GLIZ_ASPFU
ID GLIZ_ASPFU Reviewed; 489 AA.
AC Q4WMK0; Q5MBT6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=C6 finger domain transcription factor gliZ {ECO:0000305};
DE AltName: Full=Gliotoxin production protein Z {ECO:0000305};
GN Name=gliZ {ECO:0000303|PubMed:17030582}; ORFNames=AFUA_6G09630;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=15979823; DOI=10.1016/j.femsle.2005.05.046;
RA Gardiner D.M., Howlett B.J.;
RT "Bioinformatic and expression analysis of the putative gliotoxin
RT biosynthetic gene cluster of Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 248:241-248(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17030582; DOI=10.1128/iai.00780-06;
RA Bok J.W., Chung D., Balajee S.A., Marr K.A., Andes D., Nielsen K.F.,
RA Frisvad J.C., Kirby K.A., Keller N.P.;
RT "GliZ, a transcriptional regulator of gliotoxin biosynthesis, contributes
RT to Aspergillus fumigatus virulence.";
RL Infect. Immun. 74:6761-6768(2006).
RN [4]
RP INDUCTION.
RX PubMed=19915845; DOI=10.1007/s00294-009-0276-4;
RA Shin K.S., Kwon N.J., Yu J.H.;
RT "Gbetagamma-mediated growth and developmental control in Aspergillus
RT fumigatus.";
RL Curr. Genet. 55:631-641(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=20548963; DOI=10.1371/journal.ppat.1000952;
RA Schrettl M., Carberry S., Kavanagh K., Haas H., Jones G.W., O'Brien J.,
RA Nolan A., Stephens J., Fenelon O., Doyle S.;
RT "Self-protection against gliotoxin--a component of the gliotoxin
RT biosynthetic cluster, GliT, completely protects Aspergillus fumigatus
RT against exogenous gliotoxin.";
RL PLoS Pathog. 6:E1000952-E1000952(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21612254; DOI=10.1021/ja2029987;
RA Forseth R.R., Fox E.M., Chung D., Howlett B.J., Keller N.P.,
RA Schroeder F.C.;
RT "Identification of cryptic products of the gliotoxin gene cluster using
RT NMR-based comparative metabolomics and a model for gliotoxin
RT biosynthesis.";
RL J. Am. Chem. Soc. 133:9678-9681(2011).
RN [7]
RP INDUCTION.
RX PubMed=23087369; DOI=10.1128/ec.00222-12;
RA Dhingra S., Andes D., Calvo A.M.;
RT "VeA regulates conidiation, gliotoxin production, and protease activity in
RT the opportunistic human pathogen Aspergillus fumigatus.";
RL Eukaryot. Cell 11:1531-1543(2012).
RN [8]
RP INDUCTION.
RX PubMed=23671611; DOI=10.1371/journal.pone.0062591;
RA Sekonyela R., Palmer J.M., Bok J.W., Jain S., Berthier E., Forseth R.,
RA Schroeder F., Keller N.P.;
RT "RsmA regulates Aspergillus fumigatus gliotoxin cluster metabolites
RT including cyclo(L-Phe-L-Ser), a potential new diagnostic marker for
RT invasive aspergillosis.";
RL PLoS ONE 8:E62591-E62591(2013).
RN [9]
RP INDUCTION.
RX PubMed=26032501; DOI=10.1016/j.bbrc.2015.05.090;
RA Shin K.S., Kim Y.H., Yu J.H.;
RT "Proteomic analyses reveal the key roles of BrlA and AbaA in biogenesis of
RT gliotoxin in Aspergillus fumigatus.";
RL Biochem. Biophys. Res. Commun. 463:428-433(2015).
CC -!- FUNCTION: Transcription factor that regulates gliotoxin production and
CC contributes to virulence (PubMed:15979823, PubMed:17030582,
CC PubMed:20548963, PubMed:21612254). {ECO:0000269|PubMed:17030582,
CC ECO:0000269|PubMed:20548963, ECO:0000269|PubMed:21612254,
CC ECO:0000305|PubMed:15979823}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- INDUCTION: Expression is induced by gliotoxin (PubMed:20548963).
CC Expression is controled by veA (PubMed:23087369). Expression is
CC controled by brlA and abaA (PubMed:26032501). Expression is also
CC regulated by rsmA (PubMed:23671611). Expression is also influenced by
CC SfaD and GpgA (PubMed:19915845). {ECO:0000269|PubMed:19915845,
CC ECO:0000269|PubMed:20548963, ECO:0000269|PubMed:23087369,
CC ECO:0000269|PubMed:23671611, ECO:0000269|PubMed:26032501}.
CC -!- DISRUPTION PHENOTYPE: Impairs the expression of the majority of genes
CC in the gliotoxin cluster with the exception of gliT (PubMed:17030582,
CC PubMed:20548963, PubMed:21612254). {ECO:0000269|PubMed:17030582,
CC ECO:0000269|PubMed:20548963, ECO:0000269|PubMed:21612254}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW03310.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY838877; AAW03310.1; ALT_INIT; Genomic_DNA.
DR EMBL; AAHF01000006; EAL88814.1; -; Genomic_DNA.
DR RefSeq; XP_750852.1; XM_745759.1.
DR AlphaFoldDB; Q4WMK0; -.
DR SMR; Q4WMK0; -.
DR STRING; 746128.CADAFUBP00007372; -.
DR EnsemblFungi; EAL88814; EAL88814; AFUA_6G09630.
DR GeneID; 3508157; -.
DR KEGG; afm:AFUA_6G09630; -.
DR VEuPathDB; FungiDB:Afu6g09630; -.
DR eggNOG; ENOG502SSPP; Eukaryota.
DR HOGENOM; CLU_581347_0_0_1; -.
DR InParanoid; Q4WMK0; -.
DR OMA; CTRCHEY; -.
DR OrthoDB; 1052137at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043386; P:mycotoxin biosynthetic process; IMP:AspGD.
DR GO; GO:1900691; P:positive regulation of gliotoxin biosynthetic process; IMP:AspGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IMP:AspGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Virulence; Zinc.
FT CHAIN 1..489
FT /note="C6 finger domain transcription factor gliZ"
FT /id="PRO_0000435648"
FT DNA_BIND 47..73
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 51289 MW; 01710526AC19D447 CRC64;
MATAMQDVSP SFTSSPTSTM TTISTTTAAT AAAAPKPDKP RKLRSACDAC HRSKTRCSGG
NPCTRCHEYM SPCTYSYSSR CGKPKGARSR KTLEREQRVA AAAESARIAG NPSALASLPA
TSTCTSTATT AAAAAAATTT TTIATTTAPS QGPAVDSAAA AAAATTSTVA SPRADDCLGL
FDDDEESNPF FSSGSENTGG TSFSPDWIPP LPSISDSDLS FPLLESCLGP DHDCNDSLFW
STTAEPDCQP TSKEPLDPRS KLLRSCKCLQ TLSSLTARDI RRFDATFVFV RNYARAFSAF
YHCSHCPKDA GSISMAVTAL QLATTALEKT ATAGTDAAGF KSGCSGMTAA DLDEDLLTPG
AEFFLPANGR GASNPAFQLG SYQIAPLPGE PDLEEHSEIL NILIRSAVRR LLAVCWQIWD
LLRGPASRDG RGHVFEPYDP SSSSSSSSSS FSSGPEIHQL CDLSCSAEAA QFRSTLVQIP
ARLCNLLAL
