AREA_EMENI
ID AREA_EMENI Reviewed; 876 AA.
AC P17429; C8VA54; Q5ASR3;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Nitrogen regulatory protein areA;
GN Name=areA; ORFNames=AN8667;
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], AND FUNCTION.
RX PubMed=1970293; DOI=10.1002/j.1460-2075.1990.tb08250.x;
RA Kudla B., Caddick M.X., Langdon T., Martinez-Rossi N.M., Bennett C.F.,
RA Sibley S., Davies R.W., Arst H.N. Jr.;
RT "The regulatory gene areA mediating nitrogen metabolite repression in
RT Aspergillus nidulans. Mutations affecting specificity of gene activation
RT alter a loop residue of a putative zinc finger.";
RL EMBO J. 9:1355-1364(1990).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=8596437; DOI=10.1111/j.1365-2958.1995.mmi_17050877.x;
RA Langdon T., Seerins A., Ravagnani A., Caddick M.X., Arst H.N. Jr.;
RT "Mutational analysis reveals dispensability of the N-terminal region of the
RT Aspergillus transcription factor mediating nitrogen metabolite
RT repression.";
RL Mol. Microbiol. 17:877-888(1995).
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH NMRA.
RX PubMed=12764138; DOI=10.1074/jbc.m304104200;
RA Lamb H.K., Leslie K., Dodds A.L., Nutley M., Cooper A., Johnson C.,
RA Thompson P., Stammers D.K., Hawkins A.R.;
RT "The negative transcriptional regulator NmrA discriminates between oxidized
RT and reduced dinucleotides.";
RL J. Biol. Chem. 278:32107-32114(2003).
RN [6]
RP INTERACTION WITH NMRA, AND DNA-BINDING.
RX PubMed=15537757; DOI=10.1110/ps.04958904;
RA Lamb H.K., Ren J., Park A., Johnson C., Leslie K., Cocklin S., Thompson P.,
RA Mee C., Cooper A., Stammers D.K., Hawkins A.R.;
RT "Modulation of the ligand binding properties of the transcription repressor
RT NmrA by GATA-containing DNA and site-directed mutagenesis.";
RL Protein Sci. 13:3127-3138(2004).
RN [7]
RP INDUCTION BY NITROGEN.
RX PubMed=17854403; DOI=10.1111/j.1365-2958.2007.05940.x;
RA Wong K.H., Hynes M.J., Todd R.B., Davis M.A.;
RT "Transcriptional control of nmrA by the bZIP transcription factor MeaB
RT reveals a new level of nitrogen regulation in Aspergillus nidulans.";
RL Mol. Microbiol. 66:534-551(2007).
RN [8]
RP STRUCTURE BY NMR OF 663-727 IN COMPLEX WITH DNA, AND DNA-BINDING.
RX PubMed=9533883; DOI=10.1006/jmbi.1998.1625;
RA Starich M.R., Wikstroem M., Arst H.N. Jr., Clore G.M., Gronenborn A.M.;
RT "The solution structure of a fungal AREA protein-DNA complex: an
RT alternative binding mode for the basic carboxyl tail of GATA factors.";
RL J. Mol. Biol. 277:605-620(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 670-712 IN COMPLEX WITH NMRA.
RX PubMed=18602114; DOI=10.1016/j.jmb.2008.05.077;
RA Kotaka M., Johnson C., Lamb H.K., Hawkins A.R., Ren J., Stammers D.K.;
RT "Structural analysis of the recognition of the negative regulator NmrA and
RT DNA by the zinc finger from the GATA-type transcription factor AreA.";
RL J. Mol. Biol. 381:373-382(2008).
CC -!- FUNCTION: Transcription activator that binds the consensus DNA element
CC 5'-CGATAG-3' and mediates nitrogen metabolite repression. Activates the
CC transcription of uapA. {ECO:0000269|PubMed:1970293}.
CC -!- SUBUNIT: Interacts with nmrA. {ECO:0000269|PubMed:12764138,
CC ECO:0000269|PubMed:15537757, ECO:0000269|PubMed:18602114,
CC ECO:0000269|PubMed:9533883}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: Down-regulated in nitrogen-sufficient conditions and up-
CC regulated in nitrogen-limiting conditions.
CC {ECO:0000269|PubMed:17854403}.
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DR EMBL; X52491; CAA36731.1; -; Genomic_DNA.
DR EMBL; AACD01000158; EAA60701.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF78221.1; -; Genomic_DNA.
DR PIR; A57988; A57988.
DR RefSeq; XP_681936.1; XM_676844.1.
DR PDB; 2VUS; X-ray; 2.60 A; I/J/K/L/M/N/O/P=670-712.
DR PDB; 2VUT; X-ray; 2.30 A; I/J/K/L/M/N/O/P=670-712.
