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Database: UniProt
Entry: A0A1E3QQ47_9ASCO
LinkDB: A0A1E3QQ47_9ASCO
Original site: A0A1E3QQ47_9ASCO 
ID   A0A1E3QQ47_9ASCO        Unreviewed;      1369 AA.
AC   A0A1E3QQ47;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Exocyst complex component Sec3 PIP2-binding N-terminal domain-containing protein {ECO:0000259|SMART:SM01313};
GN   ORFNames=BABINDRAFT_161511 {ECO:0000313|EMBL:ODQ79823.1};
OS   Babjeviella inositovora NRRL Y-12698.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX   NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ79823.1, ECO:0000313|Proteomes:UP000094336};
RN   [1] {ECO:0000313|Proteomes:UP000094336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SEC3 family.
CC       {ECO:0000256|ARBA:ARBA00006518}.
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DR   EMBL; KV454431; ODQ79823.1; -; Genomic_DNA.
DR   RefSeq; XP_018985151.1; XM_019128847.1.
DR   STRING; 984486.A0A1E3QQ47; -.
DR   GeneID; 30146700; -.
DR   OrthoDB; 1547052at2759; -.
DR   Proteomes; UP000094336; Unassembled WGS sequence.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   CDD; cd13315; PH_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, ECO:0000256|SAM:Coils};
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094336};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          96..181
FT                   /note="Exocyst complex component Sec3 PIP2-binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01313"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          729..780
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        280..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1369 AA;  153719 MW;  FC354B28050E6119 CRC64;
     MLSPSQMSRR LKGIGKKSSP SSPIQNLLLN ESPTLNQAPS ADLARQYETD KASLIKYCFS
     GRDGLGNLHE SYITHVRIIE DSHYPYDVPP ATSAAKNKKQ RVLVLGVKKS GRVHIHKGRQ
     NDDGTFQIGR TWDLEELKQI TKLDSFSGFQ MTIGKTYYWE TNSPLERMVF CKTIIQNYMK
     YTGGRIPELK GWDLATFHLE TLRPGTAEKS VDKGKYVVLG STAPVREPTV RRAKEEVQLK
     KKPTQPGSPK TPGALYGGID FTVNGTLPMK PMVEMIVDRT PGRVETDVKQ RSKSERSTLD
     GKSRSMLDAG KPRSMLDAGK PRSMLDAGKP ERGMVTGNTG RSLFGLNERP DPRTSRSMLD
     PGEPGRVSAP SIDKLGNTSG ALINSSLASQ LLRRASPSYP ERNAARLQSK ESTTPTSVSL
     HLRESAPNHP FRGLSATSSP VYTRGNAVID KENETSYYEP HSFMEEKALN LRREIGVLEP
     AIEVNPISFK TVAPVSMEPA LDNSFGGLLP TLSEKEMIER EIMELLPGSD TEEISRPDPK
     PVYGEPVPGF GKEPKEVLNG KGLHASLNNA SAPLNEDFDL NASLDNDDYS KTSLSTKELP
     PLGKDVDLNS AEDGDLQASL QGGALGNGTL GVTSEALDVP QNSLALEEYQ PDTNNELEDI
     LDMVNWNMND SSDELIKKLQ NQINSMKYHS ANDLLGMNLD LKKLDNYVDL VIGEVDNLGA
     YFKNFQIDLK MIEHDIHAIE NESQGLQVET INKKVLYAEL KEILEKVTIK EQDMKVLQRA
     DFAHELQDIE LTLVAFYSAL QTVVFSKEKL DLSDMKALKQ HRETFEGITR DFSQSVKLFL
     EGRIKSLVKR ITSHENAITI ADLLSYFSRL LKYSAILLFV KEIAPEVYSA LLAYFETSIA
     PFYNALLGEK IAWIQTSMDM SVKDIPVTVE ASRTKSIKFN ENKLKEKLGL AEVSHFSGSK
     RVSAVPSTAK VGTDPTSTII AFIEEFRDLI ITQQDFQLKF FHLSSASGEY PEYIEDNPID
     RRKEMLDRPF FLIEANRQFA ATLFNSMNNL FNEHMHTFLK IASPPVSSLP ALLLTTERIQ
     KKYEQTNQEF LSKFLYRLAE KFKITWLKAV NEKMKGLAKV TFGKRSGVSP IIKEFLQFVD
     STEHALMSVL SLDPAASSDS PTRAMLDHSY LELGESIKNA LVKANPSQDT HHSNKERTHA
     MINMIINLNY LVDESGTHDN ESLLTMQSEF NQLLQRETVE YIDSIMAIPF GKLIEFVESI
     ESLTKDSIAI NLSKSSVYNK AATKKLLASF DLKELRLKIE MLHKKLEKHF IVENSEFENR
     VRDRIWLSLQ NQCISTFKRL NFILSRYYGE VEYGVSKEAI ISEFRVYTK
//
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