ID A0A3M9Y2T2_9PEZI Unreviewed; 1065 AA.
AC A0A3M9Y2T2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=KRE33 {ECO:0000313|EMBL:RNJ54362.1};
GN Synonyms=NAT10 {ECO:0000256|HAMAP-Rule:MF_03211};
GN ORFNames=D7B24_000538 {ECO:0000313|EMBL:RNJ54362.1};
OS Verticillium nonalfalfae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ54362.1, ECO:0000313|Proteomes:UP000267145};
RN [1] {ECO:0000313|EMBL:RNJ54362.1, ECO:0000313|Proteomes:UP000267145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ54362.1,
RC ECO:0000313|Proteomes:UP000267145};
RA Stajich J.E., Kasson M.T.;
RT "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL Submitted (OCT-2018) 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:RNJ54362.1}.
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DR EMBL; RBVV01000107; RNJ54362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9Y2T2; -.
DR STRING; 1051616.A0A3M9Y2T2; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000267145; 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 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..499
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 541..771
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 778..1015
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 436..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1054
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 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 642..644
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 649..655
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 743
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1065 AA; 118888 MW; C2493FBE3DFE034C CRC64;
MSQKQKQVDS RIPALIRNGL QEKKRSFFVV VGDRGKDIIV NLHHIMSQME LKQNKSVLWA
YKSKLLNFTS HRQKRENKIK KEVKRGIREA NDMDPFEAFV TLHNIRYVYY KETEKVLGNT
FGMCVLQDFE ALTPNILAKT METVEGGGLV ILLLKGMNSL KQLYNLSMDV HNRYRTEAHD
DVVARFNERF ILSLGGCDSC LVIDDEMNVL PISGGKNVAA LPPPDLDQPV SETQKELDGM
KESLQDTQPV GSLVTLAKTV DQAKALLTFV DAIAEKTLRS TVTLTAARGR GKSAAMGVAV
AAAVAHGYSN IFITSPSPEN LKTLFEFIFK GFDALGYADH ADYSIIQSTN PDFNKAIVRV
NIHRQHRQTI QYIRPQDAHV LGQAELVVID EAAAIPLPLV RKLMGPYLVF MASTINGYEG
TGRSLSLKLI KQLREQSRPG AASNGDTTVA DRSTGRASKE QSSGFQASRS LREITLSEPI
RYAKGDSVEK WLNTLLCLDA TLPRAKVSGQ GCPDPSQCEL LQVNRDTLFS FHPVSEKFLQ
QMVALYVASH YKNSPDDLQL MSDAPAHELY VLVPPVSEEN QRLPEPLCVI QVSLEGKISR
QSVLNSLSRG QRPSGDLIPW LVSQQFQDED FASLSGARVV RIATNPEYMG MGYGSKALQL
LTDFYEGKFT SLNEEDIVME DTITRVTDEE LENANLLEDN IKIRDINKMP PLFAKLSEKK
PELLDYIGVS YGLTQELHKF WKRATFAPVY LRQTANDLTG EHTCVMLRPL ENGGDRSWVG
AFSRDFHKRF LSLLSYQFRS FSAVMALSID ESANLGAKLD EQEPAPLNKT DLDRLVSPFD
LKRLESYANN MLDYHVILDL IPTISNLYFT GRLKSDIRLT GVQQAILLAI GEQRKDLDVI
STELSLPSQQ LLAMFIKILR KVTAHFTALV SKAVEAELPQ SKSLGVSREN ATGVHDDEVI
DQRFQPLETT LDDELEEGGD EVLQTLRKKQ RELIDSLPLD EYEIEGDTPA WQEAEAQVAK
GPASTVVSVK SKSKRKAGQT AAEVYDEAVG EKSRKKAKKG GKRDR
//