ID   PACC_NEUCR              Reviewed;         621 AA.
AC   Q7RVQ8; Q9HFS6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=pH-response transcription factor pacc-1;
GN   Name=pacc-1; ORFNames=NCU00090;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-218.
RX   PubMed=12892641; DOI=10.1016/s1087-1845(03)00051-3;
RA   Nozawa S.R., Ferreira-Nozawa M.S., Martinez-Rossi N.M., Rossi A.;
RT   "The pH-induced glycosylation of secreted phosphatases is mediated in
RT   Aspergillus nidulans by the regulatory gene pacC-dependent pathway.";
RL   Fungal Genet. Biol. 39:286-295(2003).
RN   [3]
RP   ERRATUM OF PUBMED:12892641.
RX   PubMed=14599896; DOI=10.1016/j.fgb.2003.09.005;
RA   Nozawa S.R., Ferreira-Nozawa M.S., Martinez-Rossi N.M., Rossi A.;
RL   Fungal Genet. Biol. 40:287-288(2003).
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-1 itself) and represses transcription of acid-
CC       expressed genes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to DNA. Interacts with palA/prr-1, which binds to the
CC       two 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG17467.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM002238; EAA27978.2; -; Genomic_DNA.
DR   EMBL; AF304568; AAG17467.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_957214.2; XM_952121.3.
DR   PDB; 6P6E; X-ray; 1.99 A; B/C=281-304.
DR   PDBsum; 6P6E; -.
DR   AlphaFoldDB; Q7RVQ8; -.
DR   SMR; Q7RVQ8; -.
DR   STRING; 5141.EFNCRP00000000438; -.
DR   PRIDE; Q7RVQ8; -.
DR   EnsemblFungi; EAA27978; EAA27978; NCU00090.
DR   GeneID; 3873377; -.
DR   KEGG; ncr:NCU00090; -.
DR   VEuPathDB; FungiDB:NCU00090; -.
DR   HOGENOM; CLU_012842_1_1_1; -.
DR   InParanoid; Q7RVQ8; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..621
FT                   /note="pH-response transcription factor pacc-1"
FT                   /id="PRO_0000046838"
FT   ZN_FING         95..120
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         131..155
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         161..183
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           464..467
FT                   /note="YPX[LI] motif 1"
FT   MOTIF           614..617
FT                   /note="YPX[LI] motif 2"
FT   COMPBIAS        29..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        116
FT                   /note="I -> V (in Ref. 2; AAG17467)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="K -> R (in Ref. 2; AAG17467)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   621 AA;  67304 MW;  03A45124D973C2CD CRC64;
     MSSTPAQENG TVNGANAAPA PAPAQTTPTP APATAATPTT APAASANGTA ANAMKPEASS
     NSSNSASNGT TPAPSTTPTT ASNSSAPAAA QDESLVCRWA ECNERFTSAE VLYEHICEKH
     VGRKSTNNLN LTCQWNSCRT TTVKRDHITS HVRVHVPLKP HKCDFCGKCF KRPQDLKKHV
     KTHADDSVLV GRSPQDQNGG MNGAYRAQAP VHKAPSGFYD HNGHMRGTNQ VPFGQPHQNG
     QASYYHAQYP ASQPYHAPMY YPAQTMGGQR NDFTGHQAAP FDARKRQFDD LNDFFGSVKR
     RQINPTSYES VGRALMPLHA PLGLHSGGLA TEYMAQPPHT LGMASAHHPL TQHYYLPPMP
     NLRTKEDLQQ MDHFLEQMQA TVYENTAVDM RHHSPTYATR PSIDPYHGAS LASPLSATSP
     HSAGTPAVTP TPSNMSYTSG HSPSTSSTSL SPTSRHSSTP SVSYPTLPSR PGLPYPSTSG
     LGSNFTHNER RLSGGVLQSA RRAADEADRA PTPKASEQAT VSSPSEDSET GDVNGPETYD
     DWLQHMRVIE YLRQGIRARL ERQDFDEDDT SRIDPMVLES SDRNQQQRNQ QQQQQKSPNE
     PTAAGPSAPE KPLYPVLPRI N