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Protein

RNA cytidine acetyltransferase

Gene

NAT10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) at positions 1280 and 1773 in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25086048, PubMed:25653167). Catalyzes the formation of ac4C at position 12 in serine and leucine tRNAs. Requires the tRNA-binding adapter protein TAN1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167).UniRule annotation2 Publications

Catalytic activityi

A cytidine in 18S rRNA + ATP + acetyl-CoA + H2O = an N(4)-acetylcytidine in 18S rRNA + ADP + phosphate + CoA.UniRule annotation2 Publications
A cytidine in tRNA + ATP + acetyl-CoA + H2O = an N(4)-acetylcytidine in tRNAA + ADP + phosphate + CoA.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei475 – 4751ATPUniRule annotationBy similarity
Binding sitei739 – 7391Acetyl-CoAUniRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi286 – 29510ATPUniRule annotationBy similarity

GO - Molecular functioni

GO - Biological processi

  • ribosomal small subunit biogenesis Source: SGD
  • rRNA processing Source: UniProtKB-KW
  • tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

rRNA processing, tRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33152-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA cytidine acetyltransferaseUniRule annotationCurated (EC:2.3.1.-UniRule annotation)
Alternative name(s):
18S rRNA cytosine acetyltransferase1 PublicationUniRule annotation
Killer toxin-resistance protein 331 Publication
Ribosomal RNA cytidine acetyltransferase 11 Publication
Gene namesi
Name:NAT10UniRule annotation
Synonyms:KRE331 Publication, RRA11 Publication
Ordered Locus Names:YNL132WImported
ORF Names:N1216, N1858
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL132W.
SGDiS000005076. KRE33.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: UniProtKB-SubCell
  • preribosome, small subunit precursor Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Leads to a strong inhibition of 18S rRNA synthesis (PubMed:25653167). Deletion results in an altered alkali-soluble beta-glucan phenotype (PubMed:12150911). Heterozygous mutants show haploinsufficiency in K1 killer toxin resistance (PubMed:12663529).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi289 – 2891K → A: Reduces 18S rRNA acetylation by 80% and tRNA acetylation by 47%. 1 Publication
Mutagenesisi545 – 5451H → A: Total loss of 18S rRNA acetylation and tRNA acetylation. 1 Publication
Mutagenesisi637 – 6371R → A: Total loss of 18S rRNA acetylation and tRNA acetylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10561056RNA cytidine acetyltransferasePRO_0000215890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1001 – 10011PhosphoserineCombined sources
Modified residuei1007 – 10071PhosphoserineCombined sources
Modified residuei1010 – 10101PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53914.
PeptideAtlasiP53914.

PTM databases

iPTMnetiP53914.

Interactioni

Subunit structurei

Interacts with TAN1 (PubMed:25653167). Associates with 90S pre-ribosomal particles (PubMed:12150911).UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BFR2Q066312EBI-28914,EBI-36432
ESF2P537432EBI-28914,EBI-28537
HCA4P204488EBI-28914,EBI-5612
LYS20P485704EBI-28914,EBI-8502
SSB1P114843EBI-28914,EBI-8627

Protein-protein interaction databases

BioGridi35695. 106 interactions.
DIPiDIP-6588N.
IntActiP53914. 70 interactions.
MINTiMINT-607534.

Structurei

3D structure databases

ProteinModelPortaliP53914.
SMRiP53914. Positions 280-654.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini566 – 706141N-acetyltransferaseUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni638 – 6403Acetyl-CoA bindingUniRule annotationBy similarity
Regioni645 – 6517Acetyl-CoA bindingUniRule annotationBy similarity

Sequence similaritiesi

Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily.UniRule annotation
Contains 1 N-acetyltransferase domain.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000009140.
HOGENOMiHOG000210833.
InParanoidiP53914.
KOiK14521.
OMAiYHVVLDL.
OrthoDBiEOG7W15C7.

