ID A0A164TW63_9AGAM Unreviewed; 816 AA.
AC A0A164TW63;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=DHS-like NAD/FAD-binding domain-containing protein {ECO:0000313|EMBL:KZS92688.1};
GN ORFNames=SISNIDRAFT_455281 {ECO:0000313|EMBL:KZS92688.1};
OS Sistotremastrum niveocremeum HHB9708.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS92688.1, ECO:0000313|Proteomes:UP000076722};
RN [1] {ECO:0000313|EMBL:KZS92688.1, ECO:0000313|Proteomes:UP000076722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB9708 {ECO:0000313|EMBL:KZS92688.1,
RC ECO:0000313|Proteomes:UP000076722};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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DR EMBL; KV419409; KZS92688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164TW63; -.
DR STRING; 1314777.A0A164TW63; -.
DR OrthoDB; 1344271at2759; -.
DR Proteomes; UP000076722; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 3.40.50.1220; TPP-binding domain; 2.
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; 3.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000076722};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 32..492
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 816 AA; 86900 MW; 85EC96F6B2ADD844 CRC64;
MTLLVPLDPS SSPACPSFVR KSKSVGKNKE GEIGENEDLK VVVKALLGAK RIAVVSGAGI
SVGAGIPDFR SSEGLYNSLS LGSGSGSGSG SSSQDATSSG SGAGPSTSGS SGSISGKDLF
DASVFSSESK ASLFCQMIAK LSTLSLAAQP TSFHSLLRAL DERGTLLRTY TQNIDGLESK
VGLSFGVPEF GISASLTSST QTSSDETPSA QTLSSARTKS SPLPLPRCIP LHGTLQTLRC
FLCSTSVPLE PHIPLLQRGV LPDCSACEDV DDARKAVGKR RRGVGKMRPS IVLYGEMHRD
GEGIGEIVRR DLRVGVGAST KDSGANAGAK ESGSGSNAAK KAKDGKEGEK KEAKGKRKAV
DLLIVVGTSL KVHGTKKIVR DFSKALRSSD PLPIPPPPSP TKRSARLSQQ PPTPTRRSHL
PSPSPSPRRS LKSSPSPSSL ETEEEEMTPP KTIFINFDFP APAREWEGVF DVWIQGDVQK
FSDIVLETIR EESEKKAKRK RPAAAKVEEG AGGKGVKRKR SLKVDTKKKT ALPTPSPSPL
PLKKKPRLEF CVEIPLPPHP PPFRPAVSVS FPTSNTRLTA PSLSPSLSPS RSPPPRGLVE
IMHMEDSRGD QYKRRTGVSV LKSSRRSTAS IPPSLPPLSL KSLPEPLPSS LSHPLPLPYP
LTLPGSSDQS HAHEYDRFSM IPPPPLLVYD RDEGDEGDTP PSSSPLTPDT DMDSGDGSSD
SSSDSESGSE SEAEEDKDAT RILTPSPSPM RTSRTSRSRP SVQVTAGPRD ISPDVPLIDL
MSSAQHERER AIPMKEVARP LKPLKTYARR GVRVKQ
//
