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Database: UniProt
Entry: W9C1V3_SCLBF
LinkDB: W9C1V3_SCLBF
Original site: W9C1V3_SCLBF 
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
//
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