ID A0A093RC17_PYGAD Unreviewed; 1051 AA.
AC A0A093RC17;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE Flags: Fragment;
GN ORFNames=AS28_02799 {ECO:0000313|EMBL:KFW68524.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW68524.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW68524.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW68524.1};
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; KL225169; KFW68524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093RC17; -.
DR STRING; 9238.A0A093RC17; -.
DR Proteomes; UP000054081; 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:UP000054081};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 34..124
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 654..967
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 110..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 778
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 731
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 951
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW68524.1"
FT NON_TER 1051
FT /evidence="ECO:0000313|EMBL:KFW68524.1"
SQ SEQUENCE 1051 AA; 116720 MW; C3D5DAB9EBA00844 CRC64;
FLPTVDVKSE VPVGLEPISP LDLRTDLRMM VPMVDPIMRE KQLQQELLLI QQQQQIQKQL
LIAEFQKQHE NLTRQHQAQL QEHIKLQQEL LAIKQQQELL EKEQKLEQQR QEQELERHRR
EQQLPPLRGK ERSRERAVAS TEVKQKLQEF LLSKSATKDS PANGKNHSMS RHPKLWYTAA
HHTSLDQSSP PLSGASPPYK YTLPGAQDAK DDFPLRKTAS EPNLKVRSRL KQKVTERRSS
PLLRRKDGHV VCSFKKRLFE VTESSVSSSS PGSGPSSPSN GPTSSITENE TSVLPSNVQA
EHLVSQQRLL IQDESVNLLS LYTSPSLPNI TLGLPAVQPQ ISASSSFKEK QKGETQSLRQ
GGALAGQYGG NIPPSSTHPH VALEGKPNSS HQALLQHLLL KEQMRQQKLL VTGAVPLHPQ
SPLAAKERVS PGIRAAHKLP RHRPLNRTQS APLPQSTLAQ LVIQQQHQQF LEKQKQYQQQ
IHMNKMLSKS IEQLKQPGHL EEAEEELHGD HSMQEERAPA GGASVRAESS SAGVDDRIGQ
QVGAVKVKEE PPDSDEDVQT QQMESGEQAA FMQQEFLAHR RVHQLQIYQA QMATVGMAGL
DKHRPVSRTP SSPADSTLPH PAMDQPSQHV YTTGVVYDSL MLKHQCMCGN YANHPEHAGR
IQSIWSRLQE TGLLNKCERI RGRKASLEEI QLVHSEHHSL LYGTSPLNRQ KLDPRKLLGN
VSQKLFSLLP CGGLGVSRCL VFCKRDSTQH MYSFMNSLAL SHYQFKNGFA VVRPPGHHAE
ESTAMGFCFF NSIAITAKYL RDKLNIGKIL IVDLDVHHGN GTQQAFYADP SILYVSLHRY
DEGNFFPGSG APNEVGSGPG EGYNINIAWT GGLDPPMGDV EYLTAFRTVI MPAANEFDPE
IVLVSAGFDA VEGHDPPLGG YKVTAKCFGH LTKQLLKLAD GRVVLALEGG HDLTAICDAS
EACINALLGN ELEPLPEDIV HQIPNMNAIA SLKKTTEIQS KYWKSVEPYS VPVNCALAES
QKQEREETET VSAMASLSVD VEQCIPQEGS R
//
