ID A0A2K6PWX1_RHIRO Unreviewed; 444 AA.
AC A0A2K6PWX1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Sirtuin 1 {ECO:0000313|Ensembl:ENSRROP00000021024.1};
GN Name=SIRT1 {ECO:0000313|Ensembl:ENSRROP00000021024.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000021024.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000021024.1}
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};
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DR AlphaFoldDB; A0A2K6PWX1; -.
DR Ensembl; ENSRROT00000045209.1; ENSRROP00000021024.1; ENSRROG00000034429.1.
DR GeneTree; ENSGT00940000159406; -.
DR Proteomes; UP000233200; Unplaced.
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; 3.40.50.1220; 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; PTHR47651; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 1.
DR PANTHER; PTHR47651:SF4; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 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|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 1..193
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 219..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 444 AA; 49166 MW; 8D25E19B0F5A3593 CRC64;
MCLCSGRKTI LEIYPGQFQP SLCHKFIALS DKEGKLLRNY TQNIDTLEQV AGIQRIIQCH
GSFATASCLI CKYKVDCEAV RGDIFNQVVP RCPRCPADEP LAIMKPEIVF FGENLPEQFH
RAMKYDKDEV DLLIVIGSSL KVRPVALIPS SIPHEVPQIL INREPLPHLH FDVELLGDCD
VIINELCHRL GGEYAKLCCN PVKLSEITEK PPRTQKELAY LSDLPPTPLH ISEDSSSPER
TSPPDSSVIV TLLDQAAKSN DDLDVSESKG LMEEKPQEVQ NSRNVESIAE QMGNPDLKNV
GSSTGEKNER TSVAGTVRKC WPSRVAKEQI SKRLDGNQYL FLPPNRYIFH GAEVYSDSED
DVLSSSSCGS NSDSGTCQSP SLEEPMEDES EIEEFYNGLE DEPDVPERAG GAGFGTDGDD
QEAINEAISM KQEVTDMNYP SNKS
//