ID   A0A137QNA0_9AGAR        Unreviewed;       515 AA.
AC   A0A137QNA0;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=NAD-dependent histone deacetylase HST3 {ECO:0000313|EMBL:KXN88747.1};
GN   ORFNames=AN958_06614 {ECO:0000313|EMBL:KXN88747.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN88747.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN88747.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN88747.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) 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; KQ962127; KXN88747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137QNA0; -.
DR   STRING; 1714833.A0A137QNA0; -.
DR   OrthoDB; 1344271at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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   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:SF7; NAD-DEPENDENT HISTONE DEACETYLASE HST3; 1.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02146; SIR2; 2.
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   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          13..363
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          364..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   515 AA;  56595 MW;  AC5451D32F558214 CRC64;
     MTITVDLPAA STDVHTRRTL YDLSLAVIKS KRIVVVTGAG ISCSCGIPDF RSSDGLYTLV
     KQKYPDVVLK GRDLFDASLF RDPTSTAVFY TFISGLKRSI DSASPAPAHQ FIRALDAKKR
     LLRSYTQNID GLEERAGLLG TSCEDAKATG KGKSKLKIKD IRNVQLHGDI HRVRCVSCSA
     EYPCTEEHLS MFEQGTAPDC PECLIRSEAR VARSARAIKV GTLRPAIVLY DEPHPLGDEI
     GSIQTADVGR KPDLLIIMGT SLKVHGLKKL VKDFARTIHE TASKSSTLDS KPRPKVIFVN
     KTAPSSEWAD VIDYHVAGET DAWVAKVTED WKKIKPADWE TQQTLDGASS IASPFKALKL
     GTEITSTKKA NKKTKPLQRR DENKMPSGSQ APPLSPSKRR QGTSHYDNLE SSPSKRQSLN
     QPKPPKHALP PSERKLLFGE STNHASTGLE DAAPMDISLV DLSMRDVVPD LEKPEVKPTS
     TTRKTSTFKS RPKPQVASTA KRRTTQKRVV EVIIP
//