ID   W6Z8D2_COCMI            Unreviewed;      1060 AA.
AC   W6Z8D2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Exocyst complex component SEC5 {ECO:0000256|RuleBase:RU365069};
GN   ORFNames=COCMIDRAFT_93839 {ECO:0000313|EMBL:EUC46048.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC46048.1};
RN   [1] {ECO:0000313|EMBL:EUC46048.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC46048.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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; KI963972; EUC46048.1; -; Genomic_DNA.
DR   RefSeq; XP_007687416.1; XM_007689226.1.
DR   AlphaFoldDB; W6Z8D2; -.
DR   STRING; 930090.W6Z8D2; -.
DR   GeneID; 19128338; -.
DR   KEGG; bor:COCMIDRAFT_93839; -.
DR   eggNOG; KOG2347; Eukaryota.
DR   HOGENOM; CLU_011308_0_0_1; -.
DR   OrthoDB; 37589at2759; -.
DR   Proteomes; UP000054032; 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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365069}.
FT   DOMAIN          87..1035
FT                   /note="Exocyst complex component EXOC2/Sec5 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15469"
FT   REGION          30..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  118702 MW;  F8E07FC5C3229787 CRC64;
     MSSSIETEIL NKYNLTTLYP AVWPEEKDAA DEDEEYVEPA TKVTQKPVRR SQSRFSILEP
     SPRFSRQIPG AERSKDGVET LVQKDEQDPL GMYPSVVQVL RAKNVQVEDD IKLRNRFLLS
     STTFSPSLFL SQVHNEASTD ALLSGLDFLS RSIEKKSASL KVLVESNFDR FVGAKATIDR
     VYNEMRAQGK DQSESLSAPP QGRARSRSSF SGRKSSANLS SGMIDAVPAE KRKNALVKES
     EYGVQGIKVP LTEVAVKAEE VWGPALNGRE REETLKSILE SVEHHRGMFE VGSAIEEAIR
     HKDHETIVEE YKRARKYAEE ARYITEQATS AQTPLTDAEI HQVIVTARMW SDVERQIERF
     KRDSWKRLTA THFTNLQTGS EETKSDEYLG IISILLELGV EENPIWAWLI SRYEHLKLHI
     NSTCQRSVVE IEILRRHLVH GEKPSLRLLQ KHLRSVPTSS NISAEPSKLD TPKVIEFWEH
     VYALMNTLLS TKGGLLGELI EYWEIAQSFL SGRAQRNLPT GHHGQSSVHH RLSSENKAEL
     ERGTTELIGI LRDHLFSFFS DPPIEDVSLL FSPLPPTTPT PTTPGTPRSG ILSPTSATRS
     RFDLSKVPPP SPSRGETWEK YAFWPPHSNA LSGSHYLSKT LVLIGTAANE LASLQVPEPG
     GSGRVDESLR LLLGGVRERS VQAVCAAWNT DAEKLKVLED WTRHVDRKDV TNLPQRFLAV
     QSFLLNNLQK ILYVEASSKT KIDVVVPPSN KLLQMVRSQF VTSLYRTLSG MVECAERGRK
     ALGDEFEVKS DDLTIDEQED HTGNEWGRVD ANKKSIRLLL TLANMSAFQS EITPTLLNLF
     ETLFSVQLTD ETNRIRDVLS QLDSQLFRSY TKPHATKINS TIQSGIFSPA WAPPPGPTQK
     SVADRDPSPY VFSVLLDLVI VHTESSTTSA PLTPRILRSL FESTTASLIQ TFQSDNIPAI
     SLPQLMQATL DVEFMAQTLS AYTTEQASQI QTDIYQVLDQ KTDNAARVKL QDELGNLRTV
     LKRLREGTKV QFACFRRVKR ANTGQMAGPG GGGEEDRGRR
//