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Database: UniProt
Entry: I3J443_ORENI
LinkDB: I3J443_ORENI
Original site: I3J443_ORENI 
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
//
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