XLNR_ASPTN
ID XLNR_ASPTN Reviewed; 963 AA.
AC Q0CV52;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Xylanolytic transcriptional activator xlnR;
DE AltName: Full=Xylanase regulator;
GN Name=xlnR; ORFNames=ATEG_02432;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU37394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAU37394.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476596; EAU37394.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001211610.1; XM_001211610.1.
DR AlphaFoldDB; Q0CV52; -.
DR SMR; Q0CV52; -.
DR STRING; 341663.Q0CV52; -.
DR GeneID; 4316904; -.
DR eggNOG; ENOG502QUI0; Eukaryota.
DR OrthoDB; 1430629at2759; -.
DR Proteomes; UP000007963; 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; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..963
FT /note="Xylanolytic transcriptional activator xlnR"
FT /id="PRO_0000393155"
FT DNA_BIND 127..153
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 104308 MW; C3259C8B679216FF CRC64;
MSTTSLQPFA PSFSPFPSTQ SLGMAPSQTI GLDTLAEGSQ YSLEQLQLSR EAGNDAATAT
SSTSLRSSSF SKSTDQSVSN PSGNHHSNNG PPSDFKSSQR DPLAEARSAI RKNSTSAPVR
RRISRACDQC NQLRTKCDGQ HPCAHCIEFG LTCEYARERK KRGKASKKDL AAAAAAAAAA
GSTSSSTAND GGPMLTKGHS PSDGRSSHEI NGRYDPAFDA ARTLTNSAQS QLQSHADVPG
MVGMQNSQQP HSQPPLGAAL DALHLNHFSA LNESNRPQMS VPDLRTLQML HPSGTNPRSP
SAVLPSQGLN SYNETAYSLM NPQESNPASM NHFRLGSSAE NQPPSFLGLS PPAQSPGWLP
LPSPSPANFP SFSMNPYPST LRYPVLQPVL PHIASIIPQS LACDLLDVYF TSFSPSHLSP
LSPYVVAYIF RKQSFLHPTK PRVCSPGLLA SMLWVAAQTS DAAFLTSPPS ARGRVCQKLL
ELTIGLLRPL IHGPAPGETS PNYAANMVIN GVALGGFGVS MDQLGAQSTA TGAVDDVATY
VHLATVVSAS EYKAASIRWW TAAWSLAREL KLGRELPPNT NTARQDGDRD ADSDVDMSKR
NLPSLVTSVG HGSGTPLNVT EEEREERRRL WWLLYATDRH LALCYNQPLR LLDKECEGLL
QPMNDDLWQA GDFGAVGYRQ VGPPIECSGH SMFGYFLPLM TILGGIVDLQ QAKEHPRFGI
AFRNSSEWEH QVLELTRQLE TYGQSLKEFE SRYTSSLALG AADNETIVDG GHLDHVSPSG
RSSSTVGSRI NESIVHTKMV VAYGTHIMHV LHILLAGKWD PINLLEDQDL WISSESFITA
MGHAVGAADA AADILEYDPD LSFMPFFFGI YLLQGSFLLL LAADKLQGDA SPSVVRACET
IVRAHEACVV TLNTEYQTFR KVMRSALAQV RGRMPEDFGE QQQRRREVLA LYRWTGDGSG
LAL
