ID A0A0D2XQG4_FUSOF Unreviewed; 487 AA. AC A0A0D2XQG4; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 13-SEP-2023, entry version 37. DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305}; GN Name=28948117 {ECO:0000313|EnsemblFungi:FOXG_06210P0}; OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium oxysporum species complex. OX NCBI_TaxID=660025 {ECO:0000313|EnsemblFungi:FOXG_06210P0, ECO:0000313|Proteomes:UP000002489}; RN [1] {ECO:0000313|Proteomes:UP000002489} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fo5176 {ECO:0000313|Proteomes:UP000002489}; RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212; RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.; RT "A highly conserved effector in Fusarium oxysporum is required for full RT virulence on Arabidopsis."; RL Mol. Plant Microbe Interact. 25:180-190(2012). RN [2] {ECO:0000313|EnsemblFungi:FOXG_06210P0} RP IDENTIFICATION. RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936 RC {ECO:0000313|EnsemblFungi:FOXG_06210P0}; RG EnsemblFungi; RL Submitted (MAY-2023) to UniProtKB. 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 AlphaFoldDB; A0A0D2XQG4; -. DR STRING; 426428.A0A0D2XQG4; -. DR EnsemblFungi; FOXG_06210T0; FOXG_06210P0; FOXG_06210. DR KEGG; fox:FOXG_06210; -. DR VEuPathDB; FungiDB:FOXG_06210; -. DR OMA; PTHEFIR; -. DR OrthoDB; 10545at2759; -. DR Proteomes; UP000002489; Unassembled WGS sequence. DR GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi. DR GO; GO:0031934; C:mating-type region heterochromatin; IEA:EnsemblFungi. DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi. DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi. DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi. DR GO; GO:0031078; F:histone H3K14 deacetylase activity; IEA:EnsemblFungi. DR GO; GO:1990162; F:histone H3K4 deacetylase activity; IEA:EnsemblFungi. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070403; F:NAD+ binding; IEA:EnsemblFungi. DR GO; GO:0046969; F:NAD-dependent histone H3K9 deacetylase activity; IEA:EnsemblFungi. DR GO; GO:0046970; F:NAD-dependent histone H4K16 deacetylase activity; IEA:EnsemblFungi. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0031507; P:heterochromatin formation; IEA:EnsemblFungi. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi. 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; PTHR47651; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 1. DR PANTHER; PTHR47651:SF4; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 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:UP000002489}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}. FT DOMAIN 157..454 FT /note="Deacetylase sirtuin-type" FT /evidence="ECO:0000259|PROSITE:PS50305" FT ACT_SITE 285 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 296 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 320 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236" SQ SEQUENCE 487 AA; 54592 MW; F20FF1B4F1F44E70 CRC64; MHTKKGNGRT VALSKRKAQP NALDKLGDNP TEDEIKTAEA NVALAELEER VADVRESWET DSLFEDAFDE LNADNTVAIN DPKVCTPEEA SRLRRELREY GPTVFCQRTV DAGHYTARKL LSAFGIRPPP FLEGQPDDAY FSLLSLAITR ELSKRAKLLR HNTVDDAVDL ITKSNNIILI TGAGISTSLG IPDFRSKGTG LYSKLEHLGL SDPQEVFDIG VFRQDPTIFY SVAKDILPST DRYTPTHKFI AMLHEKGKLL TNYSQNIDNL EVKAGVPKDK LIQCHGSFGT ATCVQCGYKC PGEAIFPEIK ADKIPRCPRC IQTLRTTGGA PKRKRSAGTE KKRRRWSADS SDESEYDIPS AGVMKPDITF FGEALPDEFS RRLTEHDRDK VDLVIVIGTS LKVTPVSEIV SWLPAHIPQI YVSRQAVNHI NFDIDLLGDC DVVVSELCRR LRWPMVHDMV PKNQKVEVRT EPGYKSRHVF EEQKTKK //