NAT10_YEAST
ID NAT10_YEAST Reviewed; 1056 AA.
AC P53914; D6W150;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=RNA cytidine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000305};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03211};
DE AltName: Full=18S rRNA cytosine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000303|PubMed:25653167};
DE AltName: Full=Killer toxin-resistance protein 33 {ECO:0000303|PubMed:12663529};
DE AltName: Full=Ribosomal RNA cytidine acetyltransferase 1 {ECO:0000303|PubMed:25086048};
GN Name=KRE33 {ECO:0000303|PubMed:12663529};
GN Synonyms=NAT10 {ECO:0000255|HAMAP-Rule:MF_03211},
GN RRA1 {ECO:0000303|PubMed:25086048};
GN OrderedLocusNames=YNL132W {ECO:0000312|SGD:S000005076};
GN ORFNames=N1216, N1858;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THE 90S PRE-RIBOSOMAL PARTICLE BY MASS SPECTROMETRY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12150911; DOI=10.1016/s1097-2765(02)00579-8;
RA Grandi P., Rybin V., Bassler J., Petfalski E., Strauss D., Marzioch M.,
RA Schaefer T., Kuster B., Tschochner H., Tollervey D., Gavin A.-C., Hurt E.;
RT "90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit
RT processing factors but predominantly lack 60S synthesis factors.";
RL Mol. Cell 10:105-115(2002).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=12663529; DOI=10.1093/genetics/163.3.875;
RA Page N., Gerard-Vincent M., Menard P., Beaulieu M., Azuma M.,
RA Dijkgraaf G.J.P., Li H., Marcoux J., Nguyen T., Dowse T., Sdicu A.-M.,
RA Bussey H.;
RT "A Saccharomyces cerevisiae genome-wide mutant screen for altered
RT sensitivity to K1 killer toxin.";
RL Genetics 163:875-894(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001; SER-1007 AND SER-1010,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25086048; DOI=10.1074/jbc.m114.593996;
RA Ito S., Akamatsu Y., Noma A., Kimura S., Miyauchi K., Ikeuchi Y.,
RA Suzuki T., Suzuki T.;
RT "A single acetylation of 18 S rRNA is essential for biogenesis of the small
RT ribosomal subunit in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 289:26201-26212(2014).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-289; HIS-545 AND ARG-637,
RP INTERACTION WITH TAN1, AND DISRUPTION PHENOTYPE.
RX PubMed=25653167; DOI=10.1093/nar/gkv075;
RA Sharma S., Langhendries J.L., Watzinger P., Koetter P., Entian K.D.,
RA Lafontaine D.L.;
RT "Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine
RT acetyltransferases that modify tRNAs assisted by the adaptor
RT Tan1/THUMPD1.";
RL Nucleic Acids Res. 43:2242-2258(2015).
CC -!- FUNCTION: RNA cytidine acetyltransferase with specificity toward both
CC 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine
CC (ac4C) at positions 1280 and 1773 in 18S rRNA. Required for early
CC nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S
CC rRNA synthesis (PubMed:25086048, PubMed:25653167). Catalyzes the
CC formation of ac4C at position 12 in serine and leucine tRNAs. Requires
CC the tRNA-binding adapter protein TAN1 for full tRNA acetyltransferase
CC activity but not for 18S rRNA acetylation (PubMed:25653167).
CC {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000269|PubMed:25086048,
CC ECO:0000269|PubMed:25653167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = ADP + an
CC N(4)-acetylcytidine in 18S rRNA + CoA + H(+) + phosphate;
CC Xref=Rhea:RHEA:51424, Rhea:RHEA-COMP:13575, Rhea:RHEA-COMP:13576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03211,
CC ECO:0000269|PubMed:25086048, ECO:0000269|PubMed:25653167};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in tRNA + acetyl-CoA + ATP + H2O = ADP + an N(4)-
CC acetylcytidine in tRNA + CoA + H(+) + phosphate;
CC Xref=Rhea:RHEA:53876, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:13671,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03211,
CC ECO:0000269|PubMed:25653167};
CC -!- SUBUNIT: Interacts with TAN1 (PubMed:25653167). Associates with 90S
CC pre-ribosomal particles (PubMed:12150911). {ECO:0000255|HAMAP-
CC Rule:MF_03211, ECO:0000269|PubMed:12150911,
CC ECO:0000269|PubMed:25653167}.
