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Database: UniProt
Entry: A0A1L9UU47_ASPBC
LinkDB: A0A1L9UU47_ASPBC
Original site: A0A1L9UU47_ASPBC 
ID   A0A1L9UU47_ASPBC        Unreviewed;      1512 AA.
AC   A0A1L9UU47;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-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=ASPBRDRAFT_193782 {ECO:0000313|EMBL:OJJ75120.1};
OS   Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ75120.1, ECO:0000313|Proteomes:UP000184499};
RN   [1] {ECO:0000313|Proteomes:UP000184499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC   {ECO:0000313|Proteomes:UP000184499};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- SIMILARITY: Belongs to the SEC3 family.
CC       {ECO:0000256|ARBA:ARBA00006518}.
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DR   EMBL; KV878681; OJJ75120.1; -; Genomic_DNA.
DR   STRING; 767769.A0A1L9UU47; -.
DR   VEuPathDB; FungiDB:ASPBRDRAFT_193782; -.
DR   OMA; SFMRVFP; -.
DR   OrthoDB; 1547052at2759; -.
DR   Proteomes; UP000184499; 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};
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          95..196
FT                   /note="Exocyst complex component Sec3 PIP2-binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01313"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          218..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..250
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..321
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..676
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1512 AA;  167510 MW;  EB48FCB69384EF3C CRC64;
     MSSRDRMRGP PPGEMPPQRD PRRAGDSRNG GNAGPGDASM SRAEKFEDEK RRIIHSCFGK
     KDSDGSLVES YITHVRILED AAYPSTPAPP NSPPENKKPR VIIVAVRRSG RVRMHKAREN
     NDGSFSIGKT WMLDDLSSIQ SYNALVPSTP LEQQHKQWAA NVGFIVTVGK PYYWHARTSK
     EKDFFIGSLV KIYRKYTGGK VPTLIGFDDR ERQLLAGASA AGPPAPKGPP PGPPRPDVSL
     PPPRPPSSQG SRPQSPYSSR APSRDGPRRP PPSSSEEHAL RAQRSRDQMG RPSTGQSGKS
     GTPPFSPPQH PPPLPPDQRE QPPPRAAERL ATEPRVPKVP IISPPEPRNR DYPSSLQAAP
     VAGQRERPNG SFEEARSGSP LPDSRPPSSR DGRKGPESRP TLRTHDLHPS RSTDGLRPTT
     PGSVSGENHT FMHSPGSSVG PRSPLREAAE KPVATPARAE QQEPEPPSNS IKTPAVEVPA
     ALTPGSSGFS KAPPTVESAE APVPTAPTLP ISTKDPEPIE PLAETAAAAV PPPPSALEAA
     EPVEENDPDA HRPGLGPMIK KKQAKDVASA FRKAATAHGA FKPRPGGAGE RLLAAAKKQK
     AAADEPDGIT SVVPAPFLLR TNSENTVTSP ETPEAETPPV VSSSPEKEVQ PPAPLAPPAA
     PAAPAVQPPS EPPRIEPPAV EITQAAPVEP TMGLTEVLAG PRDTSRASVK VDTERSRSVS
     PSPHDRRRRR HEDNTIKYCQ ALGLDPTVLE GRGIDFDDIL TDLGWNGRLG DEKKIEDLEA
     DIRREIGRVE ATSWLGNLEQ QEGKIDQLAK LIDKTIVECE ELDNLLTLYS HELNTLNDDV
     AYIETQSQGL QVQTANQKLL QNELQNLLKT LSISSDDVRA LKESSLSNPD GLRDTELALS
     TLYKAMLMID SDIWHNKRRL ADAAGDHGSL GVYADTEIGQ MRAIKEKKEE YRTHARVFLQ
     RLKQFMAIAY KVAEQKRIDA AAHGQKDPLK LDSEARGYCR RELWQYHAVI LFAREVSSGE
     WHALINLYEQ QAKHPYQNDF RDNNLAWKKA ARKPSGEEQE LLFTHQEKEK ESEGITMAAR
     KLTVRRGKTI RAAAGLKLPS GDKQHGKLEP CEAFGGTLQE TLHMISEEQN FIVYFFHLNS
     LSTVDFPDLV MSGAPDERRI PSFNSKQLHD PDRAMAKKVE QIMDELFAFW PTDMQNLVDW
     AIRADPLQGI GILLAIEKAI SEFDDTNQDF IIHSLQKLHS RLLGLFNRFV DEQIRGIEET
     KVKVNKRKGV ISFMRVFPHF STAVENMLSQ EFYDIRVNVN EAYDRINRAM WESLKFIAKE
     APGQPTGAAA TSGDPEDKEI LNYHILLIEN MNHYIEEVDV RSLPVLERWR DRAHQDMQEH
     MKLYLDSIIH RPLGKLLEFI ESVENLVATG INPADIASRP SHSRSVAKKV LATYDAKEIR
     RGIEMLKKRV EKHFGDADDP GLSRSLVLKV LRECEGRYGE AYDRTRRVVD AVYEGQLELE
     WRKEDAIAMF QR
//
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