DR PDB; 2VUU; X-ray; 2.80 A; I/J/K/L/M/N/O/P=670-712.
DR PDB; 4GAT; NMR; -; A=663-727.
DR PDB; 5GAT; NMR; -; A=663-727.
DR PDB; 6GAT; NMR; -; A=663-727.
DR PDB; 7GAT; NMR; -; A=663-727.
DR PDBsum; 2VUS; -.
DR PDBsum; 2VUT; -.
DR PDBsum; 2VUU; -.
DR PDBsum; 4GAT; -.
DR PDBsum; 5GAT; -.
DR PDBsum; 6GAT; -.
DR PDBsum; 7GAT; -.
DR AlphaFoldDB; P17429; -.
DR BMRB; P17429; -.
DR SMR; P17429; -.
DR STRING; 162425.CADANIAP00006378; -.
DR PRIDE; P17429; -.
DR EnsemblFungi; CBF78221; CBF78221; ANIA_08667.
DR EnsemblFungi; EAA60701; EAA60701; AN8667.2.
DR GeneID; 2868505; -.
DR KEGG; ani:AN8667.2; -.
DR VEuPathDB; FungiDB:AN8667; -.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_009509_0_0_1; -.
DR InParanoid; P17429; -.
DR OMA; WRMMAMS; -.
DR OrthoDB; 124231at2759; -.
DR EvolutionaryTrace; P17429; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:AspGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000821; P:regulation of arginine metabolic process; IMP:AspGD.
DR GO; GO:0034251; P:regulation of cellular amide catabolic process; IMP:AspGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:AspGD.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IMP:AspGD.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR013860; AreA_GATA.
DR InterPro; IPR011420; AreA_N.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 1.
DR Pfam; PF07573; AreA_N; 1.
DR Pfam; PF08550; DUF1752; 1.
DR Pfam; PF00320; GATA; 1.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 1.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Metal-binding; Nitrate assimilation;
KW Nucleus; Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..876
FT /note="Nitrogen regulatory protein areA"
FT /id="PRO_0000083465"
FT ZN_FING 673..697
FT /note="GATA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT DNA_BIND 721..742
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:4GAT"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:2VUT"
FT STRAND 682..686
FT /evidence="ECO:0007829|PDB:2VUS"
FT TURN 688..690
FT /evidence="ECO:0007829|PDB:4GAT"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:2VUS"
FT HELIX 695..704
FT /evidence="ECO:0007829|PDB:2VUT"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:4GAT"
SQ SEQUENCE 876 AA; 94196 MW; 9ADC2273EE536F98 CRC64;
MSGLTLGGGS GRVRPTQAAA AFPTSHDFAD PDRSSVARNA NRPSRRFAAP PQLSDDFSLE
SPTDSAQVHD NLLQDALFPE WKANSPRGVD SPDEMQKKDP LATQIWKLYS RTKAQLPNQE
RMENLTWRMM ALSLRRQERE RAQQQARASS QKSPVPGMSG IAQLRLSDRV SNTPTTTADT
VSDAMNLDDF IIPFSPSDHP SPSTTKASEA TTGAIPIKAR RDQSASEATP VPASFPHPAQ
DQRRESEFGY VPRRVRKTSI DERQFFNLQI PSRKRPAESS PHVPPVSTSM LAHDPDFSHA
VPEYTLDTSH GLSLQNQMNA QQLANAQNHT SPNMAFALDT FNLGDDPILP SAGPYQQQFT
FSPSESPMTS GNPFANLYAQ TPIASSLNST DFFSPPPSGY QSTASTPQPA YDGEHSKYFD
MPVDARSQRR VVPAYITQRS SNLSASLQPR YMYNQGGSSQ DITQQNAHMG AQSSSMQSPG
FSIPQHVDPT QVLNPNEFNG NHAAMFSFGA DSDVEDDDGN QFSAGGLAMP AEFGDDSISD
MNSNMAWETS YPNSFQSLPA FAAQHRKHVT IGSADMMDTP SEWNQGGSLG RTHESAASVS
EVRNRDQDPR RQKIARTSST PNTAQLLRQS MQNQSSHTSP NTPPESGLNS AAPSRPASPG
GTKNGEQNGP TTCTNCFTQT TPLWRRNPEG QPLCNACGLF LKLHGVVRPL SLKTDVIKKR
NRNSANSLAV GSSRVSKKSA RKNSVQQVTP TAPTSSRAQS NTTSESPPAM PGSSGRGSGV
VPIAAAPPKS SSAATTSPGT NNGCGAVQVA PKRQRRLEKA SDVDMAESPS STSSGGRSKV
VPLAPAMPPA AVNPANHSIA AGQGASQEWE WLTMSL
