XLNR_NEOFI
ID XLNR_NEOFI Reviewed; 950 AA.
AC A1DIC0;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Xylanolytic transcriptional activator xlnR;
DE AltName: Full=Xylanase regulator;
GN Name=xlnR; ORFNames=NFIA_090850;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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=EAW19127.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAW19127.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DS027696; EAW19127.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001261024.1; XM_001261023.1.
DR AlphaFoldDB; A1DIC0; -.
DR SMR; A1DIC0; -.
DR STRING; 36630.CADNFIAP00007051; -.
DR GeneID; 4587582; -.
DR KEGG; nfi:NFIA_090850; -.
DR eggNOG; ENOG502QUI0; Eukaryota.
DR OrthoDB; 1430629at2759; -.
DR Proteomes; UP000006702; 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..950
FT /note="Xylanolytic transcriptional activator xlnR"
FT /id="PRO_0000393157"
FT DNA_BIND 119..145
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 103771 MW; 606F9D26F41F36D9 CRC64;
MSTTSLQHFS HSYSPFPSSR SSNRMAQSQT SGLDTLAEGS QYALEQLQMS REAAGDGEAT
NSMGKPKDQY QIDNDNHHNN HSLPSFKNSS QRDPLVEARS TIRKNSASAP VRRRISRACD
QCNQLRTKCD GQNPCAHCIE FGLTCEYARE RKKRGKASKK DLAAAAAAAT NPGQPNGSSG
KEDAAMVGGH TSPDRRPTLN GRYDPAFEVP RNLNGSAQHS EASGMVGMQN SQHLPPHSQS
SMGGGLEGLS LNGYNGLNDS SRPSMPVPEL QSLHMLHNSH TNPRSPSSVL PHHRYNGGYN
DSAYSLMNPQ EPNSTSISHF RLGSSTENPP NSFLGLSPPA QSPGWLPLPS PSPANFPSFS
MASFSTTLRY PVLHPVLPHI ASIIPQSLAC DLLDVYFTSS SSSHLSPQSP YVVGYIFRKQ
SFLHPTKPRV CTPGLLASML WVAAQTSDAP FLTSPPSARG RVCQKLLELT IGLLRPLIHG
PAPGETSPNY AANMVINGVA LGGFGVSMDQ LGAQSSATGA VDDVATYVHL ATVISASEYK
AASMRWWTAA WSLARELKLG RELPPNTPHS RPDAERDGDP DADLSKRHPP PLITSMGHGP
GNTVINITEE EREERRRLWW LLYATDRHLA LCYNRPLTLL DKECEGLLQP MNDDLWQAGD
FATYRQAGPP VECTGHSMFG YFLPLMTILG EIVDLQQARN HPRFGLAFRN SAECEAQVLE
IARQLDVYAQ SLKEFETRYT SSLALGAAET EAAMEGSHLN HVSPSGRSSS TVESRVNESI
VHTKMVVAYG THIMHVLHIL LAGKWDPINL LDDNDLWISS ESFVAAMGHA VGAAEAASEI
LEYDPDLSFM PFFFGIYLLQ GSFLLLLTAD KLQGDASPSV VRACETIVRA HEACVVTLNT
EYQRTFRKVM RSALAQVRGR LPEDFGEQQQ RRREVLALYR WTGDGSGLAL
