MIG1_KLUMA
ID MIG1_KLUMA Reviewed; 543 AA.
AC P52288;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Regulatory protein MIG1;
GN Name=MIG1;
OS Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=4911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12424 / NRRL Y-610;
RX PubMed=9230894; DOI=10.1007/s004380050469;
RA Cassart J.-P., Oestling J., Ronne H., Vandenhaute J.;
RT "Comparative analysis in three fungi reveals structurally and functionally
RT conserved regions in the Mig1 repressor.";
RL Mol. Gen. Genet. 255:9-18(1997).
CC -!- FUNCTION: Involved in glucose repression of glucose metabolism genes.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; Z50018; CAA90321.1; -; Genomic_DNA.
DR AlphaFoldDB; P52288; -.
DR SMR; P52288; -.
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; 1.
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..543
FT /note="Regulatory protein MIG1"
FT /id="PRO_0000046880"
FT ZN_FING 32..54
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 60..84
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 59315 MW; DFC01BD92144622F CRC64;
MSSEVVPLQK KGRKKAGAGV VVDGEKDGSR PYMCPICHRG FHRLEHQTRH IRTHTGERPH
ACDFPGCAKR FSRSDELTRH RRIHDSDKPK GKRGRKKKSE TIAREKELEL QRQRQQQQLQ
QQQQQQLQQQ QHQVLPAEIK ISAPMASSMM EVTQAINQRY QDTHNLSLSY NSGSNSNASS
GSNSNSSLNQ VFSITSQPAR DLAAKPMFQL GSDESEETSN TTTLHSVHSQ QQNNGSVELL
LNAARFESEK STTLLNNNTP SFKFIDRPPL TSSLSSPALS LVSQSPVAGA GPGFGPANGN
GNGAANNNGL LLPRPTSRPK LSALSTLKRM TPLSQVSEPQ QPAASLPHLQ QVSSNGFLDT
NGHAASVARN KSWTNLGVMP SPSESGSSAL VSRFSSSASL NKLMDPSSRT SSAVSIATLM
NEDKLQSQDD LSVVDEFGRS RKKSKTSTPI RRPSSNMGFG TGPASHAMEF CNELQSRLKS
VDQYSDRSAG DEKDYYFQSR SSSSVCTPIN SPPSERLVSS TSNNKTIKLP SLRSLDILPR
EQH