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Database: UniProt
Entry: E9H991_DAPPU
LinkDB: E9H991_DAPPU
Original site: E9H991_DAPPU 
ID   E9H991_DAPPU            Unreviewed;       357 AA.
AC   E9H991;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Histone deacetylase domain-containing protein {ECO:0000259|Pfam:PF00850};
GN   ORFNames=DAPPUDRAFT_308757 {ECO:0000313|EMBL:EFX71695.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX71695.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX71695.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
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};
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DR   EMBL; GL732608; EFX71695.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9H991; -.
DR   STRING; 6669.E9H991; -.
DR   EnsemblMetazoa; EFX71695; EFX71695; DAPPUDRAFT_308757.
DR   KEGG; dpx:DAPPUDRAFT_308757; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_007727_8_7_1; -.
DR   InParanoid; E9H991; -.
DR   OMA; FFQHPFY; -.
DR   PhylomeDB; E9H991; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
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:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000305}.
FT   DOMAIN          12..306
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
SQ   SEQUENCE   357 AA;  39309 MW;  60ED66AC6D400D20 CRC64;
     MALHRNVKQP SHLEQPARIT SVYQKLQESG VLDRCLQLDA RIATREELLW LHTADYVDEL
     SATSEKKQSI LTALERQYDS VFLCPETYQA ALLSAGSSLQ VVESILSGES RSGFAVIRPP
     GHHAESDEAF GFCYFNNTAL AAKYAIENHQ LERILIVDWD IHHGNGIQKM FEEDPRVLYI
     SLHRLDIFPF NPENCDCNMV GTGPGVGFNV NIAWPSKGMG DSEYLAAFRR IIMPIANQYN
     PQLVLVAAGF DAALGDPLGG CKVSPEGYGQ MCHMLTSLAE GRVAVLLEGG YNLKSVSDSM
     LMCANALLGD PLPTTLIGAL QPGAAVTIQR VANYLLPYWT SLVVDVNSEE KNTKHKR
//
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