RIA1_USTMD
ID RIA1_USTMD Reviewed; 381 AA.
AC A0A0U2WFX7;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Regulator of itaconic acid biosynthesis {ECO:0000303|PubMed:26639528};
DE AltName: Full=Itaconic acid/2-hydroxyparaconate biosynthesis cluster protein RIA1 {ECO:0000305};
GN Name=RIA1 {ECO:0000303|PubMed:26639528}; ORFNames=UMAG_05080;
OS Ustilago maydis (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=5270;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=MB215;
RX PubMed=26639528; DOI=10.1111/1751-7915.12329;
RA Geiser E., Przybilla S.K., Friedrich A., Buckel W., Wierckx N., Blank L.M.,
RA Boelker M.;
RT "Ustilago maydis produces itaconic acid via the unusual intermediate trans-
RT aconitate.";
RL Microb. Biotechnol. 9:116-126(2016).
RN [2]
RP FUNCTION.
RX PubMed=27750034; DOI=10.1016/j.ymben.2016.10.006;
RA Geiser E., Przybilla S.K., Engel M., Kleineberg W., Buettner L.,
RA Sarikaya E., Hartog T.D., Klankermayer J., Leitner W., Boelker M.,
RA Blank L.M., Wierckx N.;
RT "Genetic and biochemical insights into the itaconate pathway of Ustilago
RT maydis enable enhanced production.";
RL Metab. Eng. 38:427-435(2016).
CC -!- FUNCTION: Transcription factor that specifically regulates the
CC expression of the gene cluster that mediates the biosynthesis of
CC itaconic acid and 2-hydroxyparaconate (PubMed:26639528,).
CC {ECO:0000269|PubMed:26639528}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of itaconic acid
CC (PubMed:26639528). {ECO:0000269|PubMed:26639528}.
CC -!- CAUTION: Contains a degenerate basic motif not likely to bind DNA.
CC {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR EMBL; KT852988; ALS30795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2WFX7; -.
DR VEuPathDB; FungiDB:UMAG_05080; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 3: Inferred from homology;
KW Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..381
FT /note="Regulator of itaconic acid biosynthesis"
FT /id="PRO_0000438680"
FT DOMAIN 90..142
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 81..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..103
FT /note="Basic motif; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 104..142
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 212..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 41513 MW; 0B7320E319747E9A CRC64;
MRFAGMSCDD ERPANMFDLM APQLASTSCN EHYFSTADLG ASTLYATTTD APATIAGILT
PQPATLAPMY STCPVRFDDQ RSAPASTSVS GKRKHSDVEK DRRRSISNGF AVLQNVLHNE
SNAKPISKSI LLQQACDEIR ELRKKLDAST TIISRFGLEN LFVPTPSSTH ASPPNASSRI
YSPINQASDV LADTRRASIS TSATPILYSE EKRKANAKRR HSYDGSWQAS DRGSIDDEAS
ASASASASAS SSASCSSSSH THSDDTDCDD TDTDIPAESA LKERTKRHKA RSKKERDRTK
PRYRPKPSTN RSPTPSSCAS STPNSPPTSS NRNRDLQQAI LSLLLELPSH LEDVKNKRRA
SQPTELADPS SVKSRSKKRH R