ID   ARAR_EMENI              Reviewed;         825 AA.
AC   Q5BGE2; C8VTP5;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Arabinolytic transcriptional activator araR;
GN   ORFNames=AN0388, ANIA_00388;
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 [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   [2]
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   [3]
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 arabinanolytic system.
CC       Involved in the regulation of extracellular arabinanolytic genes and in
CC       the regulation of the intracellular activities of L-arabinose catabolic
CC       genes in the pentose catabolic pathway (PCP) in response to the
CC       presence of L-arabinose. {ECO:0000269|PubMed:21484208}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Impairs growth on L-arabinose, but only a small
CC       growth reduction on L-arabitol. {ECO:0000269|PubMed:21484208}.
CC   -!- SIMILARITY: Belongs to the xlnR/xlr1 family. araR subfamily.
CC       {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; AACD01000007; EAA66487.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF89583.1; -; Genomic_DNA.
DR   RefSeq; XP_657992.1; XM_652900.1.
DR   AlphaFoldDB; Q5BGE2; -.
DR   PRIDE; Q5BGE2; -.
DR   EnsemblFungi; CBF89583; CBF89583; ANIA_00388.
DR   EnsemblFungi; EAA66487; EAA66487; AN0388.2.
DR   GeneID; 2876164; -.
DR   KEGG; ani:AN0388.2; -.
DR   VEuPathDB; FungiDB:AN0388; -.
DR   eggNOG; ENOG502QUI0; Eukaryota.
DR   HOGENOM; CLU_006123_1_0_1; -.
DR   InParanoid; Q5BGE2; -.
DR   OMA; CHDHSIF; -.
DR   OrthoDB; 1430629at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
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:0019568; P:arabinose catabolic process; IMP:AspGD.
DR   GO; GO:0043609; P:regulation of carbon utilization; IMP:AspGD.
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; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..825
FT                   /note="Arabinolytic transcriptional activator araR"
FT                   /id="PRO_0000425612"
FT   DNA_BIND        35..61
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  91031 MW;  3AAA93ADC71B2B1A CRC64;
     MASSHQGNGT VPNSQTDAPP DSSTKRRWRR NRIACDSCHA RRVRCDRQFP CSRCLRSEIT
     CEFTRERRKR GRIARSKLAE MAKNKMETSE TPAPAKTMNG IPAPAGTEIP GHVSPASTFH
     HRSPPANAPT VSAPSVDGRR SQTDPQLPVR RPEIGGNVTE EWLAGTHVSP GSYEFLNGPA
     FGEGLGPFPH MFDVWNGVDL AAYSAGTSQG SKATNAPSTS TAPLKYPVLQ PLMPFVEATL
     PRKLVFDLLD LYFTSAFSTH MHPVSFLSKD APRPSSPALL SSMLWVAALD DRAFSLPISP
     PQRKRICQFL CALTIRLLRP LIHVSFKDQG GAAAAVAAAA AAATNNPAFA GVGQDLPPTT
     VHHPFEGGGD DRGLVGPAGS LDDVITYIHV ASIISSSEQK AASMRWWHAA FTLARELKLN
     QEIEVMPNGD SQVEGSSPPF GYSLPGWDGA DPGPVFNYSN PTRSSLNCVC DRQDQNTITE
     EHREERRRTW WLLYIMDRHL ALCYNRPLAL LDAESEDLLL PLDEASWQSG IIHSNSPKSD
     GPQCLLSADK NKRRLFPNFI CHDHSVFGFF LPLMTITGEL IDLNQARNHP MLGMRLNGKD
     AWNVHVSEVL RQLEIYKASL TTFAATTSDP EAPLSAYAHA QSEHLPAEPS LSQAYAWHTQ
     TVISYASYLV HVLHILLVGK WDPVSLIEDK DFWTSSPAFA STISHALDAA DSVDQILRYD
     PDISFMPYFF GIQLLQGSFL LLLIVERLQK EAGEGILNAC EVMIRATESC VVTLNTEYQR
     NFRQVMRSAV AQARGRPVNH SEIRHRRKAV LALYRWTRKG TGLAL