ID E3RVE6_PYRTT Unreviewed; 1915 AA.
AC E3RVE6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=PTT_13137 {ECO:0000313|EMBL:EFQ90274.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ90274.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ90274.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL535264; EFQ90274.1; -; Genomic_DNA.
DR RefSeq; XP_003301601.1; XM_003301553.1.
DR STRING; 861557.E3RVE6; -.
DR EnsemblFungi; EFQ90274; EFQ90274; PTT_13137.
DR KEGG; pte:PTT_13137; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_0_1_1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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 InterPro; IPR001683; PX_dom.
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 SMART; SM00312; PX; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
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:UP000001067}.
FT DOMAIN 962..989
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1268..1295
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1696..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1696..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1915 AA; 214072 MW; B374DBB51DBE2A0D CRC64;
MAGSTHGDGP PAARSPRSRS PVTARGTEDS GRLLSPLRPG PKNETQDIYN PSPSDNAPRI
MRSAATGSPL SPKEPGEFPF HAPGNSNGGS YPTEQASEVP MRASKPSSHM SNASSSSYYP
PFAPVSRHPT EGELSDVPRE RKSVQFARSA PFTSEQPGGT SRQQSWEVDE GDGKGKERTQ
ASSLMGKLRA LASPSSHGRS MSAFAGGSSG PEGVSPHGQL SPTSEHDELR FEGHDSEADA
DGESSAGEGA LRRPRQKRRK SSRRWFDGEV EGTQTAPTTP KQTGFFSRDT RDSPNMTPTS
SRPGFLRRST MDDIPENERQ GYSEDEGRSR IAKESAWSRG LHSARGLSYG GLRRHDPNAD
EEGQQSRPTN LRSLTTFRGA AGDGQPSPWR MRSERTSSLS AQKWKSIKQS LKLLGNRQKA
ERQIDHAKSA ELMAELLAGA PAALFLASMF QRDEHGHKRI PVLLEQLKVT ITDTDRPGRK
EGDRHTALRI ELEYGSGLTR MKWVVYRSVA DFANLHLKFK VQEKQDAFRS RPSKREIKDK
NAKDGENDGE EEKEDPRTKL PRFPRSVLPY LRGLRGYGIL DDEEEEEEEE TAVGGAASGP
DGDASATERP ARAKRGKSSF LGRRQSSVSG SQAQGAVGVL AARQGSFAGT VNQPLQAKQN
HHERQRKKLE SYLRGLMTYL IFRPDSNRLC KFLELSALGV RLAAEGGYHG KEGYMMIKSS
KGVDNRKGWT KIALMNRHWP KWFLVRHSYV VCVDSPEEMN VYDVFLVDAD FTLESKSGRI
RDKKARDIAS EAKASATGHH QLKLVNAERK MKLLARNDRM LQQFEESINF MSQNTLWSQR
QRFDSFAPVR KKIYAQWLVD GRDYMWNVSR AISMARDVIY IHDWWLSPEL YLRRPAAISQ
KWRLDRLLQR KAQEGVKIFV IMYRNIGAAI PIDSEYSKFS LLDLHPNIFV QRSPNQIRQN
TFFWSHHEKI CVIDHTVAFC GGVDLCFGRW DTPQHVVVDD KPTGFELDDT PKDADHCQLW
PGKDYSNPRV QDFFALDKPY EEMYDRAKVP RMPWHDVGMQ IVGQPARDLT RHFVQRWNYL
LRQRKPSRPT PFLLPPPDFN PADIEALGLD GTCEVQILRS ACAWSLGTPN KVEHSIMNAY
VQMIATSEHF VYIENQFYIS SSEVLGTKIE NKINDAIVDR IKRAHANDED WRACIMLPLM
PGYQNTVDEQ EGSSVRLIMT CQYHSICRGE GSIFGRLRAA GIEPEDYIQF YALRSWGEVG
PNKMLVTEQL YIHAKIMVVD DRVAIIGSAN INERSMLGSR DSEIAAIIRD TELLDSYMGG
QPYKVGKFPH TLRMRLMREH LGIDVDCISE EEMISQMSDD ADSVGFHTES SGPGSPTAQR
ATEQKLEENN YRMQDELIEK AEKLHSFNHD FDWAQDQNPH LHNSKKPSAD TRVQNNPAHS
RDVRGEGPDH MLEVSQQRPE ISQGRDSYID EHGHEKLVTD IAAEGHAATP RKSGTLKTRK
RSGTTGTRHS TTSAQTDGTG YAGLPPPKLP RMDTTKLGLT QLSQLPALPI LDDTDIGGPP
ALQRSFSQGS SAAINPLLSE MRRPIVTEDC MRDPINDSFF LDTWHQIAEN NTKLFRQVFR
CMPDNEVRTW KEYQEYAAFS ERFTKSQGGD KGQMHKQQDA PGTTGPPGTG ITSKLTSTAG
NMGKQVGALG EKLSEKMTNN SDGHRGGAQG ENTHHSSMGG VEQWAEDQEQ RVQSSKLAPT
ATASRQNLHL DTASGSTLNE KLAPEPADDA VVSPMNPGLP EKTFTFPAPP PIPSDFASTD
FASHGPPQTS HSMRDRGRQV TISEPVAHPN QTGQAQGTTP NRSNTKRSRR RATTKSSNKT
FNATDADIML DKEDAKRLLE MVQGHIVLWP YDWLESEERG GGWLYNVDQI APLEI
//
