ID   A0A0J1B1L4_9TREE        Unreviewed;       558 AA.
AC   A0A0J1B1L4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=DHS-like NAD/FAD-binding domain-containing protein {ECO:0000313|EMBL:KLT41504.1};
GN   ORFNames=CC85DRAFT_328993 {ECO:0000313|EMBL:KLT41504.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT41504.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT41504.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT41504.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) 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}.
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DR   EMBL; KQ087217; KLT41504.1; -; Genomic_DNA.
DR   RefSeq; XP_018277995.1; XM_018426751.1.
DR   AlphaFoldDB; A0A0J1B1L4; -.
DR   STRING; 879819.A0A0J1B1L4; -.
DR   GeneID; 28987354; -.
DR   OrthoDB; 1344271at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1220; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          35..405
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          150..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..475
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..521
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  59169 MW;  82EBEE9168A87029 CRC64;
     MTVLVRLPRA GTSAAAGSGW DADPLPPIRF AEPSTDPDDP DLCTVVRRIR GAKRVVVVCG
     AGVSTAAQIP DFRSAHGLFA RGARNVKDLF HVKSLTSPAL LPDHHALLST LSRLAGEAQP
     TAFHAFMRDI DREGRLLRVY TQNIDGLEER AGLKTGIPPP PRSRRRTADA SRSSSQPHSQ
     RPSRSHSQSL QPSQPASAAQ SPSASASGAS SPATRESSPV RCIPLHGLLS SLHCTQCAAS
     VPSAAHALHG APIPCPRCDE MATIRSALSE RQRRVGTLRA SVVLYGEEHP QGEAIGSVME
     RDLRGTGPRG EREGRADLLV VAGTSLSIPG VKRIVKEMAK SLASRPEASV RDGREPPVRV
     VYVNAEPPAK PAEWDGVFDV WVHGDVQDFA ALVADASFAP PLPKTPRRKK ASGLSTPNTA
     STTRKRKADD SDVTPTKKRP TFPPTPASTP RIESSSSSLP PASPSLPPSP PPKPEFLRVA
     KRKCAQGDPK KRAKPNMSAG TKPAAPSPSP SPSPSPPPPL SLYDKCRAVA RFSPPPPYDD
     MAGLYGRRGG AESCAVPR
//