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Database: UniProt
Entry: A0A093K5N4_STRCA
LinkDB: A0A093K5N4_STRCA
Original site: A0A093K5N4_STRCA 
ID   A0A093K5N4_STRCA        Unreviewed;       284 AA.
AC   A0A093K5N4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE            EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
DE   Flags: Fragment;
GN   ORFNames=N308_11508 {ECO:0000313|EMBL:KFV85759.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV85759.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV85759.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV85759.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037938-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037938-3};
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DR   EMBL; KL206789; KFV85759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093K5N4; -.
DR   STRING; 441894.ENSSCUP00000022113; -.
DR   Proteomes; UP000053584; 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:0017136; F:NAD-dependent histone deacetylase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd01408; SIRT1; 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; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR   InterPro; IPR017328; Sirtuin_class_I.
DR   InterPro; IPR026590; Ssirtuin_cat_dom.
DR   PANTHER; PTHR11085:SF15; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02146; SIR2; 1.
DR   PIRSF; PIRSF037938; SIR2_euk; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037938-3, ECO:0000256|PROSITE-
KW   ProRule:PRU00236};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR037938-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037938-3}.
FT   DOMAIN          8..270
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         36..40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   BINDING         46..48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   BINDING         118..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         210..211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   BINDING         234..236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV85759.1"
FT   NON_TER         284
FT                   /evidence="ECO:0000313|EMBL:KFV85759.1"
SQ   SEQUENCE   284 AA;  31878 MW;  79490210F612A544 CRC64;
     VGSWGDDGGK QKLTLQNVAE LVRKKECHRV VVMAGAGIST PSGIPDFRSP GSGLYSNLEQ
     YNIPYPEAIF ELNYFFLNPK PFFTLAKELY PGNYRPNYAH YFLRLLHDKG LLLRLYTQNI
     DGLERVAGIP PDRLVEAHGT FATATCTVCR RTFAGEDFRG DVMADKVPHC PVCTGIVKPD
     IVFFGEELPH RFFLHVTDFP MADLLFVIGT SLEVEPFASL AGAVRSSVPR VLINRDLVGP
     FAWQQRYNDI AQLGDVVSGV KKLVELLDWN EEMQTLIQKE KEKV
//
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