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Database: UniProt
Entry: A0A139WP11_TRICA
LinkDB: A0A139WP11_TRICA
Original site: A0A139WP11_TRICA 
ID   A0A139WP11_TRICA        Unreviewed;       819 AA.
AC   A0A139WP11;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Histone deacetylase 6-like Protein {ECO:0000313|EMBL:KYB29663.1};
GN   Name=AUGUSTUS-3.0.2_14236 {ECO:0000313|EMBL:KYB29663.1};
GN   ORFNames=TcasGA2_TC014236 {ECO:0000313|EMBL:KYB29663.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB29663.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB29663.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB29663.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:KYB29663.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB29663.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
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; KQ971307; KYB29663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139WP11; -.
DR   STRING; 7070.A0A139WP11; -.
DR   EnsemblMetazoa; TC014236_002; TC014236_002; TC014236.
DR   eggNOG; KOG1343; Eukaryota.
DR   InParanoid; A0A139WP11; -.
DR   OMA; CETILNC; -.
DR   Proteomes; UP000007266; Linkage group 1.
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   CDD; cd10002; HDAC10_HDAC6-dom1; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 2.
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; 2.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT   DOMAIN          68..365
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   DOMAIN          486..769
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  91797 MW;  E75608137F728251 CRC64;
     MSGSSGRESL RAMMAEKKKQ KHQNLPDLEL VDPFANATAC NSITRGKTGI VYDREVLKHK
     CDWDENYPEN PQRLESILEK CTGQGLFERC VTLPNYKRSD LYEKVIAKHN PDLFAKLERV
     SKMDLKAREQ EASSYDAIYF NQSTFDAACR SLSSVLNLVT AVAKRDVQNG MALVRPPGHH
     AMENEYNGYC YFNNVAIAAE SVLREGHSKR VMIVDFDVHH GQGTQRMFYE RNDVLYFSIH
     RYEHGTFWPN LLESNFNYIG RGDGLGFNVN VPLNETMLGD DDYLAIVFNL LLPLGFEFNP
     DLIVISAGYD AAIGCPEGRM NVTPGFYSHL ISLLSTLARG QIAVVLEGGY FLPSLSEGAC
     MTLNSLLGSP CPLLEPIKSV HPSVITTICN VKRMLHTRWK CFDVAELKTE ATHKFEICYF
     GDKRTPPFDN GPGSYPGICD ENSRYYSKLT DALHERYICA SDLPVNYIYD DQMLQHTPQS
     GDLERPERPE RLTSIMKVLQ EFGLLGRMQR TPIVPRDFTE YSPHARGYLG TVNEAMEQSK
     DVYVNEHTHD SVVLAVSGLL SLVDGVMSGT SQAGVAVIRP PGHHAEHDKA MGYCFVNNIA
     VAANYLLDKY EVERVLIVDF DIHHGNGTQN MFYENDRVMY VSIHKDEHGK FFPANSPRNY
     TFDGYGRGRG FNVNIPFNND KMGDSEYLAV FHNVILPVAY SFGPQVVLVS GGFDAGIHDP
     LGGYVVSPET FGHFIHMLKG LAKGRLILAL EGGYNLTTTS YAFAICAKAL LGDPIIMPKN
     KIKGFKEKYY GEVLATAIDP TRVQDNEYVE SEMNKLNNS
//
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