PACC_ASPPA
ID PACC_ASPPA Reviewed; 662 AA.
AC Q96UW0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=pacC;
OS Aspergillus parasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5067;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90816 / SK1;
RA Pinero D., Keller N.P.;
RT "Isolation and characterization of the Aspergillus parasiticus pacC gene.";
RL Submitted (AUG-2001) 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; AF408430; AAK98616.1; -; Genomic_DNA.
DR AlphaFoldDB; Q96UW0; -.
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; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
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..662
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046823"
FT ZN_FING 68..93
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 104..128
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 134..156
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 450..453
FT /note="YPX[LI] motif 1"
FT MOTIF 646..649
FT /note="YPX[LI] motif 2"
FT COMPBIAS 376..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 70854 MW; F6EE8740F410078B CRC64;
MSEPQDTTSP STAAAPITAS TSQEQSQTQS PPQVSATTTS SVTATAAAAT AAVASPPVNG
AARPTEELSC LWQGCSEKCP TPESLYEHVC ERHVGRKSTN NLNLTCQWGS CRTTTVKRDH
ITSHIRVHVP LKLHKCDFCG KAFKRPQDLK KHVKTHADDS VLVRSPEPGS RNPDIMFGGN
PAKGYATATH YFEPALNPVP SQGYAHGAPQ YYQAHHPPQP ANPSYGNVYY ALNHGHEAGH
ASYESKKRGY DALNEFFGDL KRRQFDPNSY AAVGQRLLGL QSLSLPILSG GPLPEYQPMP
APVAVGGGGY SPGGHPPAPA YHLPPMSNVR TKNDLINIDQ FLQQMQDTIY ENDDNVAAAG
VAQPGAHYVH GGMSYRTTHS PPSQLPPSHA TATTSAGPMM ANPATHSPTG TPALTPPSSA
QSYTSGRSPI SLPSTSRVSP PHHEGGSSMY PRLPSATMPD SMTAGYPTTS SAAPPSTLGG
IFDHDDRRRY TGGTLQRARP EERHLPEPMD LSHDNKDDGE RTPPAKPRQA PSSPGRISAS
LIDPALSGSA NEAETMRTAQ AATEVAERSD VQWVEKVRLI EYLRNYIASR LERGEYDGDS
GMTRESRTPE AGPDGHMEGV ETEPVSHPAK SESPVKPEAG GDTVMYPTLR GVDEDGDSKM
PN