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Database: UniProt
Entry: A0A0G4IK50_PLABS
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ID   A0A0G4IK50_PLABS        Unreviewed;       334 AA.
AC   A0A0G4IK50;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE            EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN   ORFNames=PBRA_004223 {ECO:0000313|EMBL:CEO95497.1};
OS   Plasmodiophora brassicae (Clubroot disease agent).
OC   Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC   Plasmodiophoridae; Plasmodiophora.
OX   NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO95497.1, ECO:0000313|Proteomes:UP000039324};
RN   [1] {ECO:0000313|EMBL:CEO95497.1, ECO:0000313|Proteomes:UP000039324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:CEO95497.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC       {ECO:0000256|ARBA:ARBA00038170}.
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DR   EMBL; CDSF01000024; CEO95497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4IK50; -.
DR   STRING; 37360.A0A0G4IK50; -.
DR   EnsemblProtists; CEO95497; CEO95497; PBRA_004223.
DR   OMA; HRHTTGR; -.
DR   OrthoDB; 1947602at2759; -.
DR   Proteomes; UP000039324; 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   Gene3D; 2.20.28.200; -; 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; IPR026590; Ssirtuin_cat_dom.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR11085:SF13; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-6; 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:UP000039324};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          26..272
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          291..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   334 AA;  36702 MW;  9BD6DDDB2EE19C4B CRC64;
     MTSYAAKLIQ KRDKGLCGDP ERVDDDGVVR AQVAELARLV RSSRHCIVHT GAGISTSAGV
     HDFRGPDGVW TRQQRKLPPL HGVAFGDAVP TITHMAIVAL VRAGLVKHVV SQNVDGLHVR
     SGLPRQHLCE VHGTAFAEWC DQRLPKCQCE FRRADEVATI GLRPTGNACK RCGGPLRDLL
     CDWDSNLPQD EVEYAIEQHR MADLAICVGT SLRIRPAGLW PLRTIRLNGK KEPGRICVIN
     LQKTHLDRRC AVRIFARCDH VFTMLMDELG VDIPKWVAVE CPYAKLGWRP TDRNPSADVA
     DRHAGDDDAG STGSSAAPTE DGKSDDDSGY TPDR
//
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