CC -!- INTERACTION:
CC P53914; Q05022: RRP5; NbExp=2; IntAct=EBI-28914, EBI-16011;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03211, ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Leads to a strong inhibition of 18S rRNA
CC synthesis (PubMed:25653167). Deletion results in an altered alkali-
CC soluble beta-glucan phenotype (PubMed:12150911). Heterozygous mutants
CC show haploinsufficiency in K1 killer toxin resistance
CC (PubMed:12663529). {ECO:0000269|PubMed:12150911,
CC ECO:0000269|PubMed:12663529, ECO:0000269|PubMed:25653167}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03211}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z46843; CAA86893.1; -; Genomic_DNA.
DR EMBL; Z71408; CAA96014.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10416.1; -; Genomic_DNA.
DR PIR; S55151; S55151.
DR RefSeq; NP_014267.1; NM_001182970.1.
DR PDB; 5WLC; EM; 3.80 A; LX/LY=1-208.
DR PDB; 6KE6; EM; 3.40 A; RL/RM=1-1056.
DR PDB; 6LQP; EM; 3.20 A; RL/RM=1-1056.
DR PDB; 6LQQ; EM; 4.10 A; RL/RM=1-1056.
DR PDB; 6LQR; EM; 8.60 A; RL/RM=1-1056.
DR PDB; 6LQU; EM; 3.70 A; RL/RM=1-1056.
DR PDB; 6LQV; EM; 4.80 A; RL/RM=1-1056.
DR PDB; 6ZQB; EM; 3.90 A; JA/JB=1-1056.
DR PDB; 6ZQC; EM; 3.80 A; JA/JB=1-1056.
DR PDB; 7AJT; EM; 4.60 A; JA/JB=1-1056.
DR PDB; 7D63; EM; 12.30 A; RL/RM=1-1056.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P53914; -.
DR SMR; P53914; -.
DR BioGRID; 35695; 232.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-6588N; -.
DR IntAct; P53914; 90.
DR MINT; P53914; -.
DR STRING; 4932.YNL132W; -.
DR iPTMnet; P53914; -.
DR MaxQB; P53914; -.
DR PaxDb; P53914; -.
DR PRIDE; P53914; -.
DR EnsemblFungi; YNL132W_mRNA; YNL132W; YNL132W.
DR GeneID; 855591; -.
DR KEGG; sce:YNL132W; -.
DR SGD; S000005076; KRE33.
DR VEuPathDB; FungiDB:YNL132W; -.
DR eggNOG; KOG2036; Eukaryota.
DR GeneTree; ENSGT00390000009140; -.
DR HOGENOM; CLU_004652_0_0_1; -.
DR InParanoid; P53914; -.
DR OMA; QDEEFAG; -.
DR BioCyc; YEAST:G3O-33152-MON; -.
DR PRO; PR:P53914; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53914; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:1990883; F:rRNA cytidine N-acetyltransferase activity; IDA:SGD.
DR GO; GO:0030515; F:snoRNA binding; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0016556; P:mRNA modification; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:1904812; P:rRNA acetylation involved in maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03211; RNA_acetyltr_Nat10; 1.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR007807; Helicase_dom.
DR InterPro; IPR033688; NAT10.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032672; TmcA/NAT10/Kre33.
DR InterPro; IPR013562; TmcA_N.
DR InterPro; IPR027992; tRNA_bind_dom.
DR PANTHER; PTHR10925; PTHR10925; 1.
DR Pfam; PF08351; DUF1726; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 1.
DR Pfam; PF05127; Helicase_RecD; 1.
DR Pfam; PF13725; tRNA_bind_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; ATP-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; rRNA processing; Transferase;
KW tRNA processing.
