ID H0YZX4_TAEGU Unreviewed; 996 AA.
AC H0YZX4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 71.
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 Name=LOC100219847 {ECO:0000313|Ensembl:ENSTGUP00000003859.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000003859.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000003859.2}
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; H0YZX4; -.
DR STRING; 59729.ENSTGUP00000036613; -.
DR Ensembl; ENSTGUT00000003901.2; ENSTGUP00000003859.2; ENSTGUG00000003694.2.
DR GeneTree; ENSGT00940000159065; -.
DR HOGENOM; CLU_006530_1_1_1; -.
DR TreeFam; TF106174; -.
DR Proteomes; UP000007754; 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 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:UP000007754};
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 585..902
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 122..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 714
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 887
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 996 AA; 107799 MW; ACE805B763B164E0 CRC64;
MSGDDKAAVT PCTSPRVPQA VPMDLRIGQR VVKPQDTALL ALKQQQLQHQ LFLASLHQQQ
VEQLAHQHVR VAMESPHREA EPGQQEQELR QILNKDKSKR SAVASTVVKQ KLAEVILKKQ
QAALERTSNP PAAALPYRSL EPLEPEGPSP AMLSTFLSPV PSTSLDTPEH FPLRKTASEP
NLKVRCKPRK CLDRRKNPLT RKESAPPSLK RRPPDAIDSS PSSSSTPVSG CSSPNDSLPA
EHAALPSAPG VAHETPLAQR LMMQESSLAQ FALQSAASLP AITLGLPATT GARGDAERRA
LPGLAHRVPV LNGPVLPGTH SPVFIPASLE QHEAGSALSP RLQPVIILEP SVTHAPLVAV
PGLGTVPLSL APSLVPAERL ALPGQHKPLG RTRSEPLPPS PRAVQQHLLF QQHHAHFLRQ
QPHLGKRPAK SSEKPRLRQI PSSEDMEAEG TLPEAEPGDP PRARPEPPRP GGSAKEPERT
QKMGQPPEEL VLQQALLWDS FQRVQQQLLK RQPLADPPVL PPGHRPLSRA QSSPATATVS
LPAQDTKALA LPVQEQPPKP LFTTGLVYDS VMLKHQCSCG DNSNHPEHAG RIQSIWSRLQ
ERGLRSRCEC LRGRKATLEE LQSVHSERHV LLYGTNPLNR LKLDNGKLAG ILSQRTFVML
PCGGLGVDSD TIWNELHSSN AARWAAGSVT ELAFKVATRE LKNGFAVVRP PGHHADPSTA
MGFCFFNSVA IAARQLQQKG KLSKILIVDW DVHHGNGTQQ IFYRDPEVLY ISLHRHDDGN
FFPGSGAADE VGAGPGEGFN VNVAWAGGLD PPMGDPEYLA AFRTVVMPIA HEFCPDVVLV
SAGFDAAEGH PPPLGGYKVS AKCFGYMTKQ LMSLAGGAVV LALEGGHDLT AICDASEACV
SVLLGHEPEP LPEDSLRQKP NANAVRSLEA VIQVQSKYWV AVQRFASKLG CSFLEAQHHE
ADEVETVTAL ASLSVAVMVE KRAQEEPMEQ EEPMTQ
//
