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Database: UniProt
Entry: A0A3M9Y2T2_9PEZI
LinkDB: A0A3M9Y2T2_9PEZI
Original site: A0A3M9Y2T2_9PEZI 
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
//
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