ID A0A1J9S365_9PEZI Unreviewed; 630 AA.
AC A0A1J9S365;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Exocyst complex protein EXO70 {ECO:0000256|RuleBase:RU365026};
GN ORFNames=BKCO1_2300069 {ECO:0000313|EMBL:OJD34444.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD34444.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD34444.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD34444.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the secretory pathway as part of the exocyst
CC complex which tethers secretory vesicles to the sites of exocytosis.
CC Also plays a role in the assembly of the exocyst.
CC {ECO:0000256|RuleBase:RU365026}.
CC -!- SUBCELLULAR LOCATION: Bud {ECO:0000256|RuleBase:RU365026}. Bud neck
CC {ECO:0000256|RuleBase:RU365026}.
CC -!- SIMILARITY: Belongs to the EXO70 family.
CC {ECO:0000256|ARBA:ARBA00006756, ECO:0000256|RuleBase:RU365026}.
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:OJD34444.1}.
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DR EMBL; MNUE01000023; OJD34444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9S365; -.
DR STRING; 236234.A0A1J9S365; -.
DR OrthoDB; 460764at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0000145; C:exocyst; IEA:InterPro.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1280.170; Exocyst complex component Exo70; 1.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR004140; Exo70.
DR InterPro; IPR046364; Exo70_C.
DR PANTHER; PTHR12542:SF41; EXOCYST COMPLEX COMPONENT 7; 1.
DR PANTHER; PTHR12542; EXOCYST COMPLEX PROTEIN EXO70; 1.
DR Pfam; PF03081; Exo70_C; 1.
DR Pfam; PF20669; Exo70_N; 1.
DR SUPFAM; SSF74788; Cullin repeat-like; 1.
PE 3: Inferred from homology;
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483, ECO:0000256|RuleBase:RU365026};
KW Protein transport {ECO:0000256|RuleBase:RU365026};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365026}.
FT DOMAIN 246..626
FT /note="Exocyst complex subunit Exo70 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03081"
SQ SEQUENCE 630 AA; 69760 MW; 98EAE2DCCE6887E9 CRC64;
MVGVKKAALA EESAEVEVLF ANMEKLKGLT KKIQGSLNRL ETSGKSVQEA IGPIYGNTQK
LQTTNSNVDR IIDAIDRIRQ PLDQRGREEQ IINAGPKKAG LGDFIASLDR TTQALGDLKY
SNLRSNQQAI AELNSLLKRG TKQLEDVFKE ILREDARPVE PLHYITKQLP FPTLPQEKMS
NLRTINSHMA ASAAQMAQAD ARETPSAKIY AEVRGEYITN TMRNLAAACI NTARKTTADA
IYRQGTNGIG TYASGLEGLF MAEYENICPI FAREDWARVY SQACQMALNE FAKTLRELNN
HVKSNLTTDC FLAYEIIDIV SNLSLRLEKQ TGELKRPIAD SVKPIRETAK VSLRTLMEEA
RNKVATLIAI PIDGGASNTT NEMMARLQQM TNYLDPLASI LISLGDGGWS TASASSSTTS
LSKSFDVGAD GRQLFAHYAM EMIETQLKEL DAKGRMLHKG KALQGVFIAN NVAIVERMIR
SSDLAILLAG AAKLVETWRK RATQMYLDAW KEPSGCLLDV QYTNRGGRPH SGGAGSVDSA
SVVKNLSSKD KDNVKEKWKS FNTSFDELIA KHRSYAMEKE VKAHLAREVQ TMIEPLYGRF
WDRYHEIDKG KGKYVKYDKS QLAATLAGLA
//
