ID G1R7G4_NOMLE Unreviewed; 470 AA.
AC G1R7G4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 2.
DT 27-MAR-2024, entry version 62.
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:ENSNLEP00000009137.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000009137.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000009137.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000009137.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G1R7G4; -.
DR STRING; 61853.ENSNLEP00000009137; -.
DR Ensembl; ENSNLET00000009574.3; ENSNLEP00000009137.2; ENSNLEG00000007509.3.
DR eggNOG; KOG1905; Eukaryota.
DR GeneTree; ENSGT00940000159703; -.
DR HOGENOM; CLU_023643_6_2_1; -.
DR InParanoid; G1R7G4; -.
DR OMA; CTKGTKR; -.
DR TreeFam; TF106184; -.
DR Proteomes; UP000001073; 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:0036055; F:protein-succinyllysine desuccinylase activity; IEA:Ensembl.
DR GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; 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: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:1901836; P:regulation of transcription of nucleolar large rRNA by RNA polymerase I; 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:UP000001073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 82..329
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 470 AA; 52466 MW; 7515D4B99D4AD235 CRC64;
MAAGGLSRSE RKAAERVRRL REEQQRERLR QVSRILRKAA AERSAEEGRL LAESADLVTE
LQGRSRRREG LKRRQEEVCD DPEELRGKVR ELAGAVRNAK YLIVYTGAGI STAASIPDYR
GPNGVWTLLQ KGRSVSAADL SEAEPTLTHM SITRLHEQKL VQHVVSQNCD GLHLRSGLPR
TAISELHGNM YIEVCTSCVP NREYVRVFDV TERTALHRHQ TGRTCHKCGT QLRDTIVHFG
ERGTLGQPLN WEAATEAASR ADTILCLGSS LKVLKKYPRL WCMTKPPSRR PKLYIVNLQW
TPKDDWAALK LHGKCDDVMR LLMAELGLEI PAYSRWQDPI FSLATPLRDG EEGSHSRKSL
CRSREEAPPG DRGAPLSSAP ILGGWFGRGC TKRTKRKKVT PGAVAHACNP STLGGRGGWI
TRSGDRDHSE TPSLLKIQKI SRAQWRAPVV PATPEAETGE WREPGRQSLQ
//
