ID   BYE1_YEAS7              Reviewed;         594 AA.
AC   A6ZZW1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Transcription factor BYE1;
DE   AltName: Full=Bypass of ESS1 protein 1;
GN   Name=BYE1; ORFNames=SCY_3371;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Negative regulator of transcription elongation.
CC   -!- SUBUNIT: Interacts with the RNA polymerase RPB1 subunit and
CC       specifically with the trimethylated H3 histone H3K4me3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00651}.
CC   -!- DOMAIN: The PHD domain is involved in the binding to H3K4me3.
CC   -!- SIMILARITY: Belongs to the BYE1 family. {ECO:0000305}.
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DR   EMBL; AAFW02000152; EDN59904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZZW1; -.
DR   SMR; A6ZZW1; -.
DR   EnsemblFungi; EDN59904; EDN59904; SCY_3371.
DR   HOGENOM; CLU_495285_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.472.30; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR003618; TFIIS_cen_dom.
DR   InterPro; IPR036575; TFIIS_cen_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF07744; SPOC; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00510; TFS2M; 1.
DR   SUPFAM; SSF46942; SSF46942; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..594
FT                   /note="Transcription factor BYE1"
FT                   /id="PRO_0000324852"
FT   DOMAIN          254..365
FT                   /note="TFIIS central"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT   ZN_FING         72..134
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36106"
SQ   SEQUENCE   594 AA;  67917 MW;  17EEC437FD939594 CRC64;
     MSVRTSSRSN KGQNKYIEYL LQEETEAPKK KRTKKKVDSA TEKNKKSDSS QEPRKDTENV
     RTDEVDEADE GYVRCLCGAN NENYDAAEYS HGDMVQCDGC DTWQHIKCMT DGKDTIDGLM
     SEDSKYYCEL CDPSLYAHLE TSKEAEVSED EDYHDDVYKP VNDHDDNDAD VFLDEESPRK
     RKRSPDSAKG IHIKSKQVKK SNGSKKRNKS IDAAKSDTAE NEMPTRKDFE SEKEHKLRYN
     AEKMFSTLFS KFIVPETIEA KLYELPDGKD VISISQEFAH NLEEELYKAC LNIEFGTLDK
     IYTEKVRSLY SNLKDKKNLE LKAHVVEGKL PLNKLVNMNA SELANPDLQE FKEKRDKVIL
     ENFIVEVPDK PMYVKTHKGD ELIEDIAEPQ EDILYSKDSI RLHNIDSIDS DKSKIEQTHA
     ISKEPSPSTI INEESLNCAF LYPGLGLEFT GYLNYIGVSQ KLRRDIFKEA IGDGKLYVEG
     RLPTTTAAPY LKEISCSRAI LVYQLFPSND SESKTTFADV VDSLENKGRI AGIKPKTRYE
     KDFYIVPSKG GEIPEILKDI LGSHNDERSE RFSRMKSDER TLFAFVVVKQ EFIH