PACC_MAGO7
ID PACC_MAGO7 Reviewed; 559 AA.
AC Q52B93; A4RMA1; G4MUA0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=RIM101; ORFNames=MGG_10150;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(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 RIM101 itself) and represses transcription of acid-
CC expressed genes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to DNA. Interacts with RIM20, 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; CM001232; EHA53981.1; -; Genomic_DNA.
DR RefSeq; XP_003713788.1; XM_003713740.1.
DR AlphaFoldDB; Q52B93; -.
DR STRING; 318829.MGG_10150T0; -.
DR EnsemblFungi; MGG_10150T0; MGG_10150T0; MGG_10150.
DR GeneID; 2681777; -.
DR KEGG; mgr:MGG_10150; -.
DR VEuPathDB; FungiDB:MGG_10150; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_012842_1_1_1; -.
DR InParanoid; Q52B93; -.
DR OMA; QWGNCRT; -.
DR OrthoDB; 507875at2759; -.
DR PHI-base; PHI:3701; -.
DR Proteomes; UP000009058; 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; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
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..559
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046837"
FT ZN_FING 52..77
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 88..112
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 118..140
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 430..433
FT /note="YPX[LI] motif 1"
FT MOTIF 553..556
FT /note="YPX[LI] motif 2"
FT COMPBIAS 181..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 60106 MW; C4330081A6624619 CRC64;
MSAQQPSAQP AQQAPATTQA PTTESSSSNS NGNTPAPSTS TTATSQSSDD SLICRWNQCS
ERFPSAEALY DHICERHVGR KSTNNLNLTC HWNSCRTTTV KRDHITSHIR VHVPLKPHKC
DFCGKSFKRP QDLKKHVKTH ADDSVLARSP QDPNANLGPG AYRGHASKAP SSYYDHNGHV
RTNSSAFGQP HHHQNGHASY YSHPPAPYGG GMYYQPPHMG PRGDIFGHPG AGAYDSRKRG
YDDLNDFFGN LKRRQFDASS YAHVGRSLVP LHGALSVHTG GVGGMAAEYM AAPPPSSSVS
MGSAGPLAQH YYLPPMPSLR TKNDLEQIDQ ILEHMQSTVY ENSGSSPGAH YGSGSGYDMR
HQSPVGIRPP MSDHYGQQQH SPMTAVSSSH GGSPAVTPPS SNLSYTSGHS PGASSAALSP
SSRQGSSISY PTLPAAAGSS ATAQLGSNFS SVERRLSGGI LQSASRDRER ESSYDGASTP
RGPESVGSPS ACSDASGSEP ESYDSWVQNM RTIEALRDLV RERLRRGQYD DVEESVNLPP
IKTERPDEEK PLYPSLRMS
