ID A0A167CEH2_9HYPO Unreviewed; 1043 AA.
AC A0A167CEH2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=Exocyst complex component SEC5 {ECO:0000256|RuleBase:RU365069};
GN ORFNames=BBO_05646 {ECO:0000313|EMBL:OAA41110.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA41110.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA41110.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41110.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA41110.1}.
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DR EMBL; AZHA01000017; OAA41110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167CEH2; -.
DR OrthoDB; 37589at2759; -.
DR Proteomes; UP000076863; 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 80..1014
FT /note="Exocyst complex component EXOC2/Sec5 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15469"
FT REGION 584..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 115405 MW; D3A12AC103A09540 CRC64;
MADFERTVLE FYQLPTSYPS EWPAEKDAED AATEGTDAWG NNRRLSSYQA LESAVNERRS
FLGGADGKGG MNSLVQRDEP DPLGFSDSVV RSLKNLGLPV QDDIRLRNRF LLSSTTFSPA
LFLSQMHSDA DTRNLLQGLD ALSASIDQKS ASLKVLVESN FERFVKAKAT IDNVYKEMKY
RGEDPQTKTH SRHASRSSFR NSGTKLAFNN QLAFSVSDSR KKNALTKESE YGVLGIKAPL
LDVSAKAEEV WGPALGGREK EEHLKDVSIY MSNFREYVDL SGVVADSIKR KDYESLVESY
NRARTFADQA RHLGKQLKGA TPDDAQLYQI LLAARMWHDV NRQVESFKTE IWKKLSSCSS
HSKPNAAAGR VQDQHIELIS LLLELGVKES PIWVWLISRY DHLKSKIQVT GDRQKTEIEV
LRRRLATGEK PTPKQAGMYL NGLGRQAMDR KPPVNDSAEV IELWEKMYTF LSNLISSQGI
MGEIVEFWSL AQGFIDGRTQ RTLPIGYNGE SQVHHELSGE RVSQLSQGAR ELVEQIREHI
YAFFAGLPPE DISILLSPLT PNPGSPASNS AGIAGSLSPT ALRDPRFNFD PSNPPPPSPS
RGEPWEKLAF WPPWSNSLSG VHYLSRMLAL VGSGASELAT ITPVAAAQGA NQELERLKLL
IGASRERCVT ALCAAWNRDA ENIKHVEDWQ RSTEGGDVTR MPASFAAFEG TLLTGMQKIL
YIADATTEQG APSIVMPPPP KLLQMVRSQY VTTLYKALSG MVENAERSLK ITDEDDWSQA
AAVYTSTSSA GKSTLDAGDR NVRMLLTLSN LQALRSQVVP GLNSQFENAF SVKLTDESKT
IKDVLGQIDA RLFQSYTKHS IEKLRDIIQT GLASPNWVCK PNQRPSAAKP YIYEALLTLV
LVHSQVSTTA PSLTPQVLSF LLEQTSLQLL ETFRTRPKYS LEALMQATLD VEFVAQTLSH
YTTDRASELQ SQIYQELDGR TDNDARARLQ GELPEMRNVL KKLRENSKNE FACFKKPKRA
AGAGATATKQ DGQSGAGSGT AAA
//