ID A0A851K1A2_VIDCH Unreviewed; 1076 AA.
AC A0A851K1A2;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN Name=Hdac4 {ECO:0000313|EMBL:NXB83611.1};
GN ORFNames=VIDCHA_R05704 {ECO:0000313|EMBL:NXB83611.1};
OS Vidua chalybeata (Village indigobird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Estrildidae; Viduinae; Vidua.
OX NCBI_TaxID=81927 {ECO:0000313|EMBL:NXB83611.1, ECO:0000313|Proteomes:UP000634236};
RN [1] {ECO:0000313|EMBL:NXB83611.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OUT-0048 {ECO:0000313|EMBL:NXB83611.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXB83611.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXB83611.1}.
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DR EMBL; WBNB01000149; NXB83611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A851K1A2; -.
DR Proteomes; UP000634236; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC.
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; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1.
DR CDD; cd10006; HDAC4; 1.
DR FunFam; 3.40.800.20:FF:000002; Histone deacetylase; 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; HDACs.
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:SF13; 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|ARBA:ARBA00022853};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037911-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000634236};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 62..151
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 679..996
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 132..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..311
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 807
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 755
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 980
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXB83611.1"
FT NON_TER 1076
FT /evidence="ECO:0000313|EMBL:NXB83611.1"
SQ SEQUENCE 1076 AA; 118914 MW; F6C32F7EE7F1D793 CRC64;
FSLLFPDGLS GRDQPVELLN PPRVNHMPSS VDVSTALPLQ VAPSSVPMDL RLDHQFSIPV
TEPTLREQQL QQELLALKQK QQIQRQILIA EFQRQHEQLS RQHEAQLHEH IKQQQEMLAM
KHQQELLEHQ RKLEQHRQEQ ELEKQHREQK LQQLKNKEKG KESAVASTEV KMKLQEFVLN
KKKALAHRNL NHCISSDPRF WYGKTQHSSL DQSSPPQSGV SGTYNHPVLG MYDSKDDFPL
RKTASEPNLK LRSRLKQKVA ERRSSPLLRR KDGPVVTALK KRPLDVTGTA DSACNSAPGS
GPSSPNNSSN NISTENGIAG SVTSIQAETS LAHRLVNREG SVTQLPLYTS PSLPNITLGL
PATGPSSAGQ AQPDAERLAI PALQQRISLF PGTHLTPYLS TTALERDGGT AHNPLLQHMV
LLEQPTAQTS LVTDWYLSGL PLHAQPLVGG ERVSPSIHKL RQHRPLGRTQ SAPLPQNAQA
LQQLVIQQQH QQFLEKHKQQ FQQQQLHINK IISKPTEPAR QHESHPEETE EELREHQALL
EEPYGDRATG QKEPPGLASV VQVKQEPIES DEEEAEPQQE LESGQRQAEQ ELLFRQQALL
LEQQRIHQLR NYQASLEAAG MPVSFGGHRP LSRAQSSPAS ATFPMSMQEP PTKPRFTTGL
VYDTLMLKHQ CTCGNTNSHP EHAGRIQSIW SRLQETGLRG KCECIRGRKA TLEELQTVHS
EAHTLLYGTN PLNRQKLDSK KLLGSLTSMF VRLPCGGVGV DSDTIWNEVH SSGAARLAVG
CVIELVFKVA TGELKNGFAV VRPPGHHAEE STPMGFCYFN SVAIAAKLLQ QRLNVSKILI
VDWDVHHGNG TQQAFYNDPN VLYISLHRYD DGNFFPGSGA PDEVGTGAGV GFNVNMAFTG
GLDPPMGDTE YLTAFRTVVM PIANEFAPDV VLVSSGFDAV EGHPTPLGGY NLSAKCFGYL
TKQLMGLAGG RVVLALEGGH DLTAICDASE ACVSALLGNE LDPLPEKVFQ QRANANAVHS
MEKVIEIHSK YWHSLQRFAS TVGYSLVEAQ KCENEEAETV TAMASLSVGV KPAEKR
//
