ID A0A074VHA7_9PEZI Unreviewed; 325 AA.
AC A0A074VHA7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=DHS-like NAD/FAD-binding domain-containing protein {ECO:0000313|EMBL:KEQ59878.1};
DE Flags: Fragment;
GN ORFNames=M437DRAFT_19416 {ECO:0000313|EMBL:KEQ59878.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ59878.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ59878.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ59878.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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DR EMBL; KL584846; KEQ59878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VHA7; -.
DR STRING; 1043003.A0A074VHA7; -.
DR HOGENOM; CLU_021544_1_1_1; -.
DR OrthoDB; 1327719at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF6; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 33..325
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT NON_TER 325
FT /evidence="ECO:0000313|EMBL:KEQ59878.1"
SQ SEQUENCE 325 AA; 36362 MW; 6EA73D3491BC4732 CRC64;
MDASDSQRPA KRRRISEKPS RTTEYLDLTK TLRPEDKTQL DRVLNVLHKR QKIVVVAGAG
ISVAAGIPDF RSSTGLFNSL RAQHNLKGSG KDLFDASHVY KDASSTASFH QMVREMSHMT
KSAQPTLFHQ MLATLAQQDR LLRLYSQNVD GIDTSLEPLA TRIPLKKEEG KWPKTIQLHG
GLDKMVCSKC HEISDFDAKC FEDSVPSVCT NCEELNRVRT EVAGKRSHGV GMLRPRMVLY
NEHNPDDEAI GAVTREDLRK RPDAIIVVGT TLKVPGVKRI VREMCATVRD RRDGVAIWIN
AGPEPSGKEF EDCWDIVVKG TCDEI
//