ID A0A1E1JWI6_9HELO Unreviewed; 574 AA.
AC A0A1E1JWI6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Related to NAD-dependent histone deacetylases {ECO:0000313|EMBL:CZS90218.1};
GN ORFNames=RCO7_08628 {ECO:0000313|EMBL:CZS90218.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZS90218.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZS90218.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZS90218.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-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; FJUW01000004; CZS90218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1JWI6; -.
DR STRING; 914237.A0A1E1JWI6; -.
DR InParanoid; A0A1E1JWI6; -.
DR OrthoDB; 1327719at2759; -.
DR Proteomes; UP000178129; 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 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:SF17; DEACETYLASE SIRTUIN-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47651; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 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:UP000178129};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 95..394
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 574 AA; 62218 MW; 92DB06E3C01E4531 CRC64;
MASPSSSSSL SSMSSPLSSI ASRSPSPPGD YPSPPSSHES EKGMKPKSRK VLHSSHCDDS
SPPAPKRQRI TKDKDTNTEY LDISELNASD NEDMHQKEDV KMRKLINVLR TKRRIVVIAG
AGISVSAGIP DFRSSTGLFS SLRNQHKLKT SGKHLFDAAV YRNDNSTSSF HDMVRELGTS
TQNAKPTLFH HMLATLAEEG RLMRLYTQNV DGIDTALPPL ATTVPLNRKG PWPKTIQLHG
GLDKMVCSKC GDLQDFNGGL FEGPEAPLCA RCEEVDIARS AAGFRSHGIG RLRPRMVLYN
EHNPDEDAIG AVSVSDLKRV PDAVIVVGTS LKIPGTRRLT KELCSVTRAR RGGFTAWINL
DPEPIGVEFK DCWDMVVRAE SDEVARAVAL PKWDDKDCGD YVVGGPLLSD MKYARPTVEV
RVKPALINAL NAQGLAIPTD TPRQQSPDSI PLPKLKQTSL AFAPPLTGDL APKKKKSSRP
RKALPSSKPT RAVNAINNTF PATKTTKQPT TKKAFDQENF PSSALFPGLL FTKPTAAPSK
SPKSSQVSVG LPCDRLETIS PVGPIPSGMA KLLD
//