BDF1_SCHPO
ID BDF1_SCHPO Reviewed; 578 AA.
AC Q9Y7N0; Q9UUN2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=SWR1 complex bromodomain subunit bdf1;
GN Name=bdf1; Synonyms=brf1; ORFNames=SPCC1450.02, SPCC191.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; SER-223; SER-224;
RP THR-225; SER-226; SER-239 AND SER-511, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP IDENTIFICATION IN THE SWR1 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT "Chromatin Central: towards the comparative proteome by accurate mapping of
RT the yeast proteomic environment.";
RL Genome Biol. 9:R167.1-R167.22(2008).
CC -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex.
CC {ECO:0000269|PubMed:19040720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAB41059.1; -; Genomic_DNA.
DR PIR; T40984; T40984.
DR RefSeq; NP_588301.2; NM_001023291.2.
DR AlphaFoldDB; Q9Y7N0; -.
DR SMR; Q9Y7N0; -.
DR BioGRID; 275529; 77.
DR STRING; 4896.SPCC1450.02.1; -.
DR iPTMnet; Q9Y7N0; -.
DR MaxQB; Q9Y7N0; -.
DR PaxDb; Q9Y7N0; -.
DR PRIDE; Q9Y7N0; -.
DR EnsemblFungi; SPCC1450.02.1; SPCC1450.02.1:pep; SPCC1450.02.
DR GeneID; 2538955; -.
DR KEGG; spo:SPCC1450.02; -.
DR PomBase; SPCC1450.02; bdf1.
DR VEuPathDB; FungiDB:SPCC1450.02; -.
DR eggNOG; KOG1474; Eukaryota.
DR HOGENOM; CLU_001499_4_2_1; -.
DR InParanoid; Q9Y7N0; -.
DR OMA; CYAFNPD; -.
DR PhylomeDB; Q9Y7N0; -.
DR PRO; PR:Q9Y7N0; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000812; C:Swr1 complex; IDA:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd05498; Bromo_Brdt_II_like; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR043509; Bromo_Brdt_II.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW Activator; Bromodomain; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..578
FT /note="SWR1 complex bromodomain subunit bdf1"
FT /id="PRO_0000211220"
FT DOMAIN 101..173
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 271..343
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 430..510
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 578 AA; 65193 MW; C3FDBE1E094E1BBB CRC64;
MSSESRENEV KAETKDEIAN DGSPQLNGDN NIQSSDGHND ENEESLSRKR DSSGATVGDL
KQEEKESMPK KEPEPTVKKI RGSGMPPPQQ KYCLAIVRQL KRTKNSAPFK VPVDPIKQNI
PDYPTIVKNP MDLGTIEKKL TSYEYSVPQE FIDDMNLMFS NCFLYNGTES PVGSMGKALQ
EVFERQLKQL PDAEQPAAAP VKKSKQKSAS TAPPRTRRNS SVSSTSASVA ASTAPKAASP
AVLPEGKPRR RKNNSQMRFC STVLKELYKR QYESFAFPFY QPVDPVACDC PDYFDVIKEP
MDLSTIQSKL NKNEYSTLEE FESDILLMFN NCFTYNPPGT PVHVMGRQLE NVFKEKWEAR
PKFDDATLVK QQEAETDALF DNGEEEEALM SEEEINGAKF AAVDKQISML QDTLEAMKAK
KMNRMRKPRR RDLTKEYGPI TYAMQNELAE RCNYLSAEQL SNVAEILREE MPWLRDTDEI
EIDVGNMKPE VFHRIYRYVC KPDADSSEPA SPVLMPTKPE KKKGRVLSET EQAEKIRRLQ
QQLDRFAGKT SPTSPESNNA ANVSDSESDN ESESSESA
