PHD1_SCHPO
ID PHD1_SCHPO Reviewed; 434 AA.
AC O13298;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Histone deacetylase phd1;
DE EC=3.5.1.98 {ECO:0000269|PubMed:9781677};
GN Name=phd1; Synonyms=hda1; ORFNames=SPAC3G9.07c;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9781677; DOI=10.1016/s0014-5793(98)01124-7;
RA Kim Y.B., Honda A., Yoshida M., Horinouchi S.;
RT "phd1+, a histone deacetylase gene of Schizosaccharomyces pombe, is
RT required for the meiotic cell cycle and resistance to trichostatin A.";
RL FEBS Lett. 436:193-196(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 CHARACTERIZATION.
RX PubMed=9628926; DOI=10.1093/nar/26.13.3247;
RA Olsson T.G.S., Ekwall K., Allshire R.C., Sunnerhagen P., Partridge J.F.,
RA Richardson W.A.;
RT "Genetic characterisation of hda1+, a putative fission yeast histone
RT deacetylase gene.";
RL Nucleic Acids Res. 26:3247-3254(1998).
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 plays an important role in transcriptional regulation,
CC cell cycle progression and developmental events (PubMed:9781677).
CC Histone deacetylases act via the formation of large multiprotein
CC complexes (By similarity). Is not essential (PubMed:9781677).
CC {ECO:0000250, ECO:0000269|PubMed:9781677}.
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:0000269|PubMed:9781677};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000269|PubMed:9781677};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9781677}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AB008888; BAA23598.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA15916.1; -; Genomic_DNA.
DR PIR; T11643; T11643.
DR RefSeq; NP_594079.1; NM_001019506.2.
DR AlphaFoldDB; O13298; -.
DR SMR; O13298; -.
DR BioGRID; 280057; 160.
DR STRING; 4896.SPAC3G9.07c.1; -.
DR MaxQB; O13298; -.
DR PaxDb; O13298; -.
DR EnsemblFungi; SPAC3G9.07c.1; SPAC3G9.07c.1:pep; SPAC3G9.07c.
DR GeneID; 2543643; -.
DR KEGG; spo:SPAC3G9.07c; -.
DR PomBase; SPAC3G9.07c; -.
DR VEuPathDB; FungiDB:SPAC3G9.07c; -.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; O13298; -.
DR OMA; HFGMTHP; -.
DR PhylomeDB; O13298; -.
DR PRO; PR:O13298; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; IDA:PomBase.
DR GO; GO:0034967; C:Set3 complex; IDA:PomBase.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:PomBase.
DR GO; GO:0034739; F:histone deacetylase activity (H4-K16 specific); IMP:PomBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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; Hydrolase; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..434
FT /note="Histone deacetylase phd1"
FT /id="PRO_0000114725"
FT REGION 26..339
FT /note="Histone deacetylase"
FT ACT_SITE 158
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 49381 MW; CA2FF0D34CA536EA CRC64;
MDTPETSTPY EQVEKGSFFS FRPQKKRVTY HLDEQVGNYH YGDKHPMKPH RITITNHLVM
GYGLHNKMSV FSPRMATFGE MSEFHREDYL DFLKRVTPDN AEQFADKFQQ FNIGDDCPVF
DGTYEFSQRS AGASLDASRK LVQGQTDIAI NWSGGLHHAK RGEASGFCYV NDIVLAILNM
LRFFPRVLYI DIDIHHGDGV QQAFYESDRV LTVSFHKYNG DFFPATGNFD ENGVKGGKYF
ALNVPLEDGI GDEQYTSLFK SIIEPTINTF QPSAIVLQCG ADSLGYDRLG VFNLSIHAHG
ECVRFTRSFN IPMLVVGGGG YTLRNVARAW CYETSICVNE QIPSELPRET LYYEFFAPDY
TLHPRLTTKI ENKNTPKALE DLRIRALEQL RYLGGAPSVQ MQQIPPDLTG HLEEEDERLN
DEYLDKAVDV RVRG
