HST3_CANAL
ID HST3_CANAL Reviewed; 487 AA.
AC Q5A1W9; A0A1D8PN58; Q5A1R1;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=NAD-dependent histone deacetylase HST3;
DE EC=2.3.1.286;
DE AltName: Full=Homologous to SIR2 protein 3;
DE AltName: Full=Regulatory protein SIR2 homolog 3;
GN Name=HST3; OrderedLocusNames=CAALFM_C501340WA;
GN ORFNames=CaO19.1934, CaO19.9490;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
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DR EMBL; CP017627; AOW29568.1; -; Genomic_DNA.
DR RefSeq; XP_715697.2; XM_710604.2.
DR AlphaFoldDB; Q5A1W9; -.
DR SMR; Q5A1W9; -.
DR STRING; 237561.Q5A1W9; -.
DR PRIDE; Q5A1W9; -.
DR GeneID; 3642641; -.
DR KEGG; cal:CAALFM_C501340WA; -.
DR CGD; CAL0000186930; HST3.
DR VEuPathDB; FungiDB:C5_01340W_A; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_021544_4_0_1; -.
DR InParanoid; Q5A1W9; -.
DR OrthoDB; 1503290at2759; -.
DR PRO; PR:Q5A1W9; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Cytoplasm; Metal-binding; NAD; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Transferase; Zinc.
FT CHAIN 1..487
FT /note="NAD-dependent histone deacetylase HST3"
FT /id="PRO_0000417413"
FT DOMAIN 23..328
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 397..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 261..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 291..293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 487 AA; 55080 MW; 1483C2D2C161B1F6 CRC64;
MISIDLLDNS GTSMPADTSI KLHEVIKFIS KSKKMTVLTG AGISCNAGIP DFRSSDGLYN
MVKAKHPKAV VRGQDLFDIS LFRDEMSLSV FCTFMESLYK SSLNAKPTET HKFIKILKDK
NKLLRCYTQN IDCIEQHINL KLGINLQEFD NNKFKQVWNQ LDVVQLHGNL HKLSCTNCFS
QFNWNEEFQT LLANGLNPEC SKCMDKYQQR LYSGKRLTGQ TIGLLRPDIV LYGEHHPQME
ILTQGLNSDL KSRPDCLIIM GTSLKVAGVK SLVKSLSKII HNKGGKVIYV NKTKLSASSW
KNYIDYEVVS DCDEFVRMLK TEIPDLFLTQ EQLDSEKLNQ VAVKGSSLNK PIVKPEAKVK
IEPGIKQEDA IQYSPEREVT IKQEVNIKQE PIVKREVESV SVKEEPIPTP PTTPHKPKQA
TKLKRKSPDE ISANEVHSRV KRLRPRNDQL SSPASSINGS EEEEEEDEPV AKVLFENARK
GITLDQH
