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Database: UniProt/TrEMBL
Entry: E0VLQ7_PEDHC
LinkDB: E0VLQ7_PEDHC
Original site: E0VLQ7_PEDHC 
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
//
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