ID   NSUN4_XENLA             Reviewed;         406 AA.
AC   Q5M7E3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC088687; AAH88687.1; -; mRNA.
DR   RefSeq; NP_001088881.1; NM_001095412.1.
DR   AlphaFoldDB; Q5M7E3; -.
DR   SMR; Q5M7E3; -.
DR   DNASU; 496225; -.
DR   GeneID; 496225; -.
DR   KEGG; xla:496225; -.
DR   CTD; 496225; -.
DR   Xenbase; XB-GENE-948194; nsun4.S.
DR   OrthoDB; 1239772at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 496225; Expressed in testis and 20 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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_0000289236"
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;  46061 MW;  353B25B23B980783 CRC64;
     MSACRGFLLR RINDSCLTFR RHKFKKKWAT TLPKIPCSRL ALQYFDINYS MQFGDLWPSI
     RISLLTEQKY GALVNNFSHK ETVLNNLSAL KAKDFISEAQ SVISLLQTQN NVDTSEKMVF
     TEVPLNLVGE KNDAEQTQAT NLLSSLSNSK LTCFTFSRGD ISRFPQSRSD CFGLLEYYLM
     DAASLLPVLA LDIQHGHSVL DLCAAPGGKT LALLQTENCQ YLAANDLSTS RSSRLHRVLH
     SYVPRDQRAE HKVRITSWDG RLWGDLEAST YDRVLVDVPC TTDRHSLLEE ENNIFHRIRT
     KQRQMLPLLQ TELLVSGLRA VRPGGEVVYS TCSLSQLQNE CVVQRAIELA ATDHGVLVKP
     QDLSCFREVF KNTFNFFQDC RVGELVVPHL TANFGPMFFC KLLRIK