XLNR_ASPOR
ID XLNR_ASPOR Reviewed; 971 AA.
AC Q2UD93; Q9P953;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Xylanolytic transcriptional activator xlnR;
DE AltName: Full=Xylanase regulator;
GN Name=xlnR; ORFNames=AO090012000267;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DNA-BINDING.
RX PubMed=11848678; DOI=10.1006/fgbi.2001.1321;
RA Marui J., Tanaka A., Mimura S., de Graaff L.H., Visser J., Kitamoto N.,
RA Kato M., Kobayashi T., Tsukagoshi N.;
RT "A transcriptional activator, AoXlnR, controls the expression of genes
RT encoding xylanolytic enzymes in Aspergillus oryzae.";
RL Fungal Genet. Biol. 35:157-169(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [3]
RP FUNCTION.
RX PubMed=12297320; DOI=10.1016/s0014-5793(02)03328-8;
RA Marui J., Kitamoto N., Kato M., Kobayashi T., Tsukagoshi N.;
RT "Transcriptional activator, AoXlnR, mediates cellulose-inductive expression
RT of the xylanolytic and cellulolytic genes in Aspergillus oryzae.";
RL FEBS Lett. 528:279-282(2002).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=19777228; DOI=10.1007/s00253-009-2236-9;
RA Noguchi Y., Sano M., Kanamaru K., Ko T., Takeuchi M., Kato M.,
RA Kobayashi T.;
RT "Genes regulated by AoXlnR, the xylanolytic and cellulolytic
RT transcriptional regulator, in Aspergillus oryzae.";
RL Appl. Microbiol. Biotechnol. 85:141-154(2009).
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:11848678, ECO:0000269|PubMed:12297320,
CC ECO:0000269|PubMed:18332432, ECO:0000269|PubMed:19777228}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- INDUCTION: Expressed in presence of xylose.
CC {ECO:0000269|PubMed:18332432}.
CC -!- SIMILARITY: Belongs to the xlnR/xlr1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE60472.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB042843; BAA95967.1; -; Genomic_DNA.
DR EMBL; AP007161; BAE60472.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2UD93; -.
DR STRING; 510516.Q2UD93; -.
DR VEuPathDB; FungiDB:AO090012000267; -.
DR Proteomes; UP000006564; Chromosome 4.
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:2000999; P:positive regulation of cellulose catabolic process; IMP:AspGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:2001002; P:positive regulation of xylan catabolic process; IDA:AspGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:AspGD.
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 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..971
FT /note="Xylanolytic transcriptional activator xlnR"
FT /id="PRO_0000393154"
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