FT CHAIN 1..1056
FT /note="RNA cytidine acetyltransferase"
FT /id="PRO_0000215890"
FT DOMAIN 566..706
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT REGION 433..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P76562, ECO:0000255|HAMAP-
FT Rule:MF_03211"
FT BINDING 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P76562, ECO:0000255|HAMAP-
FT Rule:MF_03211"
FT BINDING 638..640
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P76562, ECO:0000255|HAMAP-
FT Rule:MF_03211"
FT BINDING 645..651
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P76562, ECO:0000255|HAMAP-
FT Rule:MF_03211"
FT BINDING 739
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P76562, ECO:0000255|HAMAP-
FT Rule:MF_03211"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 289
FT /note="K->A: Reduces 18S rRNA acetylation by 80% and tRNA
FT acetylation by 47%."
FT /evidence="ECO:0000269|PubMed:25653167"
FT MUTAGEN 545
FT /note="H->A: Total loss of 18S rRNA acetylation and tRNA
FT acetylation."
FT /evidence="ECO:0000269|PubMed:25653167"
FT MUTAGEN 637
FT /note="R->A: Total loss of 18S rRNA acetylation and tRNA
FT acetylation."
FT /evidence="ECO:0000269|PubMed:25653167"
SQ SEQUENCE 1056 AA; 119348 MW; 76721ED0867ED618 CRC64;
MAKKAIDSRI PSLIRNGVQT KQRSIFVIVG DRARNQLPNL HYLMMSADLK MNKSVLWAYK
KKLLGFTSHR KKRENKIKKE IKRGTREVNE MDPFESFISN QNIRYVYYKE SEKILGNTYG
MCILQDFEAL TPNLLARTIE TVEGGGIVVI LLKSMSSLKQ LYTMTMDVHA RYRTEAHGDV
VARFNERFIL SLGSNPNCLV VDDELNVLPL SGAKNVKPLP PKEDDELPPK QLELQELKES
LEDVQPAGSL VSLSKTVNQA HAILSFIDAI SEKTLNFTVA LTAGRGRGKS AALGISIAAA
VSHGYSNIFV TSPSPENLKT LFEFIFKGFD ALGYQEHIDY DIIQSTNPDF NKAIVRVDIK
RDHRQTIQYI VPQDHQVLGQ AELVVIDEAA AIPLPIVKNL LGPYLVFMAS TINGYEGTGR
SLSLKLIQQL RNQNNTSGRE STQTAVVSRD NKEKDSHLHS QSRQLREISL DEPIRYAPGD
PIEKWLNKLL CLDVTLIKNP RFATRGTPHP SQCNLFVVNR DTLFSYHPVS ENFLEKMMAL
YVSSHYKNSP NDLQLMSDAP AHKLFVLLPP IDPKDGGRIP DPLCVIQIAL EGEISKESVR
NSLSRGQRAG GDLIPWLISQ QFQDEEFASL SGARIVRIAT NPEYASMGYG SRAIELLRDY
FEGKFTDMSE DVRPKDYSIK RVSDKELAKT NLLKDDVKLR DAKTLPPLLL KLSEQPPHYL
HYLGVSYGLT QSLHKFWKNN SFVPVYLRQT ANDLTGEHTC VMLNVLEGRE SNWLVEFAKD
FRKRFLSLLS YDFHKFTAVQ ALSVIESSKK AQDLSDDEKH DNKELTRTHL DDIFSPFDLK
RLDSYSNNLL DYHVIGDMIP MLALLYFGDK MGDSVKLSSV QSAILLAIGL QRKNIDTIAK
ELNLPSNQTI AMFAKIMRKM SQYFRQLLSQ SIEETLPNIK DDAIAEMDGE EIKNYNAAEA
LDQMEEDLEE AGSEAVQAMR EKQKELINSL NLDKYAINDN SEEWAESQKS LEIAAKAKGV
VSLKTGKKRT TEKAEDIYRQ EMKAMKKPRK SKKAAN
