ID   NSUN4_XENTR             Reviewed;         406 AA.
AC   Q66KI9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=5-methylcytosine rRNA methyltransferase NSUN4;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q95XR2};
DE   AltName: Full=5-methylcytosine tRNA methyltransferase NSUN4 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q95XR2};
DE   AltName: Full=NOL1/NOP2/Sun domain family member 4;
GN   Name=nsun4; ORFNames=TGas136a10.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in mitochondrial ribosome large subunit biogenesis.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in rRNA + S-adenosyl-L-methionine = a 5-
CC         methylcytidine in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:61484, Rhea:RHEA-COMP:15836, Rhea:RHEA-COMP:15837,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC         Evidence={ECO:0000250|UniProtKB:Q95XR2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in tRNA + S-adenosyl-L-methionine = a 5-
CC         methylcytidine in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:61468, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:15827,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC         Evidence={ECO:0000250|UniProtKB:Q95XR2};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CR848182; CAJ83825.1; -; mRNA.
DR   EMBL; BC080376; AAH80376.1; -; mRNA.
DR   RefSeq; NP_001007930.1; NM_001007929.1.
DR   AlphaFoldDB; Q66KI9; -.
DR   SMR; Q66KI9; -.
DR   PaxDb; Q66KI9; -.
DR   DNASU; 100493736; -.
DR   Ensembl; ENSXETT00000052934; ENSXETP00000052934; ENSXETG00000024501.
DR   GeneID; 100493736; -.
DR   KEGG; xtr:100493736; -.
DR   CTD; 387338; -.
DR   Xenbase; XB-GENE-948188; nsun4.
DR   eggNOG; KOG2198; Eukaryota.
DR   InParanoid; Q66KI9; -.
DR   OrthoDB; 1239772at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000024501; Expressed in 2-cell stage embryo and 15 other tissues.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR   GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; PTHR22808; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Mitochondrion; Reference proteome; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..406
FT                   /note="5-methylcytosine rRNA methyltransferase NSUN4"
FT                   /id="PRO_0000289237"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         203..209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         259
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         277
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   406 AA;  45829 MW;  AA3D7A53F294A2BD CRC64;
     MAACRGFLLR RINDSCLTFR RHKFKKKWAT TLPKIPCSRL ALQYFDMNYS MQFGDLWPSI
     RISLLTEQKY GALVNNFSHK ETVLKNLSAF NAKDFISEAQ HVISLLQIQN NLDTSEKMTS
     GEASLNLVGQ KNNAEKTQAT NLLSSLSNTK LTCFKFSRGD ISRFPQSRSD SFGLLEYYLM
     DAASLLPVLA LDVQHGHSVL DLCAAPGGKT LALLQTENCQ YLAANDLSTS RSSRLHRVLR
     SYVPRAQRTE HKVCITSQDG RLWGDAEANT YDRVLVDVPC TTDRHSLLEE ENNIFHRIRT
     KQRQMLPLLQ AELLVAGLRA VRPGGEVVYS TCSLSQLQNE CVVERAVELA ASDHGVHVKP
     QDLSCFREVF KNTFNFFQGC RVGELVLPHL TANFGPMFFC KLLRIE