HST1_EMENI
ID HST1_EMENI Reviewed; 489 AA.
AC C8V3W5; Q5B733;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=NAD-dependent protein deacetylase hst1;
DE EC=2.3.1.286;
DE AltName: Full=Homologous to SIR2 protein 1;
DE AltName: Full=Regulatory protein SIR2 homolog 1;
GN ORFNames=AN10449;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
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., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., 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.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., 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]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
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: NAD-dependent histone deacetylase, which could function in
CC telomeric silencing, cell cycle progression and chromosome stability.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA59855.1; Type=Erroneous gene model prediction; Note=The predicted gene AN3647 has been split into 3 genes: AN10433, AN10449 and AN10450.; Evidence={ECO:0000305};
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DR EMBL; AACD01000061; EAA59855.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF75701.1; -; Genomic_DNA.
DR RefSeq; XP_661251.1; XM_656159.1.
DR AlphaFoldDB; C8V3W5; -.
DR SMR; C8V3W5; -.
DR STRING; 162425.CADANIAP00005090; -.
DR EnsemblFungi; CBF75701; CBF75701; ANIA_10449.
DR EnsemblFungi; EAA59855; EAA59855; AN3647.2.
DR GeneID; 2873064; -.
DR KEGG; ani:AN3647.2; -.
DR VEuPathDB; FungiDB:AN10449; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_005651_0_0_1; -.
DR InParanoid; C8V3W5; -.
DR OMA; CHGSWAT; -.
DR OrthoDB; 973532at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi.
DR GO; GO:0031934; C:mating-type region heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0031078; F:histone deacetylase activity (H3-K14 specific); IEA:EnsemblFungi.
DR GO; GO:1990162; F:histone deacetylase activity (H3-K4 specific); IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:EnsemblFungi.
DR GO; GO:0046969; F:NAD-dependent histone deacetylase activity (H3-K9 specific); IEA:EnsemblFungi.
DR GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); IMP:AspGD.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031507; P:heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR Gene3D; 3.30.1600.10; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Metal-binding; NAD; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..489
FT /note="NAD-dependent protein deacetylase hst1"
FT /id="PRO_0000417409"
FT DOMAIN 166..461
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 266..269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 403..405
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 428..430
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 489 AA; 54296 MW; 806A36BCF452F33C CRC64;
MDLASAPRGE SPPLKAPLVE IEAAEVERSL PQENAAPEEK GSNSQSEYES DSDALDDEWE
TQSLYEDAIQ MIRDDQLRDG TIPGACTLEE AIEFRKRLHE VGKAQFVEET IARDTVTAKK
LCTAFGILPP SFLEGAPDEA YHPLLAIAIS REFARRQKLP QYNSVDDAVK LLKESKNIIV
LTGAGISTSL GIPDFRSKDT GLYSKLENLG LNDPQEVFDI RIFREDPGIF YSIAKDILPT
EKKFSPTHGF IRLLQDKGKL LTNYTQNIDN IEANAGVFPE NIVQCHGSFA TATCVKCQYK
VAGDEIYDDI KKGLIPECAQ CRKRIAEDSQ KPQGQKRKRN STSAHKDRSK SGEDSSDGED
YEIPTPGVMK PDITFFGEDL PDEFGRRLLH HDRDKVDLVI VIGTSLKVAP VAEVPGVLPP
HIPQIYISRT PVAHTNFDID LLGDCDVVVS ELCRRAGWEL KHEMISPDEK VDVTPVFGYG
SRHVFKVSG
