ID A7EC18_SCLS1 Unreviewed; 446 AA.
AC A7EC18;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN ORFNames=SS1G_02855 {ECO:0000313|EMBL:EDN99996.1};
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:EDN99996.1, 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; CH476623; EDN99996.1; -; Genomic_DNA.
DR RefSeq; XP_001596634.1; XM_001596584.1.
DR AlphaFoldDB; A7EC18; -.
DR STRING; 665079.A7EC18; -.
DR EnsemblFungi; EDN99996; EDN99996; SS1G_02855.
DR GeneID; 5493073; -.
DR KEGG; ssl:SS1G_02855; -.
DR VEuPathDB; FungiDB:sscle_04g037620; -.
DR eggNOG; KOG2682; Eukaryota.
DR HOGENOM; CLU_023643_0_0_1; -.
DR InParanoid; A7EC18; -.
DR OMA; ECKEEYP; -.
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:0017136; F:NAD-dependent histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd01408; SIRT1; 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:SF10; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-2; 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:UP000001312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 17..279
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 342..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 446 AA; 48388 MW; 1DE206083A31E20C CRC64;
MGQEASHAQI NPDDPPHTLP ARSIEGVAEF IKNGQAKNIV VLTGAGISTS AGIPDFRSPE
TGIYANLAEL DLPYAEAVFD IDFFRENPAP FYVLAKELYP GQFYPTISHA FVALIEKKGL
LRMLFTQNID CLERRAGVSS EKVIEAHGSF ATQRCIDCKT EYPDDMMKKA IQEGDPATCL
VPQCGGLVKP DIVFFGEQLP EAFHSHKMIP ATADLIIVMG TSLSVQPFAM LPSLPADTVP
RLLFNMISVG DFGSRLDDVV VLGDCDTGVR KLADALGWRA ELEELWISVG GNTRQKEAEK
AAEARLNMSR DERHEVDIEK LTTEIDEALK FSGNHTHRVI ADLQKSPPIN STPSPPPPEA
MPTRAPTEFT ADKSSLLSDI TNGAALKDAT TIVRSTPIID EKGATTKPAL ADSHSSAGKR
DENSSVVLDA TMPQNMPNSF NLTTNS
//
