CLR6_SCHPO
ID CLR6_SCHPO Reviewed; 405 AA.
AC O59702;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Histone deacetylase clr6;
DE EC=3.5.1.98;
DE AltName: Full=Cryptic loci regulator 6;
GN Name=clr6; ORFNames=SPBC36.05c;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9755190; DOI=10.1093/genetics/150.2.563;
RA Grewal S.I.S., Bonaduce M.J., Klar A.J.S.;
RT "Histone deacetylase homologs regulate epigenetic inheritance of
RT transcriptional silencing and chromosome segregation in fission yeast.";
RL Genetics 150:563-576(1998).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 340-368 AND 381-404, FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12773392; DOI=10.1093/emboj/cdg248;
RA Nakayama J., Xiao G., Noma K., Malikzay A., Bjerling P., Ekwall K.,
RA Kobayashi R., Grewal S.I.S.;
RT "Alp13, an MRG family protein, is a component of fission yeast Clr6 histone
RT deacetylase required for genomic integrity.";
RL EMBO J. 22:2776-2787(2003).
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. Histone deacetylases act via the formation of
CC large multiprotein complexes. Has a role in chromatin assembly and
CC chromosome segregation. {ECO:0000269|PubMed:12773392}.
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 -!- SUBUNIT: Heterotetramer of alp13, clr6, prw1 and pst2.
CC {ECO:0000269|PubMed:12773392}.
CC -!- INTERACTION:
CC O59702; O13919: pst2; NbExp=7; IntAct=EBI-904651, EBI-904686;
CC O59702; Q09819: SPAC16C9.05; NbExp=2; IntAct=EBI-904651, EBI-15632828;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773392}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF064206; AAD05211.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19053.1; -; Genomic_DNA.
DR PIR; T40300; T40300.
DR RefSeq; NP_595333.1; NM_001021241.2.
DR AlphaFoldDB; O59702; -.
DR SMR; O59702; -.
DR BioGRID; 276897; 55.
DR DIP; DIP-29339N; -.
DR IntAct; O59702; 8.
DR STRING; 4896.SPBC36.05c.1; -.
DR MaxQB; O59702; -.
DR PaxDb; O59702; -.
DR EnsemblFungi; SPBC36.05c.1; SPBC36.05c.1:pep; SPBC36.05c.
DR GeneID; 2540368; -.
DR KEGG; spo:SPBC36.05c; -.
DR PomBase; SPBC36.05c; clr6.
DR VEuPathDB; FungiDB:SPBC36.05c; -.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_6_1; -.
DR InParanoid; O59702; -.
DR OMA; FHSEEYM; -.
DR PhylomeDB; O59702; -.
DR Reactome; R-SPO-3214815; HDACs deacetylate histones.
DR Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR PRO; PR:O59702; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:1990483; C:Clr6 histone deacetylase complex I''; IPI:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0033698; C:Rpd3L complex; IDA:PomBase.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; IDA:PomBase.
DR GO; GO:0032221; C:Rpd3S/Clr6-CII complex; IDA:PomBase.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0031078; F:histone deacetylase activity (H3-K14 specific); IMP:PomBase.
DR GO; GO:0032129; F:histone deacetylase activity (H3-K9 specific); IMP:PomBase.
DR GO; GO:0034739; F:histone deacetylase activity (H4-K16 specific); IMP:PomBase.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IMP:PomBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:PomBase.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Direct protein sequencing; Hydrolase; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..405
FT /note="Histone deacetylase clr6"
FT /id="PRO_0000114740"
FT REGION 6..318
FT /note="Histone deacetylase"
FT ACT_SITE 138
FT /evidence="ECO:0000250"
SQ SEQUENCE 405 AA; 46112 MW; 8EDEA43D5839E367 CRC64;
MGFGKKKVSY FYDEDVGNYH YGPQHPMKPH RVRMVHNLVV NYNLYEKLNV ITPVRATRND
MTRCHTDEYI EFLWRVTPDT MEKFQPHQLK FNVGDDCPVF DGLYEFCSIS AGGSIGAAQE
LNSGNAEIAI NWAGGLHHAK KREASGFCYV NDIALAALEL LKYHQRVLYI DIDVHHGDGV
EEFFYTTDRV MTCSFHKFGE YFPGTGHIKD TGIGTGKNYA VNVPLRDGID DESYESVFKP
VISHIMQWFR PEAVILQCGT DSLAGDRLGC FNLSMKGHSM CVDFVKSFNL PMICVGGGGY
TVRNVARVWT YETGLLAGEE LDENLPYNDY LQYYGPDYKL NVLSNNMENH NTRQYLDSIT
SEIIENLRNL SFAPSVQMHK TPGDFTFENA EKQNIAKEEI MDERV
