PACC_ASPOR
ID PACC_ASPOR Reviewed; 662 AA.
AC Q9HFB3; Q2UKL6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=pacC; ORFNames=AO090003000758;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RA Sano M., Machida M.;
RT "Cloning of a genomic DNA for pacC from Aspergillus oryzae.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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 pacC itself) and represses transcription of acid-
CC expressed genes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to DNA. Interacts with palA, 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 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; AB035899; BAB20756.1; -; Genomic_DNA.
DR EMBL; AP007155; BAE57899.1; -; Genomic_DNA.
DR RefSeq; XP_001819901.1; XM_001819849.2.
DR AlphaFoldDB; Q9HFB3; -.
DR STRING; 510516.Q9HFB3; -.
DR EnsemblFungi; BAE57899; BAE57899; AO090003000758.
DR GeneID; 5991884; -.
DR KEGG; aor:AO090003000758; -.
DR VEuPathDB; FungiDB:AO090003000758; -.
DR HOGENOM; CLU_012842_1_0_1; -.
DR OMA; QWGNCRT; -.
DR Proteomes; UP000006564; Chromosome 2.
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; 2.
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..662
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046822"
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..43
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 597..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 597..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 271
FT /note="A -> T (in Ref. 1; BAB20756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 70801 MW; A30E387B1796C9D0 CRC64;
MSEPQDTTSP STAAAPIAAS TSHEQPQTQS PPQVSATTTS SVTATAAAAT AAVASPPVNG
AARPTEELSC LWQGCSEKCP TPESLYEHVC ERHVGRKSTN NLNLTCQWGS CRTTTVKRDH
ITSHIRVHVP LKPHKCDFCG KAFKRPQDLK KHVKTHADDS VLVRSPEPGS RNPDIMFGGN
PAKGYATATH YFEPALNPVP SQGYAHGAPQ YYQSHHPPQP ANPSYGNVYY ALNHGHEAGH
ASYESKKRGY DALNEFFGDL KRRQFDPNSY AAVGQRLLGL QSLSLPILSG GPLPEYQPMP
APVAVGGGGY SPGGHPPAPA YHLPPMSNVR TKNDLINIDQ FLQQMQDTIY ENDDNVAAAG
VAQPGAHYVH GGMSYRTTHS PPSQLPPSHA TATTSAGPIM ANPATHSPTG TPALTPPSSA
QSYTSGRSPI SLPSTSRVSP PHHEGGSSMY PRLPSATMSD SMAAGYPTTS SAAPPSTLGG
IFDHDDRRRY TGGTLQRARP EERHLPEPMD LSHDNKDDGE RTPPAKPRQA PSSPGRISAS
LIDPALSGSA NEAETMRTAQ AATEVAERSD VQWVEKVRLI EYLRNYIASR LERGEYDGDS
GMTRESRTPE AGPDGHMEGV ETEPVSHPAK CESPVKPEAG GDTVMYPTLR GVDEDGDSKM
PN
