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}.
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; 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
//