ID E1ZAA5_CHLVA Unreviewed; 1177 AA.
AC E1ZAA5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
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};
GN ORFNames=CHLNCDRAFT_57403 {ECO:0000313|EMBL:EFN57025.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN57025.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN57025.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
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}.
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DR EMBL; GL433840; EFN57025.1; -; Genomic_DNA.
DR RefSeq; XP_005849127.1; XM_005849065.1.
DR AlphaFoldDB; E1ZAA5; -.
DR STRING; 554065.E1ZAA5; -.
DR GeneID; 17356698; -.
DR KEGG; cvr:CHLNCDRAFT_57403; -.
DR eggNOG; KOG2036; Eukaryota.
DR InParanoid; E1ZAA5; -.
DR OMA; HLHYIMS; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000008141; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000008141};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03211}.
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..200
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 220..431
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 472..706
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 716..933
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 568..570
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 575..581
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 679
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1177 AA; 127360 MW; 7CD57D2B1D4353AE CRC64;
MRKKVDSRIR TLVENCVKTG QRSLFVIVGD KGRDQVVNLH YMLSKTVVKA RPSVLWCYKK
ELHLSSHKKK RMAQIKKMAQ RGLLDPEKED PFSLFVASTS IRYCYYADTH KILGNTYGML
VLQDFEAVTP NLLARTVETV EGGGVVVLLL STLDSLSQLY SLTMDVHARL RTESHQNVTG
RFNERLVLSL ASCPSCILMD DELNILPTSS HKTLRATVAL TAARGRGKSA ALGLAVAGAL
ALGYSNIFVT APSPENLRTL FEFVFKGLDE LEYKEHIDYD LVESTNPSFG RAVVRVNVYR
THRQTVQYIQ PQHHARLAQA ELLVIDEAAA IPLPLVKAML GPYLVFLCST VNGYEGTGRS
LSLKLIQQLR QQGAKLASGD GRKGGGGGGG GDATAAGGSM RTFREVVLGE PIRYSLGDKV
ERWLNELLCL DAAEHTPAPP ARLPHPDECE LYYVERDTLF SYHKASETFL QRMMALYVAS
HYKNTPNDLI LMSDAPAHHL FVLLGPNALP DVLAVVQVAL EGSISQRSAR ASLAAGQLPQ
GDLIPWTVGQ QFQDSEFPAL SGARVVRIAV HPEVPRAGYG TRAVDQLRRY YEGQIADVMS
EDEAAAGGGG GAPAGHRSSN GPTAAAAQGA GGGLLSEELK PRAGLPPLLV NLSDRPAERL
HYLGTSFGLT QQLYSFWRRS AFRPVYLRQT PSDVTGEHTV IMLRPLRSAD VADTAWLDPF
VADFRARFMT LLAGAFRDFP PALVLSMLDP KLSWSEAESG AAVAGGVVVR KPDGAGLSPY
DLKRLQAYSN NLVDHHLILD LLPPLAHAYF GGRLPAPLSY SQAAILACVG LQQHEIGKLE
EWLGLPPSQA LALFNKAVRR LHGLLRAAQE AEVERSLPRP AARGGGGGAD LAPHDADLDA
EVEEAAEEIK AAMREEFRPE DLARFAIAAD ADFEGAVGGG GAALKPGGIV AVKAAGEARK
REKGGGQQRQ AQRQQGGGRE AREGRKHKGG SGGGEGSKAK KKARHSGVRS GGLGSHNVLL
GRRRRASRNS LSAVSNFRLA TFSSRWKVTS HFVATMAPAE SKLRVDAPAF CPRSNPIDVP
SSSAGDQDTH GLPEDPWALS SEMSVSPAEL EELEEVEGWV SLMAELEGME QDHLIELSLR
HADKGKIAQI KAAAMAHKNK HKLHAKHAHH AAMAQKA
//
