位置:首页 > 蛋白库 > ARAR_ASPNC
ARAR_ASPNC
ID   ARAR_ASPNC              Reviewed;         832 AA.
AC   A2QJX5;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Arabinanolytic transcriptional activator araR;
GN   Name=araR; ORFNames=An04g08600;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
RN   [2]
RP   FUNCTION.
RX   PubMed=12724380; DOI=10.1099/mic.0.25993-0;
RA   de Groot M.J., van de Vondervoort P.J., de Vries R.P., vanKuyk P.A.,
RA   Ruijter G.J., Visser J.;
RT   "Isolation and characterization of two specific regulatory Aspergillus
RT   niger mutants shows antagonistic regulation of arabinan and xylan
RT   metabolism.";
RL   Microbiology 149:1183-1191(2003).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
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).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
RX   PubMed=21892241; DOI=10.3114/sim.2011.69.03;
RA   Battaglia E., Visser L., Nijssen A., van Veluw G.J., Woesten H.A.,
RA   de Vries R.P.;
RT   "Analysis of regulation of pentose utilisation in Aspergillus niger reveals
RT   evolutionary adaptations in Eurotiales.";
RL   Stud. Mycol. 69:31-38(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:12724380,
CC       ECO:0000269|PubMed:21484208, ECO:0000269|PubMed:21892241}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- DISRUPTION PHENOTYPE: Reduces growth on L-arabinose, xylitol, arabinan,
CC       Arabic gum, arabinogalactan and apple pectin, and shows poor growth on
CC       L-arabitol. {ECO:0000269|PubMed:21892241}.
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; AM270089; CAK38947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QJX5; -.
DR   PaxDb; A2QJX5; -.
DR   PRIDE; A2QJX5; -.
DR   EnsemblFungi; CAK38947; CAK38947; An04g08600.
DR   VEuPathDB; FungiDB:An04g08600; -.
DR   HOGENOM; CLU_006123_1_0_1; -.
DR   Proteomes; UP000006706; Chromosome 6L.
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; 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..832
FT                   /note="Arabinanolytic transcriptional activator araR"
FT                   /id="PRO_0000425611"
FT   DNA_BIND        38..64
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          84..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   832 AA;  92118 MW;  F753EAA8FB34A337 CRC64;
     MDSAQSGDAQ APNVPAATEE PTGEATTKRR WRRNRIACDS CHSRRVRCDR AFPCSRCLRS
     DIRCEFTRER RKRGRIARSR LVETKTAVEK ASQPVETRDS APAPAEAGSG PVPNGSPSST
     FHHRSPATND VTGSAPSIDE RRSQADVSLP PRKPGHTVNA TEEWLAGTHV SPGSYEPLAG
     IGPGEGPFPR IFDIWNGVDL AGYSDPASQG SKITGLGQTP APSATILKYP VLQPVMPYLE
     SSLPRKLVYD LLDLYFTSAF STHMHPVCHH IHCYVLRKAS FLSREAPRPS SPALLASMLW
     VAALDDRAFA LPISPPQRKK ICQFLCALTL RLLRPLIHVS FKEQEGAAAS DPLHAAVGQD
     GPPTTVHHPF EVGGDDRGLV GPAGSLDDVI TYIHVASIIS SSEQKAASMR WWHAAFTLAR
     ELKLNQEIEV MPSEENHPEG SSPSFDYSLA GWSGVDTGPF FDYSNPARPS LNCVCDRGHE
     LRGAITEEHR EERRRTWWLL YIMDRHLALC YNRPLALLDA ESEDLLLPLD EGSWQSGNIH
     SNSPKPDGPQ CPLSGEKNKR RVFPNFICHD HSIFGFFLPL MTITGELIDL NQARNHPMLG
     ARLNGKDPWD AHVGEVLRQL ELYKASLTTF AATASDPDAP LSSAFPPKPD QQPVEPSLAQ
     AYSWHTQTVI SYASYLVHVL HILLVGKWDP VSLIEDKDFW TSSPAFASTI SHALDAADSV
     DHILRYDPDI SFMPYFFGIQ LLQGSFLLLL IVERLQKEAG EGILNACEVM IRATESCVVT
     LNTEYQRNFR QVMRSAVAQA RGRPVNHSEI RHRRKAVLAL YRWTRKGTGL AL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024