XLNR_MAGO7
ID XLNR_MAGO7 Reviewed; 1009 AA.
AC G4MZJ4;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Xylanolytic transcriptional activator xlnR homolog;
DE AltName: Full=Xylanase regulator 1 homolog;
GN Name=xlr1; ORFNames=MGG_01414;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23810898; DOI=10.1016/j.fgb.2013.06.005;
RA Battaglia E., Klaubauf S., Vallet J., Ribot C., Lebrun M.H., de Vries R.P.;
RT "Xlr1 is involved in the transcriptional control of the pentose catabolic
RT pathway, but not hemi-cellulolytic enzymes in Magnaporthe oryzae.";
RL Fungal Genet. Biol. 57:76-84(2013).
CC -!- FUNCTION: Transcriptional activator of the pentose catabolic pathway
CC (PCP). Involved in the induction of a variety of PCP enzymes during
CC growth on D-xylose. Has no effect on cellulolytic and xylanolytic
CC enzyme activities. {ECO:0000269|PubMed:23810898}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- DISRUPTION PHENOTYPE: Reduces growth on D-xylose and xylan, but not on
CC L-arabinose or arabinan. {ECO:0000269|PubMed:23810898}.
CC -!- SIMILARITY: Belongs to the xlnR/xlr1 family. {ECO:0000305}.
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DR EMBL; CM001232; EHA54553.1; -; Genomic_DNA.
DR RefSeq; XP_003714360.1; XM_003714312.1.
DR AlphaFoldDB; G4MZJ4; -.
DR SMR; G4MZJ4; -.
DR STRING; 318829.MGG_01414T0; -.
DR EnsemblFungi; MGG_01414T0; MGG_01414T0; MGG_01414.
DR GeneID; 2679715; -.
DR KEGG; mgr:MGG_01414; -.
DR VEuPathDB; FungiDB:MGG_01414; -.
DR eggNOG; ENOG502QUI0; Eukaryota.
DR HOGENOM; CLU_006123_1_0_1; -.
DR InParanoid; G4MZJ4; -.
DR OMA; WLVYIVD; -.
DR OrthoDB; 1430629at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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 3: Inferred from homology;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..1009
FT /note="Xylanolytic transcriptional activator xlnR homolog"
FT /id="PRO_0000425610"
FT DNA_BIND 97..123
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 134..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 108983 MW; C39F611B1E244A8E CRC64;
MLSNPLHRFS GYHAMPSNTL MSNGHMSQGH LHNNGLDGLG QSSHYALQQL QQHVGVHNPH
LARAAPHMKH HRQHPYGPAV RTAGIAGPIR RRISRACDQC NQLRTKCDGN HPCAHCIEFG
LGCEYIRERK KRGKASRKDL AQQAAAQAAT TGSSSGQKSP THSANTTKKD DQKVDGGSST
GNAPNSEQHS PDDKDLDNDA MQRSQRMGSM DSLDEMDHQG HISGHHHQQA ALDREHHTMS
NPSALDPNSY GGVHNGYERQ GGMGTATSHI MGGAAHGGYG SQGGMSSYPE LPYLQTQSPT
GYSGGGASYR IGTSPLSAYP LSGETASPGW GLPIPSPPAS HGQYHSQHMQ QQSSASYGAG
TSGGLASGHP QHLRYPVLDP LVPHLGNIIP LSLACDLIDL YFASSSSAQV HPMSPYVLGF
VLRKRSFLHP SKPRLCQPAL LASILWVAAQ TSDAPFLTSV PSARGKICQK LLELTVSLLK
PLIHTPSGDV SPVSSPVIDG AALGGLGVAM PGSISMEALS GETGAFGAAG TLDDVVTYIH
LATVVSASEY KGASLRWWNA AWSLARELKL GRELPQNAPS AMSDTAGNER NDNDDTTEAL
GGGPNVITDE EREERRRIWW LVYIVDRHLA LCYNRPLFLL DIECDGLLQP LDDTAYQNGE
FRPHQVVTDP DMLGEDRRSS QKSETALIRG PSFECTGHGI FGYFLPLMTI LGEIVDLNHA
RNHPRFGINF RSHSEWDEQT SEIARHLELY EQSLRRFEQQ HLSAAAQAQA QAADAAKAAA
AAQAQAHAQA QAQQTSSDDS AISADNISVT DVGTPSALSV HSVAHSAHTT SSSRLTESDV
QTRIVLAYGT HVMNVLHILL TGKWDPINLL DDNDLWISSQ GFITATGHAV DAAEAIGSIL
EFDPGLEFMP FFFGIYLLQG SFLLLLIADK LQSEASPSVV KACETIIRAH EACVVTLNTE
YQRNFSKVMR SALAQVRGRV PEDLGEQHQR RRELLALYRW TGDGTGLAL
