ID A0A1E3HE53_9TREE Unreviewed; 830 AA.
AC A0A1E3HE53;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Name=NAT10 {ECO:0000256|HAMAP-Rule:MF_03211};
GN ORFNames=L202_07517 {ECO:0000313|EMBL:ODN74046.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN74046.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN74046.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN74046.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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 the tRNA-
CC binding adapter protein TAN1 for full tRNA acetyltransferase activity
CC but not for 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 -!- SUBUNIT: Interacts with TAN1. {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: 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:ODN74046.1}.
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DR EMBL; AWGJ01000012; ODN74046.1; -; Genomic_DNA.
DR RefSeq; XP_018989908.1; XM_019142265.1.
DR AlphaFoldDB; A0A1E3HE53; -.
DR GeneID; 30158826; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000094065; 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 CDD; cd04301; NAT_SF; 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; 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; PF13725; tRNA_bind_2; 1.
DR PROSITE; PS51186; GNAT; 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}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03211};
KW Reference proteome {ECO:0000313|Proteomes:UP000094065};
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 332..532
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 197..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 404..406
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 411..417
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 504
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 830 AA; 91213 MW; 95D8CB0297227F08 CRC64;
MKESLEGVDI VGSLSKLAKT VDQAKALLTF VEAISEKTLS STVALTAARG RGKSAALGLA
IGAALAHDYS NIFVTSPDPE NLKTLFEFVF KALDALGYEE HIDYDVVQST NPDFKKAIVR
VNIFRGHRQT IQYISPEDHH VLGQAELVII DEAAAIPLPL VRKLIGPYLV FMASTINGYE
GTGRSLSIKL IQQLREQTRP TITKDNDTTT GAGNGGSSKS ASAGPSGAGL ARSLREIKLD
EPIRYSPGDN VEKWLNNLLC LDASIVSKSI QGCPHPSKCD LYYVGRDTLF SYHPASEVFL
QRMMALYVAS HYKNSPNDLQ MLSDAPAHHL FVLLPPIDEN DNTLPDPLCV LQVALEGNIS
RDAILKEMSQ SGMRSSGDMI PWIVSQQYQD NDFATLSGAR IVRIATHPDY ARMGYGSRAI
EALTSFYNGE LYNFEDATND SGESFADAAK VGPNASLQND TIAIRDPTRM PPLLQRLSER
KPEPLDYLGV SFGLTRDLMK FWKKAGFTPL YASQKENTLT GEYTFVMLKT LLGAGNGEWL
GAFAQDFRQR FMNLLSFESF KKFEASQSLS ILESTVPRNS PSPQPKPLTA SELSTLLTPF
DLKRLESYTD SMVDYHVVLD LVPTIANLFF ARRLDVSLAP AQQAILLALG LQRKNVEALE
TELGLTATQT LALFGKILRK IAKALEDVQK EGIVSELPAE SAPRGKQNFV ALQQTVEQEL
ADSLPRINQG AETEEEKQSK KEQRELLDSL DMSEFAVNQG GDWSAAEKQV EKLAEGGNAR
LSNTVSVKFD KVTDAEEKKG GKGKEAVKDG KKKKRDSLGD KGGKKKMRRE
//
