ID   D2VWA2_NAEGR            Unreviewed;       297 AA.
AC   D2VWA2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Silent information regulator family protein {ECO:0000313|EMBL:EFC38796.1};
GN   ORFNames=NAEGRDRAFT_73309 {ECO:0000313|EMBL:EFC38796.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC38796.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC38796.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00236}.
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DR   EMBL; GG738904; EFC38796.1; -; Genomic_DNA.
DR   RefSeq; XP_002671540.1; XM_002671494.1.
DR   AlphaFoldDB; D2VWA2; -.
DR   STRING; 5762.D2VWA2; -.
DR   EnsemblProtists; EFC38796; EFC38796; NAEGRDRAFT_73309.
DR   GeneID; 8858639; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_73309; -.
DR   eggNOG; KOG2684; Eukaryota.
DR   InParanoid; D2VWA2; -.
DR   OMA; KCATIAF; -.
DR   OrthoDB; 5476256at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:SF12; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..283
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
SQ   SEQUENCE   297 AA;  33229 MW;  64EADD204540B7A0 CRC64;
     MSDDQKQEEI ASEETMEHIA QLINKARRVV VFSGAGMSAE SGIDTFRGGG GLWTGLMGKL
     FLAYGGTPFG WNITPQICWG QYIKRFYGPI AKADPNNGHF ALAKLEQEVF GDYMEVITQN
     VDGLHQRAGS THVYEVHGTV MRHCCIAERH IFDFDEYWGE ENDEKKMDLP DKSPKCKHPG
     CNSTLRPDCV LFTEALPMDQ WEPSFHAVDR MRKGDVMICV GTSAKVYPAA SLPGRAARRG
     AHLIEFNLEE TDYNQLPNYI FVKGPSGQTL PTIVDRVIEL RNANQSIPSE NISQIVE
//