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Database: UniProt
Entry: A0A319CD86_9EURO
LinkDB: A0A319CD86_9EURO
Original site: A0A319CD86_9EURO 
ID   A0A319CD86_9EURO        Unreviewed;       627 AA.
AC   A0A319CD86;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=MATE efflux family protein {ECO:0000313|EMBL:PYH83124.1};
GN   ORFNames=BO82DRAFT_46305 {ECO:0000313|EMBL:PYH83124.1};
OS   Aspergillus uvarum CBS 121591.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH83124.1, ECO:0000313|Proteomes:UP000248340};
RN   [1] {ECO:0000313|EMBL:PYH83124.1, ECO:0000313|Proteomes:UP000248340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH83124.1,
RC   ECO:0000313|Proteomes:UP000248340};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC       2.A.66.1) family. {ECO:0000256|ARBA:ARBA00010199}.
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DR   EMBL; KZ821691; PYH83124.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319CD86; -.
DR   STRING; 1448315.A0A319CD86; -.
DR   VEuPathDB; FungiDB:BO82DRAFT_46305; -.
DR   OrthoDB; 661905at2759; -.
DR   Proteomes; UP000248340; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR   CDD; cd13132; MATE_eukaryotic; 1.
DR   InterPro; IPR045069; MATE_euk.
DR   InterPro; IPR002528; MATE_fam.
DR   NCBIfam; TIGR00797; matE; 1.
DR   PANTHER; PTHR11206:SF153; ETHIONINE RESISTANCE-CONFERRING PROTEIN 1; 1.
DR   PANTHER; PTHR11206; MULTIDRUG RESISTANCE PROTEIN; 1.
DR   Pfam; PF01554; MatE; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        194..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        410..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        486..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        558..581
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        587..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  68676 MW;  F1D68A7E18B4ABB2 CRC64;
     MTPRDSDFHS PRMSDEHHYL SRSPLARSAI ARDLEDYADD EGSMLTTDDD DDASETSTIR
     AIGSQPGTRA HSLAGSYQRP SYFTTVSRAT VVPYRPEQEG LTRRERDQAI EDERNLLTDN
     HFIEPSRKKS RRSASESAPS TEETALLGGE GSSRAPQYDS VDSEEIDRKW EEAVTAGLIQ
     TTWKREAQVI GKNAAPLVFT FLLQYSLTVA SIFTLGHLGK KELGAVSLAS MSANITGYAI
     YQGLATSLDT LCAQAYGSGK KKLVGLQMQK MVFFLWTISI PIVILWFFAD KVLVRIVPER
     EVAELAGLYL KVVALGAPGY ACFESGKRFV QAQGLFSASL YVLLVCAPLN AVMNYVFVWQ
     FGWGFVGAPI AVAITDNLMP LFLFLYVYFV AGSECWNGVT RRALRNWGPM IKLALPGLLM
     VEAECLAFEV LTLASSYLGT TPLAAQSILS TISSITFQIP FPVSISGSTR VANLIGATLV
     NAAKTSAKVT MVGAVIVGLL NMLLLSSLRY YIPRLFTSED EVIELVAQVL PLCAAFQLFD
     ALAANCNGIL RGIGRQEIGG YVQLFCYYAI AMPISFGTTF ALDWGLFGLW SGVALALMLV
     SIIEGFFLTQ TNWNRSVEDA LKRNSMN
//
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