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Database: UniProt
Entry: A0A1Q9DY51_SYMMI
LinkDB: A0A1Q9DY51_SYMMI
Original site: A0A1Q9DY51_SYMMI 
ID   A0A1Q9DY51_SYMMI        Unreviewed;       248 AA.
AC   A0A1Q9DY51;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=NAD-dependent protein deacylase 2 {ECO:0000313|EMBL:OLQ00092.1};
GN   Name=cobB2 {ECO:0000313|EMBL:OLQ00092.1};
GN   ORFNames=AK812_SmicGene17256 {ECO:0000313|EMBL:OLQ00092.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ00092.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLQ00092.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ00092.1,
RC   ECO:0000313|Proteomes:UP000186817};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA   Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA   Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT   adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00236}.
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:OLQ00092.1}.
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DR   EMBL; LSRX01000339; OLQ00092.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9DY51; -.
DR   OrthoDB; 167219at2759; -.
DR   Proteomes; UP000186817; 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; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 2.
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; 2.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..248
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
SQ   SEQUENCE   248 AA;  26999 MW;  FF22213503F46498 CRC64;
     MLLVGQTLAF TGAGISKESG VPTYRDGDGL WKRYDAMEVS SISGLAGQPS KVWAFEREFY
     DILQRCQGLA FGGPNPGHRA LAALEESGVP TYRDGDGLWK RYDAMEVSSI SGLAGQPSKV
     WAFEREFYDI LQRCQGLAFG GPNPGHRALA ALEDMVVTQN VDGFHQAAGS KVVELHGSEV
     HAICLNKSRL FAPDAGDLWE VFRSTGYPEI SVDLAAWGLR WPEASGSEFI EFQSFENRAG
     DGIGVFLD
//
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