ID A0A0E0F9Y4_9ORYZ Unreviewed; 983 AA. AC A0A0E0F9Y4; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 24-JAN-2024, entry version 33. DE RecName: Full=RNA cytidine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03211}; DE EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_03211}; DE AltName: Full=18S rRNA cytosine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03211}; OS Oryza meridionalis. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI12G02480.2}; RN [1] {ECO:0000313|EnsemblPlants:OMERI12G02480.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI12G02480.2}; RA Wing R.A., Panaud O., Henry R.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblPlants:OMERI12G02480.2} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03211}; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|HAMAP-Rule:MF_03211}. CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03211}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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 AlphaFoldDB; A0A0E0F9Y4; -. DR EnsemblPlants; OMERI12G02480.2; OMERI12G02480.2; OMERI12G02480. DR Gramene; OMERI12G02480.2; OMERI12G02480.2; OMERI12G02480. DR Proteomes; UP000008021; Chromosome 12. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule. DR GO; GO:0000154; P:rRNA modification; IEA:UniProtKB-UniRule. DR GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.11040; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; N-ACETYLTRANSFERASE 10; 1. DR PANTHER; PTHR10925:SF5; RNA CYTIDINE ACETYLTRANSFERASE; 1. DR Pfam; PF13718; GNAT_acetyltr_2; 1. DR Pfam; PF05127; Helicase_RecD; 1. DR Pfam; PF08351; TmcA_N; 1. DR Pfam; PF13725; tRNA_bind_2; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_03211}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03211}; Coiled coil {ECO:0000256|SAM:Coils}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03211}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03211}; KW Reference proteome {ECO:0000313|Proteomes:UP000008021}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_03211}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03211}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_03211}. FT DOMAIN 7..200 FT /note="tRNA(Met) cytidine acetyltransferase TmcA N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08351" FT DOMAIN 298..438 FT /note="Helicase" FT /evidence="ECO:0000259|Pfam:PF05127" FT DOMAIN 478..705 FT /note="N-acetyltransferase" FT /evidence="ECO:0000259|Pfam:PF13718" FT DOMAIN 719..935 FT /note="Possible tRNA binding" FT /evidence="ECO:0000259|Pfam:PF13725" FT REGION 946..983 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 889..916 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 952..983 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 420 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" FT BINDING 579..581 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" FT BINDING 586..592 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" FT BINDING 677 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211" SQ SEQUENCE 983 AA; 112038 MW; 808A35DAC49C3C6F CRC64; MRKKVDERIR TLIENGVRER QRSMFVIVGD KSRDQIVNLN YMLAKSRVKS RPSVLWCYRD KLEISSHKKK RAKQIKKLMQ RGLMDPEKAD PFSLFLETSD ITYCLYKDSE RVLGNTFGMC ILQDFEALTP NLLARTIETV EGGGLIILLL RSLSSLTSLY TMVMDVHERF RTESHTQAAA RFNERFLLSI ASCKSCVVMD DELNILPISS HMKFIQPVTN NEDSEGLSER ERELKDLKDQ FREDFPVGPL IGKCFTMDQG KAVINFLDSI LDKSLRSTGM NALEYKLMNA SFHPFQEHLH YDVVKSADPE LKKATIQINV YKQHRQTIQY LKPHDHAKLS QVELLVIDEA AAIPLPIVKS LLGPYLVFLS STVNGYEGTG RSLSLKLLQQ LESQSQPSAP SNGPNSSRLF KKIELNESIR YASGDPIESW LNDLLCLDLA NSIPNISRLP HPKECDLYYV NRDTLFSYHK ESEIFLQRMM ALYVASHYKN SPNDLQLMAD APAHHLFVLL GPVDESKNQL PDILCVVQVC LEGQISRKSA MKSLSEGRSP SGDQIPWKFC EQFQDNVFPS LSGARIVRIA VHPSAVRLGY GSAAVDLLTR YYEGQMTLFA EDEEENEEPE VRITEAAEKA SLLEETVKPR ANLPPLLVHL RERRPEKLHY LGVSFGLTQE LFRFWRKHNF YPFYVGQIPS AVTGEHTCMV LRPLNSDDIE VNESSKCGFL DPFYQDFRQR FRRLLGTSFR HLNFKLAMSV LASKIDFSDH EPSDYYTNIT SKILGDMLSP HDMKRLEAYS NNLVDYHLIL DLVPILAHQY FSEKLPVTLH GAQAAVLFCM GLQDKDIGAT KEELGIEREQ VLSNFIKTMK KLYGYLHNIA GKEIEATLPR LKEIDTAPLK SLDEDLDEAA REVKEQRRAI DEDDVDPKFL QKYAIDADDD EIEKALNGGK ISASGVISVK SNKADKQEKR KEMKKSKRKG NDGEKSESKK KRS //