ID A0A553I637_9PEZI Unreviewed; 1409 AA.
AC A0A553I637;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 05-FEB-2025, entry version 19.
DE RecName: Full=Exocyst complex component Sec3 PIP2-binding N-terminal domain-containing protein {ECO:0000259|SMART:SM01313};
GN ORFNames=FHL15_003620 {ECO:0000313|EMBL:TRX95662.1};
OS Xylaria flabelliformis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=2512241 {ECO:0000313|EMBL:TRX95662.1, ECO:0000313|Proteomes:UP000319160};
RN [1] {ECO:0000313|Proteomes:UP000319160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G536 {ECO:0000313|Proteomes:UP000319160};
RA Mead M.E., Raja H.A., Steenwyk J.L., Knowles S.L., Oberlies N.H., Rokas A.;
RT "Draft genome sequence of the griseofulvin-producing fungus Xylaria
RT cubensis strain G536.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SEC3 family.
CC {ECO:0000256|ARBA:ARBA00006518}.
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:TRX95662.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VFLP01000015; TRX95662.1; -; Genomic_DNA.
DR STRING; 2512241.A0A553I637; -.
DR OrthoDB; 27109at2759; -.
DR Proteomes; UP000319160; Unassembled WGS sequence.
DR GO; GO:0000145; C:exocyst; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:TreeGrafter.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:TreeGrafter.
DR CDD; cd13315; PH_Sec3; 1.
DR FunFam; 2.30.29.90:FF:000003; Exocyst complex component Sec3; 1.
DR Gene3D; 2.30.29.90; -; 1.
DR InterPro; IPR028258; Sec3-PIP2_bind.
DR InterPro; IPR048628; Sec3_C.
DR InterPro; IPR019160; Sec3_CC.
DR PANTHER; PTHR16092:SF14; EXOCYST COMPLEX COMPONENT 1 ISOFORM X1; 1.
DR PANTHER; PTHR16092; SEC3/SYNTAXIN-RELATED; 1.
DR Pfam; PF15277; Sec3-PIP2_bind; 1.
DR Pfam; PF20654; Sec3_C-term; 1.
DR Pfam; PF09763; Sec3_CC; 1.
DR SMART; SM01313; Sec3-PIP2_bind; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Reference proteome {ECO:0000313|Proteomes:UP000319160};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 82..179
FT /note="Exocyst complex component Sec3 PIP2-binding N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01313"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 156187 MW; D56A0D1DBB8C5766 CRC64;
MEPPRPRAAG PGPGPGPGPG HGYGRDMSRA ERFEEEKRRI VESCFNKKDT DGSVIETYIT
HIRITEYASH PTSPPPPESR RESEKPRVII VSVRKSGRVR MHKSKENGNG SFSIGKTWDL
NDLTAIESFT APTTEPQQRQ WAGDTGFIVN LGKPYYWQAQ ADKEKKFFIA SLIKIYGKYT
GGGQPELKGF DPRELDQVLG SRKPPPMRQP APPNAAVPPR PDQTSTPPRP SPMPPRPDAK
GPAPSPRLDG LPPPRAPNRP PSRPGSRPAS RSRPEPKPLW TEASPAQPIP AAMPSPRPNQ
MPSTPPIRTL GPNGTSSPAP SLDLNRVPNQ PPALRRLASN NKSQDSLAAS ISTAKSDDAG
SIPPRSRGGM SGSGTLGKLG EPPDVPTSQF DLPDRRRPPM DPLRPQGPTD NDLVPAPLMS
QGARKEPPLR NNERANPQND SVASRPGTGS RTEKSEPTPE HVNETSTVTS AGLNGTPDAP
ASQSPVAQTP STDPPKEEEE TRPGLGPMIK AKSSQQKLAG ALWKAAAAAG AGSFKPRPGG
AGERLREAAK KTLVDEPDGI TSVVPAPPRP TPVPEAPKPV EPTQKPDAKL ESVPEVKVTL
PSSNQPTTLE AVAKEAQKKH REETRKEEET RRIAVIGNDT RYFSTLGVDI TLLADPATEF
ARWLDHFGWV PGNQMRTRNF DEMKLDIERE LNKAQAGGWV ARFQEEDERV DAIKKGLDVA
ITECDELDNL LTLYSVELSG QGLQVQASNQ KLLRNELESL LDICAITADD LQPLKVAPLE
NTSGLEEIEA ALVTLYKAMM KIDPSVTGSD SRKSEDASMN EQQASLNPDY GKMRIVQEKK
EMYLSESKAF LSRLGGFMSR QFDKSIQETK SAIAGALSKK VDPRNHDTGR DLLWQYSPLI
LYAREANLEE WDRYLHIYQE KHNPLYRSEF KDILDAWKRN ARKPAGEESE LLFTAQIEKQ
QEGTMATARR VTVKRSQTLA RSLGRPLGEG SKTSLEKMHD GRSHAYEIFA GIMDDLLPLV
EIEQNFIVDF FHATTLETAD FPDLVAAARP RDRQGGDLKR HRLMEPDREL ARRITRAMEA
IFLFLEQDLQ NLILWVLAQD PLQGVGILAV LERKQIAITS SNQDFLNNVL QKLNGNLESR
FSKFVEEQIR AIEDTKVKIK KRKGVISFMR VFPNFSAAVE NMLSTTDTAS SVRRAVDREY
ERIIKSMFDS LKVIARENPA TLTSSGADPE DKEALNYHIL LIENMNHFSE ELNTHGLEVL
EDWKEAAASE MAEHMNLYLN AVMRRPLGKL LEYLENLETQ IASGKTMTII AAQPSNSKAT
FNKVLSTYDG REVRKGIEAL RKRVEKHFGD ADDPSLSRDL VNRVMRECEK FYNEVEVRIS
TITTTVYGGD VLFEWPRADV KIAFSTTGR
//
