ID E2ACU4_CAMFO Unreviewed; 1084 AA.
AC E2ACU4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911};
GN ORFNames=EAG_14668 {ECO:0000313|EMBL:EFN68742.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN68742.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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|ARBA:ARBA00001028,
CC ECO:0000256|PIRNR:PIRNR037911};
CC -!- SUBCELLULAR LOCATION: Nucleus {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; GL438582; EFN68742.1; -; Genomic_DNA.
DR RefSeq; XP_011255707.1; XM_011257405.2.
DR AlphaFoldDB; E2ACU4; -.
DR STRING; 104421.E2ACU4; -.
DR InParanoid; E2ACU4; -.
DR OMA; XAVASTE; -.
DR Proteomes; UP000000311; 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:SF15; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 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 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:UP000000311};
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 668..985
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 155..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 796
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 668
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
SQ SEQUENCE 1084 AA; 118671 MW; 326520AF1B2FFF4A CRC64;
MKVYVERASA FDRYSRAGSS KVKLVGDIHH RHATAHESML PNVCCCYYMC VEMARDTPGS
PMPRPRNLGA GGGGGAATAT LTSGAYHAAA TDTANLHDHA LQQKMLELQQ HHHFQQQILR
QQYQAQERHL AELHEQQMHQ LKLWEQQKLE EKREKDRLEA LRKKDKHDHS ANASTEVKQR
LQSFLVNKKQ REAAAAANGA VPGTPGYRSW LQPQSESSST TNAAHPYRMP QMLQEKFGDD
FPLRKTASEP NLLKVRLKQR VERNMAASRN SPLMARRKDR LLSHLKRKSL LANSGSNPES
GPNSPPTVNN SQASPTAGSN TAIQEEGESP AYGGRLTSSS QQGSLSDLSL FSSPSMPNIS
LGRPHVPSSS SSGTKLAPVS EAEVRAAFTA RLGMPLTGQM LHGTLPFYPS LTVIEGEPAY
IHKQIQQNLQ EQTAPPPSAA AGSRQHPAAA AATVYHTAPP ITDTQVAHAR LHKAGHRPLG
SRTQSAPLPL GHPMLQGGII APTTHYEEYL AEKQIHDQQQ AHNYLKQQIR QTVLTRVGSR
GQANQLDEAP ETEESEVIDL TGKKDHPEES EISKQQRDRE QFLQQQRDLM MRHTLQTNES
TVYAGSRTSQ SARPLSRALS SPLVHLGPQG NSGDMFARVS PHRPTTGLAY DPLMLKHACV
CGETVRGHPE HGGRLQSVWA RLSETGLLQR CDRVRSRKAS LEEIQTCHSE AHALLFGTNP
LNRQKLDMSK LSQLPIKSFV RLPCGGVGVD SDTTWNELNT APAARMAVGC VVELAFKTAL
GDIKNGFAVV RPPGHHAETN QAMGFCFFNS VAIATRLLQQ KLDVRKILIL DWDVHHGNGT
QQMFYDDPRV LYLSIHRHDD GNFFPGTGGP TECGAGEGLG YNVNVAWSGG LNPPMGDAEY
LAAFRTIVMP IAKEYDPDLV IVSAGFDAAV GHPAPLGGYK VSPACFGKMT QQLLNLADGK
VVLALEGGYD LAAICDSAQE CVRALLGDEP SPLRDEELAR IPCQNAIDTL QKTIAIQMSH
WPCVKLTAHT VAMSAIEASQ KEHDETETVS AMASLSMQQP TNLTTTPEHS REVSEEPMEQ
DEAK
//
