ID A0A395HCR8_9EURO Unreviewed; 371 AA.
AC A0A395HCR8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=GAT-like domain-containing protein {ECO:0000313|EMBL:RAL05313.1};
GN ORFNames=BO80DRAFT_431270 {ECO:0000313|EMBL:RAL05313.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL05313.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL05313.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL05313.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
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; KZ824421; RAL05313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HCR8; -.
DR STRING; 1448316.A0A395HCR8; -.
DR VEuPathDB; FungiDB:BO80DRAFT_431270; -.
DR OrthoDB; 2148459at2759; -.
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:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:InterPro.
DR CDD; cd21383; GAT_GGA_Tom1-like; 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; IPR044836; TOL_plant.
DR PANTHER; PTHR45898:SF2; TARGET OF MYB PROTEIN 1; 1.
DR PANTHER; PTHR45898; TOM1-LIKE PROTEIN; 1.
DR Pfam; PF03127; GAT; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF89009; GAT-like domain; 1.
DR PROSITE; PS50909; GAT; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT DOMAIN 160..249
FT /note="GAT"
FT /evidence="ECO:0000259|PROSITE:PS50909"
FT REGION 248..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 40899 MW; 31FF691069E1D121 CRC64;
MAYQNGNEFV HLPGIVESAE SSPNAAREAA LRIRKLLSDP VRTPSNVQYN AIMLIRILID
NPGHTFSRNL DAKFVATVKD LLRQGKDANV HNFLRETLDA LEMQRSWDED LKLLLGMWSK
EKGKTSIRTT HSPGLTQPLV QPYRQTPNYF NVPNHNGSLP SPEELSARIS EAKTSAKLLI
QFVQSTPPAE MLENELIKEF SDRCRTASRA VQNYIHSTNP TPDEDTLVTL IETNDELSVA
LSKHQHALLQ ARRTQGQPGS QSPASSSQVS ASGSVQPAPP LPPAPPVPPR DTQSPLSSGS
STAPTVPRTY SNGAGRYEYR SEDFQVQNPF ADTSGTATPL LHGENSRGEG SSTDWWPEGQ
QQQQPRPVQH F
//