PACC_ASPGI
ID PACC_ASPGI Reviewed; 678 AA.
AC Q5XL24;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=pacC;
OS Aspergillus giganteus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5060;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Meyer V.;
RT "Putative transcription factor PacC of Aspergillus giganteus.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; AY763122; AAV28549.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5XL24; -.
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; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..678
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046820"
FT ZN_FING 83..108
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 119..143
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 149..171
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 462..465
FT /note="YPX[LI] motif 1"
FT MOTIF 662..665
FT /note="YPX[LI] motif 2"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 72618 MW; F3E76B82ECFFAB2D CRC64;
MSEHQDNNNN NTAATAASPS STVAPVPTPV PQEQLSSQLP APAAPAPVSA ATPVPSVTAT
AAAATAAVAS PPMNGSPRPS EELSCLWQGC SEKCSSAEAL YEHICERHVG RKSTNNLNLT
CQWGSCRTTT VKRDHITSHI RVHVPLKPHK CEFCGKAFKR PQDLKKHVKT HADDSVLVRS
PEPGSRNPDM MFPGGGKGYA AAAHYFEPSL NPVPSQAYGH GAPQYYQAHP PPQPANPSYG
NVYYALNHGH DGHASYESKK RGYDALNEFF GDLKRRQFDL HSYAAVGQRL LGLQNLSLPI
LAGGPLPEYQ PMPAPVAVGG GYSPGGHGPP VYHLPPMSNV RTKNDLLNID QFLQQMQETI
YENDDHVAAA GVAQPGAHYV HGGMSYRTTH SPPSQLPPSH ATATTSAATM MSHPATHSPS
TGTPALTPPS SAQSYTSGRS PISMSSAHRV SPPHHDGGSG MYPRLPSATM ADSMTAGYPT
TSSAAPPSTL GGIFDDDRRR YTGGTLQRAR PEERRLSVDM DIRQDGKEVG DRTPTGKEAG
SQSASPVRIS ANLIDPALHS NSSSDAESAL RTAQAATEVA ERTDSQWVEK VRLLEYLRNY
IASRLDRGEY DADARRALAR HSPEMRHDGH MEGVETSHTL TKPEEPAASP AIRSLSDDSV
MYPTLRGLGG DEDTKMHS