ID A0A0D7BUJ8_9AGAR Unreviewed; 1069 AA.
AC A0A0D7BUJ8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=CYLTODRAFT_485001 {ECO:0000313|EMBL:KIY73854.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY73854.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY73854.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY73854.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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}.
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DR EMBL; KN880433; KIY73854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BUJ8; -.
DR STRING; 1314674.A0A0D7BUJ8; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000054007; 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:UP000054007};
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 10..200
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 277..496
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 539..767
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 777..1018
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 433..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 641..643
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 648..654
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 740
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1069 AA; 118260 MW; 040D40EE431F0E01 CRC64;
MRKQLDPRIP ILIDNNVKKN HRSFIVLVGD KGRDQVVNLH YLLSQARVSA RPSVLWCYKK
ELGFTSHRKK REAKIKRDVK RGVREANDQN PFEIFVTVTD IRYTYYKESH KILGRTYGMC
VLQDFEAITP NLLARTIETV EGGGVVILLL KTMSSLRQLY SMTMDVHSRY RTSSHDSVTA
RFNERFILSL GSCPDCLFLD DELNVLPISR GKDITAYEPP SAEPKSTHEL KELVASLANA
KPAGDLVKLA KTTDQAQAIL TFIEAIAEKT LSSTVTLTAG RGRGKSAALG LGIAAALAHG
YSNIFLTSPS PENLNTVFEF LFKGLDALGY EEHLDYDIAQ STNPDYNKAI VRVNVFNDHR
QTVQYIQPED AHVLGQAELV IIDEAAAIPL PLVRNLFGPY LVFLASTING YEGTGRSLSL
KLIQQLRDST RPSVDSVTEV PTKDDDKSAT KSGKQPTTVA APRALRTLRE VALTTPIRYS
EGDEIESWLN ILLCLNATHS PSMTHLSAGC PHPSQCELYY VNRDTLFSFH PASEAFLQRM
MALYVASHYK NQPNDLQLMS DAPAHHLFVL LPPINESNAS VLPEPLAVIQ VALEGSISKA
SILEGLNRGI RAGGDLIPWL VAQQFQESRF AEMSGARVVR VAVSPEMANM GYGSRAVQAL
NSYYSGELFD FDNAEKAEEH FPNPAIVEKD VDLHDDTPAI RSPNSMPPLL QRLSERKPEA
LEYLGVSYGM TGQLLRYWKR LGFVPLYIGQ RANDLTGEHT SVMIRGLNSS VDSDLEWLAE
FAADFRSRFL TLLSFPKFRD FSAVTALSIL DAVNTFSGVR NLDKNGGGAK TLTPALLPSI
LTPFDLKRLE AYGNNILDYH VIMDLLPLLA QLYFQCRLDG VQQDGADPKS KVHLSPVQGA
IILGMGLQRK SVEELEAELT LPVSQVLALL VKIIHKITGR LISIQKEAIS ETMNTISKAA
SRTLFIQAPQ RTIEEELDEA GEEEAHARET RERQREMINA LDLKKYAIDD SMDWAAAETR
IGSGVGTSAV VSVKQSGVVQ KRKASDGEAA AASDNSQAKK KTRRGKAKK
//
