ID   A0A1X7R2F6_9SACH        Unreviewed;       395 AA.
AC   A0A1X7R2F6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Similar to Saccharomyces cerevisiae YDR191W HST4 Member of the Sir2 family of NAD(+)-dependent protein deacetylases {ECO:0000313|EMBL:SMN19848.1};
GN   ORFNames=KASA_0O04466G {ECO:0000313|EMBL:SMN19848.1};
OS   Kazachstania saulgeensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1789683 {ECO:0000313|EMBL:SMN19848.1, ECO:0000313|Proteomes:UP000196158};
RN   [1] {ECO:0000313|EMBL:SMN19848.1, ECO:0000313|Proteomes:UP000196158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC       {ECO:0000256|ARBA:ARBA00006924}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FXLY01000004; SMN19848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7R2F6; -.
DR   STRING; 1789683.A0A1X7R2F6; -.
DR   OrthoDB; 1327719at2759; -.
DR   Proteomes; UP000196158; Unassembled WGS sequence.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00296; SIR2; 1.
DR   Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 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   PANTHER; PTHR11085:SF6; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 1.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196158};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          95..395
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        234
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   395 AA;  44545 MW;  1A63749A32DFED7A CRC64;
     MASSTSNSSS TVPLTPPNTL KRKQQHNVES LNVSPLKPKL LLHDLLQYEK LTPTSSPEKK
     SHKLTSSKNK RKLNGSIRRP IPNSTLSLDC YPMIKPNEKS HNKYLHCILN ECQNIVVVAG
     AGISTYAGIP DFRSKNSGLY SKNKCNKSLM DLNMIYSNES MTLKFNELMV SLYSKSINAK
     ITPFHQLLDK LAEQKRLKRV YTQNIDSLET KLPHVMETQI NKTKGNYPIL VQLHGNISET
     RCNKCNNIRK FDPNRLQTSE NPKGRLIPSC LECEELESVR SIAGLRSKGV GTIRPTITLY
     NEVHNKGDAI ADIINYDTKL KSIDLLIIVG TMLSIPHVKK LCQNMAHSLK NGRRRKGHVI
     FVSNEPPTQS ILNTFKDTLD MIVIGDCQTL YNYID
//