(data stored in SCRATCH zone)

SWISSPROT: C4KKV4_SULIK

ID   C4KKV4_SULIK            Unreviewed;       247 AA.
AC   C4KKV4;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|HAMAP-Rule:MF_01968};
DE            EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_01968};
DE   AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01968};
GN   Name=cobB {ECO:0000256|HAMAP-Rule:MF_01968};
GN   OrderedLocusNames=M164_0285 {ECO:0000313|EMBL:ACR40919.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40919.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40919.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC       activities of several enzymes which are inactive in their
CC       acetylated form. Deacetylates the N-terminal lysine residue of
CC       Alba, the major archaeal chromatin protein and that, in turn,
CC       increases Alba's DNA binding affinity, thereby repressing
CC       transcription. {ECO:0000256|HAMAP-Rule:MF_01968}.
CC   -!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
CC       acetyl-ADP-ribose + a protein. {ECO:0000256|HAMAP-Rule:MF_01968}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01968};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01968};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01968}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class U subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01968}.
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DR   EMBL; CP001402; ACR40919.1; -; Genomic_DNA.
DR   RefSeq; WP_012710436.1; NC_012726.1.
DR   EnsemblBacteria; ACR40919; ACR40919; M164_0285.
DR   GeneID; 7813393; -.
DR   KEGG; sid:M164_0285; -.
DR   HOGENOM; HOG000085951; -.
DR   KO; K12410; -.
DR   OMA; SMQVYPA; -.
DR   OrthoDB; POG093Z06CT; -.
DR   BioCyc; SISL426118:GI01-287-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   HAMAP; MF_01968; Sirtuin_ClassU; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR028628; Sirtuin_class_U.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KKV4.
DR   SWISS-2DPAGE; C4KKV4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01968};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01968};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01968};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01968};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_01968};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01968};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01968}.
FT   DOMAIN        4    246       Deacetylase sirtuin-type.
FT                                {ECO:0000259|PROSITE:PS50305}.
FT   NP_BIND      21     40       NAD. {ECO:0000256|HAMAP-Rule:MF_01968}.
FT   NP_BIND      98    101       NAD. {ECO:0000256|HAMAP-Rule:MF_01968}.
FT   NP_BIND     186    188       NAD. {ECO:0000256|HAMAP-Rule:MF_01968}.
FT   NP_BIND     212    214       NAD. {ECO:0000256|HAMAP-Rule:MF_01968}.
FT   ACT_SITE    116    116       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01968}.
FT   METAL       124    124       Zinc. {ECO:0000256|HAMAP-Rule:MF_01968}.
FT   METAL       127    127       Zinc. {ECO:0000256|HAMAP-Rule:MF_01968}.
FT   METAL       149    149       Zinc. {ECO:0000256|HAMAP-Rule:MF_01968}.
FT   METAL       151    151       Zinc. {ECO:0000256|HAMAP-Rule:MF_01968}.
SQ   SEQUENCE   247 AA;  27550 MW;  4404070983BE4C00 CRC64;
     MIYEKVAEEL ISSSYAIAFT GAGISTASGI PDFRGPQGLW KKYSPELASI EYFEKDPKNF
     WGFYSLRMRG LFEAQPNKAH YSLAELEKMG IIKVIITQNI DGLHQKAGSK NVIELHGTMR
     RSYCVLCLRT YDSLNVLSMI EKGNLPPRCD CGGIIRPDVV LFGEPVKNIY EALSIAYESD
     LVISIGSSLT VYPANLIPQT VKERGGKLII LNMEETPLDS IADYVVREPV EISLPKIVEN
     VRQKILS
//

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