ID A0A3Q3SY44_9TELE Unreviewed; 1066 AA.
AC A0A3Q3SY44;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 27.
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};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000032655.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000032655.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q3SY44; -.
DR Ensembl; ENSMAMT00000033504.2; ENSMAMP00000032655.2; ENSMAMG00000021971.2.
DR GeneTree; ENSGT00940000157440; -.
DR Proteomes; UP000261640; Unplaced.
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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1.
DR Gene3D; 6.10.250.1550; -; 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; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF11; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 54..142
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 656..973
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 198..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..148
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 198..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 784
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 656
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 957
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1066 AA; 117101 MW; 2A2E3D873A8454A5 CRC64;
NLLKSQCDSL SKLSSSVFLP LPVPAVDINS ALPLRLPPAA IPMDLRASGG VVAASVREQQ
LQQELLALKQ KQQIQRQILI AEFQRQHEQL SRQHEAQLQE HIKQQQELLA LKHQQELLEH
QRKMENHRLE QEMEKQQREQ KLQLLKNKER GQESAVASTE VKMRLQEFVL NKKKALAQRS
LNQGGLPNDA PYWYRKTQHS SLDQSSPPQT GVSTYNHPVL GVYNPRDDFP LRKTASEPNL
KLRSRLKQKV SERRSSPLLR RRDSPITTAK KRSLDMADSA CSSAPGSGPS SPNNSSNNIP
NENGITVTVS NNTEASLAQR LCSSAERGSV NQLSLYTSPS LPNITLGLPA TATATAASNV
RRKLLPSLQP ALSLSPPFLS GGHLSPYLAE AGAGTGGHGA HSPLLQHMVL MEQSPAQSPL
VTGVSGLSMS SAASMAKLQR QHRPLGRTQS APLPQGSAAQ AHAQALALQQ LVVQQQHQQF
LEKHKQQFQQ QQLHLNKMIA KPSESPVGRQ HQSHPEETEE ELREHQDGGA LPPGVTIKQE
PPDPQELQEE VLQQHRERER QAEQELLFRQ QALLLEQQRI HQLRNYQASM EAAGLSVPFP
GHRPLSRAQS SPASASSFPI SVPAPDPPIK PRFTTGLVYD SLMQKHQCMC GNTNSHPEHA
GRIQSIWSRL QETGLRAQCE YVCIYNIYIP LKATLEELQT VHSEAHVLLY GTNPLRQKLD
CSITPMFVRL PCGGVGVDSD TIWNEVHSSS AARLAVGSVV ELVFKVATEE LKNGFAVVRP
PGHHAEESTP MGFCYFNSVA IAAKLLQQRL NISKILIVDW DVHHGNGTQQ AFYDDPNVLY
VSIHRYDDGN FFPGSGAPDE VGSGPGVGFN VNVAFTGGLD PPMGDAEYLA AFRSVVMPIA
NEFAPDIVLV SCGFDAVEGH PPPLGGYTLS SKCFGYLTRQ LMTLAGGRVV LALEGGHDLT
AICDASEACV AALLGQELDP LPKAVLEQRP NPNAVHSLEK VLETHSKYWR SVHRYSPRLG
LSLLEAKRGD SEEAEAVSAM ASLSVANTNT MDQRPEEEPM EEEEPL
//
