ID A0A091INB1_CALAN Unreviewed; 1047 AA.
AC A0A091INB1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN ORFNames=N300_01028 {ECO:0000313|EMBL:KFP01156.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP01156.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP01156.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP01156.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KL218015; KFP01156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091INB1; -.
DR STRING; 9244.A0A091INB1; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; 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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd10163; ClassIIa_HDAC9_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 Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 31..121
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 652..963
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 107..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 774
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 644
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 652
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 947
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP01156.1"
FT NON_TER 1047
FT /evidence="ECO:0000313|EMBL:KFP01156.1"
SQ SEQUENCE 1047 AA; 116091 MW; 057B5BC2D8F7DF0E CRC64;
TVDVKSEVPV GLEPISPLDL RTDLRMMVPM VDPIMREKQL QQELLLIQQQ QQIQKQLLIA
EFQKQHENLT RQHQAQLQEH IKLQQELLAI KQQQELLEKE QKLEQQRQEQ ELERHRREQQ
LPPLRGKERG RERAVASTEV KQKLQEFLLS KSATKDSPAN GKNHSMNRHP KLWYTAAHHT
SLDQSSPPLS GASPPYKYAL PGAQDAKDDF PLRKTASEPN LKVRSRLKQK VTERRSSPLL
RRKDGNVVSS FKKRLFEVTE SSVSSSSPGS GPSSPSNGPT SSITENETSV LPSNIQAEHL
VSQQRLLIQD ESVNLLSLYT SPSLPNITLG LPAIQPPISA SSSFKEKQKG ETQSLRQGVA
LAGQYGGNIP PSSTHPHVAL EGKPNSSHQA LLQHLLLKEQ MRQQKLLVTG AVPLHPQSPL
VAKERVSPGI RAAHKLPRHR PLNRTQSAPL PQSTLAQLVI QQQHQQFLEK QKQYQQQIHM
NKMLSKSIEQ LKQPGSHLEE AEEELQGDQS MQEERVPASS ASVRAESSSA GVDDRIGQQV
GAVKVKEEPP DSDEDVQTQQ MESGEQAAFM QQEFLAHRRV HQLPIYQAQM ASVGMTGLDK
HRPVSRTSSS SADSTLPHPD VDQPSQHVYT TGIVYDSLML KHQCMCGNYA NHPEHAGRIQ
SIWSRLQETG LLNKCERIRG RKASLEEIQL VHSEHHSLLY GTSPLNRQKL DPRKLLGNMS
QKLFSLLPCG GLGVSKCLVF LQEGQHATYV FIHEFLSTTA LSNGFAVVRP PGHHAEESTA
MGFCFFNSIA ITAKYLRDKL NVGKILIVDL DVHHGNGTQQ AFYADPSILY VSLHRYDEGN
FFPGSGAPNE VGSGPGEGYN INIAWTGGLD PPMGDVEYLA AFRTVIMPAA NEFDPEIVLV
SAGFDAVEGH DPPLGGYKVT AKCFGHLTKQ LLKLADGRVV LALEGGHDLT AICDASEACI
NALLGNELEP LPEDIVHQIP NMNAIASLKK TTEIQSKYWK SVEPYSVPVD CALAESQKRE
REETETVSAM ASLSVDVEQC IPQEGNR
//
