(data stored in ACNUC16935 zone)

SWISSPROT: ALCR_EMENI

ID   ALCR_EMENI              Reviewed;         821 AA.
AC   P21228; C8VL74; Q59DL3; Q5ARV2;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   05-JUL-2017, entry version 119.
DE   RecName: Full=Regulatory protein alcR;
GN   Name=alcR; ORFNames=AN8978;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3072264; DOI=10.1016/0378-1119(88)90503-3;
RA   Felenbok B., Sequeval D., Mathieu M., Sibley S., Gwynne D.I.,
RA   Davies R.W.;
RT   "The ethanol regulon in Aspergillus nidulans: characterization and
RT   sequence of the positive regulatory gene alcR.";
RL   Gene 73:385-396(1988).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RX   PubMed=2053973; DOI=10.1016/0014-5793(91)80193-7;
RA   Kulmburg P., Prange T., Mathieu M., Sequeval D., Scazzocchio C.,
RA   Felenbok B.;
RT   "Correct intron splicing generates a new type of a putative zinc-
RT   binding domain in a transcriptional activator of Aspergillus
RT   nidulans.";
RL   FEBS Lett. 280:11-16(1991).
RN   [3]
RP   ERRATUM.
RA   Kulmburg P., Prange T., Mathieu M., Sequeval D., Scazzocchio C.,
RA   Felenbok B.;
RL   FEBS Lett. 283:166-166(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kocialkowska J., Cochet M.-F., Fillinger S., Felenbok B., Flipphi M.;
RT   "Functional analysis of the Aspergillus nidulans akeP gene provides
RT   evidence for a second regulatory circuit responsive to alcohols,
RT   ketones and esters, independent from the activator of ethanol
RT   utilization, AlcR.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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   [6]
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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [7]
RP   STRUCTURE BY NMR OF 1-60.
RX   PubMed=10656785; DOI=10.1006/jmbi.1999.3417;
RA   Cerdan R., Cahuzac B., Felenbok B., Guittet E.;
RT   "NMR solution structure of AlcR (1-60) provides insight in the unusual
RT   DNA binding properties of this zinc binuclear cluster protein.";
RL   J. Mol. Biol. 295:729-736(2000).
CC   -!- FUNCTION: Positive regulatory protein for the ethanol regulon,
CC       alcA and aldA. It control positively its own expression and
CC       possibly in a negative fashion the expression of the gene coding
CC       for ADH-II.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: By ethanol, threonine and acetaldehyde. Expression is
CC       autoregulated and subject to carbon catabolite repression.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA64310.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF496548; AAQ06627.1; -; Genomic_DNA.
DR   EMBL; AACD01000168; EAA64310.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF84528.1; -; Genomic_DNA.
DR   PIR; JS0076; JS0076.
DR   PIR; S14292; S14292.
DR   RefSeq; XP_682247.1; XM_677155.1.
DR   PDB; 1F4S; NMR; -; P=1-60.
DR   PDB; 1F5E; NMR; -; P=1-63.
DR   PDB; 2ALC; NMR; -; A=1-63.
DR   PDB; 3ALC; NMR; -; A=1-63.
DR   PDBsum; 1F4S; -.
DR   PDBsum; 1F5E; -.
DR   PDBsum; 2ALC; -.
DR   PDBsum; 3ALC; -.
DR   ProteinModelPortal; P21228; -.
DR   SMR; P21228; -.
DR   STRING; 162425.CADANIAP00007877; -.
DR   EnsemblFungi; CADANIAT00007877; CADANIAP00007877; CADANIAG00007877.
