XLNR_EMENI
ID XLNR_EMENI Reviewed; 900 AA.
AC Q5AVS0; C8VBV6; Q8J128;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Xylanolytic transcriptional activator xlnR;
DE AltName: Full=Xylanase regulator;
GN Name=xlnR; ORFNames=AN7610;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION.
RX PubMed=18420433; DOI=10.1016/j.fgb.2008.03.002;
RA Tamayo E.N., Villanueva A., Hasper A.A., de Graaff L.H., Ramon D.,
RA Orejas M.;
RT "CreA mediates repression of the regulatory gene xlnR which controls the
RT production of xylanolytic enzymes in Aspergillus nidulans.";
RL Fungal Genet. Biol. 45:984-993(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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, AND DISRUPTION PHENOTYPE.
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).
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:18332432, ECO:0000269|PubMed:18420433,
CC ECO:0000269|PubMed:21484208}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- INDUCTION: Expressed in presence of xylose. Repressed in presence of
CC glucose through the action of the creA transcription repressor.
CC {ECO:0000269|PubMed:18332432, ECO:0000269|PubMed:18420433}.
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:21484208}.
CC -!- SIMILARITY: Belongs to the xlnR/xlr1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC81360.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CBF79739.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAA61796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ272537; CAC81360.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AACD01000130; EAA61796.1; ALT_INIT; Genomic_DNA.
DR EMBL; BN001304; CBF79739.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_680879.1; XM_675787.1.
DR AlphaFoldDB; Q5AVS0; -.
DR SMR; Q5AVS0; -.
DR STRING; 162425.CADANIAP00000725; -.
DR EnsemblFungi; EAA61796; EAA61796; AN7610.2.
DR GeneID; 2869741; -.
DR KEGG; ani:AN7610.2; -.
DR eggNOG; ENOG502QUI0; Eukaryota.
DR HOGENOM; CLU_006123_1_0_1; -.
DR InParanoid; Q5AVS0; -.
DR OrthoDB; 1430629at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; 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; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IMP: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 2: Evidence at transcript level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..900
FT /note="Xylanolytic transcriptional activator xlnR"
FT /id="PRO_0000393156"
FT DNA_BIND 98..124
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 53..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 627..629
FT /note="GHS -> ATG (in Ref. 1; CAC81360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 98441 MW; 294DD655F52034C8 CRC64;
MSTTSLQQFA TATSFSPFSN SQSARMSQSQ SQTIGLDTLA EGSQYVLEQL QLSREGGNSE
NNSTFKPSSV RDSLAEARSM IRKNSSSAPV RRRISRACDQ CNQLRTKCDG QNPCAHCIEF
GLTCEYARER KKRGKASKKD IAAAAAAAGH QGGMGNRSPT DRRLSQEPGG RYDSVLEASR
VQSHLPANGL SSIHNTQAAH SQPPLGSALD ALHLNHFTQL NESGRSQMPV SDLRSLQILH
NNPRSPSALP HGLNAYNDNT FSLLNSQEPN TTSLNHFRLG NSTDNPSAQF LGLSPPAQSP
GWLPLPSPSP ANFPSFPMAP FSGTSLRYPV LQPVLPHIAS IIPQSLACDL LDLYFTSSSS
SHLSPQSPYV VGYIFRKQSF LHPTKPRVCS PGLLASMLWV GAQTSDAPFL TSPPSARGRV
CQKLLELTIG LLRPLIHGPA LGEASPNYAA NMVINGVALG GFGVSMDQLG AQSTATGAVD
DVATYVHLAT VVSASEYKAA SMRWWTAAWS LARELKLGRE LPPNASQPGQ DGERENEGDN
PSKRNQSLHG GNSNVNVTEE EREERRRLWW LLYATDRHLA LCYNRPLTLL DKECSQLLQP
MNDDLWQAGD FPAATYRAVG PPIECTGHSM FGYFLPLMTI LGGIIDLQQA REHPRYGLTF
RSGPDLDQYI MAITQQLDAY GQSLKDFEAR YINSLALAEN EPPENPHIDH LSPSGRSSST
VGSRVNESIV HTKMVVAYGT HIMHVLYVLL AGKWDPINLL EDHDMWISSE SFLAAMSHAV
GAAEAAADIL EYDPDLSFMP FFFGIYLLQG SFLLLLAADK LQGDANPSVV RACETIVRAH
EACVVTLNTE YQRTFRKVMR SALAQVRGRV PDDFGEQQQR RREVLSLYRW TGDGTGLALS
