ID A0A135US11_9PEZI Unreviewed; 1821 AA.
AC A0A135US11;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=CSAL01_10789 {ECO:0000313|EMBL:KXH63194.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH63194.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH63194.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH63194.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH63194.1}.
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DR EMBL; JFFI01001107; KXH63194.1; -; Genomic_DNA.
DR STRING; 1209931.A0A135US11; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000070121; 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:UP000070121}.
FT DOMAIN 907..934
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1212..1239
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1821 AA; 204198 MW; 2653B459E1AAC16D CRC64;
MTDSRRDDSV SPMTRSPRAA SPAITRQPES LAPPAPPPKD GPPAPPPKDL PTPKDNHTPI
DSTVEARDYI NGGAPHDSVS PVNDGKRPQL LILNSTDSVR QTPGGLPVMP EDDTYSPEPA
SPTDRRSVQF ARTDQVLEAP ASHSRQPSWE DSGKSIGSAF ISKLKQLTGS GSMQTLKTSS
SGNLNDNGTP PSMGSSPTTG QFRSRIPHTL DEDGGSDADA DVEETADEGA TSDAVKPKKK
RRMRRSKKQN MSVPSTPNLR HLPGPDSPIG YGRMGLRRRM SMPDHPEQQH GMSEGEGRDQ
LAGPSWMRSH KVNGDGTESP GGRRMGHVRR ITVLGGGGVS DGDAITPKRP FFGTERASTW
KYVKNTLKLL RQKKEDRFDF AKSAELMAEL RAGAPAVLML ASMIQRDEHG NKRIPVLLEQ
VRLRITDSQP ESDDDSERHW VFTMDLEYGS GPSRMKWIII RTLKDIYNLH VRYKLAMSND
KYLHGRADVG ARPKMPKFPW GAFPYLRSAR NKDDSEDDDD ASIRGDDLGE VTAGEGTAAE
GTAGEGTASE WEGGRAGPGV RKKSRLGMLG MRRKSTGFTE PGDSGGENQA DQIQARKRYF
ERQRRVLEKY LQDMIRWLMF RADSNRLCKF LELSALGVRL AAEGSYHGKE CYLHIQSSKG
MDFRRVLTPK KVIARHSRKW FLVRSSYIVC VESPEKMSVY DVYLVDSKFR IVSKRSTLKQ
LSKGKTKAEE KEIDLAEEGD PEKHHTLTLH TAERKVKLFS RNQHIMKQFE DSIAEMLKQT
KWYDTNRFDS FSPVRNGVFA QWLVDGRDYM WNVSRAISMA RDVIYIHDWW LSPELYMRRP
AAISQKWRLD RLLQRKAREG VKIFIIVYRN VEAAIPIDSE YTKYSLLNLH PNIFVQRSPN
QFKKNQFFFA HHEKLCIVDH DVAFVGGIDL CFGRWDCPQH PITDDKPTGF EHSEQPKDAE
HCQLFPGKDY SNPRVQDFFK LDEPYEEMYD RSKVPRMPWH DIAMQVVGQP ARDLTRHFVQ
RWNYVKRGRK TTRPLPFLLP PPDVKMHELD ALGLTGTCEV QILRSAANWS LGIEHVECSI
QNAYVKMIED SDHFVYMENQ FFITSTEAFN TKIVNRIGDA LVQRIIRAHE NDEDWKACIV
IPLMPGFQNT VDEQEGTSVR LILQCQYRSI CRGEFSIFER LRAAGIEPEE YIQFYSLRQW
GKIGPRNALV TEQLYIHAKC IVVDDRVALI GSANINERSM LGSRDSELAA VVRDTDMIWS
TMAGRPYQVG RFAHTLRLRL MREHLGLDVD EILEEERQAD MDRQAEYEAE MDQIYDEDTE
SLPVAGPSAP QAANKPTKPA MHGQAASFNH DAAEADAAAE EASSVSSSDK GKDRDDRATG
NEAHDLEVAG FGKDHWKEAA QLGLDRGRDS IIINGREVLV NNVNSEGKGT LQSPMQPHER
KPSGDHHVEE EGGVSNDALP PIPALNRRTT DQLGLPRTAG LPTLPAVDDT DIGGPPVHLD
QHGQPTNGPV HPLAADIRQA HIDKDCMRDP VNSTFFDDIW NRIAENNTKL YRRVFRCMPD
SEVLTWPDYR EAVSYTERFR QSMEGQTKGN DGDPNLNRHQ TPVSGGGAGM GAPGPGAIAS
AVADKTEEKL HLKTNQSNHP RIVIPADDDH DLNDKSEQPG SRGGLNLNTD VEKAASSRRP
PDDPSPILPA GDVPFPAFEP GPAADANMLE PAREKSRERR TTFSPLEKPP SRDVNIPAQQ
AQGSVRRRRR ATTKGSRRGM PPEEVLGRAE AEELLSMIQG HIVNFPYDWL LTEEQNGNWG
FQVDGVAPLQ IYSERSHGPA G
//
