ID A7EMW8_SCLS1 Unreviewed; 533 AA.
AC A7EMW8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN ORFNames=SS1G_06667 {ECO:0000313|EMBL:EDO04184.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO04184.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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DR EMBL; CH476628; EDO04184.1; -; Genomic_DNA.
DR RefSeq; XP_001592426.1; XM_001592376.1.
DR AlphaFoldDB; A7EMW8; -.
DR STRING; 665079.A7EMW8; -.
DR GeneID; 5488440; -.
DR KEGG; ssl:SS1G_06667; -.
DR VEuPathDB; FungiDB:sscle_13g094440; -.
DR InParanoid; A7EMW8; -.
DR OMA; PTHEFIR; -.
DR OrthoDB; 10545at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0046970; F:NAD-dependent histone H4K16 deacetylase activity; IBA:GO_Central.
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; IPR007654; NAD-dep_histone_deAcase_SIR2_N.
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; PF04574; DUF592; 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:UP000001312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 190..489
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 23..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 533 AA; 59200 MW; E162F9FEF1BAF8E5 CRC64;
MNSATLNGVG SVTKSPLSKT INLLSDAEDS ENDDVLQGVS RDTSRGMPHH QNAVPQELEE
ALSANESSVE DESEGFAAEP ESEDRDEEED SESSLLEDLM DGLTDEALYD DESNPERCTR
EEAQNYRRDL RRLGPREFCR VTVESNTVTA KKLLTAFAIR PPSYLEGQPD EEYYQLLSYA
LRRELMKRLK LPDYNTVDDA IVLIKNAKKI IVITGAGIST SLGIPDFRSA NGLYAQLEDT
GLSDPQEVFN IDLFREDPTI FFQIAKNILP SVVRFSPTHQ FIKVLQDKGK LLTNYTQNID
GIESAAGILP ENVIQCHGSF ATATCQQCST QVKGTEVFPE IKAGNIPRCK VKGCKIPAPP
PPKQTLKRKR SSNGGSKKRG RSKNDDENEE DDIPQPGIMK PDITFFGESL PDKFADRLSK
HDRDQVDLVI TIGTSLKVAP VSEVVPYLPS NVPQIQINRD PVSHVEFDID LLGECDVVVS
ELSKALGWSL DHEMIPKNQE IEVTTVPGFN NRHQFKQTHP APVRAPVPEI KTD
//
