ID M1VDT0_CYAM1 Unreviewed; 564 AA.
AC M1VDT0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN ORFNames=CYME_CMM136C {ECO:0000313|EMBL:BAM80997.1};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699 {ECO:0000313|EMBL:BAM80997.1, ECO:0000313|Proteomes:UP000007014};
RN [1] {ECO:0000313|EMBL:BAM80997.1, ECO:0000313|Proteomes:UP000007014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10D {ECO:0000313|EMBL:BAM80997.1,
RC ECO:0000313|Proteomes:UP000007014};
RX PubMed=15071595; DOI=10.1038/nature02398;
RA Matsuzaki M., Misumi O., Shin-i T., Maruyama S., Takahara M.,
RA Miyagishima S., Mori T., Nishida K., Yagisawa F., Nishida K., Yoshida Y.,
RA Nishimura Y., Nakao S., Kobayashi T., Momoyama Y., Higashiyama T.,
RA Minoda A., Sano M., Nomoto H., Oishi K., Hayashi H., Ohta F., Nishizaka S.,
RA Haga S., Miura S., Morishita T., Kabeya Y., Terasawa K., Suzuki Y.,
RA Ishii Y., Asakawa S., Takano H., Ohta N., Kuroiwa H., Tanaka K.,
RA Shimizu N., Sugano S., Sato N., Nozaki H., Ogasawara N., Kohara Y.,
RA Kuroiwa T.;
RT "Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon
RT merolae 10D.";
RL Nature 428:653-657(2004).
RN [2] {ECO:0000313|EMBL:BAM80997.1, ECO:0000313|Proteomes:UP000007014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10D {ECO:0000313|EMBL:BAM80997.1,
RC ECO:0000313|Proteomes:UP000007014};
RX PubMed=17623057; DOI=10.1186/1741-7007-5-28;
RA Nozaki H., Takano H., Misumi O., Terasawa K., Matsuzaki M., Maruyama S.,
RA Nishida K., Yagisawa F., Yoshida Y., Fujiwara T., Takio S., Tamura K.,
RA Chung S.J., Nakamura S., Kuroiwa H., Tanaka K., Sato N., Kuroiwa T.;
RT "A 100%-complete sequence reveals unusually simple genomic features in the
RT hot-spring red alga Cyanidioschyzon merolae.";
RL BMC Biol. 5:28-28(2007).
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000256|ARBA:ARBA00038170}.
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DR EMBL; AP006495; BAM80997.1; -; Genomic_DNA.
DR RefSeq; XP_005537033.1; XM_005536976.1.
DR AlphaFoldDB; M1VDT0; -.
DR STRING; 280699.M1VDT0; -.
DR EnsemblPlants; CMM136CT; CMM136CT; CMM136C.
DR GeneID; 16995165; -.
DR Gramene; CMM136CT; CMM136CT; CMM136C.
DR KEGG; cme:CYME_CMM136C; -.
DR eggNOG; KOG1905; Eukaryota.
DR HOGENOM; CLU_483458_0_0_1; -.
DR OrthoDB; 1947602at2759; -.
DR Proteomes; UP000007014; Chromosome 13.
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; 2.20.28.200; -; 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; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR11085:SF13; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-6; 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:UP000007014};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 27..306
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 71..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 564 AA; 62397 MW; 3011804D998EDB27 CRC64;
MAHDYAGRLR PYENKGRLGL APDWDRLLDV QRKVQVLAQW LRAACGDVVV HTGAGVSTAA
GVRDFRGPHG VWSEATRSKN GRSRPGVAPG AAQQHEPLTR DGARCADVID PRTQPPPPDC
SLELAAPTWS HWALTELVRR GLVRRIVTQN IDGLHLRSGL ARHRLSELHG NIFAEQCERC
GQIFLNDVVV PTVGGRRTGH QCVYCAWRGQ RASTRDMLLD WEDPLPQADL MGATEDSRNA
RLCLVMGSSL QMVPAATLPA LCLRKDGARL VIVNASWTAR DDAAHLVIRA PTDMVMLLLL
DELALLPPGD ARVRLWRPQL TLGVRWRQRP RQSRPSVDVC VWNGNGNAPG LTLDHTLHGA
CKREPSKHNS SCADTPLYWI PLHGRMIADA NQVPALEALE LDASGHLSLT VAGFGQRSCA
EPPFCTAAAV SIRLGFPLAP RGTSQPPLVV PNVWYFLSIP RAGWLEFNVV AYRAYVVRLL
ASEWVQSERI QLPPALLFYR EDDRRRCSCI VCGASVPPQK RTHHVQCVHA EALGQRAASA
PDLERQRNDL QGRRSEKRAR LPRV
//
