ID A0A0E0BPL3_9ORYZ Unreviewed; 1024 AA.
AC A0A0E0BPL3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, 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};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM12G05100.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM12G05100.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM12G05100.1}
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}.
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DR AlphaFoldDB; A0A0E0BPL3; -.
DR STRING; 40148.A0A0E0BPL3; -.
DR EnsemblPlants; OGLUM12G05100.1; OGLUM12G05100.1; OGLUM12G05100.
DR Gramene; OGLUM12G05100.1; OGLUM12G05100.1; OGLUM12G05100.
DR eggNOG; KOG2036; Eukaryota.
DR HOGENOM; CLU_004652_0_0_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
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:UP000026961};
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..744
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 758..974
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 986..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 928..955
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 992..1024
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 625..631
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 716
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1024 AA; 116025 MW; 8BB6B3346529EC94 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 KPHDHGKLSQ VELLVIDEAA AIPLPIVKSL LGPYLVFLSS TVNGYEGTGR
SLSLKLLQQL ESQSQPSAPN NGPNSSRLFK KIELNESIRY ASGDPIESWL NDLLCLDLAN
SIPNISRLPH PKECDLYYVN RDTLFSYHKE SEIFLQRMMA LYVASHYKNS PNDLQLMADA
PAHHLFVLLG PVDESKNQLP DILCVVQVCL EGQISRKSAM KSLSEGRSPS GDQIPWKFCE
QFQDNVFPSL SGARIVRIAV HPSAVRLGYG SAAVDLLTRY YEGQMTLFAE DEEENEEPEV
RITEAAEKAS LLEETVKPRA NLPPLLVHLR ERRPEKLHYL GVSFGLTQEL FRFWRKHNFY
PFYVGQIPSA VTGEHTCMVL RPLNSDDIEV NESSKCGFLD PFYQDFRQRF RRLLGTSFRH
LNFKLAMSVL ASKIDFSDHE PSDYYTNITS KILGDMLSPH DMKRLEAYSN NLVDYHLILD
LVPILAHQYF SEKLPVTLHG AQAAVLFCMG LQDKDIGATK EELGIEREQV LSNFIKTMKK
LYGYLHNIAG KEIEATLPRL KEIDTAPLKS LDEDLDEAAR EVKEQRRAID EDDVDPKFLQ
KYAIDADDDE IEKALNGGKI SASGVISVKS NKTKADKQEK RKEMKKSKRK GNDGEKSESK
KKRS
//
