XLNR_ASPNG
ID XLNR_ASPNG Reviewed; 945 AA.
AC O42804;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Xylanolytic transcriptional activator xlnR;
DE AltName: Full=Xylanase regulator;
GN Name=xlnR;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=9466262; DOI=10.1046/j.1365-2958.1998.00666.x;
RA van Peij N.N.M.E., Visser J., De Graaff L.H.;
RT "Isolation and analysis of xlnR, encoding a transcriptional activator co-
RT ordinating xylanolytic expression in Aspergillus niger.";
RL Mol. Microbiol. 27:131-142(1998).
RN [2]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=9758775; DOI=10.1128/aem.64.10.3615-3619.1998;
RA van Peij N.N., Gielkens M.M., de Vries R.P., Visser J., de Graaff L.H.;
RT "The transcriptional activator XlnR regulates both xylanolytic and
RT endoglucanase gene expression in Aspergillus niger.";
RL Appl. Environ. Microbiol. 64:3615-3619(1998).
RN [3]
RP FUNCTION.
RX PubMed=10508057; DOI=10.1128/aem.65.10.4340-4345.1999;
RA Gielkens M.M., Dekkers E., Visser J., de Graaff L.H.;
RT "Two cellobiohydrolase-encoding genes from Aspergillus niger require D-
RT xylose and the xylanolytic transcriptional activator XlnR for their
RT expression.";
RL Appl. Environ. Microbiol. 65:4340-4345(1999).
RN [4]
RP FUNCTION.
RX PubMed=10760176; DOI=10.1046/j.1365-2958.2000.01843.x;
RA Hasper A.A., Visser J., de Graaff L.H.;
RT "The Aspergillus niger transcriptional activator XlnR, which is involved in
RT the degradation of the polysaccharides xylan and cellulose, also regulates
RT D-xylose reductase gene expression.";
RL Mol. Microbiol. 36:193-200(2000).
RN [5]
RP FUNCTION.
RX PubMed=11916668; DOI=10.1128/aem.68.4.1556-1560.2002;
RA Hasper A.A., Dekkers E., van Mil M., van de Vondervoort P.J.,
RA de Graaff L.H.;
RT "EglC, a new endoglucanase from Aspergillus niger with major activity
RT towards xyloglucan.";
RL Appl. Environ. Microbiol. 68:1556-1560(2002).
RN [6]
RP FUNCTION.
RX PubMed=12242504; DOI=10.1007/s00438-002-0729-7;
RA de Vries R.P., van de Vondervoort P.J.I., Hendriks L., van de Belt M.,
RA Visser J.V.;
RT "Regulation of the a-glucuronidase encoding gene (aguA) from Aspergillus
RT niger.";
RL Mol. Genet. Genomics 268:96-102(2002).
RN [7]
RP FUNCTION.
RX PubMed=17951513; DOI=10.1128/ec.00244-07;
RA Levin A.M., de Vries R.P., Conesa A., de Bekker C., Talon M., Menke H.H.,
RA van Peij N.N., Wosten H.A.;
RT "Spatial differentiation in the vegetative mycelium of Aspergillus niger.";
RL Eukaryot. Cell 6:2311-2322(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RA de Groot M.J.L., van den Dool C., Woesten H.A.B., Levisson M.,
RA vanKuyk P.A., Ruijter G.J.G., de Vries R.P.;
RT "Regulation of pentose catabolic pathway genes of Aspergillus niger.";
RL Food Technol. Biotechnol. 45:134-138(2007).
RN [9]
RP INDUCTION, AND FUNCTION.
RX PubMed=18332432; DOI=10.1073/pnas.0709964105;
RA Andersen M.R., Vongsangnak W., Panagiotou G., Salazar M.P., Lehmann L.,
RA Nielsen J.;
RT "A trispecies Aspergillus microarray: comparative transcriptomics of three
RT Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4387-4392(2008).
RN [10]
RP FUNCTION.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=21484208; DOI=10.1007/s00253-011-3242-2;
RA Battaglia E., Hansen S.F., Leendertse A., Madrid S., Mulder H.,
RA Nikolaev I., de Vries R.P.;
RT "Regulation of pentose utilisation by AraR, but not XlnR, differs in
RT Aspergillus nidulans and Aspergillus niger.";
RL Appl. Microbiol. Biotechnol. 91:387-397(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=21892241; DOI=10.3114/sim.2011.69.03;
RA Battaglia E., Visser L., Nijssen A., van Veluw G.J., Woesten H.A.,
RA de Vries R.P.;
RT "Analysis of regulation of pentose utilisation in Aspergillus niger reveals
RT evolutionary adaptations in Eurotiales.";
RL Stud. Mycol. 69:31-38(2011).
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'-GGNTAAA-3'.
CC {ECO:0000269|PubMed:10508057, ECO:0000269|PubMed:10760176,
CC ECO:0000269|PubMed:11916668, ECO:0000269|PubMed:12242504,
CC ECO:0000269|PubMed:17951513, ECO:0000269|PubMed:18332432,
CC ECO:0000269|PubMed:21484208, ECO:0000269|PubMed:21892241,
CC ECO:0000269|PubMed:9758775, ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: Expressed in presence of xylose.
CC {ECO:0000269|PubMed:18332432}.
CC -!- DISRUPTION PHENOTYPE: Reduces growth on birchwod xylan, while growth is
CC unaffected on D-xylose, xylitol and other carbon sources like D-
CC glucose, L-arabinose or L-arabitol. {ECO:0000269|PubMed:21892241,
CC ECO:0000269|Ref.8}.
CC -!- SIMILARITY: Belongs to the xlnR/xlr1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA05082.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ001909; CAA05082.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; O42804; -.
DR SMR; O42804; -.
DR STRING; 5061.CADANGAP00012027; -.
DR VEuPathDB; FungiDB:An15g05810; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1183692; -.
DR VEuPathDB; FungiDB:ATCC64974_28320; -.
DR VEuPathDB; FungiDB:M747DRAFT_233940; -.
DR eggNOG; ENOG502QUI0; Eukaryota.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
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 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..945
FT /note="Xylanolytic transcriptional activator xlnR"
FT /id="PRO_0000114989"
FT DNA_BIND 125..151
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..118
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 59..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; 102073 MW; FA5C85409EB98602 CRC64;
MSTPSIPQFT SSFSPFSSGS HSTGMAPSQT VGLDTLAEGS QYVLEQLQLS RDAAGTGAGD
GATSTSLRNS MSHTKDQPPF DNEKNQSTGS GFRDALQRDP LVEARSAVRK TSSSAPVRRR
ISRACDQCNQ LRTKCDGQHP CAHCIEFGLT CEYARERKKR GKASKKDLAA AAAAATQGSN
GHSGQANASL MGERTSEDSR PGQDVNGTYD SAFESHHLSS QPSHMQHAST AGISGLHESQ
TAPSHSQSSL 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
