NT101_ARATH
ID NT101_ARATH Reviewed; 1028 AA.
AC Q9XIK4; Q0WVY1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=RNA cytidine acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03211};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03211};
DE AltName: Full=18S rRNA cytosine acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03211};
GN OrderedLocusNames=At1g10490; ORFNames=T10O24.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
CC -!- FUNCTION: RNA cytidine acetyltransferase with specificity toward both
CC 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine
CC (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor
CC rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the
CC formation of ac4C in serine and leucine tRNAs. Requires a tRNA-binding
CC adapter protein for full tRNA acetyltransferase activity but not for
CC 18S rRNA acetylation. {ECO:0000255|HAMAP-Rule:MF_03211}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03211}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03211}.
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DR EMBL; AC007067; AAD39570.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28585.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59172.1; -; Genomic_DNA.
DR EMBL; AK226604; BAE98717.1; -; mRNA.
DR RefSeq; NP_001318971.1; NM_001331910.1.
DR RefSeq; NP_172519.1; NM_100923.4.
DR AlphaFoldDB; Q9XIK4; -.
DR SMR; Q9XIK4; -.
DR BioGRID; 22829; 3.
DR STRING; 3702.AT1G10490.1; -.
DR iPTMnet; Q9XIK4; -.
DR PaxDb; Q9XIK4; -.
DR PRIDE; Q9XIK4; -.
DR ProteomicsDB; 249082; -.
DR EnsemblPlants; AT1G10490.1; AT1G10490.1; AT1G10490.
DR EnsemblPlants; AT1G10490.2; AT1G10490.2; AT1G10490.
DR GeneID; 837589; -.
DR Gramene; AT1G10490.1; AT1G10490.1; AT1G10490.
DR Gramene; AT1G10490.2; AT1G10490.2; AT1G10490.
DR KEGG; ath:AT1G10490; -.
DR Araport; AT1G10490; -.
DR TAIR; locus:2194579; AT1G10490.
DR eggNOG; KOG2036; Eukaryota.
DR HOGENOM; CLU_004652_0_0_1; -.
DR InParanoid; Q9XIK4; -.
DR OMA; QDEEFAG; -.
DR OrthoDB; 296129at2759; -.
DR PhylomeDB; Q9XIK4; -.
DR PRO; PR:Q9XIK4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIK4; baseline and differential.
DR Genevisible; Q9XIK4; AT.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:1990883; F:rRNA cytidine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acyltransferase; ATP-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; rRNA processing; Transferase; tRNA processing.
FT CHAIN 1..1028
FT /note="RNA cytidine acetyltransferase 1"
FT /id="PRO_0000215887"
FT DOMAIN 548..731
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT REGION 989..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1017
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:0000255|HAMAP-Rule:MF_03211"
FT BINDING 460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 619..621
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 626..632
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 719
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT CONFLICT 110
FT /note="E -> K (in Ref. 3; BAE98717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1028 AA; 115619 MW; 035D673802DA3D08 CRC64;
MRKKVDERIR TLIENGVKLR HRSMFVIIGD KARDQIVNLH HILSKSVVKS NPSVLWCYKN
RLDISSHNKK RAKQLKKMKE RGQLDPEKLD AFSLFLDVVD VTHCLYKDSE RILGNTFGIC
ILQDFEALTP NLLARTIETV EGGGLVVLLL QSLASLTSLC TMVMDVHDRF RTESHSEASG
RFNERFLLSL ASCKACVVMD DELNLLPLSS HIKSITKVPT KEDSEALSEA ERDLKSLKDA
LNDDFPVGPL INKCCTLDQG KAVVTFFDAI LDKTLRSIVA LIASRGRGKS AALGLAVAGA
VAAGYSNIYV TAPSPDNLKT VFEFVCKGFD ALEYKEHLEY DVVRSVNPEF NKAIVRINIF
KQHRQTIQYI QPHEHEKLSQ VELLVIDEAA AIPLPVVKSL LGPYLVFLSS TVSGYEGTGR
SLSLKLLQQL EEQSRAPVTG VEGSLSGCLF KKIELSESIR YASGDPIESW LNGLLCLDVA
NCLPNPACHP LPSQCDLYYV NRDTLFSYHK DSELFLQRMM ALCVSSHYKN SPNDLQLLSD
APAHHLFVLL GPVDESKNQL PDILCVIQVC LEGQISRKSA EKSLREGHSP HGDQIPWKFC
EQFRDVVFPK LSGARIVRIA VHPNAMKMGY GSAAVELLTR YFEGQLASIS EGDDELEVEP
SPVRVTEAAA KVSLLEEQIK PRANLPPLLV PLRDRRPERL HYIGVSFGLT LDLFRFWRKH
KFAPFYISQI PSAVTGEHTC MLLKPLTLSN DEFEVDESDE LGFFAPFYKD FRIRFSKLLS
DKFKKMDYKL AMSVLNPKIN FPEVDLTGNS PDGFLKKLDG VLSPYDMERF RAYTANLVDF
NLVYDICKTL AHHYFQEKLP VSLSYVQASV LLCLGLQESD FSSIERQMQL ERGQIYSLLL
KVGKKLYKYL NGIATKELES TLPRLKDRVL EPHKVSVDED LREGAKEVEE QMRARIEELL
DPELLDQFAI GDKEAEALQK SKISSSGLIS IESTKTDNKK EKPSGFDKSA KKRGNDKHSS
TSNKKRRA
