ID   PACC_FUSO4              Reviewed;         609 AA.
AC   Q870A3; J9MH66;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=pH-response transcription factor pacC/RIM101;
GN   Name=pacC; ORFNames=FOXG_02222;
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DNA-BINDING, INDUCTION, AND
RP   PROTEOLYTIC PROCESSING.
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
RX   PubMed=12694620; DOI=10.1046/j.1365-2958.2003.03465.x;
RA   Caracuel Z., Roncero M.I.G., Espeso E.A., Gonzalez-Verdejo C.I.,
RA   Garcia-Maceira F.I., Di Pietro A.;
RT   "The pH signalling transcription factor PacC controls virulence in the
RT   plant pathogen Fusarium oxysporum.";
RL   Mol. Microbiol. 48:765-779(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
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. Specifically recognizes and binds the consensus
CC       sequence 5'-GCCARG-3'. May act as a negative regulator of virulence to
CC       plants. {ECO:0000269|PubMed:12694620}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- INDUCTION: By alkaline conditions and during infection of tomato roots.
CC       {ECO:0000269|PubMed:12694620}.
CC   -!- PTM: Activated by C-terminal proteolytic cleavage. At neutral to
CC       alkaline ambient pH, the signaling protease cleaves pacC within the
CC       conserved 24-residue signaling protease box. In an ambient pH-
CC       independent reaction, the processing protease (probably the proteasome)
CC       removes additional C-terminal residues to yield the functional form.
CC       {ECO:0000269|PubMed:12694620}.
CC   -!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}.
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DR   EMBL; AY125958; AAM95700.1; -; Genomic_DNA.
DR   EMBL; AAXH01000132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q870A3; -.
DR   STRING; 426428.Q870A3; -.
DR   PHI-base; PHI:315; -.
DR   PHI-base; PHI:7241; -.
DR   Proteomes; UP000009097; Unplaced.
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; 3.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..609
FT                   /note="pH-response transcription factor pacC/RIM101"
FT                   /id="PRO_0000046833"
FT   ZN_FING         61..86
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         97..121
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         127..149
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           447..450
FT                   /note="YPX[LI] motif 1"
FT   MOTIF           601..604
FT                   /note="YPX[LI] motif 2"
FT   COMPBIAS        7..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  65832 MW;  AEE68CBD0B50CED6 CRC64;
     MSPPAPEQKP QLQQQQQQGS SSGDSSSGSA NDSKSVTPAP SATSNTSQSS TAPSTSSDDN
     LICRWNACNQ KFPAPEALYE HICERHVGRK STNNLNLTCQ WNSCRTTTVK RDHITSHIRV
     HVPLKPHKCE FCGKSFKRPQ DLKKHVKTHA DDSVLVRPSQ DPQGGLNYRP QPPKGPSSYY
     DHTGQMRTNA AAFAHQAGHP SGGYYAPQPS TNYGLYFNQP PINNARTEHL GYSAAAGGYD
     RKRTYDMVDD FFGSAKRRQI DPSSYAQIGR SLMPLHGNLS VPNGPMTATE QYMPQPAPAP
     VHAGPTPSKT PSAQQYYLPM PSARTQKDLI HIDTILGQMQ DTIYENANHA TAGVHIHHAE
     NGFNGYRNTP SPPTSHRSPT GMHVGADGYQ PVSAASMASP LTAISSTGTP AVTASSSMSY
     TSGHSPSPSS SAMSPQSRHG STASVMYPTL PTSLPAVSQG FGHSATTTLG PSFDGSERRR
     YSGGMLQRAR AGPLPLPHED TSGASTPKAS ESALSVGSPS SESDVSDATR EREEQYDRWL
     ENMRVIETLR EYVRGRLERK EFVDDNESPR SSHSDAMDVD PKSPQAPPRE LGTPREGSSL
     YPILRMPGA