ID   PACC_CRYNB              Reviewed;         917 AA.
AC   P0CS63; Q55J93; Q5KCH0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=pH-response transcription factor pacC/RIM101;
GN   Name=RIM101; OrderedLocusNames=CNBL0920;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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 RIM101 itself) and represses transcription of acid-
CC       expressed genes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to DNA. Interacts with RIM20, which binds to the YPX[LI]
CC       motifs and is required for proteolytic processing (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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; AAEY01000056; EAL17830.1; -; Genomic_DNA.
DR   RefSeq; XP_772477.1; XM_767384.1.
DR   AlphaFoldDB; P0CS63; -.
DR   EnsemblFungi; AAW44985; AAW44985; CNH00970.
DR   EnsemblFungi; EAL17830; EAL17830; CNBL0920.
DR   GeneID; 4939141; -.
DR   KEGG; cnb:CNBL0920; -.
DR   VEuPathDB; FungiDB:CNBL0920; -.
DR   HOGENOM; CLU_317828_0_0_1; -.
DR   PHI-base; PHI:2749; -.
DR   Proteomes; UP000001435; Chromosome 12.
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; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   3: Inferred from homology;
KW   Activator; Coiled coil; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..917
FT                   /note="pH-response transcription factor pacC/RIM101"
FT                   /id="PRO_0000410344"
FT   ZN_FING         67..92
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         103..127
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         133..155
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          873..914
FT                   /evidence="ECO:0000255"
FT   MOTIF           494..497
FT                   /note="YPX[LI] motif"
FT   COMPBIAS        8..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..769
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..789
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..917
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   917 AA;  99165 MW;  378D1551A4DBA3B7 CRC64;
     MAYPTLPPNL LSTPNTYSDS VSPTDPEPIT PELVSREPEK PAQKAAKTAM NNTSTASKPS
     ESKGETLPCK WTGCSHISDS PDELYDHLCT VHVGRKSTNN LCLTCGWENC GTKCVKRDHI
     TSHLRVHTPL KPHPCAVCGK TFKRPQDLKK HERIHTAEHH QLHKLSKAPT TADPEFNSRV
     SLSSATRIDR PRSPLSTSLS PTSTSSHSLH SSSSPFDHLL ATGFHTDKSV SPTPSALALL
     HKKQHEELAA YQQKEMLVLQ QLAFNQQQSQ AYAARLAAEP FGTGAGAKRG QADAFHDLLS
     DVKKRKVEPV YDQDMIHRLN ALVPPSLPTS FPTLPSLGGY NQYQTFPSFN GYPSLPSLHT
     SIYPTTAPQA QYSNQSPLPI PEIKTEADLA MFNEFMISLG RDAAANKAGP HPMTQSASGS
     GASNGYSASN SGTPLSETSG GVEDLFNAEE LASLGLAGMP GISIHSGGSH NSNDESTHSL
     SDASPPAVSF GGLYPSLDAM RNRTNSAPDV SALSGAARRP IAGLPRTSMG NAHNTSTNQS
     TKPSYLSGMF GHSSSQQYDG TTHNYLHGLS NEHHNDYSHS ANNGATNAYA SFDSLARNKQ
     SFPAATLAPK MFHNKVYRDV APLGTAVSKR ARESAERTNV EDSDREELYA DQESNHGYAV
     SNERAREERT PKIPVRSLIA SIRTLSPSTA ADGEDDLKLP AISPSHVEPG TDLPPLYSIQ
     RGGHSSGQYR RASSLSSNST STSGSSSFNS SLAPSNVASG TTTPRGSTPP RGVPTKRHTE
     DEIVRGVKRL ELGPAEPLRS TTPELPDSGT TEQALERDQK PDISALSLSS SPTPPSNNPP
     PSVSTANEEG KDMTIEEMRR RHAALIKSWL VAVNLQWRRK KMEEMQRQQR EEMEELEEGG
     EAMNVDERER ERVEVVA