ID A0A401H0U7_9APHY Unreviewed; 661 AA.
AC A0A401H0U7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN ORFNames=SCP_1202620 {ECO:0000313|EMBL:GBE88034.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE88034.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE88034.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBE88034.1}.
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DR EMBL; BFAD01000012; GBE88034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401H0U7; -.
DR STRING; 139825.A0A401H0U7; -.
DR InParanoid; A0A401H0U7; -.
DR OrthoDB; 1344271at2759; -.
DR Proteomes; UP000287166; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF7; NAD-DEPENDENT HISTONE DEACETYLASE HST3; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 2.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000287166};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 23..415
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 149..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 661 AA; 71845 MW; FE4DEDB66AAAA5F0 CRC64;
MTLFLPLEAS APFPQFPAFL VPSPAPNVHV KKVVKALLKA RRIAVVCGAG ISVQAGIPDF
RSSEGLFQTL KKDNPTLTSG RDLFDASVFN SEVTTSLFCQ MIAQLSELSQ AATPTIFHNL
LRTLDDRGRL LRVYTQNIDA LESKSGLTFG VPDSEGKRSR LRSAKGKAEP SHTEDAAPAP
IVDSPPISGR LPSPPCETPR CIPLHGTLQL MHCQICTHSF PLRNHLADLS SGHPPFCPEC
TALEATRQLV GKRSRGVGKL RPSVVLYNEM HKDGEEVGDV VRRDLIGSSK GKGRAGADLL
LVVGTSLRVP GTKRIVREFS KAVHSRGCCS NAGNDPSTLT AHTSASASSS TMGLVTPTPS
PRRSPADDDE PPVRTVYLNL DFPVPTREWE GVFDVWIRGD AQAFAQLVYE EIEQEKRAKE
AAVERKRRRE EIAEERERKK QRNGELEHAG KTNSGKKRKG APGSASRPSS TKKSKNAPVT
PISPSKIGRP GKILATSNLK TKPKMKAKTK GRADNVLPTF THDKEHTNSN VRLTIRIPPR
VAPAAPLTPP PSKRARLIPE VVITTPPRLI KTPRTPPTPS HPDSPLTPEP SPPPRLRQTP
RTSRRDPSPR KKVEAALATC PVGWNSGDEL SDLTDEDDEG DSSLPESFVR TVQYGLRSAP
G
//
