ID   A0A383VX20_TETOB        Unreviewed;       884 AA.
AC   A0A383VX20;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN   ORFNames=BQ4739_LOCUS9682 {ECO:0000313|EMBL:SZX69399.1};
OS   Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX   NCBI_TaxID=3088 {ECO:0000313|EMBL:SZX69399.1, ECO:0000313|Proteomes:UP000256970};
RN   [1] {ECO:0000313|EMBL:SZX69399.1, ECO:0000313|Proteomes:UP000256970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Cai Z.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; FNXT01000926; SZX69399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A383VX20; -.
DR   STRING; 3088.A0A383VX20; -.
DR   Proteomes; UP000256970; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 2.
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:SF14; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256970};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          14..375
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          404..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          484..518
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        647..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   884 AA;  88862 MW;  4052F8CB407A6187 CRC64;
     MGDDGSRYSF RKRRRPQQDG IDEALNQLLE LTASCGRLVI FSGSGLSANS GMSMFSTKNG
     LYERARQRFK IQDGIKLFSY PFYKQRRMDV QQFFAQIYGE AKNSKASPGH VAIAQLHELG
     KLQRHYTLNI DGLAEVRSSG SSGSSSERNT TAAAAAAAVA AAAAAAEAAV AAAVAAARET
     PQQQPQQLGD ASMVHTVPGV VGMDTWHHEK NPEGITVEMH GNISYVVCPS CHATERLSGP
     VMATMKAAQP LACTACGEDE MRFKVMLYDD EEGDCITPED VFERLEDDLA VADGVLWVGI
     SFEQSASTEY FRKVRHMLAA AGRLGSVVQV VINPSDEAAF NVLSTVSKRE DVKLLDVRGT
     SDDVLPAMVS ALHAASGTSP DPTYAKAAAE AAAAAARRKA QAQQAAAEAA EAEAAAAAPP
     PRRGRGSSSS CNIKLLAEQE QQQQQLGLEH DSAAAAALAL PAAVQQHFLQ QQLKQQQQQQ
     LSPLLKQEQQ QQQQQQQLQD LKQQVLHSLQ QQQQQQQQGS AAAAAGASPA APGAASSALG
     SLQAVLKASS SGGVSSPLAA AAAAGAASLQ ALLAQKLAAG VNSPLKAAAG AGTAAAAAAA
     AGGGASALLA LLQSTQRNAA ATAAGNGVTA PAAAGVSNLQ GLLLQALQQQ QQHQQHNGSD
     SGQPAAAAAV NGAGTLQLLL QAQQQQQQHA AVAASMAPAA AGSPVPAGNL QAVLLQALLQ
     QQQQQQVAAT NGSPLAAAGA AGAANLQALL AATLAKGGGE GSAALPPPAP TSAAAAPAVG
     LSSLLTSPAV LAALAGAQKE AAPSAAGSSA PPAAAAAAAE PLAALPNGSS VDAVAPAPAV
     TAAAAAASDD ALHAALAAFA KAAAAGAAQA GSAVQPAAAG DNDQ
//