GenomeNet

Database: UniProt
Entry: A0A194VXJ9_9PEZI
LinkDB: A0A194VXJ9_9PEZI
Original site: A0A194VXJ9_9PEZI 
ID   A0A194VXJ9_9PEZI        Unreviewed;       636 AA.
AC   A0A194VXJ9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Exocyst complex protein EXO70 {ECO:0000256|RuleBase:RU365026};
GN   ORFNames=VM1G_04257 {ECO:0000313|EMBL:KUI68732.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI68732.1};
RN   [1] {ECO:0000313|EMBL:KUI68732.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI68732.1};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM003101; KUI68732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VXJ9; -.
DR   OrthoDB; 460764at2759; -.
DR   Proteomes; UP000078559; Chromosome 4.
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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365026}.
FT   DOMAIN          249..632
FT                   /note="Exocyst complex subunit Exo70 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03081"
SQ   SEQUENCE   636 AA;  70647 MW;  13A1AB2CD5FBFAB9 CRC64;
     MVTGLSSRHA AEEEARAEVD VLKSHLEKRA GLTKKIEAQL SRVQGTGRRL NEAVAPLNGE
     TKQLQILCNN IDGVLSAIGR LRQQSDSKND EEQVMRMGPE KAGLSHYLTS LKRLNKALVE
     MKASNLRSTQ QTTADLQRLI KSGNTQLENY FDKLIRTETP RSIEPLHFIT KQQPFPVLSQ
     DKNTRLGLLN SYISGAHRES GVMQESPTVK MYAEVRGPYL SATLVNLAQA SVNTAKRKDA
     TSIYRAGTSG ISTYAQAMEG LFIAEYETIC RIFTREDWGP VFQSTCQAPL AELARTLREL
     NVHIRQHLNT DCFLAYEIVE VMSSLSNNLE TKTGELKASF AAALKPVKET AKSSLAELLE
     TMRTNVNGLQ TLPPNGAPIP IVSEIMQRLQ AMVDFMRPMS IIMVSLGDGG WRSSSAAASG
     AGDSVPNLAS FDIGADGKEI FANYCADTIE ALFSALDARA RMIYGRKPVV GVFMANSIAI
     TERMIRDSDL APLLEQKLPV IIDTWRKKAN ATYTDVCKDV SIHLLDVIHT SRANRPTSGQ
     GVVDSASIMK GLSSKDREKI KDKFQAFNAS FDDMVTKHKQ YSMEPEVRRM FAKAVQQTVE
     PLYNRFWDRY HEIDKGKGKY AKYDKSSIAA VFHTLY
//
DBGET integrated database retrieval system