ID A0A1L9VAJ2_ASPGL Unreviewed; 1036 AA.
AC A0A1L9VAJ2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=Exocyst complex component SEC5 {ECO:0000256|RuleBase:RU365069};
GN ORFNames=ASPGLDRAFT_133435 {ECO:0000313|EMBL:OJJ80948.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ80948.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
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 -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC {ECO:0000256|RuleBase:RU365069}.
CC -!- SUBUNIT: Component of the exocyst complex.
CC {ECO:0000256|RuleBase:RU365069}.
CC -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000256|ARBA:ARBA00010578,
CC ECO:0000256|RuleBase:RU365069}.
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DR EMBL; KV878908; OJJ80948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9VAJ2; -.
DR STRING; 1160497.A0A1L9VAJ2; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_133435; -.
DR OrthoDB; 37589at2759; -.
DR Proteomes; UP000184300; Unassembled WGS sequence.
DR GO; GO:0000145; C:exocyst; IEA:UniProtKB-UniRule.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR029175; EXOC2/Sec5.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR PANTHER; PTHR13043:SF1; EXOCYST COMPLEX COMPONENT 2; 1.
DR PANTHER; PTHR13043; EXOCYST COMPLEX COMPONENT SEC5; 1.
DR Pfam; PF15469; Sec5; 1.
PE 3: Inferred from homology;
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483, ECO:0000256|RuleBase:RU365069};
KW Protein transport {ECO:0000256|RuleBase:RU365069};
KW Reference proteome {ECO:0000313|Proteomes:UP000184300};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365069}.
FT DOMAIN 78..1023
FT /note="Exocyst complex component EXOC2/Sec5 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15469"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 114689 MW; 21DF1CB8A3075CF0 CRC64;
MNDTDIANHY GLPSEFPETW PAELDESDES DTESLRGDGA RSHKSRYFAL ERSGSQRKNL
GSQRGGNGKD SLAQKDEPDP LGSGDSVLKV LKKRGLPLDE ETRLRNRFLL SSTSFSPALF
LSQAHSNDSI QSLLDGLGYL SRSIDQKSAS LKVLVEANFE RFVRAKATID SVYTEMRNQG
APPQDDVPLA QIRRRSAHFR SSSLMMRGDS PAPTMLESSK NALTKESEYG MKGIRAPLVE
ASVKAEEVWG PALGGREREQ VLKSVVDTME RHRDVYEIGG QLSKAIKQRD YESVFELYTN
ARTLANNARN IAGMASSDGR SLTDEETHTI LAMGRMWMDV DQQIQAFTRD LWRRLGDAPT
TSTTATASGP VEEHMELIGA LLELGVEDNP IWIWLVNRYD FLKTKITSFC ERCKVELEIL
RRRLASGEIP SPQQVASYLR LAPREGSLDA QAMLDTDQVT ELWECIHTYL NRLLSPHGGV
LGEVLDFWEA AQSFIDGSKQ RMLPVGFEGE SRKHHRLSSE EALTLENGVV ELINLIRESV
LALFASPPTD DLSILATPIS PPSPSTPSFG VTPTESRFKL DPKNMPFPIP KRGEHWEDFA
FWPPFSNSLS GIHYLDKFLA IIGMAAGEMA ALGPVAHSGN TPDLLKSLVS TARERSVRVV
CAAWGKDAET CKMLEDWTRD PEKRDLTKMP GLFVAYESAI LGGMQKILYI PEAMAKPLQV
EVVTQPPAKL LQMVRMQFVS SVYKALSGLV ENAEHPAAPE EDNEWVLVGH ATSVNGPDVA
SSVLAADAVD AGNRNVRILL TLSNIKELQA VLVPQLISNF ETSFSVKLTD EAKTIRDALH
QIDDRLFQSY TNPTVETLKS TIFNGITAPD WEPSTNRPDQ VRPYVYNTML ALVLVHTEIS
TTIPSTSLSA SSRSSSGVPS PLMKTILTYL LSKLSSLLLS SFGARSEYTL AALMQATLDT
EFIAQTLSQY STDESSTVQS QIYVELDQRT THEARAKLQA ELGEMRGVLR NLRDRTKGEF
ACFRKPRTGT GLKSPQ
//
