ID E0VLQ7_PEDHC Unreviewed; 1002 AA.
AC E0VLQ7;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
GN Name=8229687 {ECO:0000313|EnsemblMetazoa:PHUM292420-PA};
GN ORFNames=Phum_PHUM292420 {ECO:0000313|EMBL:EEB14313.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB14313.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB14313.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB14313.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB14313.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM292420-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM292420-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|ARBA:ARBA00004123,
CC 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 EMBL; AAZO01003391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235279; EEB14313.1; -; Genomic_DNA.
DR RefSeq; XP_002427051.1; XM_002427006.1.
DR AlphaFoldDB; E0VLQ7; -.
DR STRING; 121224.E0VLQ7; -.
DR EnsemblMetazoa; PHUM292420-RA; PHUM292420-PA; PHUM292420.
DR GeneID; 8229687; -.
DR KEGG; phu:Phum_PHUM292420; -.
DR CTD; 8229687; -.
DR VEuPathDB; VectorBase:PHUM292420; -.
DR eggNOG; KOG1343; Eukaryota.
DR HOGENOM; CLU_006530_0_1_1; -.
DR InParanoid; E0VLQ7; -.
DR OMA; XAVASTE; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000009046; 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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd11681; HDAC_classIIa; 1.
DR Gene3D; 6.10.250.1550; -; 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; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF10; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046};
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 25..104
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 590..907
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 718
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
SQ SEQUENCE 1002 AA; 110621 MW; B5A9827633AF7753 CRC64;
MKRNTVAKSP ILSRQNDVNH TYPGDPGLHA QAFQQQLLQL KKQQQLQQQI LLQHYQTQQQ
QLAEQHEQQL RHHLKEFREQ QKALEEQKER REKEKLEALK RKDKHEQSAV ASSEVKQRLQ
GFLLNKKQRE AAANGTSGPL PGSASFNRSQ QWGEPPSSTP SGAGAPHPYH LNHLVAAKYD
EDFPLRKTAS EPNLLKVRLK QRVIERRASP MARRNQRLIS TLKKKSVLVN AANNSTETTS
SNSPPVVTNL RTSPSAAGST PIREEPESPT YGQLSNSSQQ GSMSDLSLYS SPSMPNISLG
RPPSSHNSGH ENKLASVSEA EVRAAFTARL GMPLTGQMLP GTLPFYPTLP AIDSEPTDSA
AVHKQMETLE QSGNPTVSGY QQMTDSQVAH ARLTKHGHRP LGRTQSAPLP LGHPMLASHN
VLTIPQRYED QRTQHNLLKQ QIRQTVLTRA GRQLEDQPEV VDETAEVIDL TDQRLEVDED
QNECEMSRQQ KDREQFLQQQ RDLMMRHNLQ ANEGSTFVPR NTSYVARPLS RALSSPLVAL
GGSDIPLSPV NCHSSHVPKL NSSVHCITTG LAFDNLMLKH ACVCGDNSSH PEHGGRLQSV
WARLLETGLV ARCDRLRARK ATIEEIQSCH SEAHALLFGT NPLNRQKLDI NKIAALPIKC
FVRLPCGGVG VDSDTTWNEL HTAPAARMAV GCVVDLAMKT AMGDMKNGFA VVRPPGHHAE
NSQAMGFCFF NSVAIAAKLL QQRLRVRKIL IFDWDVHHGN GTQQMFYDDP HVLYLSVHRH
DDGNFFPGTG GPTECGTGEG LGYNVNIAFS GGLQPPMGDA EYLAAFRTIV MPIAKKFDPD
IVLVSAGFDA AAGHPPPLGG YKVSASCFGH MTQELLNLAD GKVVLALEGG YDLPSICDAA
QECVRALLGD DPTPISEEEL TRPPCQAAVD TMQKTIAIQL THWPCLKKLA HTVGLPYAEK
EKEDSDTITR MAGLSMQQNQ YLQSPERTHR DSEEPMEEDE GK
//