ID A0A316UNX9_9BASI Unreviewed; 909 AA.
AC A0A316UNX9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE RecName: Full=Exocyst complex component SEC5 {ECO:0000256|RuleBase:RU365069};
GN ORFNames=BDZ90DRAFT_240685 {ECO:0000313|EMBL:PWN27012.1};
OS Jaminaea rosea.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Jaminaea.
OX NCBI_TaxID=1569628 {ECO:0000313|EMBL:PWN27012.1, ECO:0000313|Proteomes:UP000245884};
RN [1] {ECO:0000313|EMBL:PWN27012.1, ECO:0000313|Proteomes:UP000245884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 5214 {ECO:0000313|EMBL:PWN27012.1,
RC ECO:0000313|Proteomes:UP000245884};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819669; PWN27012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UNX9; -.
DR STRING; 1569628.A0A316UNX9; -.
DR OrthoDB; 37589at2759; -.
DR Proteomes; UP000245884; 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:UP000245884};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365069}.
FT DOMAIN 48..867
FT /note="Exocyst complex component EXOC2/Sec5 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15469"
FT REGION 26..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 101196 MW; FC01164656659561 CRC64;
MAHLGLHVDE ATLLKEYRLE SLDPSSFQDI DHAEDSPATA GLGVNEEPDP LGLHQRITTR
NLPKDIRPHV TVSSKTFDPK LFLSTIHPDA TFADLTHGLN QLKDNIEQRS QALKVLVEDN
FDRFVAVKAT TDGVYREMKE SDGGPLQRES EYGVKDLKSI LAQASARADQ VFTPVLENNL
KAMKLRSTLG VFEKSKFFFN LPGSLAESVD AKRYDAALRD YNKGKYLLEN RPGQLLAFNT
GPASGDNNIT EKQRQQQQRL FKKVWDAVEA VMKDMERKLF ASLREPKRSV DEQEKTIEVL
LELSPREDPV AVFLESQHKH IHTLMRSSYQ SAETKVGNAR TMNDLLPRTD KDRARDIQSC
LRQIGRGDPN FERSFGAPAW RAIHHLVRMV SENLLQTLPS FWRVCKNQSE GKFSKSVSPG
IQSRARSWAS ESIDSYISLL SAFFTLTDVS ILGRQPLSPL PAWVPANSSS MTAAHYMHLI
LQDLAETANT LSALGIGGTP EALKTFVINA RFSFTEVLCN LWQGDAKLFY MLEDWTINPD
EQSTTLFLKD LSSFHRSNAR AAYHIASGRT RDPFDSSSRS RSTGADRDTG VSTEATSRIK
AAFLDSIYAF LDGIVHLAFS EYDPLDPTTS TSHKVVGNSR LTVDVQELDT RILLSVTNLS
HLSRIAIPTM AKQFQEVYHC KMSEDLATIE EVASQLDKIL FHDFLKRRSE ALNDVFRTGI
LHGGIDWARL PRPSEVHPFI YEALLALVQV HAQVQSVAKA LVSRTISSLL EGLTEVILQS
FKEVPRFGMG GMLQATLEIE FVHQTLSAFV SSKAEENLKA TYDVISTKYQ QGRGGKEDGA
ELQRELEGVK KTLLASRKMT ALEFLCFRKG SGSSSSSSGS KHRKDSGSKS GEARPASSAS
ATTSSSSRR
//