REB1_KLULA
ID REB1_KLULA Reviewed; 595 AA.
AC Q05950; Q6CLB1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=DNA-binding protein REB1;
DE AltName: Full=QBP;
GN Name=REB1; OrderedLocusNames=KLLA0F04389g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8423784; DOI=10.1128/mcb.13.2.1173-1182.1993;
RA Morrow B.E., Ju Q., Warner J.R.;
RT "A bipartite DNA-binding domain in yeast Reb1p.";
RL Mol. Cell. Biol. 13:1173-1182(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: DNA-binding protein that recognizes sites within both the
CC enhancer and the promoter of rRNA transcription, as well as upstream of
CC many genes transcribed by RNA polymerase II. It is essential for cell
CC growth. May stimulate or inhibit transcription. Specifically recognizes
CC the sequence 5'-CCGGGTA-3' or 5'-CGGGTRR-3' (where R is any purine) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; L03789; AAA61343.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG97986.1; -; Genomic_DNA.
DR PIR; A48077; A48077.
DR RefSeq; XP_455278.1; XM_455278.1.
DR AlphaFoldDB; Q05950; -.
DR SMR; Q05950; -.
DR STRING; 28985.XP_455278.1; -.
DR EnsemblFungi; CAG97986; CAG97986; KLLA0_F04389g.
DR GeneID; 2895000; -.
DR KEGG; kla:KLLA0_F04389g; -.
DR eggNOG; KOG0051; Eukaryota.
DR HOGENOM; CLU_016706_0_0_1; -.
DR InParanoid; Q05950; -.
DR OMA; HVRRKYH; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR SMART; SM00717; SANT; 4.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 3: Inferred from homology;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..595
FT /note="DNA-binding protein REB1"
FT /id="PRO_0000197090"
FT DOMAIN 333..384
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 385..490
FT /note="Myb-like"
FT DNA_BIND 360..382
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 25..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 69..70
FT /note="DA -> VV (in Ref. 1; AAA61343)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="A -> R (in Ref. 1; AAA61343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 67953 MW; 15B0D34CB3ACCB7B CRC64;
MSQNDTNHES VEEAVFKYVG VGLEKSGEDD AVNKQKSVDW FLKEQDQDQD QDQDPGRDQD
QEDNAKHRDA NDVSAVAAAA VAAALSVKKR GRPSEQSSTG SSGKGSGSSG QNNKKSKKNK
NKLHLAAVDP ELASLDDNLV DGNDSEEQSH HQLVHKAIMD TDNIASQHPD FQQYLNTEDD
QEPKKEKSEE RSYGDLSNID DHVDDVSVSG SIPSQVRLKK TAEVLPKVLS SESHNDDQQD
DVSNLIQEAA AKASHIINPA TQSNGKSFDE SEEEALEQFI KEYQKIRGLS RRQICERIWS
NERRKDDFWT NICRVLPYRT RSSIYKHVRR KYHIFEQRGK WTPEEDAELA RWCAEKEGQW
SNIGKVLGRM PEDCRDRWRN YVKCGPNRAA NKWSVEEEEK LKNVIHQMLD NASTAYEDGE
DDEMKDSSTK IEDSGDADML DVQDSDKKPS ISNSKKKPAA KDIINWTVVS EQMGGSRSRI
QCRYKWNKLL KKEALNKIKN ISDDDKFWLL TKLRDMGFTE DSQVDWEELS TLMPGRRWTG
TELKLLYEKV RTTVRQYKRK TINVICKELV GYPEASLPLD DEIRQHHSGD DEDKD
