ID A0A395GLU0_9EURO Unreviewed; 400 AA.
AC A0A395GLU0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=VHS domain protein {ECO:0000313|EMBL:RAK94993.1};
GN ORFNames=BO80DRAFT_419940 {ECO:0000313|EMBL:RAK94993.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK94993.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK94993.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK94993.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC {ECO:0000256|ARBA:ARBA00011446}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; KZ824508; RAK94993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GLU0; -.
DR STRING; 1448316.A0A395GLU0; -.
DR VEuPathDB; FungiDB:BO80DRAFT_419940; -.
DR OrthoDB; 922060at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR CDD; cd14232; GAT_LSB5; 1.
DR CDD; cd16980; VHS_Lsb5; 1.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR044103; GAT_LSB5.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR045007; LSB5.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR47789; LAS SEVENTEEN-BINDING PROTEIN 5; 1.
DR PANTHER; PTHR47789:SF1; LAS SEVENTEEN-BINDING PROTEIN 5; 1.
DR Pfam; PF00790; VHS; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF89009; GAT-like domain; 1.
DR PROSITE; PS50179; VHS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT DOMAIN 18..142
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT REGION 153..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 44901 MW; EFAC28E1B5A1865A CRC64;
MFHSSKPYTA VTVQIEVLTS EQYEVEDSSG IVDLIEAIRI QGSGPTEASR ALRKKLKYGN
LHRQLRALTI LDFLIQNTGD RFLREFADEP LLERLRIAAT DPVSDPLVKE KCKQLFGQWA
ASYKNTPGME RVTGLYRQLP KRKQPAVQAK AKVLRDSGTS DEPAMGHTVS VSAGNGPATV
LTGPKHKHTS SKSSLSSFRK DKREKKTLSR SFNIDKEKPE ILQTLASSSV ASTNLLNALK
LVNRETHRVS EDAEVLNRFE TCKTLRRQIL RYIQHVESEE FLGSLIHANE ELVTALMAFE
VLDKSVDYDS DSDQDVLETG WTPDRDDLPE TFAGLVVNPR KPPRPPRPMS ISVPSSSSRR
VYSSSESESE DDDDEDNPFG DRNAIRTPGI ERHEPTWKEV
//
