ID A0A165YHF4_9AGAM Unreviewed; 488 AA.
AC A0A165YHF4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=VHS-domain-containing protein {ECO:0000313|EMBL:KZP09562.1};
GN ORFNames=FIBSPDRAFT_802010 {ECO:0000313|EMBL:KZP09562.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP09562.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP09562.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP09562.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV417697; KZP09562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165YHF4; -.
DR STRING; 436010.A0A165YHF4; -.
DR OrthoDB; 460229at2759; -.
DR Proteomes; UP000076532; 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; 1.20.58.160; -; 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; 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; 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:UP000076532};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 21..157
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 183..313
FT /note="GAT"
FT /evidence="ECO:0000259|PROSITE:PS50909"
FT REGION 345..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 53196 MW; 55CFCE900C2A0F13 CRC64;
MMLGRAYNER MSQVHILIVR ACEPTTLQPN YALQMEVAEH INSKKANTPR EAAMLLARYA
NDRNPNVGIF ALSLLDTIVK TCGYPFHLQI STKEFLNELV RRFPERPPPF PGPVMSRILD
LIHTWREGIC VHSRWKDDLA NIRDMHRLLT FKGYRFRSAP STDVTLEEAA NLKSADELES
EDRDAQSAKL QELIRRGTPR DLAAAQELMK SLAGANPEAK PDYRSQALTD LNKLEQKVIL
LNEMLDNADT ERGERFTTGD AYDQLSTILR NARPKIQKWI SDAESDDSES LDTFLQINDQ
INTVLNRYEA FKKGDYSFSS NPIPAELAVG NSSAGGVSLI DFDDGAPSAN ESAPSNPIDE
LANLFGSTPT AAQSSPPPIN PSTRPPAIST SPAAPQQLGS IMLPGTPKPG GSSETSRVAS
PNYFGQGNGN GTHQQHTVGR GTMGMGMGMG MGMGTAVSPA AQRQPQQTST ATPPAQSKDP
FADLAGLF
//
