ID A0A0E0F9Y4_9ORYZ Unreviewed; 983 AA.
AC A0A0E0F9Y4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:OMERI12G02480.2};
RN [1] {ECO:0000313|EnsemblPlants:OMERI12G02480.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI12G02480.2};
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 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; A0A0E0F9Y4; -.
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 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}; 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 298..438
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 478..705
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 719..935
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 946..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 889..916
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 952..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 579..581
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 586..592
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 677
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule: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
//
