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}.
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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
//