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Database: UniProt
Entry: B6K575_SCHJY
LinkDB: B6K575_SCHJY
Original site: B6K575_SCHJY 
ID   B6K575_SCHJY            Unreviewed;       678 AA.
AC   B6K575;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN   Name=clr3 {ECO:0000313|JaponicusDB:SJAG_03844};
GN   ORFNames=SJAG_03844 {ECO:0000313|EMBL:EEB08679.1};
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB08679.1, ECO:0000313|Proteomes:UP000001744};
RN   [1] {ECO:0000313|EMBL:EEB08679.1, ECO:0000313|Proteomes:UP000001744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression
CC       and developmental events. {ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037919};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR037919}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037919}.
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DR   EMBL; KE651167; EEB08679.1; -; Genomic_DNA.
DR   RefSeq; XP_002174972.1; XM_002174936.1.
DR   AlphaFoldDB; B6K575; -.
DR   STRING; 402676.B6K575; -.
DR   ESTHER; schjy-b6k575; Arb2_domain.
DR   EnsemblFungi; EEB08679; EEB08679; SJAG_03844.
DR   GeneID; 7050482; -.
DR   JaponicusDB; SJAG_03844; clr3.
DR   VEuPathDB; FungiDB:SJAG_03844; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_007727_4_0_1; -.
DR   OMA; FVSPACY; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi.
DR   GO; GO:0070823; C:HDA1 complex; IEA:EnsemblFungi.
DR   GO; GO:1990342; C:heterochromatin island; IEA:EnsemblFungi.
DR   GO; GO:0031934; C:mating-type region heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0070824; C:SHREC complex; IEA:EnsemblFungi.
DR   GO; GO:0110129; C:SHREC2 complex; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; IEA:EnsemblFungi.
DR   GO; GO:0090053; P:positive regulation of pericentric heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IEA:EnsemblFungi.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR019154; Arb2-like_domain.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR017321; Hist_deAcase_II_yeast.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR45364:SF10; HISTONE DEACETYLASE; 1.
DR   PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037919};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037919};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037919};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT   DOMAIN          74..378
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          431..676
FT                   /note="Arb2-like"
FT                   /evidence="ECO:0000259|Pfam:PF09757"
SQ   SEQUENCE   678 AA;  75880 MW;  EF454F47A60D4D44 CRC64;
     MLNVPPESEA DPVATVKPSQ LMLSKEVPAE VGHLDSIQDK DVEEQKPDVL NMKSGLCYDP
     RMRFHATLDE VEDHPEDPRR ILQVFEAIKE AGYVSAIPTA RDAFIRIPSR EATLEEILRV
     HSKDVYDMVK SSETMSREEL VNLEKTNDSL YFNNQTFFCA RLASGSAVET CNAVVNGKVK
     NAFAIIRPPG HHSEPNKSGG FCLFNNVAIT ARSMMARYPE QVKRVLILDW DVHHGNGTQM
     AFYDDPNVLY ISLHRYENGR FYPGTTYGSA ENCGEGEGLG KTVNIPWPCA GMSDGDYIYA
     FQKVVMPIGY EFNPDLVIIS AGFDAAAGDP LGQCYLTPAA YAHMTQMLLG LAEGKLFVSM
     EGGYSLSSIS TAGLAVAQTL LGIPPAKLHT VYATAPAVKT VEEVTRIQSR YWKCMRPIFH
     TPPTDYTHVN PLHEVVRAFQ AKKLFDNWQM TILPISRDGL SESYANQALC SNGFFHRKTL
     VLFVHDPPDV LGSSQGNSNL LNLSQSAVVD YAETYIDWCL QQDFGLIDIN VPELLTDADG
     RPYSSTEETK LLCLYIWDNY IELSSAEKII FIGEGRAVPG LIHLVSSRNV STRVKSVITF
     VGTDALCGIK TISNEDVPSW YYKHSLVLVS NGNVCWKKMK RKKKRYGRLV RTEHDHKGEL
     MQQHYESIVQ YMEKILRQ
//
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