ID A0A395SR16_FUSSP Unreviewed; 444 AA.
AC A0A395SR16;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Nad-dependent histone deacetylase sir2 {ECO:0000313|EMBL:RGP74914.1};
GN ORFNames=FSPOR_1087 {ECO:0000313|EMBL:RGP74914.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP74914.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP74914.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP74914.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGP74914.1}.
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DR EMBL; PXOF01000019; RGP74914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SR16; -.
DR STRING; 5514.A0A395SR16; -.
DR Proteomes; UP000266152; Unassembled WGS sequence.
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 CDD; cd01408; SIRT1; 1.
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:SF10; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-2; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 15..277
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 324..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 444 AA; 48626 MW; 75001ADBEA2F21EC CRC64;
MGQEESSMSY SGPPATLTER SLAAVADYVK SGRCKNIVVL TGAGISTAAG IPDFRSPGTG
LYANLARLNL PYAEAVFDIS YFREHPEPFY VLANELYPGK FHPTVSHAFI ALLARKSLLQ
MLFTQNIDCL ERVAGVPSDR IIEAHGSFAK QRCIECKEEY PDDKMKEHVF GGKVPHCDKE
GCKGLVKPDI VFFGEPLPKA FDNNTFQVAM ADLVLVVGTS LSVYPFAALP GLAQEGKPRV
LFNMEQVGQL GSRSDDVIQL GDCDAGIRKF ADELGWRDEL EALWREIVGD AEADRQNSGR
EKEAVQDEVE RLAAEVGAVV IGDSEDKTDI KHEDTKQGVL SYNEPTKLEE EQPKTENNNS
EPAPTSSTTA AQDKTEESPK TEQLKPENLE KIEAEATKTE SLVTEPPKPQ PSQEEILQTE
TSKDEPTVAS TEPASKEGEG KSKF
//
