ID A0A179GE16_PURLI Unreviewed; 1062 AA.
AC A0A179GE16;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=VFPBJ_08435 {ECO:0000313|EMBL:OAQ76075.1}, VFPFJ_09029
GN {ECO:0000313|EMBL:OAQ83226.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ76075.1, ECO:0000313|Proteomes:UP000078240};
RN [1] {ECO:0000313|EMBL:OAQ76075.1, ECO:0000313|Proteomes:UP000078240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLBJ-1 {ECO:0000313|EMBL:OAQ76075.1}, and PLFJ-1
RC {ECO:0000313|EMBL:OAQ83226.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (JAN-2016) 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:OAQ76075.1}.
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DR EMBL; LSBH01000007; OAQ76075.1; -; Genomic_DNA.
DR EMBL; LSBI01000008; OAQ83226.1; -; Genomic_DNA.
DR RefSeq; XP_018175854.1; XM_018326102.1.
DR AlphaFoldDB; A0A179GE16; -.
DR STRING; 33203.A0A179GE16; -.
DR GeneID; 28891151; -.
DR KEGG; plj:VFPFJ_09029; -.
DR OMA; HLHYIMS; -.
DR OrthoDB; 1119820at2759; -.
DR Proteomes; UP000078240; Unassembled WGS sequence.
DR Proteomes; UP000078340; 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:UP000078340};
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 9..202
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 282..495
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 537..768
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT DOMAIN 775..1012
FT /note="Possible tRNA binding"
FT /evidence="ECO:0000259|Pfam:PF13725"
FT REGION 1012..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 287..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 638..640
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 645..651
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
FT BINDING 740
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03211"
SQ SEQUENCE 1062 AA; 118762 MW; 5F259BFAC1BE5F6C CRC64;
MSRKQVDQRI QTLIRNGLQE KKRSFFVVVG DRSKDVIVHL HYIMSSMDIK QNKSVLWAYK
NKLLGFTSHR KKREQKIKKE IKRGIREANS EDPFELFVSL HNIRYTYYKE TDKILGNTFG
MCVLQDFEAL TPNILARTIE TVEGGGLVVM LLKGMNSLRQ LYNLSMDVHS RYRTEAHTDV
VARFNERFLL SLGRCESCLV IDDELNVLPI SGGKDVKALP PPDLDQPKTE QQIELDNIKD
DNQEREPVGS LISLARTVDQ AKALLTFTEA ISEKTLRSTV ALTAARGRGK SAAMGVAVAA
AVAYGYSNIF ITSPSPENLK TLFEFIFKGF DALGYADHAD YSIIQSTNPD FNKAIVRVNI
HRQHRQTIQY IRPQDAHVLG QAELVVIDEA AAIPLPLVRK LMGPYLVFMA STINGYEGTG
RSLSLKLIKQ LREQSRSASI ANGETELADR STGKAAKTEE YQAARKLREI TLSEPIRYAK
GDAVEKWLNK LLCLDATLPK AKANVHGCPD PSQCELLAVN RDTLFSFHPV SEAFLQQMVA
LYVASHYKNS PDDLQLMSDA PAHELFVLVP PNVEDTGKLP EPLCVIQVAL EGKISRQSVL
NSLSRGQRPH GDLIPWLVSQ QFQDEDFASL SGARVVRIAT NPEYVSMGYG TKALELLTDY
YEGRFASLSE DDDQVMEERM HRATDAELTK ASLLNEEITV RDQAHMPPLF AKLREKRPEA
LDYIGVSYGL TKPLHKFWKR SAFSPVYLRQ TANDLTGEHT CVMLRPLENS QDRTWLGAFS
RDFQKRFLSL LSYQFRTFTT AEALSIDESA NAGAKLDAVE AAAMDKFELD RNFSPFDLKR
LESYANNMLD YHVILDMMPV IANLYFSGKL KGDIKLTGLQ QCILLGIGLQ RKDIDVIGKE
LDVQTSQLLA MFIKILRKVT AHFGTLVSAA VDAEMPKPEK IGVSRADASG AHDDEVVDER
FAPLSTSLDD ELEEGGDEAL KALRQKQREL IDSLPLDQFE IEGDAPAWAE AEKQVKSGKS
NTVVSVKSGK QKRKAGPTAA EVYEEAMGEK SRKKAKKGKK SA
//
