ID   HMGR_ASPFU              Reviewed;         748 AA.
AC   A4D9U3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Transcription factor hmgR {ECO:0000303|PubMed:22046314};
DE   AltName: Full=L-tyrosine degradation gene cluster protein hmgR {ECO:0000303|PubMed:22046314};
DE   AltName: Full=Pyomelanin biosynthesis cluster protein hmgR {ECO:0000303|PubMed:22046314};
GN   Name=hmgR {ECO:0000303|PubMed:22046314}; ORFNames=AFUA_2G04262;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=19028908; DOI=10.1128/aem.02077-08;
RA   Schmaler-Ripcke J., Sugareva V., Gebhardt P., Winkler R., Kniemeyer O.,
RA   Heinekamp T., Brakhage A.A.;
RT   "Production of pyomelanin, a second type of melanin, via the tyrosine
RT   degradation pathway in Aspergillus fumigatus.";
RL   Appl. Environ. Microbiol. 75:493-503(2009).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22046314; DOI=10.1371/journal.pone.0026604;
RA   Keller S., Macheleidt J., Scherlach K., Schmaler-Ripcke J., Jacobsen I.D.,
RA   Heinekamp T., Brakhage A.A.;
RT   "Pyomelanin formation in Aspergillus fumigatus requires HmgX and the
RT   transcriptional activator HmgR but is dispensable for virulence.";
RL   PLoS ONE 6:e26604-e26604(2011).
CC   -!- FUNCTION: Transcription factor; part of the L-tyrosine degradation gene
CC       cluster that mediates the biosynthesis of the brownish pigment
CC       pyomelanin as an alternative melanin (PubMed:19028908,
CC       PubMed:22046314). Acts as a transcriptional activator for the genes of
CC       the tyrosine degradation cluster (PubMed:22046314).
CC       {ECO:0000269|PubMed:19028908, ECO:0000269|PubMed:22046314}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22046314}.
CC   -!- INDUCTION: Expression is induced by L-tyrosine.
CC       {ECO:0000269|PubMed:22046314}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the expression of all cluster genes
CC       (PubMed:22046314). Impairs growth on L-tyrosine as the sole carbon
CC       source and affects homogentisic acid and pyomelanin formation
CC       (PubMed:19028908). {ECO:0000269|PubMed:19028908,
CC       ECO:0000269|PubMed:22046314}.
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DR   EMBL; AAHF01000008; EBA27314.1; -; Genomic_DNA.
DR   RefSeq; XP_001481652.1; XM_001481602.1.
DR   SMR; A4D9U3; -.
DR   EnsemblFungi; EBA27314; EBA27314; AFUA_2G04262.
DR   GeneID; 5076965; -.
DR   KEGG; afm:AFUA_2G04262; -.
DR   eggNOG; ENOG502QQTI; Eukaryota.
DR   HOGENOM; CLU_007201_2_0_1; -.
DR   InParanoid; A4D9U3; -.
DR   OMA; YHVLPGI; -.
DR   OrthoDB; 842195at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009074; P:aromatic amino acid family catabolic process; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..748
FT                   /note="Transcription factor hmgR"
FT                   /id="PRO_0000453189"
FT   DNA_BIND        24..59
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          108..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   748 AA;  85402 MW;  36C3D36DCAA068CD CRC64;
     MEIRRPSRHG NHPDRTYQRT YKACISCRQR KAKCDLGTGP DGLPLGPPCA KCRREQKPCL
     FDEKRAWERV KKRGTQSTSN LANSMMRTVV SSGNDALNIL FEAANAQSQE DSMIESDSLP
     ETEQHRSGHP VTSEGSSNQI DLTVPPDVLE KAMRPVELSH VSKDVLSTWE ACRFVRMGWF
     TAREAVTFID LFFKNMSILS PVLTDFYADH KNHRWLIAHD PVLCCTILMI SSRYHVLPGV
     GGQSRNFFIH HRLWQHCQQL VTRLIFGQEL SSQPKIRNIG TIEALLLMSD WHPRSLHFPP
     ESDGWDSDLV TIDLESTEYG DDGSNSSAKR WAKDMSEPAK RSDQMSWMLL GSALSLAHEL
     GIYETGDKAR DAFVAYERFM TKDQMRLRRQ RAQRLLYVYI NQLAWRIGCV SLMPQGLSHS
     ILNRQTSREL SQYGEEWLTF MDSWMDLTKL AKSVTDMFFP SVTFARQQLQ SGRYIDLLDH
     FRPLLDKWKE RYLQPQLHDK PFYDDIFIEY HFVRVYTHSV GMQAVVERAI ADGNADEEEV
     RPMNIDPIDY EYIQEVIDGC CQILEKVTQL ADIGALRFSP VRIFVRITSA SIFLMKALSL
     GARQAKLRES LDVLERTIQA LRSNALDDIH LSTRYATLLE THVSRLRRHL VASCKSLKRR
     RESTTRHSMV PPSYASATSD EHAPLITNPP VPQNMSDMGF TPSLNDIAAD DWLSLPFDPS
     MAPFSISSGG QFPAYEGGGL NFLWNLPS