ID I3J443_ORENI Unreviewed; 623 AA.
AC I3J443;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN Name=hdac9 {ECO:0000313|Ensembl:ENSONIP00000003633.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000003633.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000003633.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00001028};
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 RefSeq; XP_005472509.1; XM_005472452.3.
DR AlphaFoldDB; I3J443; -.
DR STRING; 8128.ENSONIP00000003633; -.
DR Ensembl; ENSONIT00000003634.2; ENSONIP00000003633.1; ENSONIG00000002902.2.
DR GeneID; 100712412; -.
DR KEGG; onl:100712412; -.
DR CTD; 393789; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000166341; -.
DR HOGENOM; CLU_006530_2_1_1; -.
DR InParanoid; I3J443; -.
DR OMA; PDGHYGV; -.
DR OrthoDB; 4269773at2759; -.
DR TreeFam; TF106174; -.
DR Proteomes; UP000005207; Linkage group LG11.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR Gene3D; 6.10.250.1550; -; 1.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR PANTHER; PTHR45364:SF12; HISTONE DEACETYLASE 9; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT DOMAIN 67..161
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 69828 MW; 12F066DA74BCF2F8 CRC64;
MLQTIYEGES SFSTTEGRVG HQQFPNPSKM HNVNNSVDIK PDVPLAVEPL SPLDLRTDLR
MLGPGSDPGL WERQLQQELL LIQKQQQIQK QLLISEFQKQ HEKLTRQHQA QLQEHLKLQQ
ELQAMKQQQE LAEKERRLEQ QQQQQSQQEK EQEKHRREHH ISSLSLRGKE RSRESLTGAV
ASTEVKQKLQ EFLLSKSAKD SASNGANHSF IQHPKLWYTS SHHTSLDQSS PPLGGTSPTC
QYTLPSPVES KDDFPLRKTA SEPNLKVRSR LKQKVAERRS SPMLKRRDGN IMAPYKKRAL
ELMDSTPTNS APGSGPSSPI GASSALGAEN GPSSLPTTTK TERWPSQPRL FRPEGSVPML
SLYTSPSLPN ISLGLSTASS PISAAMGLKD RSTEIKHGLP GHLLGPVPLQ TGLESKVSPS
HQALLQHLLQ KEQMRQQKIL SSGQGSMSSH SQSPLAMKDR PSSTRPKLPK HRPLNRTQSA
PLPQNTLAQL VIQQQHQHFL EKQKQYQQQV HINKLLSKSI EQLRQPSAHL QESEEEQEEH
YREEVESMQE DRLPPGGVIR KHTLSSSSSG SSSELPDTHC GVIKVKEEPA DSEDEALTNQ
SLESEQSTYL HQVKGRLVIR AMI
//