ID A0A423VIC6_9PEZI Unreviewed; 415 AA.
AC A0A423VIC6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=VHS domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_09402 {ECO:0000313|EMBL:ROV90765.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV90765.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV90765.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV90765.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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 -!- 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:ROV90765.1}.
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; LKEA01000060; ROV90765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423VIC6; -.
DR STRING; 356882.A0A423VIC6; -.
DR Proteomes; UP000283895; Unassembled WGS sequence.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0016197; P:endosomal transport; IEA:UniProt.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR CDD; cd14235; GAT_GGA_fungi; 1.
DR CDD; cd16998; VHS_GGA_fungi; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR041198; GGA_N-GAT.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR47180; ADP-RIBOSYLATION FACTOR-BINDING PROTEIN GGA1-RELATED; 1.
DR PANTHER; PTHR47180:SF1; ADP-RIBOSYLATION FACTOR-BINDING PROTEIN GGA1-RELATED; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF18308; GGA_N-GAT; 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; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 4: Predicted;
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000283895};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 32..168
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 195..322
FT /note="GAT"
FT /evidence="ECO:0000259|PROSITE:PS50909"
FT REGION 355..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45965 MW; 555AB3717E7AB85F CRC64;
MEAASARAAA RDQWAGYGGH APSQLQRFIQ AACSPENYEP NLALNLEIAD LINSKKGSAP
REAATAIVNY INHRNPNMSL LAINLLDICV KNCGYPFHLQ ISTKEFLNEL VRRFPERPPM
RYSRVQLKIL EAIEEWRSTI CETSRYKEDL GFIRDMHRLL SYKGYTFPEV RRDDAAVLNP
SDNLKSAEEM EEEEREAQSA KLQELIRRGT PEDLQEANRL MKIMAGYDTR SKVDYRAKAA
EEVSKIQAKA KLLEERLEAF KPGDQMTDGD VFEELAAALQ SAQPKIQKMC EEESDDHEAV
ARLFEINDSI HRTVERYKLM KKGDHEGASK IARGEHVASK AAVKSAAQEL NLIDFDGEAN
GSGNGNSGPS GSNQSQSQSQ PQPGGLEDDL LGLSIGESEG STGGISLGFG NNSSE
//
