ID B2WPS6_PYRTR Unreviewed; 318 AA.
AC B2WPS6;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=HST3 protein {ECO:0000313|EMBL:EDU46142.1};
GN ORFNames=PTRG_11986 {ECO:0000313|EMBL:EDU46142.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU46142.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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}.
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; DS231639; EDU46142.1; -; Genomic_DNA.
DR RefSeq; XP_001942317.1; XM_001942282.1.
DR AlphaFoldDB; B2WPS6; -.
DR SMR; B2WPS6; -.
DR STRING; 426418.B2WPS6; -.
DR EnsemblFungi; EDU46142; EDU46142; PTRG_11986.
DR GeneID; 6350303; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_829338_0_0_1; -.
DR InParanoid; B2WPS6; -.
DR OMA; QLHGSIN; -.
DR OrthoDB; 2658269at2759; -.
DR Proteomes; UP000001471; 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; 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:SF6; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 42..304
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 35522 MW; AF2B0EED85D2D2D1 CRC64;
MDDASPATVP EKEDVDASDG RGNKLDSINH DDDKNGLRPG SSFLFPILVE DDSIPHNKNK
IVFITGAGIS TSAGVDDFQS RSRTKMSSRN MLDISAIWSE EFLSWSRALY NICSKAQPTP
FHHFLDELAS TSRLLRHYTQ NIDCLDTSLH KLSSRTISLH GRLDTFIYTI CHKTKHVPFA
VYDDTFGFPC EECRLKSERR KSGGKRGLPV GVLRPKILLY GEVSPDAEEI AATWEQDALD
NVDAVVLVGT RLKIPHTRKL AYSLCRSSKS RGGTVIWMNR VPLESEPTTE QPPEVFGIDH
VTRGTQVEQS RPPYPPPT
//