ID A0A2K6UPU2_SAIBB Unreviewed; 345 AA.
AC A0A2K6UPU2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Regulatory protein SIR2 homolog 7 {ECO:0000256|ARBA:ARBA00043038};
DE AltName: Full=SIR2-like protein 7 {ECO:0000256|ARBA:ARBA00041832};
GN Name=SIRT7 {ECO:0000313|Ensembl:ENSSBOP00000033931.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000033931.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000033931.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000256|ARBA:ARBA00038170}.
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DR AlphaFoldDB; A0A2K6UPU2; -.
DR STRING; 39432.ENSSBOP00000033931; -.
DR Ensembl; ENSSBOT00000050848.1; ENSSBOP00000033931.1; ENSSBOG00000033138.1.
DR GeneTree; ENSGT00940000159703; -.
DR OMA; HRHTTGR; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005731; C:nucleolus organizer region; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0097372; F:NAD-dependent histone H3K18 deacetylase activity; IEA:Ensembl.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:Ensembl.
DR GO; GO:0061697; F:protein-glutaryllysine deglutarylase activity; IEA:Ensembl.
DR GO; GO:0106231; F:protein-propionyllysine depropionylase activity; IEA:Ensembl.
DR GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; IEA:Ensembl.
DR GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; IEA:Ensembl.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IEA:Ensembl.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0062176; P:R-loop processing; IEA:Ensembl.
DR GO; GO:0006282; P:regulation of DNA repair; IEA:Ensembl.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IEA:Ensembl.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:1901836; P:regulation of transcription of nucleolar large rRNA by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0010526; P:retrotransposon silencing; IEA:Ensembl.
DR GO; GO:0009303; P:rRNA transcription; IEA:Ensembl.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl.
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:SF1; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-7; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 27..274
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 299..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 345 AA; 38384 MW; 908262C6BE239B85 CRC64;
MAAGGLSRSE RKAAERVRRL REVCDDPEEL RGKVRELASA IRNAKYLVVY TGAGISTAAS
IPDYRGPNGV WTLLQKGRSV SAADLSEAEP TLTHMSITRL HEQKLVQHVV SQNCDGLHLR
SGLPRSAISE LHGNMYIEVC TSCVPNREYV RVFDVTERTA LHRHQTGRTC HKCGAQLRDT
IVHFGERGTL GQPLNWEAAT EAASRADTIL CLGSSLKVLK KYPRLWCMTK PPSRRPKLYI
VNLQWTPKDD WAALKLHGKC DDVMRLLMAE LGLEIPAYSR WQDPIFSLAT PLRAGEEGSH
SRKSLCRSRE EAPPGDRGAP LSSAPILGGW FGRGCTKRTK RKKVT
//
