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Database: UniProt
Entry: A0A166SHI0_9PEZI
LinkDB: A0A166SHI0_9PEZI
Original site: A0A166SHI0_9PEZI 
ID   A0A166SHI0_9PEZI        Unreviewed;       693 AA.
AC   A0A166SHI0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Sir2 family protein {ECO:0000313|EMBL:KZL70742.1};
GN   ORFNames=CI238_09415 {ECO:0000313|EMBL:KZL70742.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL70742.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL70742.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL70742.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL70742.1}.
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DR   EMBL; LFIW01002435; KZL70742.1; -; Genomic_DNA.
DR   STRING; 1573173.A0A166SHI0; -.
DR   OrthoDB; 1327719at2759; -.
DR   Proteomes; UP000076584; 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; PTHR47651:SF17; DEACETYLASE SIRTUIN-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47651; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 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:UP000076584};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   693 AA;  76464 MW;  896567625E9FE156 CRC64;
     MDATPSTSSN MDVDAHHQVS SPSDSALSSP LSVLSKSPSI PPSPEIALDA SKRYPSPTSS
     MPSGAQSPIK LEVADDSVPA IQLDDAADSI NVNANDAPDG QPPRKRRKVT PPKERTTEHL
     NLDDCDENDS KLARLVSALK KRKKIVVIAG AGISVSAGIP DFRSKTGLFA TLPNEHKVKG
     SGKHLFDASV YKHDSSTEKF HKMICDLATM VKAAKPTKFH HLLASLAAEN RLLRLYSQNV
     DCIDTNMEPL KTNVPLNTKG PWPKTIQLHG SVEHMVCSKC TDIRPLKTEL FVGHEAPLCE
     ECKTIDELRT QFEQRRSHGI GRLRPRMVLY NEFNPDEEAI GKVSSVDLKS RPDAVIVVGT
     SLKIPGVRRL VKELCQVTRS RRDGFTAWIN TDSEPQHNDF KDCWDLVVRG KCDDVAHWAA
     LPRFDEPHGD QSAYLSEGED QRRRDRLSRD NLEVQLISPT PDSPTKSDSS TASETRKRKL
     VDPVQSIPTP TASPKIKAAE ASKKVAKPKQ SKLSFGGQQV AASASDASAK KAKKAPVKKS
     RKSNKKPTEP PKNSVTQTFK TQKNRELADM PQETLAGKLD NQHYKYAEDK LESQLPPLRP
     VQKPIQSSVY KRAEDPDVEG HEDDNSPPTR PFEKMSRPSL SERPKSSPHT SVTTEGGRNS
     NDVRPTTPMH IRRRSADTIS PESIPRGMES LMD
//
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