SIR2_LEIMA
ID SIR2_LEIMA Reviewed; 373 AA.
AC Q25337; Q4Q9H0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=NAD-dependent protein deacetylase SIR2rp1;
DE EC=2.3.1.286;
DE AltName: Full=Regulatory protein SIR2 homolog 1;
DE AltName: Full=SIR2-related protein 1;
GN Name=SIR2rp1; Synonyms=SIR2; ORFNames=LMJF_26_0210;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8635734; DOI=10.1016/0378-1119(95)00785-7;
RA Yahiaoui B., Taibi A., Ouaissi A.;
RT "A Leishmania major protein with extensive homology to silent information
RT regulator 2 of Saccharomyces cerevisiae.";
RL Gene 169:115-118(1996).
RN [2]
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 deacetylase, which probably acts as a regulator
CC of gene expression believed to help form modified chromatin structures
CC on the genes it regulates. {ECO:0000250}.
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|PROSITE-ProRule:PRU00236};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB06804.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L40331; AAB06804.1; ALT_FRAME; mRNA.
DR EMBL; FR796422; CAJ04546.1; -; Genomic_DNA.
DR PIR; JC4639; JC4639.
DR RefSeq; XP_001684028.1; XM_001683976.1.
DR AlphaFoldDB; Q25337; -.
DR SMR; Q25337; -.
DR STRING; 5664.LmjF.26.0210; -.
DR EnsemblProtists; CAJ04546; CAJ04546; LMJF_26_0210.
DR GeneID; 5652751; -.
DR KEGG; lma:LMJF_26_0210; -.
DR VEuPathDB; TriTrypDB:LmjF.26.0210; -.
DR VEuPathDB; TriTrypDB:LMJLV39_260007000; -.
DR VEuPathDB; TriTrypDB:LMJSD75_260006900; -.
DR eggNOG; KOG2682; Eukaryota.
DR InParanoid; Q25337; -.
DR OMA; PCSRLPR; -.
DR Proteomes; UP000000542; Chromosome 26.
DR GO; GO:0005856; C:cytoskeleton; ISO:GeneDB.
DR GO; GO:0005829; C:cytosol; ISO:GeneDB.
DR GO; GO:0005634; C:nucleus; ISO:GeneDB.
DR GO; GO:0004407; F:histone deacetylase activity; ISO:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISO:GeneDB.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; ISO:GeneDB.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; ISO:GeneDB.
DR GO; GO:0042903; F:tubulin deacetylase activity; ISO:GeneDB.
DR GO; GO:0042113; P:B cell activation; ISO:GeneDB.
DR GO; GO:0006281; P:DNA repair; ISO:GeneDB.
DR GO; GO:0042116; P:macrophage activation; ISO:GeneDB.
DR GO; GO:0052167; P:modulation by symbiont of host innate immune response; ISO:GeneDB.
DR Gene3D; 3.30.1600.10; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR017328; Sirtuin_class_I.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR PIRSF; PIRSF037938; SIR2_euk; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; NAD; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..373
FT /note="NAD-dependent protein deacetylase SIR2rp1"
FT /id="PRO_0000110273"
FT DOMAIN 20..351
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 263..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 39..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 216..218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 241..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 40554 MW; 963EE7E11CE2FAC9 CRC64;
MTGSPRAPHQ EHALGEPTVE GLARYIREKD VRRILVLVGA GASVAAGIPD FRSSDTGIYA
KLGKYNLDDP TDAFSLTLLR EKPEIFYSIA RELNLWPGHF QPTAVHHFIR LLQDEGRLLR
CCTQNIDGLE KAAGVSPELL VEAHGSFAAA ACIECHTPFS IEQNYLEAMS GTVSRCSTCG
GIVKPNVVFF GENLPDAFFD ALHHDAPIAE LVIIIGTSMQ VHPFALLPCV VPKSIPRVLM
NRERVGGLLF RFPDDPLDTI HDDAVAKEGR SSSSQSRSPS ASARREEGGT EDGSSSPNEE
VEDASTSSSS DGYGQYGDYY AHPDVCRDVF FRGDCQENVL KLAECLGLRE ALAKRMRFSG
AAPATARKTS NET
