BYE1_PICGU
ID BYE1_PICGU Reviewed; 752 AA.
AC A5DDB7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Transcription factor BYE1;
GN Name=BYE1; ORFNames=PGUG_01268;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Negative regulator of transcription elongation.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00651}.
CC -!- SIMILARITY: Belongs to the BYE1 family. {ECO:0000305}.
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DR EMBL; CH408156; EDK37170.2; -; Genomic_DNA.
DR RefSeq; XP_001485597.1; XM_001485547.1.
DR AlphaFoldDB; A5DDB7; -.
DR SMR; A5DDB7; -.
DR STRING; 4929.XP_001485597.1; -.
DR EnsemblFungi; EDK37170; EDK37170; PGUG_01268.
DR GeneID; 5127740; -.
DR KEGG; pgu:PGUG_01268; -.
DR VEuPathDB; FungiDB:PGUG_01268; -.
DR eggNOG; KOG1634; Eukaryota.
DR HOGENOM; CLU_370099_0_0_1; -.
DR InParanoid; A5DDB7; -.
DR OMA; RTHKGDI; -.
DR OrthoDB; 1022991at2759; -.
DR Proteomes; UP000001997; 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; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..752
FT /note="Transcription factor BYE1"
FT /id="PRO_0000324850"
FT DOMAIN 160..283
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 81..139
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..373
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 84699 MW; 6BBA2D857757B096 CRC64;
MQPRKSARSN KGQHSQWSLQ DVLRQEQDDD VNSEPRRKKS KVESDSDDVY DDAGEVANAS
SENDDDDDDD NNNDKNEEDG EVRCTPCGAN KDNYDEETDE GGTMIECDKC HTWQHAKCMG
YRNERSIPKK YMCNLCQESK SETKKKPEKE QTTPGYSFTL RDKTRISVAK AFFGVFHKNI
PPASLPDGID AVMMATKWAQ ELEAEVFKVF PSKDKHYTDK SRGLMVLIKK ENVMRRISTG
ELSFYDLVNS SPEEIDEDLK VYAEKVRQES IRRSVLTVDE GSQRIRRTHK GEEIVEDANR
QSEEADVNVV PRNIDHRRIK EDSPPREIIT NSESQTYYHN EEDDDDDEQA EADGEESNKD
DVNEDSSDSD DDELDMILKD KKDENKEEVE VRQQPAKPAP VPAKKPSFEK ESAEVWKGEI
VFPDFASFSA VAELKSCTNY VEPSDSQTAR NFSRFIKVGK ELLSRKKHEV EGRLDKNRAD
DYLNKVVSSR DFYLIEIKPT ANHPDYDKLY GYLLDREKVG VLSGKPSFAK DSYLITLEKS
RPLPPYLSTL KGFEQSTGLF ALYVVRKGYV PAAPSILKNR SSYNVPAPIP PTNSNHHSKP
MLPQPPAMAA KPKTPLLDSI LSTLGGAQAN PVPKPQPIPQ QNHQFQQPHF QHQPSGAYNR
VPSLPGKPNL PSKPTFGSNA SNAPNYNKQH QTSDLNLSGD QMRYLQELVK NNPQQARHEP
QALVGMAANS GASFGGSGLP AGDDDDEFPT YN
