ID A0A2X0MZ45_9BASI Unreviewed; 607 AA.
AC A0A2X0MZ45;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=BQ5605_C008g05105 protein {ECO:0000313|EMBL:SGY79316.1};
GN Name=BQ5605_C008g05105 {ECO:0000313|EMBL:SGY79316.1};
GN ORFNames=BQ5605_C008G05105 {ECO:0000313|EMBL:SGY79316.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY79316.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY79316.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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DR EMBL; FQNC01000048; SGY79316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0MZ45; -.
DR STRING; 796604.A0A2X0MZ45; -.
DR Proteomes; UP000249464; 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; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 3.
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: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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000249464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 17..416
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 65..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..596
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 607 AA; 66182 MW; 24DDBD22C200D807 CRC64;
MAPASKTPPT TQDVYLDCEC DAALDKMTAA IAKAKRVVVA VGAGISTSAG VPDFRTKTSG
LYARAGNGNA AGGDDHQPDD GRARRAATGT ATSPTKTASK ATTKRADSNL LKGPAMFTSS
VYTAVSTRTA HWQFMTRLKR SVDHIASASI PPKLTSSSTA LPSSPSRSTR ASAEKREKGV
TKTHAFFDTL HRRGQLGRVY TQNIDGFELT SGQLEGVGIE GIRVQADHVD YSERSSKPKG
KGKAKAQEWT GDVVQLHGSL GRVKCSSCAW VGEWDERHSN AFEKGMSVDC PACVSQAELR
VCGGKRALVL RSFVRPSIVL YGERSPAEQS IGSIITCDLS RKPDLLIVMG TTLKIPGFKR
LVVDMSREVR KNGGLAIFVN REKNAAAMWK KVFDYQGTLG SRSQVIIGVI ELIRLDPSTR
TVIGSTDDFV DRLLKRWKQT RPADWQKQAT LNDTFTVAKP SQVVVSKPVQ PVPPITSSSS
STRTPWRDPN FSLGVPGPGT PPSSPLKRRS SCSDRTNLPS MDKLPETPSK RRSPRKPRTE
QEQEQGPAFD FDYDHLDQLS KTRYPRMDQI SDPPSTPFRM PVLCVPKSPP TPTRKVLPRS
PRRAVAR
//
