ID W9C1V3_SCLBF Unreviewed; 1074 AA.
AC W9C1V3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, 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 Name=NAT10 {ECO:0000256|HAMAP-Rule:MF_03211};
GN ORFNames=SBOR_9909 {ECO:0000313|EMBL:ESZ89703.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ89703.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ89703.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(2014).
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:ESZ89703.1}.
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DR EMBL; AYSA01000806; ESZ89703.1; -; Genomic_DNA.
DR AlphaFoldDB; W9C1V3; -.
DR STRING; 1432307.W9C1V3; -.
DR HOGENOM; CLU_004652_0_0_1; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000019487; 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:UP000019487};
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 11..204
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 284..500
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 543..774
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 781..1019
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 218..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 644..646
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 651..657
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 746
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1074 AA; 119975 MW; F6DB7177E88D27DB CRC64;
MVGQRKAVDQ RIPALIRNGI QEKKRSFIVV VGDRTKDVIV HLHYIMSSMD MKQNKSVMWA
YKNKLLGFTS HRKKRETKIK KEIKRGIREA NTEDPFELFV SLHNIRYVYY KETEKILGNT
FGMCILQDFE ALTPNLLART IETVEGGGLV VLLLKGMNSL KQLYTMSMDV HSRYRTEAHD
DVTARFNERF ILSLGKCESC LVIDDELNVL PISGGKNVKA LPPPDLDEPK SESQKELDSM
KEALQDTQPV GSLVTLAKTV DQAKALLTFV DAIAEKTLRN TVTLTAGRGR GKSAALGVAV
AAAVAHGYSN IFITSPSPEN LKTLFEFIFK GFDALNYMDH VDYSIIQSTN PDFNKAIVRV
NIHRQHRQTI QYIRPQDAHV LGQAELLVID EAAAIPLPLV KKLMGPYLVF MASTINGYEG
TGRSLSLKLI KQLREQSRGT TNGTADVEVA DRSSGKAAAK GADNSFSGGR SLREITLSEP
IRYAQGDAVE KWLNQLLCLD ATLPRSRLNT LQGCPDPSQC QLLNVNRDTL FSFHDVSEKF
LQQMIALYVA SHYKNTPDDL QLMSDAPAHQ LFVLVPPIEE NSKHLPEPLC VIQVALEGKI
SKQSVMNSLS RGQRAAGDLI PWLVSQQFQD DDFAGLSGAR VVRIATNPDY IKMGYGSKAL
ELLTDFYEGK FANLSEDMND HVEETITRVT DEELTSISLL DDNIKVRDIR KMPPLFSKLS
EKRPDNLDYI GVSYGLTQPL HRFWKRASFV PLYLRQTPNE LTGEHTCVMV RTLEKSEDRE
WESAFSRDFH RRFLSLLSYQ FSEFPSILAL SIDESANAGS KSDPEAAPKP LSKSELDNLM
SPFDLKRLES YANNMLDYHV ILDLIPTLAN LYFTGRLKSD IKLTGIQSSI LLAVGLQRKD
LTAIESELSL PSSQLLAMFI KIMRKMSSHF GDLVSGAIEA EMPGRENIGV SRADANEALD
DEIVDDRFVP LEQGLEDELE EGGDEAMKAL KEKQRELIDA LPLDQYEIET GAPGWAEAEK
HVKHASKSGK KDIVVGVKSA KTKRKAGESA AEIYEQEMGE KTHKKAKKGS KKGQ
//