ID A0A0L0BS33_LUCCU Unreviewed; 900 AA.
AC A0A0L0BS33;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NAD-dependent histone deacetylase Sir2 {ECO:0000313|EMBL:KNC22852.1};
GN ORFNames=FF38_08056 {ECO:0000313|EMBL:KNC22852.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC22852.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC22852.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC22852.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC22852.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC22852.1}.
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DR EMBL; JRES01001454; KNC22852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0BS33; -.
DR STRING; 7375.A0A0L0BS33; -.
DR EnsemblMetazoa; KNC22852; KNC22852; FF38_08056.
DR OMA; QRVIECH; -.
DR Proteomes; UP000037069; 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 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 263..542
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 60..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..774
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 390
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 900 AA; 100562 MW; CF4BF7E56A3A44AF CRC64;
MMENYEQARL NSDRLEQLDD VLPIKLQERN EFFNSVEEFA VNNKQNFNFG ANILNTKTMS
TSSSSMASTT TATTNANSSS CGEEVVKTNN EIIKTLTLPP TADADLEASL IADTPVSVTD
DPEDPFKSIM DSEEEDDDEE EEQSYQTDNN DNSQLTQDSS QFRQSSKEHE DDDEDNPDTD
DSTTDSDFSD LSGLSDMSGR EWKPINQRPL NWVQKQIHSG ANPREILSKF LPSSAQRISP
ELTDMTLWRI LASMLSEPPR RKKLSYVNTF EDVIDLLNKS KNIMVLTGAG VSVSCGIPDF
RSSDGIYSRL AKDFPDLPDP QAMFDINYFS RDPRPFYKFA REIYPGQFKP SPCHRFIKML
EQKQKLLRNY TQNIDTLEQV AGIKNVIECH GSFSTASCTK CKYKCDADSI RSDIFAQRIP
VCPRCQPNVE QSLDASEPVS ENNLRQLVEN GIMKPDIVFF GEGLPDEFHT VMASDKDKCD
LLIVMGSSLK VRPVALIPSS IPNHVPQILI NREQLHHLEF DVELLGDGDV IINQICHRLG
EDWKDICFSE EVLKESKDLI PLEDDSELDE DTAKEVSSDI MDTLSMKSNH TATPTTTTCS
DSGFETSSTC SKKEGEFLSP EYMDEPMESA SFGGSCDYRH LSIDSSKDSG ILGDASNSAL
TPTFSNLMDT AELNKNSNNL NMPASTTQAI NNKPVVDNLH NTKTVDTNCS EAEKQSIKRQ
MKHQSAAERL YKGTYYVHEN TASYVFPGAQ VSWCSDSEEE DDENLDEYDD NLPHNEDEDT
NHAPLSPLMT PSVENEMVNA ISNTTTNTQQ TSNSFTNSVL LNSCLPQKPQ PQTPPPQPIQ
THRKRHSNET QAEPASFEST SPAEANEHTT GSNSHPPYKK RRDSAEQVTI TSPNISLESS
//
