ID   Q7QFC8_ANOGA            Unreviewed;      1004 AA.
AC   Q7QFC8;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 5.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911};
DE            EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911};
GN   ORFNames=AgaP_AGAP000410 {ECO:0000313|EMBL:EAA06252.5};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA06252.5};
RN   [1] {ECO:0000313|EMBL:EAA06252.5}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06252.5};
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
RN   [2] {ECO:0000313|EMBL:EAA06252.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06252.5};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAA06252.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06252.5};
RX   PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA   Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT   "The Anopheles gambiae genome: an update.";
RL   Trends Parasitol. 20:49-52(2004).
RN   [4] {ECO:0000313|EMBL:EAA06252.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06252.5};
RX   PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA   Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA   Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT   "Update of the Anopheles gambiae PEST genome assembly.";
RL   Genome Biol. 8:R5.1-R5.13(2007).
RN   [5] {ECO:0000313|EMBL:EAA06252.5}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA06252.5};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAA06252.5}.
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DR   EMBL; AAAB01008846; EAA06252.5; -; Genomic_DNA.
DR   RefSeq; XP_310688.5; XM_310688.5.
DR   AlphaFoldDB; Q7QFC8; -.
DR   STRING; 7165.Q7QFC8; -.
DR   PaxDb; 7165-AGAP000410-PA; -.
DR   GeneID; 1271834; -.
DR   KEGG; aga:AgaP_AGAP000410; -.
DR   VEuPathDB; VectorBase:AGAP000410; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   HOGENOM; CLU_006530_0_1_1; -.
DR   InParanoid; Q7QFC8; -.
DR   OMA; XAVASTE; -.
DR   OrthoDB; 124800at2759; -.
DR   PhylomeDB; Q7QFC8; -.
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   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; 3.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
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          609..908
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          230..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          962..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          66..93
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        234..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        717
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT   BINDING         601
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   BINDING         603
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   BINDING         609
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
SQ   SEQUENCE   1004 AA;  108483 MW;  A4E8ED41EE612317 CRC64;
     MEMARDSTMG RDRVLVVPNT GIALNSSSSS SQIAAPADIS QQILELQKEQ ELEKQKLWHA
     FQEKNKELEM QHRQQLEHKF QELRDQRIAE EAAQQRERRE REAIKRKEKH ECCANASSEV
     KQKLQTFLIQ KKQAAASNGL SSPLPYRNWG VVKSSSGESL PGGAVAAAVS SHPYKIPPPP
     SSIAKYDPDF PLRKTASEPN LLKIRLKQRV IEKRSLNGPL AARRQERLRR LQKQQHNQAL
     AQTNCAASAS VATTDSGPNS PPTVGSRASP TNAPIQEENE DPQYGSVTSR ASINDLSLFS
     SPSMPNISLG RPHLGSSAAA SVAHLALNAT RPTHLGVGAG IGGQAGSVPF GSPMLDLSEQ
     QQRSQNVAAE RQAYEQHMLM KQKIRQTALT RAANCVNREP QLREEVESNE VIDLTDKKQP
     PKTVLASSVI KSTSQSHLLS SSSHGVDGEP PTAQQQQQQQ QQHLSELIHQ QQHYHREREL
     FMRRSIQLSV LEDPYSHHAG SAGGSGGAAA AAAAAAAAAN LLRPLSRTSS SPLVHLSSIG
     GGGGGGKRFG RRPSDGPSKA CSPTLGRGRA VTTICHRHRE QKLRPATTGL AFDSLMLKHV
     CACGDNANHP EHSGRLQSIW ARLLGTGLAI RCDKLRSRKA TQEELQTVHT EGHALLFGTS
     QLNRQKVDTS RVSFVRLAII PAAAARMAAG CVIDLSYKVA RGENRNGFAV VRPPGHHAEA
     DAAMGFCFFN SIALAARLLR HRMPHEMRRI LIVDWDVHHG NGTQQAFYDD ASVLYLSVHR
     HDDGNFFPGT GGPAECGVGT GLGYNVNVAW SGGVNPPLGD AEYLAAFRTV VMPIARDFAP
     DIVLVSAGFD AAVGHPAPLG GYVVSPACFG HLTRELMQLA NGKIVLALEG GYDLPAICDS
     AEECVRALLG ESTSSIAPSE LARPPCQAAV ETLQKTIAIQ VSHWPCVKRL AHTVGLSALQ
     AHSSEREESD TVTAMAGLSM QPLKRTSDVS CEDSEEPMDQ DESK
//