ID A0A3R7MC11_PENVA Unreviewed; 751 AA.
AC A0A3R7MC11;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative histone deacetylase silent information regulator protein Sir2 {ECO:0000313|EMBL:ROT72550.1};
DE SubName: Full=Sirtuin 1 {ECO:0000313|EMBL:QNL90809.1};
GN Name=SIRT1 {ECO:0000313|EMBL:QNL90809.1};
GN ORFNames=C7M84_009082 {ECO:0000313|EMBL:ROT72550.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT72550.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT72550.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT72550.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT72550.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT72550.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QNL90809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=32841684;
RA Kao Z.N., Liu C.H., Liu W.J., Kumar R., Leu J.H., Wang H.C.;
RT "Shrimp SIRT1 activates of the WSSV IE1 promoter independently of the NF-
RT kappaB binding site.";
RL Fish Shellfish 106:910-919(2020).
RN [4] {ECO:0000313|EMBL:QNL90809.1}
RP NUCLEOTIDE SEQUENCE.
RA Kao Z.-N., Liu C.-H., Liu W.-J., Kumar R., Leu J.-H., Wang H.-C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MT505387; QNL90809.1; -; mRNA.
DR EMBL; QCYY01002138; ROT72550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7MC11; -.
DR SMR; A0A3R7MC11; -.
DR STRING; 6689.A0A3R7MC11; -.
DR EnsemblMetazoa; XM_027362423.1; XP_027218224.1; LOC113810777.
DR OrthoDB; 10545at2759; -.
DR Proteomes; UP000283509; 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 CDD; cd01408; SIRT1; 1.
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:SF14; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 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 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 210..512
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 751 AA; 83508 MW; 1B3597866A5C302A CRC64;
MADGARGMES AVPAKRPRLD FPEETSSHQC DSDFQYFAGT SELLSGGYSN GGEFTITSDS
GFNELTPPQS MEDEITTPTS SSQEDTSVRL ENHFGDDNTN DSSVNGCTDN WPTGMPTSQE
DDDEDDRRSV ASTASNLSGL SDFSNFSGKD WKPCAGPMSW VQQQMLRGVN PRTVLNQILG
STREIPDGVA DDALWRLIVN MLSEPPRREK LRHINTLEDV VRLMKACQKI IVLTGAGVSV
SCGIPDFRSR DGIYARLAVD FPDLPDPQAM FDIHYFRRDP RPFFKFAREI YPGQFTPSLC
HRFIRLIEQH NKLLRNYTQN IDTLEQVAGI KDVIQCHGSF ATATCQVCGY KVDAEAIKGD
IFAQRIPQCP KCTENEETTQ GSRIAGDEQK IEDAVSRQTE TNGLDFMQQR QTDPQSLPPQ
PIMKPDIVFF GEGLPDEFHD RMAEDKDECD LLIVIGSSLK VRPVALIPSS VPSHVPQILI
NREPLRHLTF DVELLGDCDI IINELCRRLG RGWDELSQTE PLTEIRELPP RPIPGISVNI
SNGDGDDTNA APGPSLIAPQ HAPHPRDESD IEALRACWAP KIRETMASRL PDNTFLYTGT
HKYIFPGAEV YYDPDDEFED NKSLSSESES EEVEPGEDSQ IEQEEESQES FHSNQTPASS
CHHPRLEDFN STDAPHLSPD DVVSLLSTAD NGQAHEHIED WTSLNASLDT SLDCDHTLPD
YDTDDTHNHI ADTTSKVPEL LADSCSPPTN L
//