SIR4_LEIMA
ID SIR4_LEIMA Reviewed; 320 AA.
AC Q4QB33;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=NAD-dependent protein deacylase SIR2rp2 {ECO:0000255|HAMAP-Rule:MF_03161};
DE EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_03161};
DE AltName: Full=Regulatory protein SIR2 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03161};
DE AltName: Full=SIR2-related protein 2;
DE Flags: Precursor;
GN Name=SIR2rp2; ORFNames=LMJF_23_1210;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
CC -!- FUNCTION: NAD-dependent protein deacylase. Catalyzes the NAD-dependent
CC hydrolysis of acyl groups from lysine residues. {ECO:0000255|HAMAP-
CC Rule:MF_03161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|HAMAP-Rule:MF_03161};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03161};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03161};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03161}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03161}.
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DR EMBL; FR796419; CAJ04804.1; -; Genomic_DNA.
DR RefSeq; XP_001683465.1; XM_001683413.1.
DR AlphaFoldDB; Q4QB33; -.
DR SMR; Q4QB33; -.
DR STRING; 5664.LmjF.23.1210; -.
DR EnsemblProtists; CAJ04804; CAJ04804; LMJF_23_1210.
DR GeneID; 5652114; -.
DR KEGG; lma:LMJF_23_1210; -.
DR VEuPathDB; TriTrypDB:LmjF.23.1210; -.
DR VEuPathDB; TriTrypDB:LMJLV39_230021800; -.
DR VEuPathDB; TriTrypDB:LMJSD75_230022200; -.
DR eggNOG; KOG2683; Eukaryota.
DR HOGENOM; CLU_023643_3_2_1; -.
DR InParanoid; Q4QB33; -.
DR OMA; KINSRCG; -.
DR Proteomes; UP000000542; Chromosome 23.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006471; P:protein ADP-ribosylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006476; P:protein deacetylation; IBA:GO_Central.
DR Gene3D; 3.30.1600.10; -; 1.
DR HAMAP; MF_01967; Sirtuin_ClassII; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026587; Sirtuin_class_II.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Metal-binding; Mitochondrion; NAD; Reference proteome; Transferase;
KW Transit peptide; Zinc.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT CHAIN 23..320
FT /note="NAD-dependent protein deacylase SIR2rp2"
FT /id="PRO_0000417349"
FT DOMAIN 23..308
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 28..48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 108..111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 248..250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
SQ SEQUENCE 320 AA; 35248 MW; E697FB0BA9C70F52 CRC64;
MRPAGTLASF LERCSARKRG RGCVVLTGAG CSTESGIPDY RGPNGQYHRA DFVLLTFQKF
MRDDNEKRRY WARSMLGYST MCGASCNAAH MALQAFTKSG AVAHILTQNV DGLHHLATYG
GVGDAEEEHY YKYTTSDAPL KELHGNIHNV ICTSCGFFMP RARLQRELRE RNPGFYEQYG
ADVSRTRPDG DYSAPTEAVN AMHLVMCPRC NGFFKPHVVL FGENVPKPIV EATMSLVRDK
ASCLLCLGTS LQVYSAYRYV LQANQLGIPV AIVNAGTTRG DAIADLKLDV ESVGSVLAET
AHEMLGVPAS MFFRRKTIQL
