKTGKTDG PMESIGHALH
QDANSHEDAP DADNGSTTTS RNHLSSITSL SRLRSHISGF SSDGSSEISP EQLHIRQARN
NEYIQQVTHY LNELIKVVGL KPSSNRLFQF FEVSPISSLL SYEGSVDGSH IGKQGVIHIG
GTAKSQGWRV GHFRANDLKG MIDRRSEKWL LVRNSYLMYV SDINSTLPLE VFLVDSHFKM
IYRGDDGQKL LARGDDEAEE DESDYDDSSL AQKAMATTAD TTANAKHKNV FNHLKITLYN
RERKLVLIPK SHKEQKMWVR AIKEMQNATV WSQPHRFDSF APVRNNCFAQ WFVDARDYFW
AISSALELAK DVIFIHDWWL SPELYLRRPA NGNQQWRIDR ILQRKAQQGV KIFVIVYRNV
GTTVATDSLY TKHSILSLHE DNIHVIRSPN QLLQNTYFWA HHEKLCVIDQ TVAFVGGIDL
CYGRYDTPDH VIIDDSKINF DTLDEQYPPT AEEFVKFQTF PGKDYSNPRV KDFFDLDKPY
ESMYDRDSVP RMPWHDVHMV TSGKVARDLA RHFVQRWNYL IRQKRPSRYT PLLLPPPDMS
DKEVEDLGLG GTCEVQLLRS SGNWSLGLKQ HEESIQNAYL KLIETSEHFV YIENQFFITS
CVVDGTFVQN RIGDALVDRI IKAHQQGQSW RAIIVIPLMP GFESQVDEPD GSAVRVIMQC
EYMSISQGST SIFAKLRRYG IDPDDYIQFF SLRKWGRIGP DRNLVTEQLY IHAKTMIVDD
RAVIIGSANI NERSMRGVRD SEVAAIVRDK EAVNSMMNGK PFKAAKFAHT LRMRLMREHL
GVSVDVVDII ERRFQKFESF AREPKGLEAA TNNFKNLEYK VMSAMVELAS RDIFGEKQGT
FRWKNFHGRQ KVQPQPESVS MDEENEAERE NDMPTPLSLP VSFNNRTGTK EANRGIRDKK
KHSYDARVQH SDNHKRDVYG KGPDKYKTRL ARRARFDSSR FLKDLAHKAI GKNPSKAFLP
PMEDVMEFLE SDDYDMSDEM DEDSEAMIHE RNKERLALLK KISYLQRVAA REKETQEEEQ
KKRAVAGLPV GTPEDGIKRS TNVSSADLIP NNSRGGEQGS ANGAERRDLE GDIPITSLDE
KDCRNLVSSL TSPNIEKFTT FVDPYGFSDP LDVGFYEDIW YEHARRNTEI FRMVFHPQPD
NRVTSWKDYK KFSKLQKAFV LAQQHESSRR RKQRPVNTDA SSENSDVQHS DAGSVSDASI
IKRDDGKRPT INFSKLNHDG GLLGDAPPSG DGSSAPNANG SKSKKKSLRR DKDDKPDPPA
MNEEIDDGDM TGGESENESD IYESSEEMFH NANETPDNDA SSFARRKKAP RLGAFARRRR
EVMGNRIFDR ETAERILNEI QGHLVVFPTE WLSRELDGGN WFYNTDRLPP IEIYD
//
