ID   HIMB_ASPJA              Reviewed;         515 AA.
AC   A0A2Z5TJB0;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Transcription factor himB {ECO:0000303|PubMed:29314577};
DE   AltName: Full=Himeic acid A biosynthesis cluster protein B {ECO:0000303|PubMed:29314577};
GN   Name=himB {ECO:0000303|PubMed:29314577};
OS   Aspergillus japonicus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=34381;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=MF275;
RX   PubMed=29314577; DOI=10.1002/cbic.201700584;
RA   Hashimoto M., Kato H., Katsuki A., Tsukamoto S., Fujii I.;
RT   "Identification of the biosynthetic gene cluster for himeic acid A: a
RT   ubiquitin-activating enzyme (E1) inhibitor in Aspergillus japonicus
RT   MF275.";
RL   ChemBioChem 19:535-539(2018).
CC   -!- FUNCTION: Transcription factor that, with himD, probably co-regulates
CC       the him gene cluster that mediates the biosynthesis of himeic acid A, a
CC       ubiquitin-activating enzyme (E1) inhibitor.
CC       {ECO:0000305|PubMed:29314577}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; LC331673; BBA91559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z5TJB0; -.
DR   SMR; A0A2Z5TJB0; -.
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   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   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..515
FT                   /note="Transcription factor himB"
FT                   /id="PRO_0000445947"
FT   DNA_BIND        22..51
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          62..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..260
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  56243 MW;  6E9E943199F2136A CRC64;
     MPRHERGGSG TSSSDLRLRK ACDRCHAQKL GCQREAIGAK CVRCEKADKP CTWSISLRNR
     RASTRKEQLP VHAQQQQQQQ QQHQHQPQHA TMARNENNEE QAQEDDNDDE DEDILYSDQL
     TPSEAIPELH SPLGDPHNRL ASESLDPTTM PIDLTSFLIS DGGLGLMTPS LTNPGSWLGE
     TQLGTTTTTT TAITTATLIG EPPRFWSSAT GGLPHTPSAG GLTTIDLPPA AFEMNLPGVP
     PSYTPSHQPD QPPPPKTGTP ALSDPQWLKE LFDNNARLYR NWHAVSSNMT TNQTINPLFP
     MSTTSQSHPS SAAFADEAVQ LSTQLIHILR GLLHQHHEST GHRPPTTPKP RARAEDLDPD
     HSGLDPGSLL IVLSSYFRIL EIFTMLSHAL EATAAATGST THYHTPRATP PILRLPAIVV
     GSLDLASNTS LSTVLFLEVI EDLLTTLATL VLSIAQWPSH PHHATSRREP GWQGSDLHAG
     SDRLGLQIQG KEDEIRRVIR AIRARLGRKG DKAGV