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NPD_CALMQ
ID   NPD_CALMQ               Reviewed;         257 AA.
AC   A8MBU4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=NAD-dependent protein deacetylase {ECO:0000255|HAMAP-Rule:MF_01968};
DE            EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_01968};
DE   AltName: Full=Regulatory protein SIR2 homolog {ECO:0000255|HAMAP-Rule:MF_01968};
GN   Name=cobB {ECO:0000255|HAMAP-Rule:MF_01968}; OrderedLocusNames=Cmaq_0442;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC       activities of several enzymes which are inactive in their acetylated
CC       form. Deacetylates the N-terminal lysine residue of Alba, the major
CC       archaeal chromatin protein and that, in turn, increases Alba's DNA
CC       binding affinity, thereby repressing transcription. {ECO:0000255|HAMAP-
CC       Rule:MF_01968}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC         ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC         Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC         EC=2.3.1.286; Evidence={ECO:0000255|HAMAP-Rule:MF_01968};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01968};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01968};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01968}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class U subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01968}.
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DR   EMBL; CP000852; ABW01287.1; -; Genomic_DNA.
DR   RefSeq; WP_012185507.1; NC_009954.1.
DR   AlphaFoldDB; A8MBU4; -.
DR   SMR; A8MBU4; -.
DR   STRING; 397948.Cmaq_0442; -.
DR   EnsemblBacteria; ABW01287; ABW01287; Cmaq_0442.
DR   GeneID; 5709925; -.
DR   KEGG; cma:Cmaq_0442; -.
DR   eggNOG; arCOG04248; Archaea.
DR   HOGENOM; CLU_023643_3_1_2; -.
DR   OMA; EQCKKCR; -.
DR   OrthoDB; 82426at2157; -.
DR   Proteomes; UP000001137; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006476; P:protein deacetylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1600.10; -; 1.
DR   HAMAP; MF_01968; Sirtuin_ClassU; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
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;
KW   Cytoplasm; Metal-binding; NAD; Reference proteome; Transcription;
KW   Transcription regulation; Transferase; Zinc.
FT   CHAIN           1..257
FT                   /note="NAD-dependent protein deacetylase"
FT                   /id="PRO_1000084997"
FT   DOMAIN          11..254
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   ACT_SITE        123
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   BINDING         28..47
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   BINDING         105..108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   BINDING         194..196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT   BINDING         220..222
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
SQ   SEQUENCE   257 AA;  28161 MW;  2582D01DEB2BAFBF CRC64;
     MGNGECLEGG RKAAVILTSS RHAIAFTGAG ISTESGIPDF RGPQGLWRRF DPALASIDYL
     NTDPKGFWEF YIERFRVLNN ARPNKAHLAL AELEKLGIIK YVITQNIDNL HQSAGSINVI
     ELHGNYTTVY CMRCKTQYPF TLALRKYEEG ENPPRCPKCG GILRPNVVLF GEPVNEINRA
     LEIAALSDVA LVVGSSLTVY PAAYVPLVVK EHGGRLIIIN LEPTDYDDYA DVVLHCSASE
     ALDLVLNEVK GIMAAGN
 
 
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