ID   NAT10_ACHAM             Reviewed;         373 AA.
AC   P54008;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=RNA cytidine acetyltransferase {ECO:0000250|UniProtKB:P76562};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P76562};
DE   AltName: Full=18S rRNA cytosine acetyltransferase {ECO:0000250|UniProtKB:P76562};
DE   Flags: Fragment;
OS   Achlya ambisexualis (Water mold).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=4768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1689271; DOI=10.1016/0888-7543(90)90444-y;
RA   Schowalter D.B., Toft D.O., Sommer S.S.;
RT   "A method of sequencing without subcloning and its application to the
RT   identification of a novel ORF with a sequence suggestive of a
RT   transcriptional regulator in the water mold Achlya ambisexualis.";
RL   Genomics 6:23-32(1990).
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:0000250|UniProtKB:P76562}.
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:0000250|UniProtKB:P76562};
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:0000250|UniProtKB:P76562};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P76562}.
CC   -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a steroid receptor on the basis
CC       of non-significant sequence similarities. {ECO:0000305|PubMed:1689271}.
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DR   EMBL; M23451; AAA32628.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54008; -.
DR   SMR; P54008; -.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR007807; Helicase_dom.
DR   InterPro; IPR032672; TmcA/NAT10/Kre33.
DR   PANTHER; PTHR10925; PTHR10925; 1.
DR   Pfam; PF13718; GNAT_acetyltr_2; 1.
DR   Pfam; PF05127; Helicase_RecD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ATP-binding; Nucleotide-binding; Nucleus; rRNA processing;
KW   Transferase; tRNA processing.
FT   CHAIN           <1..>373
FT                   /note="RNA cytidine acetyltransferase"
FT                   /id="PRO_0000215884"
FT   REGION          246..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P76562"
FT   BINDING         216..218
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P76562"
FT   BINDING         223..229
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P76562"
FT   BINDING         313
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P76562"
FT   NON_TER         1
FT   NON_TER         373
SQ   SEQUENCE   373 AA;  41425 MW;  490C3D2E7C11811E CRC64;
     IHGDNKTRKG ERKLHEERWQ AASAAAHQHL STPQTAAGGG RVLREVTLEM PIRYAPSDAV
     EKWLNNLLCL DCGSTPNRII GGTPHPRECE LYYVDRDSLF SYHKLSESFL QRIMALYVAS
     HYKNQPNDLQ LLSDAPAHHI FVLLGPQAEG QGNAGQLPDV LCVVQVALEG EISKESVAAQ
     LSRGQRASGD LIPWTVAQQF QDNEFAGLSG ARVVRIATHP DVTGMGYGSR AVELLTKYYQ
     GELASGEFEE ENEAAKPADE ESDDESNLLK EKVKPRKALP PLLLPLTDRP AERLHWFGTS
     FGLTLQLYTF WQRSGFRSVY IRQTANPLTG EHTAIMLNAL KCDDLPASPA AGWLDEFVGD
     ARKRFMALLA YEF