ID A0A081CBA7_PSEA2 Unreviewed; 1258 AA.
AC A0A081CBA7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=PAN0_004d2162 {ECO:0000313|EMBL:GAK63953.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK63953.1};
RN [1] {ECO:0000313|EMBL:GAK63953.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK63953.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) 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}.
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DR EMBL; DF830071; GAK63953.1; -; Genomic_DNA.
DR RefSeq; XP_014657593.1; XM_014802107.1.
DR AlphaFoldDB; A0A081CBA7; -.
DR GeneID; 26303152; -.
DR HOGENOM; CLU_004652_0_0_1; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000053758; 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; 3.40.50.11040; -; 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:UP000053758};
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 116..309
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 401..623
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 668..901
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 912..1147
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 325..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 769..771
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 776..782
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 874
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1258 AA; 138328 MW; 342A2BD912C0988A CRC64;
MLGWLLQHAH LFSPPLHFFF SGVASSAARD VQRSRKFRTL DEKKERRVCL CSTTALLHHT
FGPPFQHPPP SLRPFATVGH LHCTFAPSHC TLLSPASRLA VAPSTSATMR KQLDPRIPTL
IRNNVALNHR SFFVIVGDKG KDQVVNLHFL LSQSRVQSRP NVLWCYKKDL GFTTHRKKRE
QKIKNDIKRG VREKGEGDPF ELFVSLTDIR YCYYKDTPKI LGQTYGMLIL QDFEAVTPNM
LARTIETVEG GGVVILLLKT MSSLRQLYSL GMDVHRSYRS NASDDDPVAR FNERFLLSLG
ATHDTLLLDD ELNVLPLSKA KDIKPLPETS TGTGTGVGST VRKGKERVEA EEELAELKDQ
VRETKVVGEV VRHAKTLDQA KAVLTILDIL ASSSLSTTVA LTAARGRGKS AALGLCIAAA
VAHGYSNIFV TSPSPENLKT LFEFVFKGLD ALGYDEVADW DLQRGTGEWK DVVVRVNIFR
GHRQTIQYIQ PQDHQVLGQA ELVVIDEAAA IPLPLVRNLM GPYLVFLSST INGYEGTGRS
LSLKLIQQLR DNARGVASAS ADDGAASSSK TSGKDGKGSL STGRAAGAAL AARSLKEVEL
KEPIRYSRGD QIESWLHQLL CLDASLTRTS SAALKAKGCP HPSSCDLYMV NRDALFSYHP
ASELFLQRMM ALYVASHYKN SPNDLQLMSD APGHRLFVLL APLKPGEGGL PEPLCVVQVA
LEGNISRGAV LNSLSRGTRE AGDLIPWLVA QQFQDADFAS LSGARVVRIA VHPDYARMGY
GARALQALEA FYTGQLLDLD NVRDDLDDGE TFAAVRDRKI TKDTSLLQGD EIRVRDAARM
PALLQRLSER RPEQLDWLGV SYGLTPQLFK FWKKAGYTPL WVRQIANDLT GEYTAVQLKA
LDTSTSTTGS AWLGALAADF RKRFVALLSY RFRDFATVTA LTVLEAATHG AKLGETESET
STSAPLGAVE LRTLLTPFDM KRLESYANNM VELSVVLDLM PTLAALYFNN RLRAVREDEA
AASAINAAEE EEELRLSGLQ SSLLLAIGLQ RKTPDEITAE LRLPLQQALA LFVKTVRLLV
KSLRKVEKAA IAHDMPELGA GLDARAPLRR KANGSEGEDW SALKGDLNSE LRDAGRDFLA
QHKAQANPDL DGDNDEDDDE DDDEGEEDEE LRVAKQKLID EMNLSKYAIK DDADGSTDWS
QAEAEVANRL RKSGNDLSSI NTTVSVKGAK RAVDDGDKSD SPKKGADKKG KSKKQKRR
//
