EQXG_GIBF5
ID EQXG_GIBF5 Reviewed; 481 AA.
AC S0DS64;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Trichosetin biosynthesis cluster MFS transporter {ECO:0000303|PubMed:28379186};
DE Short=MFS-T {ECO:0000303|PubMed:28379186};
GN Name=MFS-T {ECO:0000303|PubMed:28379186}; ORFNames=FFUJ_02224;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28379186; DOI=10.3390/toxins9040126;
RA Janevska S., Arndt B., Baumann L., Apken L.H., Mauriz Marques L.M.,
RA Humpf H.U., Tudzynski B.;
RT "Establishment of the inducible Tet-On system for the activation of the
RT silent trichosetin gene cluster in Fusarium fujikuroi.";
RL Toxins 9:0-0(2017).
CC -!- FUNCTION: Efflux pump required for efficient secretion of trichosetin
CC or other secondary metabolies produced by the trichosetin gene cluster
CC (PubMed:28379186). Plays a crucial role in detoxification of the toxic
CC trichosetin in Gibberella fujikuroi cells (PubMed:28379186).
CC {ECO:0000269|PubMed:28379186}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced by the final product trichosetin and
CC not by the trichosetin cluster-specific transcription acticator TF22
CC (PubMed:28379186). {ECO:0000269|PubMed:28379186}.
CC -!- DISRUPTION PHENOTYPE: Resulted in the down-regulation of the three
CC biosynthetic genes from the trisetin cluster and a reduced accumulation
CC of trichosetin (PubMed:28379186). {ECO:0000269|PubMed:28379186}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; HF679025; CCT65291.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DS64; -.
DR EnsemblFungi; CCT65291; CCT65291; FFUJ_02224.
DR VEuPathDB; FungiDB:FFUJ_02224; -.
DR HOGENOM; CLU_008455_1_1_1; -.
DR Proteomes; UP000016800; Chromosome 3.
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; -; 1.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..481
FT /note="Trichosetin biosynthesis cluster MFS transporter"
FT /id="PRO_0000443992"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 481 AA; 52188 MW; 579AB365F33EE418 CRC64;
MSTTPQMSQS GFQDDQLEAG AREDVGTEAQ EKPLSTTGTM VDEPQPNPNV VDWDGPDDPQ
HPLNWSKAQK NLHVGIVSLS TLAANLAATM FAPGAAELSD EFNITSATVT AMTVSLYVLG
FALGPLLLAP LSELYGRLII YHFCNMVYMA FTIGCAFSTN VAMFLVFRII AGCAASGPMS
IGGGTVADLF VQEQRGKAMA LFAVGPLLGP VIGPIIGGFV SENVGWRWTF RILLILSGIL
ATVTFALMKE TNYTVILQKK ALRMRKETGN EKLVAKSSRD ETAGQMLARA IVRPLKLLIF
SPIVLLVSLY TGILFGLIFL LFTTFPSVFQ DVDKLLGSKK GEENAAPRPE DRLLLMKWLG
PITPLGLFIY GWTAENRVHW IVPIIGTFIV GFGSLFVVIP GQIYLVDAFG AEAAASAMAA
NLLVRSPFGA FLDLTAEPLY SKLGLGWGNS VLGFITLAFT PVPWIFYTYG ERLRTHFQVD
L
