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Database: UniProt/TrEMBL
Entry: E2ACU4_CAMFO
LinkDB: E2ACU4_CAMFO
Original site: E2ACU4_CAMFO 
ID   E2ACU4_CAMFO            Unreviewed;      1084 AA.
AC   E2ACU4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   07-JUN-2017, entry version 34.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911, ECO:0000256|SAAS:SAAS00818223};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911, ECO:0000256|SAAS:SAAS00818223};
GN   ORFNames=EAG_14668 {ECO:0000313|EMBL:EFN68742.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Vespoidea; 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
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events.
CC       {ECO:0000256|PIRNR:PIRNR037911}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|PIRNR:PIRNR037911, ECO:0000256|SAAS:SAAS00818219}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037911,
CC       ECO:0000256|SAAS:SAAS00818221}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|PIRNR:PIRNR037911}.
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DR   EMBL; GL438582; EFN68742.1; -; Genomic_DNA.
DR   RefSeq; XP_011255707.1; XM_011257405.2.
DR   ProteinModelPortal; E2ACU4; -.
DR   GeneID; 105250972; -.
DR   KEGG; cfo:105250972; -.
DR   InParanoid; E2ACU4; -.
DR   KO; K11406; -.
DR   OMA; KCENEEA; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   InterPro; IPR030703; Histone_deacetylase_5.
DR   PANTHER; PTHR10625; PTHR10625; 1.
DR   PANTHER; PTHR10625:SF159; PTHR10625:SF159; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00818226};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000311};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00490343};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW   Nucleus {ECO:0000256|SAAS:SAAS00818233};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW   Transcription {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00818215};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR037911,
KW   ECO:0000256|SAAS:SAAS00818213};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   DOMAIN      668    984       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
FT   ACT_SITE    796    796       {ECO:0000256|PIRSR:PIRSR037911-1}.
FT   METAL       659    659       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       661    661       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       668    668       Zinc. {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   METAL       744    744       Zinc. {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
//
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