ID A0A2H3HT22_FUSOX Unreviewed; 437 AA.
AC A0A2H3HT22;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN ORFNames=AU210_002543 {ECO:0000313|EMBL:PCD43448.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD43448.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD43448.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD43448.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD43448.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD43448.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037938-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037938-3};
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:PCD43448.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MABQ02000002; PCD43448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3HT22; -.
DR STRING; 327505.A0A2H3HT22; -.
DR OrthoDB; 10545at2759; -.
DR Proteomes; UP000219602; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; 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; IPR017328; Sirtuin_class_I.
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 PIRSF; PIRSF037938; SIR2_euk; 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|PIRSR:PIRSR037938-3, ECO:0000256|PROSITE-
KW ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR037938-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037938-3}.
FT DOMAIN 15..277
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 316..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-1,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 43..47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 53..55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 125..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 219..220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 243..245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
SQ SEQUENCE 437 AA; 47825 MW; B53B4D6952903B5C CRC64;
MGQEESSMSY GGPPVTLTER SLDAVAEYIK TGRSKRIVVL TGAGISTAAG IPDFRSPGTG
LYANLARLNL PYAEAVFDIS YFRNHPEPFY VLANELYPGK FSPTVSHAFI ALLARKGLLQ
MLFTQNIDCL ERVAGVPSDK IIEAHGSFAT QRCIECKEEY PDEKMKEHVF GGKVPHCDKE
GCKGLVKPDI VFFGEALPKA FDNNTYQVAM ADLVLIVGTS LTVYPFAALP GMAQEGKPRV
LFNMEKVGQI GTRSDDVMEL GDCDAGIRKL ANALGWRDEL EKLWRQTVGD AEADRQLGGR
EKDDVQDEVE RLAAEVGAVV IDESDEGVPL EKEPTKHKDG PTVSEKSKDD DKQREPETAT
ATTDLEIDTK ESPKTQQPKL DRAQVEQLEA EASKTESLVT EPPKPQTPEE EPPKAETSKA
EPTKEGTVPA ALSNEEK
//
