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Database: UniProt
Entry: A0A395HCR8_9EURO
LinkDB: A0A395HCR8_9EURO
Original site: A0A395HCR8_9EURO 
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}.
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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
//
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