ID I1IW37_BRADI Unreviewed; 465 AA.
AC I1IW37;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN Name=100826316 {ECO:0000313|EnsemblPlants:KQJ81764};
GN ORFNames=BRADI_5g02940v3 {ECO:0000313|EMBL:KQJ81764.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ81764.1};
RN [1] {ECO:0000313|EMBL:KQJ81764.1, ECO:0000313|EnsemblPlants:KQJ81764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ81764.1,
RC ECO:0000313|EnsemblPlants:KQJ81764};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ81764.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ81764.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ81764}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ81764};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000256|ARBA:ARBA00038170}.
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DR EMBL; CM000884; KQJ81764.1; -; Genomic_DNA.
DR EMBL; CM000884; KQJ81767.1; -; Genomic_DNA.
DR RefSeq; XP_003581078.1; XM_003581030.3.
DR AlphaFoldDB; I1IW37; -.
DR STRING; 15368.I1IW37; -.
DR EnsemblPlants; KQJ81764; KQJ81764; BRADI_5g02940v3.
DR EnsemblPlants; KQJ81767; KQJ81767; BRADI_5g02940v3.
DR GeneID; 100826316; -.
DR Gramene; KQJ81764; KQJ81764; BRADI_5g02940v3.
DR Gramene; KQJ81767; KQJ81767; BRADI_5g02940v3.
DR KEGG; bdi:100826316; -.
DR eggNOG; KOG1905; Eukaryota.
DR HOGENOM; CLU_023643_6_4_1; -.
DR InParanoid; I1IW37; -.
DR OMA; MMNLRIP; -.
DR OrthoDB; 1947602at2759; -.
DR Proteomes; UP000008810; Chromosome 5.
DR ExpressionAtlas; I1IW37; baseline and differential.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
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 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd01410; SIRT7; 1.
DR Gene3D; 2.20.28.200; -; 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; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR11085:SF13; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-6; 1.
DR Pfam; PF02146; SIR2; 1.
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 27..269
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 438..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 465 AA; 51829 MW; 6959040399DAE102 CRC64;
MSLGYAKKLS YREDVGSVGM PEMFDSPELL QKKIEELAVM IRKSKHLVVF TGAGISTSSG
IPDFRGPKGV WTLQRSGKGV PDASLPFHRA VPTLTHMALV ELERAGVLKF VISQNVDSLH
LRSGLPREKL AELHGNSFME ICPCCKAEYL RDFEIETIGL KDTPRRCSDK NCGTRLKDTV
LDWEDALPPE EMNSAKEQCL AADLVLCLGT SLQITPACNM PLMSIKNGGK VAIVNLQATP
KDKKASLVIH GLVDKVIAGV MCILNLRIPP YVRIDFIQLS LRHTVKKKCV RWTLRVTSIH
GLRAPLSFLR SIEVSFPERP DMKPVVLMEQ PFSLQRETSM ARAFFMLLTL NFSDGCGCSS
SSIECHVDFQ KQKENFFRDR SLVLQELKCA AERQCRAGQQ SILERQSLAR AETSMHAFVT
NMVSYDAEDL KVAKPRGTWM DSSSNLTKRH LEVPTGGSPP PKKLK
//
