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Database: UniProt
Entry: A2Q862_ASPNC
LinkDB: A2Q862_ASPNC
Original site: A2Q862_ASPNC 
ID   A2Q862_ASPNC            Unreviewed;      1507 AA.
AC   A2Q862;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Contig An01c0080, genomic contig {ECO:0000313|EMBL:CAK43685.1};
GN   ORFNames=An01g03190 {ECO:0000313|EMBL:CAK43685.1};
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK43685.1, ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43685.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC   {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- SIMILARITY: Belongs to the SEC3 family.
CC       {ECO:0000256|ARBA:ARBA00006518}.
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DR   EMBL; AM269955; CAK43685.1; -; Genomic_DNA.
DR   EnsemblFungi; CAK43685; CAK43685; An01g03190.
DR   VEuPathDB; FungiDB:An01g03190; -.
DR   HOGENOM; CLU_002075_1_0_1; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IMP:AspGD.
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; 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:UP000006706};
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          216..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..729
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        271..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..322
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..672
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..729
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1507 AA;  167150 MW;  515A7A71D9E60A38 CRC64;
     MSSRDRMRGP PPGEMPPQRD PRRAGDSRNG GNAGPGDASM SRAEKFEDEK RRIIHSCFGK
     KDSDGSLVES YITHVRILED AAYPSTPAPP NSPPENKKPR VIIVAVRRSG RVRMHKAREN
     NDGSFSIGKT WMLDDLSCIQ SYNALVPSTP LEQQHKQWAA NVGFIVTVGK PYYWHARTSK
     EKDFFIGSLV KIYRKYTGGK VPTLIGFDDR ERQLLAGGSA AGPPAPKGPP PSGPPRPEVA
     LPPPRPSSSQ GSRPQSPYSS RAPSRDGPRR PPPAPSEEHV LRAQRSRDQM GRPSTGQSGK
     SGTPPFSPPQ HPPPLPPDQR EQPPPRAAER LATEPRVPKV PIISPPEPRN RDYPSSLQAA
     PVAGQRERPN GSFEEARSGS PLPDSRPPSS RDGRKGPESR PTLRTHDLHP SRSTDGLRPT
     TPGSVSGENH TFMHSPGSSV GPRSPLREAA EKPIGSPARA ARQEPEPPSN PINTPAVEVP
     AALTPGSSAF SKAPPAVESA EAPVPTAPTL SILTKDPEPI EPIAETAAAA VPPPPSDLEA
     TEPVEENDPD AHRPGLGPMI KKKQVKDVAG AFRKAATAHG AFKPRPGGAG ERLLAAAKKQ
     KAAADEPDGI TSVVPAPFLL RTNSENTVTS PETPEAETPP VVSSSPEKEV QPPAPPAPPA
     VQPPPEPPRI EPPAVEVTQA APVEPTIGST EVLAEPRDTS RASVKVDTER SRSVSPSPHD
     RRRRRHEDNT IKYCQALGLN PTVLEGRGID FDDILTDLGW NGRLGDEKKI EDLEADIRRE
     IGRVETTSWL GNLEQQEGKI DQLAKLIDKT VVECEELDNL LTLYSHELNT LHDDVAYIET
     QSQGLQVQTA NQKLLQNELQ NLLRTLSISS DDVRALKESS LSNPDGLRDT ELALSTLYKA
     MLMIDSDIWH NKRRLADAAG DHGSLGVYAD TEIGQMRAIK EKKEEYRTHA RVFLQRLKQF
     MAIAYKVAEQ KRIDAAANGQ KDPLKLDSEA RGYCRRELWQ YNAVILFARE VSSGEWHALI
     NLYEQQAKHP YQNDFRDNNL AWKKAARKPS GEEQELLFTH QEKEKESEGI TMAARKLTVR
     RGKTIRAAAG LRLPSGDKQH GKLEPCEAFG GTLQETLHMI SEEQNFIVYF FHLNSLSTVD
     FPDLVMSGAP DERRIPSFGS KQLHDPDRAM AKKVEQIMDE LFAFWPTDMQ NLVDWAIRAD
     PLQGIGILLA IEKAISEYDD TNQDFIIHSL QKLHSRLLGL FNRFVDDQIR GIEETKVKVN
     KRKGVISFMR VFPHFSTAVE NMLSQEFYDI RVNVNEAYDR INRAMWESLK FIAKEAPGQP
     TGAAATSGDP EDKEILNYHI LLIENMNHYI EEVDVRSLPV LERWRDRAHQ DMQEHLKLYL
     DSIIHRPLGK LLEFIESVEN LVATGINPAD IASRPSHSRS VAKKVLATYD AKEIRRGIEM
     LKKRVEKHFG DADDPGLSRS LVLKVLRECE GRYGEAYNRT RRVIDAVYEG QLELEWRKED
     AIAMFQR
//
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