ID   PACC_PENCH              Reviewed;         643 AA.
AC   Q01864;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=pH-response transcription factor pacC/RIM101;
GN   Name=PACC;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DNA-BINDING, AND INDUCTION.
RC   STRAIN=ATCC 9480 / CBS 307.48 / NRRL 1951 / GB8 / QM 941;
RX   PubMed=8736532; DOI=10.1046/j.1365-2958.1996.5421065.x;
RA   Suarez T., Penalva M.A.;
RT   "Characterization of a Penicillium chrysogenum gene encoding a PacC
RT   transcription factor and its binding sites in the divergent pcbAB-pcbC
RT   promoter of the penicillin biosynthetic cluster.";
RL   Mol. Microbiol. 20:529-540(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. Specifically recognizes and binds the consensus
CC       sequence 5'-GCCARG-3'. {ECO:0000269|PubMed:8736532}.
CC   -!- SUBUNIT: Binds to DNA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- INDUCTION: By alkaline conditions. {ECO:0000269|PubMed:8736532}.
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}.
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; U44726; AAC36492.1; -; Genomic_DNA.
DR   PIR; JC6017; JC6017.
DR   AlphaFoldDB; Q01864; -.
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   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..643
FT                   /note="pH-response transcription factor pacC/RIM101"
FT                   /id="PRO_0000046840"
FT   ZN_FING         58..83
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         94..118
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         124..146
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          139..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           435..438
FT                   /note="YPX[LI] motif 1"
FT   MOTIF           625..628
FT                   /note="YPX[LI] motif 2"
FT   COMPBIAS        139..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  68823 MW;  0BBA037FDE189765 CRC64;
     MTENHTPSTT QPTLPAPVAE AAPIQANPAP SASVTATAAA ATAAVNNAPS MNGAGEQLPC
     QWVGCTEKSP TAESLYEHVC ERHVGRKSTN NLNLTCQWGT CNTTTVKRDH ITSHIRVHVP
     LKPHKCDFCG KAFKRPQDLK KHVKTHADDS EIRSPEPGMK HPDMMFPQNP RGSPAATHYF
     ESPINGINGQ YSHAPPPQYY QPHPPPQAPN PHSYGNLYYA LSQGQEGGHP YDRKRGYDAL
     NEFFGDLKRR QFDPNSYAAV GQRLLGLQAL QLPFLSGPAP EYQQMPAPVA VGGGGGGYGG
     GAPQPPGYHL PPMSNVRTKN DLINIDQFLE QMQNTIYESD ENVAAAGVAQ PGAHYVHGGM
     NHRTTHSPPT HSRQATLLQL PSAPMAAATA HSPSVGTPAL TPPSSAQSYT SNRSPISLHS
     SRVSPPHEEA APGMYPRLPA AICADSMTAG YPTASGAAPP STLSGAYDHD DRRRYTGGTL
     QRARPAERAA TEDRMDISQD SKHDGERTPK AMHISASLID PALSGTSSDP EQESAKRTAA
     TATEVAERDV NVAWVEKVRL LENLRRLVSG LLEAGSLTPE YGVQTSSASP TPGLDAMEGV
     ETASVRAASE QAREEPKSES EGVFYPTLRG VDEDEDGDSK MPE