ID A0A397HUA6_9EURO Unreviewed; 504 AA.
AC A0A397HUA6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN ORFNames=CDV56_109523 {ECO:0000313|EMBL:RHZ66785.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ66785.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ66785.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ66785.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-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:RHZ66785.1}.
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DR EMBL; NKHU02000010; RHZ66785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HUA6; -.
DR STRING; 41047.A0A397HUA6; -.
DR VEuPathDB; FungiDB:CDV56_109523; -.
DR OrthoDB; 10545at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF11; NAD-DEPENDENT PROTEIN DEACETYLASE HST2-2; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF13671; AAA_33; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..259
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
SQ SEQUENCE 504 AA; 56379 MW; C967D1D829A28196 CRC64;
MTDIENIANL IKTGQAPRIV VLVGAGISAA AGIPDFRSPE TGIYDRLKPL KLPYPEAIFH
TSYFKHTPEP FYAIARARHP RSLKPTITHA FLALLAKKNL LHFLFTQNID GLEQDVGVPE
DKILNAHGSW RTQRCWKCET PYPDDLMKQA INTGNVPYCQ VPDCGGAVKP DVVFFGQPLP
AEFAEKKTKV PEADLMLVMG TSLKVAPCSE LPRLVREGVP RVLINRETAG NLGMRPEDVC
ILGDCDDGVR KLADALGWTE EMESLWKEAI AAKDAVQEDW GDEERLEELI DKYAKTLTDA
RMISDGHKRM LENHLGKKFA DVLNRTRLGP AIQRSSSDAR PVVLMTCGVA GSGKSTLAKS
ICSAYPSFTR LSIDTYIYTH HGLYNVDYPE KHYEKYQTEA EAALKRQLVH ILEHGDANVV
LDFSFAFREV RDEWKVLISE SGGRWVLVYL NVDPTEIRRR VAARNAVVEK DGDSAFCLTE
DVLERYLRGF ERPVGEGEIV VNVD
//
