ID A0A091HZS3_CALAN Unreviewed; 1072 AA.
AC A0A091HZS3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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_02831 {ECO:0000313|EMBL:KFP01779.1};
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:KFP01779.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP01779.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP01779.1};
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; KL218047; KFP01779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HZS3; -.
DR STRING; 9244.A0A091HZS3; -.
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; 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 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 57..145
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 665..980
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 791
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 665
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 964
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP01779.1"
FT NON_TER 1072
FT /evidence="ECO:0000313|EMBL:KFP01779.1"
SQ SEQUENCE 1072 AA; 118700 MW; 2C663FF043E701F7 CRC64;
PDGLSGRDQP VELLNPPRVN HMPSSVDVTT ALPLQVAPTS VPMDLRLDHQ FSMPVTEPTL
REQQLQQELL ALKQKQQIQR QILIAEFQRQ HEQLSRQHEA QLHEHIKQQE MLAMKHQQEL
LEHQRKLEQH RQEQELEKQH REQKLQQLKN KEKGKESAVA STEVKMKLQE FVLNKKKALA
HRNLNHCISS DPRFWYGKTQ HSSLDQSSPP QTGVSGTYNH PVLGMYDSKD DFPLRKTASE
PNLKLRSRLK QKVAERRSSP LLRRKDGPVV TALKKRPLDV TDSACNSAPG SGPSSPNNSS
NNISTENGIA GSVTSIQAET SLAHRLVNRE GSVTQLPLYT SPSLPNITLG LPATGPSSGG
SAQQEAERLT IPTLQQRISL FPGTHLTPYL STATLERDGG TAHNPLLQHM VLLEQPAAQT
PLVTGLPLHA QSLVGGERVS PSIHKLRQHR PLGRTQSAPL PQNAQALQQL VIQQQHQQFL
EKHKQQFQQQ QLHINKIISK PNEPARQHES HPEETEEELR EHQALLEEPY SDRVTSQKEA
PGLTNMVQVK QEPIESDEEE AEPQQELESG QRQAEQELLF RQQALLLEQQ RIHQLRNYQA
SLEAAGMPVS FGGHRPLSRA QSSPASATFP MSVQEPPTKP RFTTGLVYDT LMLKHQCTCG
NTNSHPEHAG RIQSIWSRLQ ETGLRGKCEC IRGRKATLEE LQTVHSEAHT LLYGTNPLNR
QKLDSKKLLA VSRLSSQTKG IGVVDSDTIW NEVHSSGAAR LAVGCVIELV FKVATGELKN
GFAVVRPPGH HAEESTPMGF CYFNSVAIAA KLLQQRLNVS KILIVDWDVH HGNGTQQAFY
NDPNVLYISL HRYDDGNFFP GSGAPDEVGT GAGVGFNVNM AFTGGLDPPM GDTEYLTAFR
TVVMPIANEF APDVVLVSSG FDAVEGHPTP LGGYNLSAKC FGYLTKQLMG LAGGRVVLAL
EGGHDLTAIC DASEACVSAL LGNELDPLPD KVFQQRANAN AVHSMEKVIE IHSKYWHSLQ
RYASTVGYSL VEAQKCENEE AETVTAMASL SVGVKPAEKR PDDEPMEEEP PL
//
