XLNR_ASPNC
ID XLNR_ASPNC Reviewed; 945 AA.
AC A2R5W7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Xylanolytic transcriptional activator xlnR;
DE AltName: Full=Xylanase regulator;
GN Name=xlnR; ORFNames=An15g05810;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Transcriptional activator of the xylanolytic system. Involved
CC in the regulation of extracellular cellulolytic and xylanolytic genes
CC and in the regulation of the intracellular activities of D-xylose
CC catabolic genes in the pentose catabolic pathway (PCP) in response to
CC the presence of D-xylose. Binds to the DNA sequence 5'-GGCTAAA-3' (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- SIMILARITY: Belongs to the xlnR/xlr1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK42534.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM270347; CAK42534.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2R5W7; -.
DR PaxDb; A2R5W7; -.
DR EnsemblFungi; CAK42534; CAK42534; An15g05810.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; ISS:UniProtKB.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..945
FT /note="Xylanolytic transcriptional activator xlnR"
FT /id="PRO_0000393153"
FT DNA_BIND 125..151
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 102090 MW; B64027F642A49668 CRC64;
MSTPSIPQFT SPFSPFSSGS HSTGMAPSQT VGLDTLAEGS QYVLEQLQLS RDAAGSGAGD
GAPSTSLRNS MSHTKDQPPF DNEKNQSTGS GFRDALQRDP LVEARSAIRK TSSSAPVRRR
ISRACDQCNQ LRTKCDGQHP CAHCIEFGLT CEYARERKKR GKASKKDLAA AAAAATQGSN
GHSGQANASL MGERTSEDSR PGQDVNGTYD SAFESHHLSS QPSHMQHAST AGISGLHESQ
TAPSHSQPSL GTTIDAMHLN HFNTMNDSGR PAMSISDLRS LPPSVLPPQG LSSGYNASAF
ALVNPQEPGS PANQFRLGSS AENPTAPFLG LSPPGQSPGW LPLPSPSPAN FPSFSLHPFS
STLRYPVLQP VLPHIASIIP QSLACDLLDV YFTSSSSSHL SPLSPYVVGY IFRKQSFLHP
TKPRICSPGL LASMLWVAAQ TSEAAFLTSP PSARGRVCQK LLELTIGLLR PLVHGPATGE
ASPNYAANMV INGVALGGFG VSMDQLGAQS SATGAVDDVA TYVHLATVVS ASEYKAASMR
WWTAAWSLAR ELKLGRELPP NVSHARQDGE RDGDGEADKR HPPTLITSLG HGSGSSGINV
TEEEREERRR LWWLLYATDR HLALCYNRPL TLLDKECGGL LQPMNDDLWQ VGDFAAAAYR
QVGPPVECTG HSMYGYFLPL MTILGGIVDL HHAENHPRFG LAFRNSPEWE RQVLDVTRQL
DTYGRSLKEF EARYTSNLTL GATDNEPVVE GAHLDHTSPS GRSSSTVGSR VSESIVHTRM
VVAYGTHIMH VLHILLAGKW DPVNLLEDHD LWISSESFVS AMSHAVGAAE AAAEILEYDP
DLSFMPFFFG IYLLQGSFLL LLAADKLQGD ASPSVVRACE TIVRAHEACV VTLNTEYQRT
FRKVMRSALA QVRGRIPEDF GEQQQRRREV LALYRWSGDG SGLAL