Family and domain databases

HAMAPiMF_03211. RNA_acetyltr_Nat10.
InterProiIPR000182. GNAT_dom.
IPR007807. Helicase_dom.
IPR032672. TmcA/NAT10/Kre33.
IPR013562. TmcA_N.
IPR027992. tRNA_bind_dom.
[Graphical view]
PANTHERiPTHR10925. PTHR10925. 1 hit.
PfamiPF08351. DUF1726. 1 hit.
PF13718. GNAT_acetyltr_2. 1 hit.
PF05127. Helicase_RecD. 1 hit.
PF13725. tRNA_bind_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKAIDSRI PSLIRNGVQT KQRSIFVIVG DRARNQLPNL HYLMMSADLK
60 70 80 90 100
MNKSVLWAYK KKLLGFTSHR KKRENKIKKE IKRGTREVNE MDPFESFISN
110 120 130 140 150
QNIRYVYYKE SEKILGNTYG MCILQDFEAL TPNLLARTIE TVEGGGIVVI
160 170 180 190 200
LLKSMSSLKQ LYTMTMDVHA RYRTEAHGDV VARFNERFIL SLGSNPNCLV
210 220 230 240 250
VDDELNVLPL SGAKNVKPLP PKEDDELPPK QLELQELKES LEDVQPAGSL
260 270 280 290 300
VSLSKTVNQA HAILSFIDAI SEKTLNFTVA LTAGRGRGKS AALGISIAAA
310 320 330 340 350
VSHGYSNIFV TSPSPENLKT LFEFIFKGFD ALGYQEHIDY DIIQSTNPDF
360 370 380 390 400
NKAIVRVDIK RDHRQTIQYI VPQDHQVLGQ AELVVIDEAA AIPLPIVKNL
410 420 430 440 450
LGPYLVFMAS TINGYEGTGR SLSLKLIQQL RNQNNTSGRE STQTAVVSRD
460 470 480 490 500
NKEKDSHLHS QSRQLREISL DEPIRYAPGD PIEKWLNKLL CLDVTLIKNP
510 520 530 540 550
RFATRGTPHP SQCNLFVVNR DTLFSYHPVS ENFLEKMMAL YVSSHYKNSP
560 570 580 590 600
NDLQLMSDAP AHKLFVLLPP IDPKDGGRIP DPLCVIQIAL EGEISKESVR
610 620 630 640 650
NSLSRGQRAG GDLIPWLISQ QFQDEEFASL SGARIVRIAT NPEYASMGYG
660 670 680 690 700
SRAIELLRDY FEGKFTDMSE DVRPKDYSIK RVSDKELAKT NLLKDDVKLR
710 720 730 740 750
DAKTLPPLLL KLSEQPPHYL HYLGVSYGLT QSLHKFWKNN SFVPVYLRQT
760 770 780 790 800
ANDLTGEHTC VMLNVLEGRE SNWLVEFAKD FRKRFLSLLS YDFHKFTAVQ
810 820 830 840 850
ALSVIESSKK AQDLSDDEKH DNKELTRTHL DDIFSPFDLK RLDSYSNNLL
860 870 880 890 900
DYHVIGDMIP MLALLYFGDK MGDSVKLSSV QSAILLAIGL QRKNIDTIAK
910 920 930 940 950
ELNLPSNQTI AMFAKIMRKM SQYFRQLLSQ SIEETLPNIK DDAIAEMDGE
960 970 980 990 1000
EIKNYNAAEA LDQMEEDLEE AGSEAVQAMR EKQKELINSL NLDKYAINDN
1010 1020 1030 1040 1050
SEEWAESQKS LEIAAKAKGV VSLKTGKKRT TEKAEDIYRQ EMKAMKKPRK

SKKAAN
Length:1,056
Mass (Da):119,348
Last modified:October 1, 1996 - v1
Checksum:i76721ED0867ED618
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46843 Genomic DNA. Translation: CAA86893.1.
Z71408 Genomic DNA. Translation: CAA96014.1.
BK006947 Genomic DNA. Translation: DAA10416.1.
PIRiS55151.
RefSeqiNP_014267.1. NM_001182970.1.

