HST1_CANAL
ID HST1_CANAL Reviewed; 655 AA.
AC Q5AQ47; A0A1D8PEH2; Q5APK3;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 100.
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 Name=HST1; Synonyms=SIR21, SIR22; OrderedLocusNames=CAALFM_C109050WA;
GN ORFNames=CaO19.12225, CaO19.4761;
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: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
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DR EMBL; CP017623; AOW26539.1; -; Genomic_DNA.
DR RefSeq; XP_723447.2; XM_718354.2.
DR AlphaFoldDB; Q5AQ47; -.
DR SMR; Q5AQ47; -.
DR STRING; 237561.Q5AQ47; -.
DR GeneID; 3634770; -.
DR KEGG; cal:CAALFM_C109050WA; -.
DR CGD; CAL0000190389; HST1.
DR VEuPathDB; FungiDB:C1_09050W_A; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_023643_5_0_1; -.
DR InParanoid; Q5AQ47; -.
DR OrthoDB; 973532at2759; -.
DR PRO; PR:Q5AQ47; -.
DR Proteomes; UP000000559; Chromosome 1.
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:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); 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; IPR007654; NAD-dep_histone_deAcase_SIR2_N.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF04574; DUF592; 2.
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..655
FT /note="NAD-dependent protein deacetylase HST1"
FT /id="PRO_0000417408"
FT DOMAIN 290..585
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 307..326
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 389..392
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 527..529
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 552..554
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 655 AA; 74332 MW; 89D29DBB07E319B0 CRC64;
MPGDNDIVLV DSSSDNEEER EEDDDDESQH REIKKFKPNP NPSQTRDMNE SHVINKSNFS
TVPFNAVSSS SSSDNDQDND EEEEEEEEEE EEEEEEEEEE EEEEEEEEEE EEEESEINGN
QISLSIDDEY DSEGLTKESS RTPIGSNTSD IIINGVTIIT NNNDSSLVAS SSDDDDDDDD
DDDKDDDNDD DASDLESDFA FEEIPPSLIM ETRKYLKQNG TMKFLEKYLP TAASIENIIK
LILQLGFVPK RKLNNGLDEN DIMEYIKILN HAIIKVKSIR ERREDITTIN DALKLIENSK
NIMVITGAGI STSLGIPDFR SSQGFYSMIQ HLGLSDPQEV FDLDLFLNDP NIFYSIAHMI
LPPNHIYSPL HSFIKLLQDK NKLLRNYTQN IDNLESYAGI HKENLIQCHG SFATASCITC
GYKVDGEIIF PEIKNKEIPY CPKCNEVKQS ILKKGKKTKS KSKKKKKKKN KPYDDDDEEE
EEGETYFHES FGVMKPDITF FGEQLPENFK IAINQDINKV DLVLVIGTSL KVAPVADIVG
KIPEHIPQIL LNKDPINHCQ FDVSLLGYCD DVASYIANEL GESWDLPHPD YNKIRGEKNG
ENLSVQLLDS TLREYLISNK KNDLSSEQEQ NKMGEENRKV EESGRRPNES GGKSG
