ID S7PUN1_MYOBR Unreviewed; 1023 AA.
AC S7PUN1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
GN ORFNames=D623_10022136 {ECO:0000313|EMBL:EPQ14663.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ14663.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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:PIRNR037911}.
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:PIRNR037911};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037911}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738,
CC ECO:0000256|PIRNR:PIRNR037911}.
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DR EMBL; KE164011; EPQ14663.1; -; Genomic_DNA.
DR AlphaFoldDB; S7PUN1; -.
DR eggNOG; KOG1343; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd10008; HDAC7; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF44; HISTONE DEACETYLASE 7; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1023
FT /note="Histone deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004555516"
FT DOMAIN 612..930
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 55..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 741
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 612
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 914
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1023 AA; 110503 MW; 2030C8310526CC8C CRC64;
MGWSLLFLVS FCWRCQVLEG SSQGPAWLGH VPSLFLAPFL QPLHSISLLS TDGTQVTPGA
HCPSPPGTGC PRPHADTPGP QPQPMDLRVG QRPPVEPPLE PALLALQHPQ HLHHHLFLAG
LQQHRSVEPM RLSMDTPMPE LPVGQQEQEL RQLLNKDKSK RSAVASSVVK QKLAEVILKK
QQAALERTVH PSSPSIPYRT LEPLETEGAT RSMLSSFLPP VPSLPSDPPE HHPLRKTVSE
PNLKLRYKPK KSLERRKNPL LRKESAPPSL RRRPAETLGG CSSPNDSEHG PNPILGSEAL
LGQRLRRQET SLAPFALPTV SLLPAITLGL PAPARADGDR RIHPTLGPRG PVLGSPHAPL
FLPHGLESEA GGTMPSRLQP ILLLDPSVSH TPLLTVPGFG PLPFHFAQSL LTTERLSGSG
LHWPLSRTRS EPLPPSATAP PSLGPLQPRL ERLNPHVQLI KRSAKPSEKP RLRQIPSAED
LETDGGGVGP PGDDSLACRG SSSGQHEARG PVLQQHQQVF LWEQQRLAGR LPRVGTGDPV
LLSPAQGGHR LLSRTQSSPA APASLPTPEP PNQARVLPSS EAPARTLPFT TGLVYDSVML
KHQCSCGDNS RHPEHAGRIQ SIWSRLQERG LRGQCECLRG RKASLEELQS VHSERHVHLY
GTNPLSRLKL DNGKLAGLLA QRIFVMLPCG GVGVDTDTIW NELHSSNAAR WAAGSVTDLA
FKVASRELKN GFAVVRPPGH HADRSTAMGF CFFNSVAIAC RQLQQQGKAG RILIVDWDVH
HGNGTQHTFY EDPSVLYISL HRHDDGNFFP GSGAVEEVGA GSGEGFNVNV AWAGGLDPPM
GDPEYLAAFR IVVMPIAREF SPDLVLVSAG FDAAEGHPAP LGGYHVSAKC FGYMTQQLMS
LAGGAVVLAL EGGHDLTAIC DASEACVAAL LGNKVDPLAE KGWKQKPNLN AIRSLEAVIR
VHSKYWGCMQ RLASCPESWV PRVPGADAEE VEAVTALASL SVGILAEERP SEQLVEEEEP
MNL
//
