ID F7W302_SORMK Unreviewed; 431 AA.
AC F7W302;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=WGS project CABT00000000 data, contig 2.23 {ECO:0000313|EMBL:CCC12004.1};
GN ORFNames=SMAC_02226 {ECO:0000313|EMBL:CCC12004.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC12004.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC12004.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC12004.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC12004.1}.
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DR EMBL; CABT02000023; CCC12004.1; -; Genomic_DNA.
DR RefSeq; XP_003350513.1; XM_003350465.1.
DR AlphaFoldDB; F7W302; -.
DR STRING; 771870.F7W302; -.
DR GeneID; 10808061; -.
DR KEGG; smp:SMAC_02226; -.
DR VEuPathDB; FungiDB:SMAC_02226; -.
DR eggNOG; KOG2683; Eukaryota.
DR HOGENOM; CLU_023643_1_1_1; -.
DR InParanoid; F7W302; -.
DR OMA; RLNPIWA; -.
DR OrthoDB; 1207573at2759; -.
DR Proteomes; UP000001881; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001881};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 32..403
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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"
SQ SEQUENCE 431 AA; 46926 MW; 75CAD5FFCE7CFE0A CRC64;
MSSLATTAAG TLRMRIPYRE LPPPTTIIPA TATTLPGAVA ALKSFLTTPP PASHLPDRTV
ILTGAGLSVA SGLADYRGVN GTYRVNKSYK PIFHHEFLTS HETRQRYWAR SYIGWRGLGR
AGPNPGHYAI RDLGDLLAQR YGYSYSSGGR ADENNNSKGI TGVITQNVDS FHKMSHPDIR
TVELHGSLAS VVCTSCQNQF PRDEYQTTLA RLNPIWADFL REALASGALE TEDIEERNKR
GIKMNPDGDV DLAEAPYTTF RYPACPSCLK EPPRLADGTK TWVEIDKDGA WIPSSTAGVL
KPAVIMFGES ISAEVKREAE KAVDNAGRML ILGTSLATYS AWRLAQRAKL RGMPIAIVSI
GGVRREEMFF EDLDPKMAGP HGVRVEMATE KLLPALVEEL KSSNNGAMVA EVPIGTAFTN
GLQNGRPSLI E
//
