ID A0A090M5W4_OSTTA Unreviewed; 1030 AA.
AC A0A090M5W4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=OT_ostta05g03410 {ECO:0000313|EMBL:CEF98062.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CEF98062.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CEF98062.1}.
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DR EMBL; CAID01000005; CEF98062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090M5W4; -.
DR STRING; 70448.A0A090M5W4; -.
DR InParanoid; A0A090M5W4; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000009170; Chromosome 5.
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};
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:UP000009170};
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 8..200
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 276..477
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 518..741
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 755..970
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 980..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1030
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 619..621
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 715
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1030 AA; 114508 MW; E54CA38936B0C9A4 CRC64;
MRKKVDGRIR TLVENGVKNN ERTMFVIVGD RGRDQIVNLH YMLSKAVVKS RPNVLWCYKK
DLYLSSHKKK RAKQVKKMQN SGLMDKENED PFSLFVASTS IRYCYYADTQ KILGNTYGMA
VLQDFEALTP NLLARTIETV EGGGLIVLLL SNMESLTQLY NMTMDVHSRF RTEGHQDVVA
RFNERFTLSL GACPTCIMMD DELNILPTSS HIRGIEPVEE KRADESPELT DLKESMEEVE
PAGPLVKCCK TMDQAKAVVT FLDAASEKTL RSTVALTAAR GRGKSAAMGI AVAGAVEMGY
ANIFVTSPSP ENLKTFFDFI LKGFDALGYK EHLDYDLVES TNPAFGKCIV RINVTRRHRQ
TIQYILPQHY ERATQAELLV IDEAAAIPLP TVKALLGPYL VFLCSTINGY EGTGRALSIK
LIANLRREAA TTQQANKDGK LATGGSRLLR EVALTEPVRY CAGDRVEKWL NDLLCLDAAD
ALKPLITALP PPNACELYEV SRDTLFSAHA ASEQFLKKMM ALYVSSHYRN TPNDLQLMSD
APAHRLFVLL APVDETQNVL PEILCVVQVA LEGAISQQSA RATLAAGLSP QGDLIPWTMA
SQFQDEGFPS FTGARIVRIA VHPDLPRQGY GSRALQMIHD YYEGKLADLR EEADIDAKTN
TEHWQNTGKL LEETLKPRDN LPPLLVNLSE RRPEPINWIG TAFGLTSQLY SYWSKAGYKP
VYVRQTASET TGEHTCIMLR ACFPVGAEES PDGNWVDSFY SDFRVRFTSL LGSAFRDMPP
ALCLCLMDPK LNYDEKSGAS RESVLKADNE ILSPHDLRRI QKYAAALVDH HLIGDLVPPI
ARAYFAHRIP VTISYTQAVI LLILGLQLKT IDDAIKTLDL PGQQLMALFN KAIRRIHGSI
LMAREAEIEA ALPSVSMPEL RPHAVGLDED LEEGAAMVNA EIAAKQKALL EDGDFDRYAI
TGTDTEWASA LQGASNRSNK LLSVKRKAGA EDKHSYEPKE KKPKEPSSEK KDKKNKKHKK
SSAPKRLKGT
//