DR   EnsemblFungi; EAA64310; EAA64310; AN8978.2.
DR   GeneID; 2868306; -.
DR   KEGG; ani:AN8978.2; -.
DR   HOGENOM; HOG000173158; -.
DR   InParanoid; P21228; -.
DR   OMA; CWLTEVT; -.
DR   OrthoDB; EOG092C1EU2; -.
DR   EvolutionaryTrace; P21228; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IDA:AspGD.
DR   GO; GO:0003677; F:DNA binding; IDA:AspGD.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:AspGD.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:AspGD.
DR   GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IDA:AspGD.
DR   GO; GO:0046187; P:acetaldehyde catabolic process; IEP:AspGD.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:AspGD.
DR   GO; GO:0006068; P:ethanol catabolic process; IEP:AspGD.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:AspGD.
DR   GO; GO:0061414; P:positive regulation of transcription from RNA polymerase II promoter by a nonfermentable carbon source; IBA:GO_Central.
DR   GO; GO:0006567; P:threonine catabolic process; IMP:AspGD.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P21228.
DR   SWISS-2DPAGE; P21228.
KW   3D-structure; Activator; Complete proteome; DNA-binding;
KW   Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN         1    821       Regulatory protein alcR.
FT                                /FTId=PRO_0000114931.
FT   DNA_BIND     12     49       Zn(2)-C6 fungal-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00227}.
FT   METAL        12     12       Zinc 1.
FT   METAL        12     12       Zinc 2.
FT   METAL        15     15       Zinc 1.
FT   METAL        22     22       Zinc 1.
FT   METAL        39     39       Zinc 1.
FT   METAL        39     39       Zinc 2.
FT   METAL        42     42       Zinc 2.
FT   METAL        49     49       Zinc 2.
FT   TURN          2      4       {ECO:0000244|PDB:1F4S}.
FT   STRAND        5      8       {ECO:0000244|PDB:3ALC}.
FT   HELIX        13     18       {ECO:0000244|PDB:1F4S}.
FT   HELIX        28     33       {ECO:0000244|PDB:1F4S}.
FT   HELIX        40     44       {ECO:0000244|PDB:1F4S}.
FT   HELIX        52     57       {ECO:0000244|PDB:1F4S}.
SQ   SEQUENCE   821 AA;  91686 MW;  EF7E783964D1A449 CRC64;
     MADTRRRQNH SCDPCRKGKR RCDAPENRNE ANENGWVSCS NCKRWNKDCT FNWLSSQRSK
     AKGAAPRART KKARTATTTS EPSTSAATIP TPESDNHDAP PVINSHDALP SWTQGLLSHP
     GDLFDFSHSA IPANAEDAAN VQSDAPFPWD LAIPGDFSMG QQLEKPLSPL SFQAVLLPPH
     SPNTDDLIRE LEEQTTDPDS VTDTNSVQQV AQDGSLWSDR QSPLLPENSL CMASDSTARR
     YARSTMTKNL MRIYHDSMEN ALSCWLTEHN CPYSDQISYL PPKQRAEWGP NWSNRMCIRV
     CRLDRVSTSL RGRALSAEED KAAARALHLA IVAFASQWTQ HAQRGAGLNV PADIAADERS
     IRRNAWNEAR HALQHTTGIP SFRVIFANII FSLTQSVLDD DEQHGMGARL DKLLENDGAP
     VFLETANRQL YTFRHKFARM QRRGKAFNRL PGGSVASTFA GIFETPTPSS ESPQLDPVVA
     SEEHRSTLSL MFWLGIMFDT LSAAMYQRPL VVSDEDSQIS SASPPRRGAE TPINLDCWEP
     PRQVPSNQEK SDVWGDLFLR TSDSLPDHES HTQISQPAAR WPCTYEQAAA ALSSATPVKV
     LLYRRVTQLQ TLLYRGASPA RLEAAIQRTL YVYNHWTAKY QPFMQDCVAN HELLPSRIQS
     WYVILDGHWH LAAMLLADVL ESIDRDSYSD INHIDLVTKL RLDNALAVSA LARSSLRGQE
     LDPGKASPMY RHFHDSLTEV AFLVEPWTVV LIHSFAKAAY ILLDCLDLDG QGNALAGYLQ
     LRQNCNYCIR ALQFLGRKSD MAALVAKDLE RGLNGKVDSF L
//

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