ID AMDR_EMENI STANDARD; PRT; 765 AA. AC P15699; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE Acetamidase regulatory protein. GN Name=amdR; Synonyms=intA; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=90258911; PubMed=2188110; RA Andrianopoulos A., Hynes M.J.; RT "Sequence and functional analysis of the positively acting regulatory RT gene amdR from Aspergillus nidulans."; RL Mol. Cell. Biol. 10:3194-3203(1990). CC -!- FUNCTION: Positively regulates the expression of 5 genes involved CC in the catabolism of certain amides (amdS), omega amino acids CC (gatA and gabA), and lactams (lamA and lamB) in the presence of CC omega amino acid inducers. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Contains 1 Zn(2)-Cys(6) fungal-type binuclear cluster CC domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M31517; AAA33294.1; -. DR PIR; A36332; A36332. DR TRANSFAC; T00931; -. DR InterPro; IPR007219; Fungal_trans. DR InterPro; IPR001138; Fungi_Trscrp_N. DR Pfam; PF04082; Fungal_trans; 1. DR Pfam; PF00172; Zn_clus; 1. DR PRINTS; PR00054; FUNGALZNCYS. DR SMART; SM00066; GAL4; 1. DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1. DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1. KW Activator; DNA-binding; Metal-binding; Nuclear protein; KW Transcription regulation; Zinc. FT DNA_BIND 20 50 Zn(2)-Cys(6), fungal-type. SQ SEQUENCE 765 AA; 85837 MW; AC50F637E8A69E08 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 PVCTLNLEDS DVSPLTFSDF EGCGARVQAD FVIHFSELCT MISYIVRERF GLRISAERRK AALLEADEAL ANWSLRLPDR LRLRASDMDP WSAMLHLTYN NFLILLHRPH PRASAYSDDY GPHDAEICSA AAGVIASIFE ELRIHDRLKL LWYSGVHTLF TAMIQVRVEL RFSNPVLAIN ALRRFDSASY SLRELAQYWS HASTILRLFE ESRRLQEDLR TTTSDRPRRF SNLSNNSTNS PASQQKNTSG IPHLANINSS DATPPSAPSI PPLQPSSQLS YEVPTTESAH HNPRSQPTLS AHTHTYTTQP FDTWIPSNNL TPMDTVDNSR EMLDWRQLFS FTDLEGPVLP STMEGITELE DEWRQIYWQE TPMSDLLQDG GWMHG //