ID   PACC_ASPNG              Reviewed;         667 AA.
AC   Q00203;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=pH-response transcription factor pacC/RIM101;
GN   Name=PACC;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=8602152; DOI=10.1007/bf02174395;
RA   MacCabe A.P., van den Hombergh J.P.T.W., Tilburn J., Arst H.N. Jr.,
RA   Visser J.;
RT   "Identification, cloning and analysis of the Aspergillus niger gene pacC, a
RT   wide domain regulatory gene responsive to ambient pH.";
RL   Mol. Gen. Genet. 250:367-374(1996).
CC   -!- FUNCTION: Transcription factor that mediates regulation of both
CC       acid- and alkaline-expressed genes in response to ambient pH. At
CC       alkaline ambient pH, activates transcription of alkaline-expressed
CC       genes (including PACC itself) and represses transcription of acid-
CC       expressed genes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- INDUCTION: By alkaline conditions. {ECO:0000269|PubMed:8602152}.
CC   -!- PTM: Activated by C-terminal proteolytic cleavage by signaling protease
CC       (probably palB/RIM13) at neutral to alkaline ambient pH. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}.
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DR   EMBL; X98417; CAA67063.1; -; Genomic_DNA.
DR   PIR; S63587; S63587.
DR   AlphaFoldDB; Q00203; -.
DR   STRING; 5061.CADANGAP00002242; -.
DR   VEuPathDB; FungiDB:An02g07890; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1184997; -.
DR   VEuPathDB; FungiDB:ATCC64974_56280; -.
DR   VEuPathDB; FungiDB:M747DRAFT_260517; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   2: Evidence at transcript level;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..667
FT                   /note="pH-response transcription factor pacC/RIM101"
FT                   /id="PRO_0000046821"
FT   ZN_FING         70..95
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         106..130
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         136..158
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           450..453
FT                   /note="YPX[LI] motif 1"
FT   MOTIF           652..655
FT                   /note="YPX[LI] motif 2"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  70901 MW;  01B3E6CCC73C822B CRC64;
     MSEPQDTTTA PSTTAAPMPT STSQDSPSAQ QPAQVSSATA ASAAATAAAA SAAVANPPMN
     GTTTRPSEEL SCLWQGCSEK CPSPEALYEH VCERHVGRKS TNNLNLTCQW GSCRTTTVKR
     DHITSHIRVH VPLKPHKCDF CGKAFKRPQD LKKHVKTHAD DSVLVRSPEP GARNPDMMFG
     GGAKGYATAA HYFEPALNAV PSQGYAHGAP QYYQSHPPPQ PANPSYGNVY YALNHGPEAG
     HASYESKKRG YDALNEFFGD LKRRQFDPNS YAAVGQRLLG LQSLSLPVLS SGPLPEYQPM
     PAPVAVGGGG YSPGGAPSAP AYHLPPMSNV RTKNDLINID QFLQQMQDTI YENDDNVAAA
     GVAQPGAHYV HGGMSYRTTH SPPTQLPPSH ATATSSASMM PNPATHSPST GTPALTPPSS
     AQSYTSGRSP VSLPSATRVS PPHHEGGSMY PRLPSATMAD SMAAGYPTAS STAPPSTLGG
     IFDHDDRRRY TGGTLQRARP ETRQLSEEMD LTQDSKDEGE RTPKAKEHSS PSSPERISAS
     LIDPALSGTA AEAEATLRTA QAATEVAERA DVQWVEKVRL IEYLRNYIAS RLERGEFENN
     ESGGGNSSSN GSSHEQTPEA SPDTHMEGVE SEVPSKAEEP AVKPEAGDVV MYPTLRAVDE
     DGDSKMP