ID   W9IE11_FUSOX            Unreviewed;       953 AA.
AC   W9IE11;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN   ORFNames=FOYG_08606 {ECO:0000313|EMBL:EWY91525.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY91525.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY91525.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) 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; JH717843; EWY91525.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9IE11; -.
DR   HOGENOM; CLU_005935_0_1_1; -.
DR   OrthoDB; 1344271at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1220; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..604
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          126..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..178
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   953 AA;  104964 MW;  6BABD4A472ACAD4B CRC64;
     MPTIHVSRDS QDELQDIANG LLKARKVIVV TGAGISTNSG IPDFRSENGL YSLLSAQFDA
     AAQQARLNEG SSDDKPTDLD IRRPAKRRRI VHDVSAKVEE GPVGMKEEIE VQLEDPEPDH
     EKIADTIQVE GHPDDEEQQI RSDGMPVVNP RTTRSTIAVA QPPSSPLSSP PPEGLNIPPP
     LVFRRTRRSH LTDSTIPPSS SPLSSPPPVL FDPFSSGTSS EDAPSRRSST SPSEVDDTPP
     SNPINLSQAS FGPGKNTLPN MKGKDMFDAS IWSDPLRTSV FYTFATTLRQ KVRDVEPTSS
     HRFISHLRDR GKLVRCYTQN IDQIEEKVGL STCLHDGPGS RGRFSRKSTA NINQLNRMVD
     EVNAMTDTNS SDKSQQSSDN EASQQSQCSQ PNFESTVSAS QAESDQCATD EALTAVRNLR
     RDLPKSGVEC VFLHGSLELL RCFLCGRVCS WDDDERQLET MSGQQPECPH CVGATVAREE
     RGKRALGVGK LRPDIVLYGE EHPNAHLISP IVTHDLALCP DLLLILGTSL RVHGLKVMVR
     EFAKAVHAKG GKVVFVNYTK PPESSWGDVI DYWVEWDCDA WVSDLQDKIP KLWQTPEPPK
     LKKKRESSGV AEDAEKAETK RPVAAYPVAL RDTKATGAYW SSRIVKELHR ITGHDLLESP
     VFTPPAIITT PETLPPAHTP LKTPQGKPDR VRTRAQRSRK SAPGVLERSS MPPSTLNPNH
     GRTLRSTETR AHLLGDEMAP SNEIITHERV LLHGSSIASL VKSRARERKR KKIDGEEVSL
     PSKRTLGSLR LAPLRPQPSD PREIIPFDRL PTMELPPDTP EPYTETGQLQ SISPVMHHTE
     PLMPVSHNTR KQTHIRRSQA SFMRGQDLAA SPAPMLPPEM SHGLLVSSHD RCNLVMKHVR
     SQREADAALA LSALSQGDAR PVTTKEFAIP PCMGVGIRKS ARLIHRSGTP TST
//