Genome annotation databases

EnsemblFungiiYNL132W; YNL132W; YNL132W.
GeneIDi855591.
KEGGisce:YNL132W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46843 Genomic DNA. Translation: CAA86893.1.
Z71408 Genomic DNA. Translation: CAA96014.1.
BK006947 Genomic DNA. Translation: DAA10416.1.
PIRiS55151.
RefSeqiNP_014267.1. NM_001182970.1.

3D structure databases

ProteinModelPortaliP53914.
SMRiP53914. Positions 280-654.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35695. 106 interactions.
DIPiDIP-6588N.
IntActiP53914. 70 interactions.
MINTiMINT-607534.

PTM databases

iPTMnetiP53914.

Proteomic databases

MaxQBiP53914.
PeptideAtlasiP53914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL132W; YNL132W; YNL132W.
GeneIDi855591.
KEGGisce:YNL132W.

Organism-specific databases

EuPathDBiFungiDB:YNL132W.
SGDiS000005076. KRE33.

Phylogenomic databases

GeneTreeiENSGT00390000009140.
HOGENOMiHOG000210833.
InParanoidiP53914.
KOiK14521.
OMAiYHVVLDL.
OrthoDBiEOG7W15C7.

Enzyme and pathway databases

BioCyciYEAST:G3O-33152-MONOMER.

Miscellaneous databases

PROiP53914.

Family and domain databases

HAMAPiMF_03211. RNA_acetyltr_Nat10.
InterProiIPR000182. GNAT_dom.
IPR007807. Helicase_dom.
IPR032672. TmcA/NAT10/Kre33.
IPR013562. TmcA_N.
IPR027992. tRNA_bind_dom.
[Graphical view]
PANTHERiPTHR10925. PTHR10925. 1 hit.
PfamiPF08351. DUF1726. 1 hit.
PF13718. GNAT_acetyltr_2. 1 hit.
PF05127. Helicase_RecD. 1 hit.
PF13725. tRNA_bind_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames."
    Mallet L., Bussereau F., Jacquet M.
    Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, and 40S subunit processing factors but predominantly lack 60S synthesis factors."
    Grandi P., Rybin V., Bassler J., Petfalski E., Strauss D., Marzioch M., Schaefer T., Kuster B., Tschochner H., Tollervey D., Gavin A.-C., Hurt E.
    Mol. Cell 10:105-115(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE 90S PRE-RIBOSOMAL PARTICLE BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE.
  5. "A Saccharomyces cerevisiae genome-wide mutant screen for altered sensitivity to K1 killer toxin."
    Page N., Gerard-Vincent M., Menard P., Beaulieu M., Azuma M., Dijkgraaf G.J.P., Li H., Marcoux J., Nguyen T., Dowse T., Sdicu A.-M., Bussey H.
    Genetics 163:875-894(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001; SER-1007 AND SER-1010, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A single acetylation of 18 S rRNA is essential for biogenesis of the small ribosomal subunit in Saccharomyces cerevisiae."
    Ito S., Akamatsu Y., Noma A., Kimura S., Miyauchi K., Ikeuchi Y., Suzuki T., Suzuki T.
    J. Biol. Chem. 289:26201-26212(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  11. "Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1."
    Sharma S., Langhendries J.L., Watzinger P., Koetter P., Entian K.D., Lafontaine D.L.
    Nucleic Acids Res. 43:2242-2258(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-289; HIS-545 AND ARG-637, INTERACTION WITH TAN1, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiNAT10_YEAST
AccessioniPrimary (citable) accession number: P53914
Secondary accession number(s): D6W150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.