RUA1_USTMA
ID RUA1_USTMA Reviewed; 757 AA.
AC A0A0D1DMJ6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Transcription regulator rua1 {ECO:0000303|PubMed:17850255};
DE AltName: Full=Regulator of ustilagic acid production 1 {ECO:0000303|PubMed:17850255};
DE AltName: Full=Ustilagic acid biosynthesis cluster protein rua1 {ECO:0000303|PubMed:17850255};
GN Name=rua1 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_06458;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=17850255; DOI=10.1111/j.1365-2958.2007.05941.x;
RA Teichmann B., Linne U., Hewald S., Marahiel M.A., Boelker M.;
RT "A biosynthetic gene cluster for a secreted cellobiose lipid with
RT antifungal activity from Ustilago maydis.";
RL Mol. Microbiol. 66:525-533(2007).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, SUBCELLULAR LOCATION, INDUCTION,
RP DNA-BINDING, AND MUTAGENESIS OF CYS-748.
RX PubMed=20173069; DOI=10.1128/aem.02211-09;
RA Teichmann B., Liu L., Schink K.O., Boelker M.;
RT "Activation of the ustilagic acid biosynthesis gene cluster in Ustilago
RT maydis by the C2H2 zinc finger transcription factor Rua1.";
RL Appl. Environ. Microbiol. 76:2633-2640(2010).
CC -!- FUNCTION: Transcription factor; part of the gene cluster that mediates
CC the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA)
CC (PubMed:17850255, PubMed:20173069). UA is a secreted cellobiose
CC glycolipid that is toxic for many microorganisms and confers biocontrol
CC activity to U.maydis (PubMed:17850255). Recognizes and binds to the
CC specific 5'-T/G-G/T-C-G-C-A-T-A/T-C/T-C/T-G/A-3' upstream activating
CC sequence found in all promoters of the UA biosynthesis genes
CC (PubMed:20173069). {ECO:0000269|PubMed:17850255,
CC ECO:0000269|PubMed:20173069}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20173069}.
CC -!- INDUCTION: Expression is strongly induced under conditions of nitrogen
CC starvation. {ECO:0000269|PubMed:17850255, ECO:0000269|PubMed:20173069}.
CC -!- DISRUPTION PHENOTYPE: Results in complete loss of ustilagic acid
CC production. {ECO:0000269|PubMed:20173069}.
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DR EMBL; CM003162; KIS65754.1; -; Genomic_DNA.
DR RefSeq; XP_011392726.1; XM_011394424.1.
DR AlphaFoldDB; A0A0D1DMJ6; -.
DR EnsemblFungi; KIS65754; KIS65754; UMAG_06458.
DR GeneID; 23566040; -.
DR KEGG; uma:UMAG_06458; -.
DR VEuPathDB; FungiDB:UMAG_06458; -.
DR eggNOG; ENOG502TE7K; Eukaryota.
DR OrthoDB; 1426427at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR028012; Rua1_C.
DR Pfam; PF14616; DUF4451; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..757
FT /note="Transcription regulator rua1"
FT /id="PRO_0000452755"
FT ZN_FING 661..692
FT /note="C2H2-type 1 degenerate"
FT /evidence="ECO:0000305|PubMed:20173069"
FT ZN_FING 717..750
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000305|PubMed:20173069"
FT REGION 122..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 748
FT /note="C->R: Abolishes the nitrogen-dependent transcription
FT of the cluster and impairs the production of ustilagic
FT acid."
FT /evidence="ECO:0000269|PubMed:20173069"
SQ SEQUENCE 757 AA; 82461 MW; CEA9B643B111A998 CRC64;
MMPISATIDS KSFPFDTTPT YASLDAYQMD QRALPTSPFN GAVKRDQMFD QLLLDPPSPT
TSRFDGMWPT SNAQANASSS WTPSAGMPDA FDGVGNSLVN DASSDWSDFL MPLLATVATD
FSSGSATKSE PSTCSSSTDF SMSSTADAST APQHSSSGDS SMSSGLPVST ATCTAMPAAQ
NHQVTTQDAS VQPKLEKQCQ PPSHNVNQQN AFASSNQDNN CPQVHIIASW LDQDADRNTG
HRQHNRHQKQ QNLPQGQSCT NSGSSSRQVT RPNSPNHQRS RPQLRSRSST GNGYTWPSVD
PQVFLWAAFM MNGFQQAQAG TATASPMSDY SAMEYDDEPQ AQHGYHATEN CNVDDAMDGT
GDFCKKEDRS QSADCGLLPR PPSNSPEPHP YPLDPMAAFA RAAAESMAMS YSWPMPMPTN
MMELQHNPAR SNSTFGRVSQ RHHQPPPSHR QRSRTSASSI SNTNAAHRKH KVDAVRQSAV
RSRRQSFVEP RQCASQSPSS PSESTAATDA KLTKPRAQSA GRSHVTERLP HLHTLSYSTP
PDTSSSVSAL TSTTTTTVST GASSVASSIS GPSSASSGIG NASGSLSFTI TDKIVLKPRP
GSGDEELAYP CATNSLLEMQ NNEGPIVDAQ QQAEEAVEKV QNLFPSDLYA PRFTRRGTCG
REGWCSLCPQ GEWYSMKRSQ YLYHMQFDHG ISNLTRRLFH PPQTLRVWND AVSKTDGLCH
HCNKWIPICF GPQRKRDFKA WFKHARKCHR DDTGCPI
