ID   XLNR_ASPFN              Reviewed;         971 AA.
AC   B8N6M6;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Xylanolytic transcriptional activator xlnR;
DE   AltName: Full=Xylanase regulator;
GN   Name=xlnR; ORFNames=AFLA_015390;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- SIMILARITY: Belongs to the xlnR/xlr1 family. {ECO:0000305}.
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DR   EMBL; EQ963474; EED54287.1; -; Genomic_DNA.
DR   RefSeq; XP_002375559.1; XM_002375518.1.
DR   AlphaFoldDB; B8N6M6; -.
DR   STRING; 5059.CADAFLAP00003424; -.
DR   EnsemblFungi; EED54287; EED54287; AFLA_015390.
DR   VEuPathDB; FungiDB:AFLA_015390; -.
DR   eggNOG; ENOG502QUI0; Eukaryota.
DR   HOGENOM; CLU_006123_1_0_1; -.
DR   OMA; WLVYIVD; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..971
FT                   /note="Xylanolytic transcriptional activator xlnR"
FT                   /id="PRO_0000393150"
FT   DNA_BIND        129..155
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  105225 MW;  4EB70B4222BD8FAF CRC64;
     MSTTSIQHFT SSFSPFSSGT QPVGMAQSQT VGLDTLAEGS QYALEQLQLS REANGASAVD
     GGVPNPLRSS ISKPQGQQLY SDESSAQHTQ NATTGFRNLP QRDQLAEARS TIRKSSNSGP
     VRRRISRACD QCNQLRTKCD GQNPCAHCIE FGLTCEYARE RKKRGKASKK DLAAAAAAVA
     NNGTAPTSNG NTSNDSVSSA KRHTPSDGQS TQEVSGRYDP NFDASRNLAT AGQSQLGQHS
     DMSGMAGMQG SQQTPHSQPS LGGAIDAIHL NHFNTLNDSN RPQMSVPDLR SLQMLHPSGA
     NTRSPSGALP PQGMNSGYND GAYSLMNASE ANHPSINQYR LGNSAENPPA PFLGLSPPAQ
     SPGWLSLPSP SPANFASFSM PPFSSTLRYP VLQPVLPHIA SIIPQSLACD LLDVYFTSFS
     PSHLSPQSPY VVGYIFRKQS FLHPTKPRVC SPGLLASMLW VAAQTSDAAF LTSPPSARGR
     VCQKLLELTV GLLRPLIHGP APGETSPNYA ANMVINGVAL GGFGVSMDQL GAQSSATGAV
     DDVATYVHLA TVISASEYKA ASMRWWTAAW SLARELKLGR ELPPNAPQPR QDGEPEDDTD
     VDMSKRNLPP LITSVGGNSG STILNVTEEE REERRRLWWL LYATDRHLAL CYNRPLTLLD
     KECEGLLQPM NDDLWQAGDF AGATYRQVGP QVECTGHSMF GFFLPLMTIL GEIVDLQQAK
     EHPRFGRVFR NSADWDHQVL EITRQLDTYA QSLKEFEARY TSSLALGAGE SEAAIEGSHL
     DHVSPSGRST STAGSRVNES IVHTKMVVAY GTHIMHVLHV LLAGKWDPIN LLEDHDLWIS
     SESFIAAMSH AVGAADAAAD ILEYDPDITF MPFFFGIYLL QGSFLLLLAA DKLQGDVSPS
     VVRACETIVR AHEACVVTLN TEYQRTFRKV MRSALAQVRG RMPEDFGEQQ QRRREVLALY
     RWTGDGSGLA L