ID A0A087X6V8_POEFO Unreviewed; 919 AA.
AC A0A087X6V8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000001511.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000001511.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. {ECO:0000256|PIRNR:PIRNR037911}.
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|PIRNR:PIRNR037911};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037911}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738,
CC ECO:0000256|PIRNR:PIRNR037911}.
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DR EMBL; AYCK01005623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01005624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007554237.1; XM_007554175.2.
DR RefSeq; XP_007554238.1; XM_007554176.2.
DR RefSeq; XP_016528057.1; XM_016672571.1.
DR AlphaFoldDB; A0A087X6V8; -.
DR STRING; 48698.ENSPFOP00000001511; -.
DR Ensembl; ENSPFOT00000001514.2; ENSPFOP00000001511.2; ENSPFOG00000001452.2.
DR GeneID; 103139515; -.
DR KEGG; pfor:103139515; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000159065; -.
DR OMA; LDQKPCK; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule.
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 CDD; cd11681; HDAC_classIIa; 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; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF44; HISTONE DEACETYLASE 7; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 2.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 527..831
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 46..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 642
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 521
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 815
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 919 AA; 100997 MW; 6D69A3F5F00E3A55 CRC64;
MDLTVTHRLL HPRPDSAMLA PQPSFYLEHL TAQHCSQFSQ HHLQYNTEQR HRKMEEKRED
PQQLLPKNKN EQSAVASKHV KQILRDHIIM KNQPPHDRVP GSHCSSSPGY RPPVPDMSLK
PQPTPSDQRK DLALRRTVSE PTLKWKLKKL ISTRPNPLQR KISAPPDVKH RTENMDSSPS
RSSTSASGCS SPNDTLMSDN GSLSRAPESK RVLMNNGNVA HFALPANHTA MHNITAGLPA
QADLRVTKPV AALTLQSVYV SPMSQRLQPV FIFEPHMGLM HQQLVPLHSL STIPQQQHPH
ISSSSRREGL VALGSHRPVE RAHSEPLPYS HSVLPLHAGH HPHTHQQLSQ LYHKAGLERF
KLSTQLSKIP SEDMDVDESG SATGSGTGSL CGSELGSLSE DGHRRRESNA STDSVYDTES
ITSSRESLIE TSHPLSQRQV ILRSTLQPDA LGVPTLIWPH QSHQPVIRSR SLPPSTSLAP
TSHVPTIVPS MSLSSPAKDA KLSFTTGLVY DTQMQKHQCI CGDNSRHAEH AGRIQSIWSR
LQERGLKSQC ECILSRKATR AELLSVHSEN HVLMDNQRRT GSRTFVDLPC GGVGVDIDTV
WNEQHTAAAS QVAAGCVIDL ALKVAQRELK NGFAVVRPPG HHATRSSPLG FCYFNSVAIA
AKQLQHKLSV SKILIVDWDV HHGNGTQEAF YDDPSVLYIS LHRYDDGNFF PGSGHPNEVG
VRAGKGFNVN VGWTGGLDPP MGDAEYLAAF RAVVMPIAHE FSPDVVLVSA GFDAVEGHQP
SLGGYTVTAK LFGFLTRQLM SLAGGRVILA LEGGHDLKAI CDASEACVSA LLGMEVEPLS
QSLLDQKPCE NAVRSLQRVV QIQGEFWQSV RDSATTVDLS YLQAQRHRFR RDSDSEAVNA
IASLSMGSLT SERKPLERM
//
