ID   A0A2H3SQ66_FUSOX        Unreviewed;       968 AA.
AC   A0A2H3SQ66;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Related to silencing protein {ECO:0000313|EMBL:SCO77299.1};
GN   ORFNames=FRV6_01511 {ECO:0000313|EMBL:SCO77299.1};
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO77299.1, ECO:0000313|Proteomes:UP000219369};
RN   [1] {ECO:0000313|Proteomes:UP000219369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA   Guldener U.;
RL   Submitted (SEP-2016) 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; FMJY01000001; SCO77299.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3SQ66; -.
DR   VEuPathDB; FungiDB:FOC1_g10008182; -.
DR   VEuPathDB; FungiDB:FOC4_g10009276; -.
DR   VEuPathDB; FungiDB:FOIG_10805; -.
DR   VEuPathDB; FungiDB:FOMG_07194; -.
DR   VEuPathDB; FungiDB:FOXG_10425; -.
DR   VEuPathDB; FungiDB:FOZG_09900; -.
DR   VEuPathDB; FungiDB:HZS61_002989; -.
DR   OrthoDB; 1344271at2759; -.
DR   Proteomes; UP000219369; 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; 2.
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..619
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          141..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..193
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   968 AA;  106557 MW;  4224937113A192C8 CRC64;
     MPTIHVSRDS QDELQDIANG LLKARKVIVV TGAGISTNSG IPVSSLRHSS ACQMRFGDFR
     SENGLYSLIS AQFDAAAQQA RLNEGSSDDK PTDLDIRRPA KRRRIVHDVS AKVEEGPVGM
     KEEIEVQLED PEPDHEKIAD TIQVEGHPDD EEQQVRSDGM PVVNPRTTRS TIAVAQPPSS
     PLSSPPPEGL NIPPPSVFRR TRRSHLTNST IPPSSSPLSS PPPVLFDPFS SGTSSEDAPS
     RRSSTSPSEV DDTPPSNPIN LSQASFGSGK NTLPNMKGKD MFDASIWSDP LRTSVFYTFA
     TTLRQKVRDV EPTSSHRFIS HLRDRGKLVR CYTQNIDQIE EKVGLSTCLH DGPGSRGRFS
     RKSTANINQL NRMVDEVNAM TDTNSSDKSQ QSSDNEASQQ SQCSQPKFES TVPASQAESD
     QCATDEALTA VRNLRRDLPK SGVECVFLHG SLELLRCFLC GRVCSWDDDE RQLETMSGQQ
     PECPHCVGAT VAREERGKRA LGVGKLRPDI VLYGEEHPNA HLISPIVTHD LALCPDLLLI
     LGTSLRVHGL KVMVREFAKA VHAKGGKVVF VNYTKPPESS WGDVIDYWVE WDCDAWVSDL
     QDKIPKLWQA PEPPKLKKKR ESGGVAEDTE KTETKRPVAA YPVALRDTKA TGAYWSSRIV
     KELHRITGHD LLESPVFTPP AIITTTETLP PAHTPLKTPQ GKPDRVRTRA QRSRKSAPGV
     LERSSMPPST LNPNHGRTLR STETRAHLLG DEMAPSNEII THERVLLHGS SIASLVKSRA
     RERKRKKIDG EEVSLPSKRT LGSLRLAPLR PQPSDPRDII PFDRLPTMEL PPDTPEPYTE
     TGQLQSISPV MHHTEPLMPV SHNTRKQTHI RRSQASFMRG QDLAASPAPM LPPEMSHGLL
     VSSHDRCNLV MKHVRSQREA DAALALSALS QGDARPVITK EFAIPPCTGV GIRKSARLIH
     RSGTPTST
//