NSUN4_BOVIN
ID NSUN4_BOVIN Reviewed; 384 AA.
AC Q0V8R7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 81.
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;
DE Flags: Precursor;
GN Name=NSUN4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Involved in mitochondrial ribosome assembly. 5-methylcytosine
CC rRNA methyltransferase that probably is involved in mitochondrial
CC ribosome small subunit (SSU) maturation by methylation of mitochondrial
CC 12S rRNA; the function is independent of MTERFD2/MTERF4 and assembled
CC mitochondrial ribosome large subunit (LSU). Targeted to LSU by
CC MTERFD2/MTERF4 and probably is involved in a final step in ribosome
CC biogenesis to ensure that SSU and LSU are assembled. In vitro can
CC methylate 16S rRNA of the LSU; the methylation is enhanced by
CC MTERFD/MTERF4 (By similarity). {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 -!- SUBUNIT: Heterodimer with MTERF4/MTERFD2; this interaction may be
CC required for NSUN4 recruitment to the mitochondrial large ribosomal
CC subunit. {ECO:0000250}.
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; BT026151; ABG66990.1; -; mRNA.
DR EMBL; DY454541; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001178310.1; NM_001191381.1.
DR AlphaFoldDB; Q0V8R7; -.
DR SMR; Q0V8R7; -.
DR STRING; 9913.ENSBTAP00000021120; -.
DR PaxDb; Q0V8R7; -.
DR Ensembl; ENSBTAT00000021120; ENSBTAP00000021120; ENSBTAG00000015891.
DR GeneID; 618779; -.
DR KEGG; bta:618779; -.
DR CTD; 387338; -.
DR VEuPathDB; HostDB:ENSBTAG00000015891; -.
DR VGNC; VGNC:55638; NSUN4.
DR eggNOG; KOG2198; Eukaryota.
DR GeneTree; ENSGT00940000153665; -.
DR HOGENOM; CLU_041061_2_0_1; -.
DR InParanoid; Q0V8R7; -.
DR OMA; FCKMCRL; -.
DR OrthoDB; 1239772at2759; -.
DR TreeFam; TF321304; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000015891; Expressed in semen and 105 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:0019843; F:rRNA 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; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing; rRNA-binding;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..384
FT /note="5-methylcytosine rRNA methyltransferase NSUN4"
FT /id="PRO_0000289233"
FT ACT_SITE 310
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 181..187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CB9"
FT CONFLICT 12..13
FT /note="ML -> IP (in Ref. 1; DY454541)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="L -> P (in Ref. 1; DY454541)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="L -> P (in Ref. 1; DY454541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 43199 MW; C457DAD9CDED2BD3 CRC64;
MAALVVRGVR DMLKRADFAT VPRRQRHKKK WASTEPKFPA TRLALQNFDM TYSVQFGDLW
PSIRVSLLSE QKYGALVNNF AAGDRVSAEL EQLKARDFVN EAVFHREPEP ENSQTAAPSP
ASWACSPNLR CFTFTRGDVS RFPPARLGSL GLMDYYLMDA ASLLPVLALG LQPGDTVLDL
CAAPGGKTLA LLQTGCCRNL AANDLSTSRT SRLQRVLHSY VPQDVRDKNR VRVTSWDGRK
WGELEGDTYD RVLVDVPCTT DRHSLHEEEN SIFQRSRKKE RQMLPVLQVQ LLAAGLLATK
PGGHIVYSTC SLSHLQNEYV VQGAIELLDN QYSIKVQVED LTHFRKLFMN TFSFFPSCQV
GELVIPNLMA NFGPMYFCKM CRMT
