ID C8V606_EMENI Unreviewed; 766 AA.
AC C8V606;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037919};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037919};
GN ORFNames=ANIA_08042 {ECO:0000313|EMBL:CBF73762.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF73762.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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:PIRNR037919}.
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|PIRNR:PIRNR037919};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037919}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|PIRNR:PIRNR037919}.
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DR EMBL; BN001302; CBF73762.1; -; Genomic_DNA.
DR AlphaFoldDB; C8V606; -.
DR STRING; 227321.C8V606; -.
DR ESTHER; emend-q7z8l7; Arb2_domain.
DR EnsemblFungi; CBF73762; CBF73762; ANIA_08042.
DR VEuPathDB; FungiDB:AN8042; -.
DR eggNOG; KOG1343; Eukaryota.
DR HOGENOM; CLU_007727_4_0_1; -.
DR InParanoid; C8V606; -.
DR OMA; FVSPACY; -.
DR Proteomes; UP000000560; Chromosome II.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi.
DR GO; GO:0070823; C:HDA1 complex; IEA:EnsemblFungi.
DR GO; GO:1990342; C:heterochromatin island; IEA:EnsemblFungi.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031934; C:mating-type region heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0070824; C:SHREC complex; IEA:EnsemblFungi.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:AspGD.
DR GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:AspGD.
DR GO; GO:1900197; P:negative regulation of penicillin biosynthetic process; IMP:AspGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; IEA:EnsemblFungi.
DR GO; GO:0042316; P:penicillin metabolic process; IMP:AspGD.
DR GO; GO:0090053; P:positive regulation of pericentric heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IMP:AspGD.
DR GO; GO:0010913; P:regulation of sterigmatocystin biosynthetic process; IMP:AspGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0045460; P:sterigmatocystin metabolic process; IMP:AspGD.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR019154; Arb2-like_domain.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR017321; Hist_deAcase_II_yeast.
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; PF09757; Arb2; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037919};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037919};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037919};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Repressor {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription {ECO:0000256|PIRNR:PIRNR037919};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037919}.
FT DOMAIN 146..456
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT DOMAIN 505..742
FT /note="Arb2-like"
FT /evidence="ECO:0000259|Pfam:PF09757"
FT REGION 743..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 85236 MW; D826B9AF3E5B5159 CRC64;
MVDDEDIIMG EAGYHSANPN TAIAAGQQTT HGHLNGRSDP YLAPPLLSQP MQMPVVQAGN
SQTQESSATT DEARVLSPKI DLNSTVPADA ADITPDYQDS LVDEYSDYAE ESKEAPGLPL
ASLPSGLCYD VQMRYHCEVR PTSDVHPEDP RRIYYIYKEL CRAGLVDDIE STRPLVARPL
KRIHARNATE EEISLVHTAA HYAFVESTKD MSDEELIALE HTRDSIYFNN LTFASSLLSV
GGAIETCLAV ATRKVKNAIA VIRPPGHHAE HDKTMGFCLF NNVSVAARVC QQRLGLSCRK
IMILDWDVHH GNGIQKAFYD DPNVLYISLH VYQNGSFYPG EKDGDADFCG AGAGEGKNVN
IPWPSQGMGD GDYIYAFHQV VMPIAQEFDP DLVIIASGFD AAAGDTLGGC FVTPACYAHM
THMLMTLAQG KVAVCLEGGY NFRSISKSAL AVTKTLMGNP PDRLSFTCPS EAAISTIRRV
SSIQSDYWKC MYPKAIKNEG VWTDRLHDII RAYQAKQLYD NYKLTSLYIY RTAISKSFEN
QVLARPEIMG LPHPLTNNLE AHNCWLADVM KDYVQWAVGK GYAVIDVNIP KHVTTEPSSG
RFEEEDENRP TATEELAGYL WDNYIDPNEA TEIFLVGIGN AFYGVANLLI NRETLYQRVN
GVISFVAKDP VRAVASHTQV WLSRWYRDNS LVFVSKAHGV WKSDRKATKR YGKLIQSSRE
GLSDMLMHHK DEVFQWIEDR IEPESEETEE EKPVKRSPTK AAPKAA
//
