ID A0A1Q2YKB8_9ASCO Unreviewed; 631 AA.
AC A0A1Q2YKB8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Deacetylase sirtuin-type domain-containing protein {ECO:0000259|PROSITE:PS50305};
GN ORFNames=PMKS-003498 {ECO:0000313|EMBL:GAV29992.1};
OS Pichia membranifaciens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4926 {ECO:0000313|EMBL:GAV29992.1, ECO:0000313|Proteomes:UP000186136};
RN [1] {ECO:0000313|EMBL:GAV29992.1, ECO:0000313|Proteomes:UP000186136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS47-1 {ECO:0000313|EMBL:GAV29992.1,
RC ECO:0000313|Proteomes:UP000186136};
RA Konishi M., Ishida M., Arakawa T., Kato Y., Horiuchi J.;
RT "Whole genome shotgun sequence of Pichia membranifaciens KS47-1.";
RL Submitted (AUG-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:GAV29992.1}.
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DR EMBL; BDGI01000151; GAV29992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2YKB8; -.
DR Proteomes; UP000186136; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; 1.20.120.1710; -; 1.
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; PTHR11085:SF14; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF04574; DUF592; 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|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000186136};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 268..553
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..162
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 395
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 631 AA; 70703 MW; 5F9D0CB3F11622F9 CRC64;
MEAVLKEKME DLENGRTLKR EHESSSSERL EAGSNGSSGS PTPMPAVGSS SESYTSKRQH
TSVNPEDGIS VGNATSTVFP TNIDESSGGN PLIEFENADG ERVKLEIINS SSSAPGSDDE
GEKNSKNSNN ENNAEDQEYE DDPSDYESEG NESDISEFQF EESTSAEDEL GFDLYDPDIE
LPPLDKIKVT KKTCSQVRKY LKSEGHVAFL DLFLPSGPTP EDIITLTRLL GFEPKRFNRI
YASSSNPLHS AIFFLREAIN RVLKSRTHLQ DFHTIQNVCD ALNKAENVLV LTGAGISTSL
GIPDFRSSQG FYSKMKNLGL DDPQDVFSLE LFRRDPSVFY SIAYMILPPE NSFTPLHGFI
KLLQDKGKLL RNYTQNIDNL EANAGVTPEK LVQCHGSFAT ASCVTCKYKI PGETLYPNLR
SKKIAYCPFC ENERKNLQRK FEKLEDEGGF SSRFNDIESF GVMKPDITFF GENLPDRYHN
TIKEDVRKCD LLICIGTSLK VAPVSEIVNR VPDEVPQILI NRDPINHCEF DVELLGYCDQ
AITWLCGDKL KWEIKHKDFE QILHSGLELQ VLDEEFGRYK ISDANERVQL SLKKLEAAKT
EAKLKEEGSL RNSNPQNDTK VEASEESEVV V
//
