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Database: UniProt
Entry: A0A2T4C3Z7_TRILO
LinkDB: A0A2T4C3Z7_TRILO
Original site: A0A2T4C3Z7_TRILO 
ID   A0A2T4C3Z7_TRILO        Unreviewed;       328 AA.
AC   A0A2T4C3Z7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=DHS-like NAD/FAD-binding domain-containing protein {ECO:0000313|EMBL:PTB76265.1};
DE   Flags: Fragment;
GN   ORFNames=M440DRAFT_1306468 {ECO:0000313|EMBL:PTB76265.1};
OS   Trichoderma longibrachiatum ATCC 18648.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB76265.1, ECO:0000313|Proteomes:UP000240760};
RN   [1] {ECO:0000313|EMBL:PTB76265.1, ECO:0000313|Proteomes:UP000240760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB76265.1,
RC   ECO:0000313|Proteomes:UP000240760};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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; KZ679132; PTB76265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4C3Z7; -.
DR   STRING; 983965.A0A2T4C3Z7; -.
DR   Proteomes; UP000240760; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1600.10; 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:SF14; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 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:UP000240760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..265
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         328
FT                   /evidence="ECO:0000313|EMBL:PTB76265.1"
SQ   SEQUENCE   328 AA;  36270 MW;  AE9FDA3FE777AD39 CRC64;
     MKRAPAGKKG VALSKRSQAA ADAFDRLPEN PTIEEIKEAT VNVSLAELEE RVADVRDSWE
     TDSLLEDAIE ELTDESGVYS GRPDTCTPEE ACRLRRELRE QGPAVFCQRT IDAGRYSAKK
     LLSAFGIRPP AFLEGQPDEA YFSLLRVAKA KKSRGRLADS SDDNSEYDVP SAGVMKPDIT
     FFGEELPDEF SRRLTENDRD KVDLVIVIGT SLKVTPVSEI ASFLPPHIPQ IYISRQSVTH
     INFDIDLLGD CDVVVAELCR QLKWPLVHEM VPADQEITVK TEPGYPNRHV FTTNKPYVLE
     NGDGAKVIED AAKPVQNGKD GKQAKGGK
//
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