ID   PRTT_ASPFC              Reviewed;         696 AA.
AC   B0Y6K1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Transcriptional activator of proteases prtT;
DE   AltName: Full=Zn(2)-C6 zinc finger-containing protein prtT;
GN   Name=prtT; ORFNames=AFUB_067240;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Transcription factor required for protein utilization and
CC       degradation. Regulates transcription of major secreted proteases
CC       including a serine alkaline protease (alk1), a metalloprotease (mep),
CC       an aspergillopepsin (pep1), a sedolisin (sed2) and two dipeptidyl-
CC       peptidases (dppIV and dppV) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- SIMILARITY: Belongs to the prtT family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS499598; EDP50386.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y6K1; -.
DR   PRIDE; B0Y6K1; -.
DR   EnsemblFungi; EDP50386; EDP50386; AFUB_067240.
DR   HOGENOM; CLU_030102_0_0_1; -.
DR   PhylomeDB; B0Y6K1; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
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   GO; GO:0008152; P:metabolic process; IEA:UniProt.
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; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..696
FT                   /note="Transcriptional activator of proteases prtT"
FT                   /id="PRO_0000407031"
FT   DNA_BIND        136..165
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          106..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  78917 MW;  C4C446A1BBD059A9 CRC64;
     MMHIQTLRKI TILDVQDKQR CLSTNQNVPD NVFQLIACWC YFPPFLSIAK IKPLIALKAG
     ISENPVLIGC RRIKMAHCPY SEAMTRTTSV EDVKFEIPAW DNSNVDVADG SGRPESSTSG
     DTIRPKGRIR RSMTACNTCR KLKTRCDLDP RGHACRRCLS LRIECKLPET AERFQDNASM
     WSDATAAIPS IEERLISLER SMTEMTSMMR RMMDRSPSIS GSSVSMLTRS GITDETASIE
     GSQSSSFAPR PIRLLQDLQS DFTGEANVLP ADSRSLGDLF TKGIIDPKLS QKLIQLFVDH
     FGIWISVDNP SDIHNELRAT DPLLYSTACL LASRYVPGIP LSVIHAMYLQ IRHATVNVLW
     NKTPLKHETL QALALLALWP TAVQKETPMD SWLLSGISIN HAIISFDFLN HAPSDLIVDN
     DMVAKLRVWN ALCLTQLQSA IGNARPFHIQ QRYLEHCPRL LEHPAATFED GKIVAEIQLY
     LIALKLQNFS HRMRLGDFEY EEIERWKMEW AHLLKLSLWY CQLLLYRTAM RFHWESEHLI
     SEILRNSRLI LSKFLLVRFP NALAFPDQIY YIVGYAALNL CDFSPMDPLI DQVQTFLLHL
     SPNEDHIAYR FSYTITELKR RCATGPNPHN VVKGAFGDTR KLSMGQQIPF MNPLMDTMMG
     EYGGLEHLIP EVPPNSLPDM LTSVAGELQA FRTAIL