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Database: UniProt
Entry: A0A1E1JWI6_9HELO
LinkDB: A0A1E1JWI6_9HELO
Original site: A0A1E1JWI6_9HELO 
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
//
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