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 03-AUG-2022, entry version 143.
DE RecName: Full=Regulatory protein alcR;
GN Name=alcR; ORFNames=AN8978;
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=3072264; DOI=10.1016/0378-1119(88)90503-3;
RA Felenbok B., Sequeval D., Mathieu M., Sibley S., Gwynne D.I., Davies R.W.;
RT "The ethanol regulon in Aspergillus nidulans: characterization and sequence
RT 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-binding
RT domain in a transcriptional activator of Aspergillus nidulans.";
RL FEBS Lett. 280:11-16(1991).
RN [3]
RP ERRATUM OF PUBMED:2053973.
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, ketones
RT and esters, independent from the activator of ethanol 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., 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 [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., 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 [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 DNA
RT 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, alcA and
CC aldA. It control positively its own expression and possibly in a
CC negative fashion the expression of the gene coding 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};
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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 AlphaFoldDB; P21228; -.
DR SMR; P21228; -.
DR STRING; 162425.CADANIAP00007877; -.
DR EnsemblFungi; CBF84528; CBF84528; ANIA_08978.
DR EnsemblFungi; EAA64310; EAA64310; AN8978.2.
DR GeneID; 2868306; -.
DR KEGG; ani:AN8978.2; -.
DR VEuPathDB; FungiDB:AN8978; -.
DR eggNOG; ENOG502SHX1; Eukaryota.
DR HOGENOM; CLU_006237_0_0_1; -.
DR InParanoid; P21228; -.
DR OMA; PRWPCSY; -.
DR OrthoDB; 274391at2759; -.
DR EvolutionaryTrace; P21228; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0003677; F:DNA binding; IDA:AspGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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; 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 by RNA polymerase II; IDA:AspGD.
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 InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
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;
KW 3D-structure; Activator; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..821
FT /note="Regulatory protein alcR"
FT /id="PRO_0000114931"
FT DNA_BIND 12..49
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:1F4S"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3ALC"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:1F4S"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:1F4S"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:1F4S"
FT HELIX 52..57
FT /evidence="ECO:0007829|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
