ID   MIG1_CANAX              Reviewed;         574 AA.
AC   Q9Y7G2;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Regulatory protein MIG1;
GN   Name=MIG1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10629176; DOI=10.1128/jb.182.2.320-326.2000;
RA   Zaragoza O., Rodriguez C., Gancedo C.;
RT   "Isolation of the MIG1 gene from Candida albicans and effects of its
RT   disruption on catabolite repression.";
RL   J. Bacteriol. 182:320-326(2000).
CC   -!- FUNCTION: Involved in glucose repression of glucose metabolism genes.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AJ238242; CAB41348.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y7G2; -.
DR   SMR; Q9Y7G2; -.
DR   VEuPathDB; FungiDB:C5_02940C_A; -.
DR   VEuPathDB; FungiDB:CAWG_04675; -.
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   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
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   Carbohydrate metabolism; DNA-binding; Metal-binding; Nucleus; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..574
FT                   /note="Regulatory protein MIG1"
FT                   /id="PRO_0000046878"
FT   ZN_FING         31..53
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         59..83
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  63143 MW;  93C6E15704D9CC57 CRC64;
     MSMSTHMPTP TPSDTKKMPP KEKKNKDDRP YKCTFCDKAF HRLEHQTRHI RTHTGEKPHA
     CTFPGCVKRF SRSDELTRHL RIHTNPSSRK RKNKNQNMMI NPNATTATTT GPAGMAIPTS
     NLPPGSYAIP NTAIPFSIDR NGNHVYHQPY PVYFVPHANG YMQPMVQTQG VTVVPNTDQQ
     QHQQQQQYHQ QQQQYQFQER PQHQQQQQTN IGTNNHLQQN GSAVFSLPSS PTMASAQTPN
     SGTSSSSESI KLAPLSIPNN ISRPQQQQQQ QQQQQQIPKS ESSTSLYSDG NKLFSRPNST
     LHSLGSSPEN NNASGPLSGV PTPSFSNLND YFQQKSNSNN SRLFNASSSS LSSLSGKIRS
     SSSTNLAGLQ RLTPLTSTTN NTNNTTTSNT NNNNMTKPSI IPKQPSSTSL NLEFYNGNNQ
     QQQNYHTHKK SRPNSPSQTP IHLSSSRKSA NNSFIISPNE TPLQTPLQSP QLKPYQDQPP
     TNVNINVSAP SDTFIGTAVT EKLNNISSIA GNGTQLPPIR SVLSFTSLVD YPDPKQKNVA
     PPVVDTTNVA RGETNGSNGN NSNAKPMSLT NLLS