ID   USTT_USTVR              Reviewed;         537 AA.
AC   A0A1B5L780;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Efflux pump ustT {ECO:0000305};
DE   AltName: Full=Ustilaginoidins biosynthesis cluster protein T {ECO:0000303|PubMed:31050129};
GN   Name=ustT {ECO:0000303|PubMed:31050129}; ORFNames=UVI_02036180;
OS   Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Ustilaginoidea.
OX   NCBI_TaxID=1159556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IPU010;
RX   PubMed=27151791; DOI=10.1128/genomea.00306-16;
RA   Kumagai T., Ishii T., Terai G., Umemura M., Machida M., Asai K.;
RT   "Genome sequence of Ustilaginoidea virens IPU010, a rice pathogenic fungus
RT   causing false smut.";
RL   Genome Announc. 4:0-0(2016).
RN   [2]
RP   FUNCTION.
RC   STRAIN=IPU010;
RX   PubMed=31050129; DOI=10.1002/anie.201903759;
RA   Obermaier S., Thiele W., Fuertges L., Mueller M.;
RT   "Enantioselective phenol coupling by laccases in the biosynthesis of fungal
RT   dimeric naphthopyrones.";
RL   Angew. Chem. Int. Ed. 58:9125-9128(2019).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of ustilaginoidins, dimeric gamma-naphthopyrones isolated
CC       from different fungal species. {ECO:0000305|PubMed:31050129}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; BBTG02000019; GAO19110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B5L780; -.
DR   SMR; A0A1B5L780; -.
DR   Proteomes; UP000054053; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..537
FT                   /note="Efflux pump ustT"
FT                   /id="PRO_0000448928"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        507..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   537 AA;  57662 MW;  6FB0818F6B25EA9E CRC64;
     MAKEAQSLHE LDNMKEKEVD QEKKAPTSVG DQEEHDDPKK QASHSQNVSE NGLVDEAAQE
     APEDESQYPG PLAMAVIMVA ISMGMFLVSL LPLGRFYKFY SPKWVYMSLV FIFVIGSAVG
     AGAMNSNTVI VGRAIQGIGL GGVLSGSTIL IAENAPLHRQ PMFLGILMAT MSISAIVGPL
     IGGALTTHTS WRWCFILNIP IGGAIIAVLF FFVKAREGKE QRAQGWVEKI RQLDPLGSAL
     LLPAVVCLIL ALQWAGSQYS WDNWRIILLF VFGGLLSIGF VVSQMLRPDT ATVPPHVVCQ
     RTVFGSFLFS AMTGGAMLVV TYWISDWFQA VQNVSAAQAG IRTIALVLSQ AVGAIMGGGS
     SRLIGYPPPI MMISATFIAV GAGLLTTLNV DTKSANWIGY QILMGLGLGF GTQQASLAVQ
     TVLKKDDIPT AISLIFFGMQ LGGSIFVCIG QNVFNQVFVK LLGQAAIPGL DTDLVLRTGA
     TEIRQLVHND ADLSKLVTTY NTSVTSTFYV ALAAGITSML SAFLVQWKSV KNVEPVH