NT102_ARATH
ID NT102_ARATH Reviewed; 1028 AA.
AC Q9M2Q4; Q0WNS9;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=RNA cytidine acetyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03211};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03211};
DE AltName: Full=18S rRNA cytosine acetyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03211};
GN OrderedLocusNames=At3g57940; ORFNames=T10K17.150;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M2Q4-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03211}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB67622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AL132977; CAB67622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79720.1; -; Genomic_DNA.
DR EMBL; AK229357; BAF01220.1; -; mRNA.
DR PIR; T46016; T46016.
DR RefSeq; NP_191353.2; NM_115656.4. [Q9M2Q4-1]
DR AlphaFoldDB; Q9M2Q4; -.
DR SMR; Q9M2Q4; -.
DR BioGRID; 10278; 3.
DR STRING; 3702.AT3G57940.1; -.
DR iPTMnet; Q9M2Q4; -.
DR PaxDb; Q9M2Q4; -.
DR PRIDE; Q9M2Q4; -.
DR ProteomicsDB; 248936; -. [Q9M2Q4-1]
DR EnsemblPlants; AT3G57940.1; AT3G57940.1; AT3G57940. [Q9M2Q4-1]
DR GeneID; 824963; -.
DR Gramene; AT3G57940.1; AT3G57940.1; AT3G57940. [Q9M2Q4-1]
DR KEGG; ath:AT3G57940; -.
DR Araport; AT3G57940; -.
DR TAIR; locus:2095828; AT3G57940.
DR eggNOG; KOG2036; Eukaryota.
DR InParanoid; Q9M2Q4; -.
DR OMA; KGSEEDW; -.
DR OrthoDB; 296129at2759; -.
DR PhylomeDB; Q9M2Q4; -.
DR PRO; PR:Q9M2Q4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2Q4; baseline and differential.
DR Genevisible; Q9M2Q4; 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; Alternative splicing; ATP-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; rRNA processing; Transferase; tRNA processing.
FT CHAIN 1..1028
FT /note="RNA cytidine acetyltransferase 2"
FT /id="PRO_0000215888"
FT DOMAIN 546..729
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT REGION 982..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1015
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 458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 617..619
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 624..630
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 717
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1028 AA; 115476 MW; 5031CC843340284A CRC64;
MRKKVDERIR TLIENGVKLR HRSMFVIIGD KSRDQIVNLH HMLSKAVIKC NPSVLWCYKD
KLDISSHKQK RSKQLKRLRE RGQLDPEKLD AFSRLLDVGR VTHCLYKDSE RILGNTFGMC
ILQDFEALTP NLLARTIETV EGGGLVVLIL RSLTSLTSLC TMVMDVHDRF RTESHSEAAG
RFNERFLLSL ASCKACVVMD DELNILPLSS HIRSITQVPT EKDSEGLSEA ERDLKSLKED
LSDDFPVGPL IKKCCTLDQG KAVVTFFDAI LDKALRSIVA LIASRGRGKS AALGLAVAGA
VAAGYSNIYI TAPSPDNLKT FFEFVCKGFD ALEYKEHLDY DVVKSANPDF KKAVVRINIF
KQHRQTIQYI QPHEHEKLSQ VELLVIDEAA AIPLPVVKSL LGPYLVFLSS TVSGYEGTGR
SLSLKLLQQL DEQSRAPATG LEGSGCLFKK IELTESIRYG SGDPIESWLN GLLCLDVATC
LPNPACHPSP SQCDLYYVNR DTLFSYHKDS ELFLQRMMAL CVSSHYKNSP NDLQLLADAP
AHHLFVLLGP VDESQNKIPD ILCVIQVCLE GKISENSALQ SLRDGHSPYG DQIPWKFCEQ
FRDTEFPGFS GARIVRIAVH PNAMKMGYGS AAVELLTRYF EGQIAPISEA EDKVDVEHAP
IKVTEAAEKV SMLEEQVKPR TNLPPLLVPL HDRRPEKLHY IGVSFGLTLD LFRFWRKHNF
APFYVSQIPS AVTGEHTCML LKPLKNDELE VNESDELGFF TPFYKDFKIR FSKLLSDKFK
KMDYKLAMSV LNPKINFAEV DSSGSSSGGF LKTLNGILSP YDMERLRAYT ENLTDFNLVY
DICKTLAHQY FEEKLPVSLS YVQASILLCL GLQETDFSSI ERQMQLERGQ IHSLLLKVAR
ELYKYLNGVA GKEIKSALPR LKERELTAHN VSVDDDIREG AKQVEEQMKK EKIEGLMDSE
LQQYVIGDKE AEALQHSKIS SSGIISVKST KSENENGFDK STKKRSSDKR SSSSSKSKSS
KKRKSLKE
