ID B9L852_NAUPA Unreviewed; 264 AA.
AC B9L852;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN OrderedLocusNames=NAMH_0387 {ECO:0000313|EMBL:ACM93369.1};
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nautiliaceae; Nautilia.
OX NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM93369.1, ECO:0000313|Proteomes:UP000000448};
RN [1] {ECO:0000313|EMBL:ACM93369.1, ECO:0000313|Proteomes:UP000000448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH
RC {ECO:0000313|Proteomes:UP000000448};
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(2009).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00236}.
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DR EMBL; CP001279; ACM93369.1; -; Genomic_DNA.
DR RefSeq; WP_015902421.1; NC_012115.1.
DR AlphaFoldDB; B9L852; -.
DR STRING; 598659.NAMH_0387; -.
DR KEGG; nam:NAMH_0387; -.
DR eggNOG; COG0846; Bacteria.
DR HOGENOM; CLU_023643_2_0_7; -.
DR OrthoDB; 9800582at2; -.
DR Proteomes; UP000000448; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00296; SIR2; 1.
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; PTHR11085:SF12; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..264
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
SQ SEQUENCE 264 AA; 30392 MW; 4CA68180D9D854C5 CRC64;
MSEIRKAAKA IKEAKYLLIT AGAGMGVDSG LPDFRGNEGF WKAYPIAKRL GLSFQALANP
RWFDINPRLA WAFYGHRLNM YRNTTPHEGF NILFNMPHEK FIFTSNVDGH FQKAGFSEMK
IVEIHGSIHY LQCSEPCSDS IWENNEHIEI DEEKFEALNY PLCKNCKTIA RPNILMFSDL
RFVDKRVNLQ LARFEYWLSQ INDKLVIIEI GAGKAVPTVR MMSERVRRSF DSTLIRINPL
EADGADIQIK KGALEALREI RKFM
//
