ID   PACC_ASHGO              Reviewed;         432 AA.
AC   Q753Y2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=pH-response transcription factor pacC/RIM101;
GN   Name=RIM101; OrderedLocusNames=AFR190C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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 palB/RIM101 itself) and represses transcription of
CC       acid-expressed genes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to DNA. Interacts with RIM20, which binds to the two
CC       YPX[LI] motifs and is required for proteolytic processing (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- PTM: Activated by C-terminal proteolytic cleavage by signaling protease
CC       (probably 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; AE016819; AAS53561.1; -; Genomic_DNA.
DR   RefSeq; NP_985737.1; NM_211091.1.
DR   AlphaFoldDB; Q753Y2; -.
DR   STRING; 33169.AAS53561; -.
DR   EnsemblFungi; AAS53561; AAS53561; AGOS_AFR190C.
DR   GeneID; 4621995; -.
DR   KEGG; ago:AGOS_AFR190C; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_029652_0_0_1; -.
DR   InParanoid; Q753Y2; -.
DR   OMA; NCHWGSC; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0071469; P:cellular response to alkaline pH; IEA:EnsemblFungi.
DR   GO; GO:0071454; P:cellular response to anoxia; IEA:EnsemblFungi.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:EnsemblFungi.
DR   GO; GO:0010973; P:positive regulation of division septum assembly; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..432
FT                   /note="pH-response transcription factor pacC/RIM101"
FT                   /id="PRO_0000046818"
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          22..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           296..299
FT                   /note="YPX[LI] motif 1"
FT                   /evidence="ECO:0000255"
FT   MOTIF           427..430
FT                   /note="YPX[LI] motif 2"
FT   COMPBIAS        43..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  48344 MW;  27FC2FD0CA6FBDCE CRC64;
     MSHINHLLNS DEAIPSTALR SCAQRSPMSS DDELVGTAGY RENQPVPGST LPTSPSDVST
     DTENDEHQRL LCQWDACGSE FSQPELLYHH LCQDHVGRKS QRNLQLNCHW GSCTTKTVKR
     DHITSHLRVH VPLKPFSCST CSRKFKRPQD LKKHLKVHME DTMKERSRAA PGSRGVRKTG
     VNKGSALQEK ARTLPNLTVE SFVSQEMQNY YPYYKSRQHL DETLSHIILP PPAALGGTLA
     SEPPSYTRKA VSFFTTLSQD MSRRLPSLAP CNSPGPAGKM VMLPRPEQQY ARVPRYPAMP
     ELPPLVTSPG AESHALPRGH NFRPAPLIPG SMLPSLSRFS HDKSQFVARN SYSLNQKASL
     NEELCENELD IALENLALDD TDALRAELQT VNIIKDYLTC LLLEDVYTES FELPASVEKS
     HSTLRKYPQI KV