ID A0A2X0MDF5_9BASI Unreviewed; 629 AA.
AC A0A2X0MDF5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=BQ5605_C005g03241 protein {ECO:0000313|EMBL:SGY72946.1};
GN Name=BQ5605_C005g03241 {ECO:0000313|EMBL:SGY72946.1};
GN ORFNames=BQ5605_C005G03241 {ECO:0000313|EMBL:SGY72946.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY72946.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY72946.1, 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}.
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; FQNC01000047; SGY72946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0MDF5; -.
DR STRING; 796604.A0A2X0MDF5; -.
DR Proteomes; UP000249464; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
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; 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 Coiled coil {ECO:0000256|SAM:Coils}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000249464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 40..442
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 168..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 440..481
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 185..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 67750 MW; 27EC8B7B28B14FEB CRC64;
MSSITPLSIM SFGASAGADP TSQGLALPPF ASRIVEPVND DPASLSMQHI ARTVLKAKRV
VVVCGAGISC ASGIPDFRSS EGLFDSLKRQ HPEARLNTGK DLFDASLFSS EQNASIFYTM
IAELKSMADV AQPTAFHSFL KALDDEGKLM RVYTQNIDGL EEKAGLSYGL GDKSLPLPPR
RATARSLGKT SSSLSFSLSA NPHPSKQSNP SAAYPSPAAS PPADEVPPPP THSKIPRCIP
LHGHLGTMSC AHCSTTVPIN PFMPALAQGT APTCPSCESI DLARTVAGDR SRGVGRLRPD
VVLYGEEHRD GERVGEITHR DLIGARPDLL LVVGTTLKVP GTKRLVRELS KVTKPPVYDA
EDDEEMEMPV ASGSSTSSNS SGTTSSKTKR PKPAPVHVVY LNYEFPKPST EWKDVFDVWL
RGDIQAFVQA VHDEKDEGIR REMVRQKEKE LRELKALERA RARVEQEVAL ANVEAAEIKK
KKISDKAKVA LSQASKTERK PKPRAEAGLK ATKAKSSPEP TAVPVVVPPK KTRTTGSTAK
PRTTKTNKPM TPLPTPPSSQ AAPAPTRQTA RVAKQNVPVE SMLSPLKTRS GTVRNTAPIN
KLPFAVTKLS YTQVTSGPSF KSTRTNTRF
//
