ID A0A0E0F9Y5_9ORYZ Unreviewed; 1050 AA.
AC A0A0E0F9Y5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:OMERI12G02480.3};
RN [1] {ECO:0000313|EnsemblPlants:OMERI12G02480.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI12G02480.3};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI12G02480.3}
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}.
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DR AlphaFoldDB; A0A0E0F9Y5; -.
DR STRING; 40149.A0A0E0F9Y5; -.
DR EnsemblPlants; OMERI12G02480.3; OMERI12G02480.3; OMERI12G02480.
DR Gramene; OMERI12G02480.3; OMERI12G02480.3; OMERI12G02480.
DR eggNOG; KOG2036; Eukaryota.
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; -; 2.
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; 2.
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 281..477
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 517..626
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 653..772
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 786..1002
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 1013..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 956..983
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1019..1050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286..295
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 618..620
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 744
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1050 AA; 118982 MW; 53A2C489A87CFFC9 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 LDKSLRSTVA LLAARGRGKS AALGLAIAGA
IAAGYSNIFV TAPSPENLKT LFDFVCKGMN ALEYKEHLHY DVVKSADPEL KKATIQINVY
KQHRQTIQYL KPHDHAKLSQ VELLVIDEAA AIPLPIVKSL LGPYLVFLSS TVNGYEGTGR
SLSLKLLQQL ESQSQPSAPS NGPNSSRLFK KIELNESIRY ASGDPIESWL NDLLCLDLAN
SIPNISRLPH PKECDLYYVN RDTLFSYHKE SEIFLQRMMA LYVASHYKNS PNDLQLMADA
PAHHLFVLLG PVDESKNQLP DILCVVQVCL EGQISRKSAM KSLSEGRSPS GDQIPWKFCE
QFQDNVFPSL SGARIVRIAV HPSAVRVRFI AFIELCSARV NITLHTLNIL LSMQLGYGSA
AVDLLTRYYE GQMTLFAEDE EENEEPEVRI TEAAEKASLL EETVKPRANL PPLLVHLRER
RPEKLHYLGV SFGLTQELFR FWRKHNFYPF YVGQIPSAVT GEHTCMVLRP LNSDDIEVNE
SSKCGFLDPF YQDFRQRFRR LLGTSFRHLN FKLAMSVLAS KIDFSDHEPS DYYTNITSKI
LGDMLSPHDM KRLEAYSNNL VDYHLILDLV PILAHQYFSE KLPVTLHGAQ AAVLFCMGLQ
DKDIGATKEE LGIEREQVLS NFIKTMKKLY GYLHNIAGKE IEATLPRLKE IDTAPLKSLD
EDLDEAAREV KEQRRAIDED DVDPKFLQKY AIDADDDEIE KALNGGKISA SGVISVKSNK
ADKQEKRKEM KKSKRKGNDG EKSESKKKRS
//
