ID A0A182VKA3_ANOME Unreviewed; 1190 AA.
AC A0A182VKA3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911};
OS Anopheles merus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM016411-PA, ECO:0000313|Proteomes:UP000075903};
RN [1] {ECO:0000313|Proteomes:UP000075903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles merus MAF (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEM016411-PA}
RP IDENTIFICATION.
RC STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM016411-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182VKA3; -.
DR STRING; 30066.A0A182VKA3; -.
DR EnsemblMetazoa; AMEM016411-RA; AMEM016411-PA; AMEM016411.
DR VEuPathDB; VectorBase:AMEM016411; -.
DR VEuPathDB; VectorBase:AMEM21_004034; -.
DR Proteomes; UP000075903; 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; 2.
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 781..1094
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 228..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 64..91
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 232..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 903
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 773
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 775
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 781
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 851
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
SQ SEQUENCE 1190 AA; 125953 MW; 1A69A4A1BFBA84F4 CRC64;
MARDSTMGRD RVLVVPNTGI ALNSSSSSSQ IAAPADISQQ ILELQKEQEL EKQKLWHAFQ
EKNKELEMQH RQQLEHKFQE LRDQRIAEEA AQQRERRERE AIKRKEKHEC CANASSEVKQ
KLQTFLIQKK QAAASNGLSS PLPYRNWGVV KSSSGESLPG GAVAAAVSSH PYKIPPPPSS
IAKYDPDFPL RKTASEPNLL KIRLKQRVIE KRSLNGPLAA RRQERLRRLQ KQQHNQALAQ
TNCAASASVA TTDSGPNSPP TVGSRASPTN APIQEENEDP QYGSVTSRAS INDLSLFSSP
SMPNISLGRP HLGSSAAASV AHLALNATRP THLGVGAGIG GQTGSVPFGS PMLDLSEQQQ
RSQNVAVAAA AAAAAAAAAA AASGVVGLER AHLAAGGLHG AAGPGSAASL YHHQPSITDA
HVAQARLHKQ GHRPLGRTQS APLPLGHPML AGANSAAAAM MNINQTHFEN SEAERQAYEQ
HMLMKQKIRQ TALTRAANCV NREPQLREEV ESNEVIDLTD KKQPPKTVLA SSVIKSTSQS
HLLSSSSHGV DGEPPTAQQQ QQQQQQHLSE LIHQQQHYHR ERELFMRRSI QLSVLEDPYS
HHAGSAGGSG GAAAAAAAAA AAANLLRPLS RTSSSPLVHL SSIGGGGGGG SGSGGAHPTA
QQSMFSDTGQ GAGGDDDLPP PVNLTVQNRS RSLLSYTHEG LAAAMASASS SSPAAAGALG
GTAGASCGSP PGMALQLTTS SSASAIIGAS REQKLRPATT GLAFDSLMLK HVCACGDNAN
HPEHSGRLQS IWARLLGTGL AIRCDKLRSR KATQEELQTV HTEGHALLFG TSQLNRQKVD
TSRVSFVRLA CGGVGVDLDT TWNEHHTAAA ARMAAGCVID LSYKVARGEN RNGFAVVRPP
GHHAEADAAM GFCFFNSIAL AARLLRHRMP HEMRRILIVD WDVHHGNGTQ QAFYDDASVL
YLSVHRHDDG NFFPGTGGPA ECGVGTGLGY NVNVAWSGGV NPPLGDAEYL AAFRTVVMPI
ARDFAPDIVL VSAGFDAAVG HPAPLGGYVV SPACFGHLTR ELMQLANGKI VLALEGGYDL
PAICDSAEEC VRALLGESTS SIAPSELARP PCQAAVETLQ KTIAIQVSHW PCVKRLAHTV
GLSALQAHSS EREESDTVTA MAGLSMQPLK RTSDVSCEDS EEPMDQDESK
//
