QUTA_EMENI
ID QUTA_EMENI Reviewed; 825 AA.
AC P10563; C8VTB3; Q5BE96;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Quinic acid utilization activator;
GN Name=qutA; ORFNames=AN1134;
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].
RX PubMed=3313276; DOI=10.1093/nar/15.19.7991;
RA Beri R.K., Whittington H., Roberts C.F., Hawkins A.R.;
RT "Isolation and characterization of the positively acting regulatory gene
RT QUTA from Aspergillus nidulans.";
RL Nucleic Acids Res. 15:7991-8001(1987).
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).
CC -!- FUNCTION: Transcription activation of genes for enzymes and proteins of
CC quinate metabolism by binding to a 16 base-pair sequence (consensus 5'-
CC GGATAANNNNTTATCC-3') in front of each qut gene.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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; X06252; CAA29594.1; -; Genomic_DNA.
DR EMBL; AACD01000016; EAA66252.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF88076.1; -; Genomic_DNA.
DR PIR; A26983; A26983.
DR RefSeq; XP_658738.1; XM_653646.1.
DR AlphaFoldDB; P10563; -.
DR SMR; P10563; -.
DR STRING; 162425.CADANIAP00001495; -.
DR PRIDE; P10563; -.
DR EnsemblFungi; CBF88076; CBF88076; ANIA_01134.
DR EnsemblFungi; EAA66252; EAA66252; AN1134.2.
DR GeneID; 2876901; -.
DR KEGG; ani:AN1134.2; -.
DR VEuPathDB; FungiDB:AN1134; -.
DR eggNOG; ENOG502S3FG; Eukaryota.
DR HOGENOM; CLU_007607_1_1_1; -.
DR InParanoid; P10563; -.
DR OMA; QPEFMQN; -.
DR OrthoDB; 263891at2759; -.
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:0003700; F:DNA-binding transcription factor activity; IMP:AspGD.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:AspGD.
DR GO; GO:0019631; P:quinate catabolic process; 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 4: Predicted;
KW Activator; DNA-binding; Metal-binding; Nucleus; Quinate metabolism;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..825
FT /note="Quinic acid utilization activator"
FT /id="PRO_0000114970"
FT DNA_BIND 49..76
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 444
FT /note="L -> V (in Ref. 1; CAA29594)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="A -> P (in Ref. 1; CAA29594)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="E -> Q (in Ref. 1; CAA29594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 825 AA; 90398 MW; D94C11571C3C3416 CRC64;
MSSDTRQTSG GNARSKRRLT DAVDEDGRPT ATAEDPTSNP KRQRVSRACD SCRSKKDKCD
GAQPICSTCA SLSRPCTYRA NPKKRGLPTG YIRTLELLWG LVFNKIQGSE EVVRTLLRAA
NIPSHLATMG KESEGSDTLL SSWKNSIVLK EIERLLTFLE QPEGDQERSA RGEIDSPADA
EESSVLSPET LEWQLPDSIA VASQSPLASG PSPVRLPRPS TTRLVRDSGT QTIPLGEIED
LTTNGSSHDR PVIASNSARE EHRLPPNPWP LLDIYFSYTQ CWFPILEKHD ILRTAFRQGD
DDQYNSPSAA GDNAALWAVL ALASIQQTSI STTRQLSDLP EDRPDPDQLY AKARSLIPTE
SGTYQLGHIQ ALLILSLIKL GQQDCAAAWM LVGQAVRSAQ SLGLNDPSDA TGVEKTAGRS
KHVFLGCFVL ETLVAAKLGL LPSLRKTDLT KVGLINEDGL EEWHPWEDQT GLRPIESSRS
FQRGPLHALS TFNRLLSLMC ILNELCCVRQ TPANSMSYLG TLERQLQLWV SALPTSYRID
LQTVSTKPAS PHIFGLEMMY EAVATAISLQ LAVQKNERNG LRRASEGSKR LVSLLQAYME
TYSLSATCPT FGIALTLGLP LPCMKKTAPW AFEASHGINH KLQSFSAHLA TVWIHNTGSQ
RRPRHATQQG THPRSPMAIS LPGNNMRLTN LIEESRTGNL STTDSYLSPT WMRTSNDENA
VLSLPTPASS LNIASGVETN PTSQQITHQH RSSVVGKPNS ALIMSDLTTP FPASGHHYQQ
TYDDASLHFN SLADIESTSS AQRPRIAPDL DALFDELASL DGTDR