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Database: UniProt
Entry: A0A0F2M9S6_SPOSC
LinkDB: A0A0F2M9S6_SPOSC
Original site: A0A0F2M9S6_SPOSC 
ID   A0A0F2M9S6_SPOSC        Unreviewed;       426 AA.
AC   A0A0F2M9S6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=SIR2 family histone deacetylase {ECO:0000313|EMBL:KJR85844.1};
GN   ORFNames=SPSK_09319 {ECO:0000313|EMBL:KJR85844.1};
OS   Sporothrix schenckii 1099-18.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR85844.1, ECO:0000313|Proteomes:UP000033710};
RN   [1] {ECO:0000313|EMBL:KJR85844.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR85844.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA   Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA   Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA   Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA   Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA   Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA   Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA   Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA   Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA   Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT   "Comparative genomics of the major fungal agents of human and animal
RT   Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL   BMC Genomics 15:943-943(2014).
RN   [2] {ECO:0000313|EMBL:KJR85844.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR85844.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25480940;
RA   Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA   Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA   Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA   de Camargo Z.P., Felipe M.S.;
RT   "Asexual propagation of a virulent clone complex in a human and feline
RT   outbreak of sporotrichosis.";
RL   Eukaryot. Cell 14:158-169(2015).
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:KJR85844.1}.
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DR   EMBL; AXCR01000007; KJR85844.1; -; Genomic_DNA.
DR   RefSeq; XP_016588520.1; XM_016735893.1.
DR   AlphaFoldDB; A0A0F2M9S6; -.
DR   GeneID; 27671170; -.
DR   KEGG; ssck:SPSK_09319; -.
DR   VEuPathDB; FungiDB:SPSK_09319; -.
DR   OrthoDB; 1207573at2759; -.
DR   Proteomes; UP000033710; 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; 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; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR11085:SF2; NAD-DEPENDENT PROTEIN LIPOAMIDASE SIRTUIN-4, MITOCHONDRIAL; 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|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00236}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          26..400
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         166
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         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   426 AA;  45953 MW;  F35136A0DCC1B876 CRC64;
     MAVRRPLLRI PYTEVFAAPR IIPRHATTPS AAVEALSAFM TAPPRPGLPS STVVLTGAGL
     SVASGLADYR GENGTYRVNK TYRPIYFHEF LASHEARKRY WARSFLGWTT LHEAKPNTSH
     YALRDLGRLG YVHSVITQNV DSFHHAAHPD LPSTVELHGY LRATVCTTCY REYPRDTFQD
     ELARLNPIWA EFLADAIAAG AFAPEDPTTE APARREPASL SAIRGVRTNP DGDVDLPNAP
     YTTFRYPPCA HCLANPPVAD DGTTMAVEVD ADGAWALPHT SNQTDCGTNV RFPGILKPAV
     IMFGESISPS AKHAAEAAVD GAGRLLVLAT SLATYSAWRL AKRAKDRGMP IAVVNVGGVR
     GEDAFFADLD DNQPGAAGVR VEVPTDAVLP PLVDELHRLA PGGVYQQGTG HGTSQVDPAL
     FRDMLS
//
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