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   14-DEC-2011, entry version 87.
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;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   MEDLINE=98429513; PubMed=9755190;
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
RT   yeast.";
RL   Genetics 150:563-576(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=22658054; 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
RT   histone deacetylase required for genomic integrity.";
RL   EMBO J. 22:2776-2787(2003).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Has a role in
CC       chromatin assembly and chromosome segregation.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Heterotetramer of alp13, clr6, prw1 and pst2.
CC   -!- INTERACTION:
CC       O13919:pst2; NbExp=5; IntAct=EBI-904651, EBI-904686;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily.
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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_001021241.1.
DR   ProteinModelPortal; O59702; -.
DR   DIP; DIP-29339N; -.
DR   IntAct; O59702; 4.
DR   STRING; O59702; -.
DR   EnsemblFungi; SPBC36.05c.1; SPBC36.05c.1:pep; SPBC36.05c.
DR   GeneID; 2540368; -.
DR   GenomeReviews; CU329671_GR; clr6.
DR   KEGG; spo:SPBC36.05c; -.
DR   NMPDR; fig|4896.1.peg.1199; -.
DR   GeneDB_Spombe; SPBC36.05c; -.
DR   eggNOG; fuNOG05981; -.
DR   GeneTree; EFGT00050000000513; -.
DR   HOGENOM; HBG396919; -.
DR   OMA; QHGCDTH; -.
DR   OrthoDB; EOG4RV60J; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-003413-MONOMER; -.
DR   ArrayExpress; O59702; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_Spombe.
DR   GO; GO:0033698; C:Rpd3L complex; IDA:GeneDB_Spombe.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; IDA:GeneDB_Spombe.
DR   GO; GO:0032221; C:Rpd3S complex; IDA:GeneDB_Spombe.
DR   GO; GO:0034739; F:histone deacetylase activity (H3-K16 specific); IEA:EC.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:EC.
DR   GO; GO:0046969; F:NAD-dependent histone deacetylase activity (H3-K9 specific); IEA:EC.
DR   GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006338; P:chromatin remodeling; NAS:GeneDB_Spombe.
DR   GO; GO:0030702; P:chromatin silencing at centromere; IMP:GeneDB_Spombe.
DR   GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IGI:GeneDB_Spombe.
DR   GO; GO:0030261; P:chromosome condensation; IMP:GeneDB_Spombe.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; TAS:GeneDB_Spombe.
DR   GO; GO:0051570; P:regulation of histone H3-K9 methylation; NAS:GeneDB_Spombe.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEP:GeneDB_Spombe.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   KO; K06067; -.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Complete proteome; Direct protein sequencing;
KW   Hydrolase; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    405       Histone deacetylase clr6.
FT                                /FTId=PRO_0000114740.
FT   REGION        6    318       Histone deacetylase.
FT   ACT_SITE    138    138       By similarity.
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
//