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Database: UniProt
Entry: A0A1A0HFW8_9ASCO
LinkDB: A0A1A0HFW8_9ASCO
Original site: A0A1A0HFW8_9ASCO 
ID   A0A1A0HFW8_9ASCO        Unreviewed;       515 AA.
AC   A0A1A0HFW8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=SIR2-domain-containing protein {ECO:0000313|EMBL:OBA22792.1};
GN   ORFNames=METBIDRAFT_34825 {ECO:0000313|EMBL:OBA22792.1};
OS   Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX   NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA22792.1, ECO:0000313|Proteomes:UP000092555};
RN   [1] {ECO:0000313|EMBL:OBA22792.1, ECO:0000313|Proteomes:UP000092555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA22792.1,
RC   ECO:0000313|Proteomes:UP000092555};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OBA22792.1}.
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DR   EMBL; LXTC01000001; OBA22792.1; -; Genomic_DNA.
DR   RefSeq; XP_018713273.1; XM_018856528.1.
DR   AlphaFoldDB; A0A1A0HFW8; -.
DR   STRING; 869754.A0A1A0HFW8; -.
DR   GeneID; 30029504; -.
DR   OrthoDB; 10545at2759; -.
DR   Proteomes; UP000092555; 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:0033558; F:protein lysine deacetylase activity; IEA:UniProtKB-EC.
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; IPR007654; NAD-dep_histone_deAcase_SIR2_N.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   PANTHER; PTHR47651; NAD-DEPENDENT HISTONE DEACETYLASE HST4; 1.
DR   PANTHER; PTHR47651:SF4; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 1.
DR   Pfam; PF04574; DUF592; 2.
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|PROSITE-ProRule:PRU00236};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092555};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          180..453
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        307
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   515 AA;  56255 MW;  735CEB5D4368396B CRC64;
     MEESDDESAA SSPASDSERC RGEPAERPEG RAPEKTAPAA GAGRRAGFGA RTTPAAPPLA
     GSLLAETAEL PGGRTDTEGS GGLTDSEAAA VVLSDLEEAE PSETYANVHA FRKFVKRFGP
     QKFLERFLPP DVSGESIVQL LLSLGYVPRN LPPRVGAAHY VKLMRLLELA MGRICELRPR
     LENFCSVAHV LGALRTARNI LVITGAGIST SLGIPDFRSS EGFYSKMAAL GLEDPQEVFD
     IRVFHDNPMV FYSIAHMILP PKDVRAPLHR FLTLLQDKGK LLRNYTQNID NIEANAGLRP
     EKMVQCHGSL ASASCVTCRY QVEGTRLYPA LEKGELAYCP RCDKKRLACM RRDDSADDPS
     FGVMKPDITF FGEDLPRAYH SQHARDLRDC DLLLSIGTSL RVAPVSDMVD KVAPHVPQVL
     INRDPIPSCN FDVSFLGYCD DTVSYLCDQL GRDWDIDHPD YRSIVGADRR NLEVHGTGEK
     GVFEVHNRAR AAKLAAAAPK PAPGPDLVLL EPELP
//
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