ID   A0A0E0F9Y4_9ORYZ        Unreviewed;       983 AA.
AC   A0A0E0F9Y4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-JUN-2019, entry version 22.
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; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI12G02480.2, ECO:0000313|Proteomes:UP000008021};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI12G02480.2, ECO:0000313|Proteomes:UP000008021}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI12G02480.2,
RC   ECO:0000313|Proteomes:UP000008021};
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
CC       both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-
CC       acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar
CC       cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA
CC       synthesis. Catalyzes the formation of ac4C in serine and leucine
CC       tRNAs. Requires a tRNA-binding adapter protein for full tRNA
CC       acetyltransferase activity but not for 18S rRNA acetylation.
CC       {ECO:0000256|HAMAP-Rule:MF_03211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in 18S rRNA + acetyl-CoA + ATP + H2O = ADP +
CC         an N(4)-acetylcytidine in 18S rRNA + CoA + H(+) + phosphate;
CC         Xref=Rhea:RHEA:51424, Rhea:RHEA-COMP:13575, Rhea:RHEA-
CC         COMP:13576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:74900, ChEBI:CHEBI:82748,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP-Rule:MF_03211};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in tRNA + acetyl-CoA + ATP + H2O = ADP + an
CC         N(4)-acetylcytidine in tRNA + CoA + H(+) + phosphate;
CC         Xref=Rhea:RHEA:53876, Rhea:RHEA-COMP:13670, Rhea:RHEA-
CC         COMP:13671, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:74900, ChEBI:CHEBI:82748,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|HAMAP-Rule:MF_03211};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC       Rule:MF_03211}.
CC   -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family.
CC       NAT10 subfamily. {ECO:0000256|HAMAP-Rule:MF_03211}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03211}.
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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   HAMAP; MF_03211; RNA_acetyltr_Nat10; 1.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR007807; Helicase_dom.
DR   InterPro; IPR033688; NAT10.
DR   InterPro; IPR032672; TmcA/NAT10/Kre33.
DR   InterPro; IPR013562; TmcA_N.
DR   InterPro; IPR027992; tRNA_bind_dom.
DR   PANTHER; PTHR10925; PTHR10925; 2.
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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03211};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008021};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_03211};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03211};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_03211}.
FT   DOMAIN      106    200       DUF1726. {ECO:0000259|Pfam:PF08351}.
FT   DOMAIN      303    438       Helicase_RecD. {ECO:0000259|Pfam:
FT                                PF05127}.
FT   DOMAIN      478    705       N-acetyltransferase. {ECO:0000259|Pfam:
FT                                PF13718}.
FT   DOMAIN      719    935       tRNA_bind_2. {ECO:0000259|Pfam:PF13725}.
FT   REGION      579    581       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03211}.
FT   REGION      586    592       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03211}.
FT   REGION      946    983       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0E0F9Y4}.
FT   COILED      220    240       {ECO:0000256|SAM:Coils}.
FT   COILED      889    916       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    952    983       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0E0F9Y4}.
FT   BINDING     420    420       ATP. {ECO:0000256|HAMAP-Rule:MF_03211}.
FT   BINDING     677    677       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                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
//