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Database: UniProt
Entry: A0A397TT62_9GLOM
LinkDB: A0A397TT62_9GLOM
Original site: A0A397TT62_9GLOM 
ID   A0A397TT62_9GLOM        Unreviewed;       209 AA.
AC   A0A397TT62;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=DHS-like NAD/FAD-binding domain-containing protein {ECO:0000313|EMBL:RIB00964.1};
GN   ORFNames=C2G38_2298640 {ECO:0000313|EMBL:RIB00964.1};
OS   Gigaspora rosea.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX   NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB00964.1, ECO:0000313|Proteomes:UP000266673};
RN   [1] {ECO:0000313|EMBL:RIB00964.1, ECO:0000313|Proteomes:UP000266673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB00964.1,
RC   ECO:0000313|Proteomes:UP000266673};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC       {ECO:0000256|ARBA:ARBA00006924}.
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:RIB00964.1}.
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DR   EMBL; QKWP01003424; RIB00964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397TT62; -.
DR   STRING; 44941.A0A397TT62; -.
DR   Proteomes; UP000266673; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   PANTHER; PTHR11085:SF7; NAD-DEPENDENT HISTONE DEACETYLASE HST3; 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   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..209
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
SQ   SEQUENCE   209 AA;  23483 MW;  52DCC8271B8FA2A5 CRC64;
     MEDIAKFNLK SENDNFQIRE INRLVVKAKK CVIIAGAGIS CSAGIPDFRS SDGLHNMIQS
     LCPNAFYSGK DLFDAQLPRT QDSIKAFNIF IGILKELIVK ARPTATHSFI KILADMNKLK
     RVYTQNIDNL KEEVGLKPWN FEIKNCQAPV VQLHGTLANL QCSTCTNVYS FTKNIVIFSR
     KLKCQVATNV KRKKTLGLNK GDNYILLDN
//
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