ID   AMDR_EMENI              Reviewed;         798 AA.
AC   P15699; C8V5M9; Q5B5Z5;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Acetamidase regulatory protein;
GN   Name=amdR; Synonyms=intA; ORFNames=AN4035;
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=2188110; DOI=10.1128/mcb.10.6.3194-3203.1990;
RA   Andrianopoulos A., Hynes M.J.;
RT   "Sequence and functional analysis of the positively acting regulatory gene
RT   amdR from Aspergillus nidulans.";
RL   Mol. Cell. Biol. 10:3194-3203(1990).
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: Positively regulates the expression of 5 genes involved in
CC       the catabolism of certain amides (amdS), omega amino acids (gatA and
CC       gabA), and lactams (lamA and lamB) in the presence of omega amino acid
CC       inducers.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33294.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CBF74839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA59506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; M31517; AAA33294.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000065; EAA59506.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001302; CBF74839.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A36332; A36332.
DR   RefSeq; XP_661639.1; XM_656547.1.
DR   AlphaFoldDB; P15699; -.
DR   STRING; 162425.CADANIAP00004647; -.
DR   EnsemblFungi; EAA59506; EAA59506; AN4035.2.
DR   GeneID; 2873450; -.
DR   KEGG; ani:AN4035.2; -.
DR   eggNOG; ENOG502SIAM; Eukaryota.
DR   HOGENOM; CLU_006329_4_0_1; -.
DR   InParanoid; P15699; -.
DR   OrthoDB; 917119at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
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: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   4: Predicted;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..798
FT                   /note="Acetamidase regulatory protein"
FT                   /id="PRO_0000114936"
FT   DNA_BIND        20..50
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          68..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        563..564
FT                   /note="QV -> LL (in Ref. 1; EAA59506)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   798 AA;  90005 MW;  8BB709EF86C50EFA CRC64;
     MSSTAHPTNL APSGNGSAAC VHCHRRKVRC DARLVGLPCS NCRSAGKTDC QIHEKKKKLA
     VRSILDPVPI RCRPPNPEEA PKPISSLSPS SEPPNAFTTA LRAVQSDITA PSGVANRVAH
     IRSRSSQYDT KGTRSNNNSG NNTQYQNVLP EPDSPPYSRP AASDPSEGES RADIEKRLVN
     LIDGEASDSR AIQRGVRAIY VGHELSNMSF LIRQQRDTGD DVYHFAGNEI PRRQLRTGHD
     QLLMDALTLP EPALADELVH AYFAQVNPGY PIVEEELFMS QYRNRDPADA PPILLLQTIL
     LVGAHVTRPK SERDTLKDIF FRRAKWLFDN RIERNRDILV QAALLLTWHS DLADDDVSAN
     AHYWIGIAAR IATGLGMHRN PVCSRFVPRD RRMWRRLWYI LVQFDVMVSL SYGRPQALNL
     EDSDVSPLTF SDFEGCGARV QADFVIHFSE LCTMISYIVR ERFGLRISAE RRKAALLEAD
     EALANWSLRL PDRLRLRASD MDPWSAMLHL TYNNFLILLH RPHPRASAYS DDYGPHDAEI
     CSAAAGVIAS IFEELRIHDR LKQVWYSGVH TLFTAMIQVR VELRFSNPVL AINALRRFDS
     ASYSLRELAQ YWSHASTILR LFEESRRLQE DLRTTTSDRP RRFSNLSNNS TNSPASQQKN
     TSGIPHLANI NSSDATPPSA PSIPPLQPSS QLSYEVPTTE SAHHNPRSQP TLSAHTHTYT
     TQPFDTWIPS NNLTPMDTVD NSREMLDWRQ LFSFTDLEGP VLPSTMEGIT ELEDEWRQIY
     WQETPMSDLL QDGGWMHG