NAT10_SCHPO
ID NAT10_SCHPO Reviewed; 1033 AA.
AC P87115;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=RNA cytidine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000303|PubMed:25402480};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03211};
DE AltName: Full=18S rRNA cytosine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03211};
GN Name=nat10 {ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000303|PubMed:25402480};
GN ORFNames=SPAC20G8.09c {ECO:0000312|PomBase:SPAC20G8.09c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-285.
RX PubMed=25402480; DOI=10.1371/journal.pone.0112156;
RA Taoka M., Ishikawa D., Nobe Y., Ishikawa H., Yamauchi Y., Terukina G.,
RA Nakayama H., Hirota K., Takahashi N., Isobe T.;
RT "RNA cytidine acetyltransferase of small-subunit ribosomal RNA:
RT identification of acetylation sites and the responsible acetyltransferase
RT in fission yeast, Schizosaccharomyces pombe.";
RL PLoS ONE 9:E112156-E112156(2014).
CC -!- FUNCTION: RNA cytidine acetyltransferase with specificity toward both
CC 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine
CC (ac4C) at positions 1297 and 1815 in 18S rRNA. Required for early
CC nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S
CC rRNA synthesis (PubMed:25402480). Catalyzes the formation of ac4C in
CC serine and leucine tRNAs. Requires the tRNA-binding adapter protein
CC tan1 for full tRNA acetyltransferase activity but not for 18S rRNA
CC acetylation (By similarity). {ECO:0000250|UniProtKB:P53914,
CC ECO:0000255|HAMAP-Rule:MF_03211, ECO:0000269|PubMed:25402480}.
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:0000255|HAMAP-Rule:MF_03211,
CC ECO:0000269|PubMed:25402480};
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:0000255|HAMAP-Rule:MF_03211};
CC -!- SUBUNIT: Interacts with tan1. {ECO:0000255|HAMAP-Rule:MF_03211}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03211, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03211}.
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DR EMBL; CU329670; CAB08603.1; -; Genomic_DNA.
DR PIR; T38131; T38131.
DR RefSeq; NP_593326.1; NM_001018757.2.
DR AlphaFoldDB; P87115; -.
DR SMR; P87115; -.
DR BioGRID; 278978; 14.
DR STRING; 4896.SPAC20G8.09c.1; -.
DR iPTMnet; P87115; -.
DR SwissPalm; P87115; -.
DR MaxQB; P87115; -.
DR PaxDb; P87115; -.
DR PRIDE; P87115; -.
DR EnsemblFungi; SPAC20G8.09c.1; SPAC20G8.09c.1:pep; SPAC20G8.09c.
DR GeneID; 2542520; -.
DR KEGG; spo:SPAC20G8.09c; -.
DR PomBase; SPAC20G8.09c; nat10.
DR VEuPathDB; FungiDB:SPAC20G8.09c; -.
DR eggNOG; KOG2036; Eukaryota.
DR HOGENOM; CLU_004652_0_0_1; -.
DR InParanoid; P87115; -.
DR OMA; QDEEFAG; -.
DR PhylomeDB; P87115; -.
DR PRO; PR:P87115; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030686; C:90S preribosome; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:1990883; F:rRNA cytidine N-acetyltransferase activity; IMP:PomBase.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0051392; F:tRNA N-acetyltransferase activity; TAS:PomBase.
DR GO; GO:1904812; P:rRNA acetylation involved in maturation of SSU-rRNA; IMP:PomBase.
DR GO; GO:0051391; P:tRNA acetylation; TAS:PomBase.
DR Gene3D; 3.40.50.300; -; 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; PTHR10925; 1.
DR Pfam; PF08351; DUF1726; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 1.
DR Pfam; PF05127; Helicase_RecD; 1.
DR Pfam; PF13725; tRNA_bind_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; ATP-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; rRNA processing; Transferase; tRNA processing.
FT CHAIN 1..1033
FT /note="RNA cytidine acetyltransferase"
FT /id="PRO_0000215889"
FT DOMAIN 560..694
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT REGION 988..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 465
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 626..628
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 633..639
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT BINDING 727
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03211"
FT MUTAGEN 285
FT /note="G->D: Completely lacks 18S rRNA acetylation and
FT produces only trace amounts of the 40S small ribosomal
FT subunit."
FT /evidence="ECO:0000269|PubMed:25402480"
SQ SEQUENCE 1033 AA; 116463 MW; 8432B313D818E135 CRC64;
MPKKALDSRI PTLIKNGCQE KQRSFFVVVG DRARDQVVNL HWLLSQSKVA ARPNVLWMYK
KDLLGFTSHR KKRENKIKKE IKRGIRDPNS EDPFELFCSI TNIRYCYYKE SEKILGQTYG
MLVLQDFEAL TPNLLARTIE TVEGGGIVVL LLHKLNSLKQ LYTMSMDIHS RYRTEAHSDV
TARFNERFIL SLGNCENCLV IDDELNVLPI SGGKNVKALP PTLEEDNSTQ NSIKELQESL
GEDHPAGALV GVTKTLDQAR AVLTFVESIV EKSLKGTVSL TAGRGRGKSA ALGLAIAAAI
AHGYSNIFIT SPSPENLKTL FEFIFKGFDA LNYEEHVDYD IIQSTNPAYH NAIVRVNIFR
DHRQTIQYIS PEDSNVLGQA ELVVIDEAAA IPLPLVRKLI GPYLVFMAST INGYEGTGRS
LSLKLLQQLR EQSRIYSGSG NNKSDSQSHI SGRTLKEISL DEPIRYAMGD RIELWLNKLL
CLDAASYVSR MATQGFPHPS ECSLYRVSRD TLFSYHPISE AFLQRMMSLY VASHYKNSPN
DLQLMSDAPA HQLFVLLPPV DLKNPKLPDP ICVIQLALEG SISRESIMNS LSRGQRAGGD
LIPWLISQQF QDENFAALGG ARIVRIAVSP EHVKMGYGTR AMQLLHEYFE GKFISASEEF
KAVKHSLKRI GDEEIENTAL QTEKIHVRDA KTMPPLLLKL SELQPEPLHY VGVSYGLTPS
LQKFWKREGY CPLYLRQTAN DLTGEHTCVM LRVLEGRDSE WLGAFAQNFY RRFLSLLGYQ
FREFAAITAL SVLDACNNGT KYVVNSTSKL TNEEINNVFE SYDLKRLESY SNNLLDYHVI
VDLLPKLAHL YFSGKFPDSV KLSPVQQSVL LALGLQYKTI DTLEKEFNLP SNQLLAMLVK
LSKKIMKCID EIETKDIEEE LGSNKKTESS NSKLPEFTPL QQSLEEELQE GADEAMLALR
EKQRELINAI DLEKYAIRGN EEDWKAAENQ IQKTNGKGAR VVSIKGEKRK NNSLDASDKK
TKEKPSSKKK FRK
