ID T0QQM2_SAPDV Unreviewed; 1085 AA.
AC T0QQM2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=SDRG_06315 {ECO:0000313|EMBL:EQC36205.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC36205.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC36205.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC36205.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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; JH767148; EQC36205.1; -; Genomic_DNA.
DR RefSeq; XP_008610311.1; XM_008612089.1.
DR AlphaFoldDB; T0QQM2; -.
DR STRING; 1156394.T0QQM2; -.
DR EnsemblProtists; EQC36205; EQC36205; SDRG_06315.
DR GeneID; 19947042; -.
DR VEuPathDB; FungiDB:SDRG_06315; -.
DR eggNOG; KOG2036; Eukaryota.
DR InParanoid; T0QQM2; -.
DR OMA; CGDSNNC; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000030762; 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};
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:UP000030762};
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 9..201
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 280..517
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 558..794
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 806..1027
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 437..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 662..664
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 669..675
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 766
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1085 AA; 120559 MW; 3718FBD34EF77387 CRC64;
MVKKKVDARV RTLLENCVKT NHRSFIVLVG DHGKDQVVNL HYILSKTVVK ARPKVLWCYK
KELGFSTHKQ KRMKQIKKQM SRGLYDSNTE DPFELFISST DIRWCYYKET QKILGQTYGM
CVLQDFEAVT PNILARTIET VEGGGVVVLL LRTMSSLKKL YTMSMDVHSR FRTEAHQDVV
ARFNERFILS LSGCDKCLVL DDELNVLPIS KHARNIEALP PVDDELTPDM RELADLKESL
KDTQPVGSLV AQAKTLDQAK AILTFAEAIS EKTLRSTVTL TAGRGRGKSA ALGMSLAAAV
AYGYSNIFVT APSPENLGTV FDFVFKGFDA LKYKEHLDYE IIQSTNPEFN RAVVRVNIFR
EHRQTIQYIQ PHHHEKLAQA ELLAIDEAAA IPLPVVKNLL GPYLVFMSST INGYEGTGRS
LSLKLIQKLR EQQGSAGMAA QHAMSSIHGD NKTRKGERKL HEERWQAASA AAHQHMAAPQ
TAAGGGRVLR EVTLDIPIRY AQNDAVEKWL NNLLCLDCGS TPQRIMGGTP HPRECELYYV
DRDSLFSYHK LSENFLQRLM SLYVASHYKN QPNDLQLLSD APAHHIFVLL GPQAEGQGNA
GQLPDVLCVV QIALEGEISK ESVAAQLSRG QRASGDLIPW TVAQQFQDNE FAGLSGARVV
RIATHPDVTN MGYGSRAIEL LTKYYQGELA SGDLDGSDDE AETKKSKKKD DDNDSDDEGN
LLKEKVKPRK ALPPLLLPLT DRPAERLHWF GTSFGLTLPL YTFWSRAGFR SVYIRQTANA
LTGEHTAIML NALKCDDLPA SPSTGWLDEF VGDARKRFMA LLSYEFRTLP PTLALSLLSD
AKTKTTDETA NLLRVSSGLI SSNDLQVSLT PFDIKRLQSY AKNMVDYHMI VDLIPSVARL
YFLNRLPDTT LSYLQRAILM SIGLQHQSVD TLVSELNVPS NQLLALFNKS VRKFATAFNG
ILEAEVEETI AAPTAVAAMA PTTLTLEEDL ADAKDQALKK LKQKELLDTL NLGQYAVRGD
DADWAAALDE KKDPTAKGVS VKNTKKMAKK READESADAK DDSKAKKFKK GAPAKGKKSK
YANLK
//
