ID A0A3N1MHY8_9MICO Unreviewed; 316 AA.
AC A0A3N1MHY8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=NAD-dependent SIR2 family protein deacetylase {ECO:0000313|EMBL:ROQ05472.1};
GN ORFNames=EDF54_2090 {ECO:0000313|EMBL:ROQ05472.1};
OS Rathayibacter sp. PhB93.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=2485103 {ECO:0000313|EMBL:ROQ05472.1, ECO:0000313|Proteomes:UP000270764};
RN [1] {ECO:0000313|EMBL:ROQ05472.1, ECO:0000313|Proteomes:UP000270764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PhB93 {ECO:0000313|EMBL:ROQ05472.1,
RC ECO:0000313|Proteomes:UP000270764};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:ROQ05472.1}.
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DR EMBL; RJLA01000014; ROQ05472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1MHY8; -.
DR Proteomes; UP000270764; 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; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR11085:SF2; NAD-DEPENDENT PROTEIN LIPOAMIDASE SIRTUIN-4, MITOCHONDRIAL; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00236}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 40..316
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 316 AA; 34166 MW; B453511AEB544290 CRC64;
MESGPTPIAD GRRAEDEQSD ERKADQQAER LQAAEADLQR ADAQRSAALD RTVELLAGRR
IAAVTGAGVS TDSGIPDYRG AGAPVRSPMT YSQFVADPDY RRRYWAGSQL GWRRFTATLP
NDGHRALARL EERGLLTGVV TQNVDGLHVR AGSQRVVDLH GSADRVRCMT CGQYFARDAI
AERIEALNPW LDDPDISSLN PDGDAEVHDV SAMTVPECTV CGGILKPDIV FFGEFIPTER
FEEARAIVAG ADALLVAGSS LVVNSGIRFL EIARRAKMPI VIVNRGTTKG DSRAGIKIDG
GTSEVLRALA ERLPSR
//
