PACC_USTMA
ID PACC_USTMA Reviewed; 827 AA.
AC Q6H8R9; A0A0D1DTY7; Q4P6I9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 3.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=PACC; ORFNames=UMAG_10426;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 201384 / FB2;
RX PubMed=15947192; DOI=10.1128/ec.4.6.999-1008.2005;
RA Arechiga-Carvajal E.T., Ruiz-Herrera J.;
RT "The RIM101/pacC homologue from the basidiomycete Ustilago maydis is
RT functional in multiple pH-sensitive phenomena.";
RL Eukaryot. Cell 4:999-1008(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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). Not required for the pH-induced
CC dimorphic transition. {ECO:0000250, ECO:0000269|PubMed:15947192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Activated by C-terminal proteolytic cleavage by signaling protease
CC at neutral to alkaline ambient pH. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}.
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DR EMBL; AJ748125; CAG34353.1; -; Genomic_DNA.
DR EMBL; CM003151; KIS67779.1; -; Genomic_DNA.
DR RefSeq; XP_011390778.1; XM_011392476.1.
DR AlphaFoldDB; Q6H8R9; -.
DR STRING; 5270.UM04274P0; -.
DR EnsemblFungi; KIS67779; KIS67779; UMAG_10426.
DR GeneID; 23566463; -.
DR KEGG; uma:UMAG_10426; -.
DR VEuPathDB; FungiDB:UMAG_10426; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_354964_0_0_1; -.
DR InParanoid; Q6H8R9; -.
DR OrthoDB; 677041at2759; -.
DR Proteomes; UP000000561; Chromosome 12.
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; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
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..827
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046845"
FT ZN_FING 66..91
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 102..126
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 132..154
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 88598 MW; EFF06FD9C9957C8A CRC64;
MNHLSPAAAS EHSSYATSSS HIAASPAPSH QSSATSFSSS SPSPSAKMNA SASSDSADFE
PPAKPITCRW DDCGKIFYDP EVVYKHLCDD HVGRKSTNNL CLTCKWEGCD VSCAKRDHIT
SHIRVHTPLK PHNCDACGKT FKRPQDLKKH ERIHTEQHQQ QRQQKAAQNA AARAYSMSEH
ATAFGGAYPY PPQLHAANAY LGYPQLPTQH GLYPSASTYP SAYPSLPPTS DYHYAHSTPS
ASLSPMSSRI DTPQGSSPAP NHHQHQHPHH HAQDAASYIH LASGLDPRSK VTTDPTSYTY
LAHGATTSQN LAGSKRGHEQ VEHFFGDLRR KKMAPAYDSH MAERLTQTFG MGGIDDVSLN
AILSAFDPSA TYSQTPSNPS VKPDSASATR PALKQEPTDL AQLNSFLLQL GASAASFGSS
LSSASSSASS SFSSQGNNAD FDLSSLSQYG LNNIPGFDES LLATHNTNAA GRAIAQLPSR
AHSHFPDALL SHQVHQPAYD SVRFSRGAAV VPQLAPMDAG GHSYRRVEAL TRAAPDERVA
RPDVHRVSVK SEHADDDDAM EEDELEDDGS RVSSRFRSIS PAASSESGWS EAGAGAGAGG
RCGSSSSSPS HGLYPRVSPT EASRRLPPIR SNSSTASSSA SISSPIDSDR RATQRRNSDS
LDGPLSRHSA PAASPSSPSM SETSLASTNS LYPSLVDRVS QMQGLGRSSD EANAEALRRK
HVQLIRDLLI AINFPDRARA KLRADHDRVR LPPILSSVAR RRTEEGEVTP SAADELVSAS
CSDASTDRNS TPTPPGRPTL PTLSQLLNDL PGRPSRPMDE REMECDV
