ID VDTG1_BYSSP Reviewed; 555 AA.
AC A0A443HJZ5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=MFS-type transporter VdtG {ECO:0000303|PubMed:31304040};
DE AltName: Full=Viriditoxin biosynthesis cluster protein G {ECO:0000303|PubMed:31304040};
GN Name=VdtG {ECO:0000303|PubMed:31304040}; ORFNames=C8Q69DRAFT_488624;
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075;
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Maekelae M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
RN [2]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=31304040; DOI=10.1186/s40694-019-0072-y;
RA Urquhart A.S., Hu J., Chooi Y.H., Idnurm A.;
RT "The fungal gene cluster for biosynthesis of the antibacterial agent
RT viriditoxin.";
RL Fungal Biol. Biotechnol. 6:2-2(2019).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of viriditoxin, one of the 'classical' secondary
CC metabolites produced by fungi and that has antibacterial activity
CC (PubMed:31304040). Is not essential for viriditoxin production
CC (PubMed:31304040). {ECO:0000269|PubMed:31304040}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:31304040}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of viriditoxin but
CC leads to a sporulation defect. {ECO:0000269|PubMed:31304040}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; RCNU01000014; RWQ92172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443HJZ5; -.
DR SMR; A0A443HJZ5; -.
DR STRING; 264951.A0A443HJZ5; -.
DR GlyCosmos; A0A443HJZ5; 4 sites, No reported glycans.
DR OrthoDB; 1368647at2759; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd17502; MFS_Azr1_MDR_like; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 1.20.1720.10; Multidrug resistance protein D; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR23501; MAJOR FACILITATOR SUPERFAMILY; 1.
DR PANTHER; PTHR23501:SF153; MFS AFLATOXIN EFFLUX PUMP; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..555
FT /note="MFS-type transporter VdtG"
FT /id="PRO_0000448347"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 555 AA; 58308 MW; 7CCCE50649B5A0D7 CRC64;
MNGNGTADKP GPPGGKPFGP GMGPPIQYPT GFKLYSIMTG LYLASFLTAL DRTVLVVAIP
QITDHFNSID DIGWYGSAYL LTFCAFQLLF GKIYSFYNPK WVFLSAVLIF EIGSAICGAA
PNSTALIIGR AIAGLGSSGI FGGSVIITFF TVPLHQRPIY TGIAGVIFAL ASSVGPLIGG
GFTNNVSWRW CFYINLPVGA LTVVTILLFL NLPPARKAGT PLREQLLQMD PLGNLCLIPG
IICLLLAIQW GGSTYAWSNG RIVALLVLAG VLLIAFVGVQ LWLQDKGTIP PRVMKQRSIA
AGMAFTICVT AGFMSFNYYL PIWFQAIKNA SSFHSGVMML PTVISSGVAS LACGFIIHRV
GYYTPFMIGG SVLMAIGAGL LTTFTPTTEH PKWIGYQVLW ALGCGMSMQQ ASLAAQTVLP
KPDAPIGISL IFFSQSLGGS VFLAVDDSIY SNRLAAKLGS IPNLPQSALT NTGATNIRNL
VAPQYLGRLL GGYNDALMDV FRVAVASSCA CVVAAAFMEW KNVRAAKAAG PGGPGGPGGP
GGPGGPEGLR GGNKV
//
