NSUN3_BOVIN
ID NSUN3_BOVIN Reviewed; 338 AA.
AC Q0P5D8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=tRNA (cytosine(34)-C(5))-methyltransferase, mitochondrial {ECO:0000250|UniProtKB:Q9H649};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H649};
DE AltName: Full=NOL1/NOP2/Sun domain family member 3 {ECO:0000250|UniProtKB:Q9H649};
GN Name=NSUN3 {ECO:0000250|UniProtKB:Q9H649};
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].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial tRNA methyltransferase that mediates
CC methylation of cytosine to 5-methylcytosine (m5C) at position 34 of mt-
CC tRNA(Met). mt-tRNA(Met) methylation at cytosine(34) takes place at the
CC wobble position of the anticodon and initiates the formation of 5-
CC formylcytosine (f(5)c) at this position. mt-tRNA(Met) containing the
CC f(5)c modification at the wobble position enables recognition of the
CC AUA codon in addition to the AUG codon, expanding codon recognition in
CC mitochondrial translation. {ECO:0000250|UniProtKB:Q9H649}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in mitochondrial tRNA + S-adenosyl-L-methionine =
CC 5-methylcytidine(34) in mitochondrial tRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:53076, Rhea:RHEA-COMP:13451, Rhea:RHEA-
CC COMP:13453, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q9H649};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53077;
CC Evidence={ECO:0000250|UniProtKB:Q9H649};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9H649}.
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; BC120181; AAI20182.1; -; mRNA.
DR RefSeq; NP_001069469.1; NM_001076001.2.
DR AlphaFoldDB; Q0P5D8; -.
DR SMR; Q0P5D8; -.
DR STRING; 9913.ENSBTAP00000020876; -.
DR PaxDb; Q0P5D8; -.
DR Ensembl; ENSBTAT00000020876; ENSBTAP00000020876; ENSBTAG00000015728.
DR GeneID; 533791; -.
DR KEGG; bta:533791; -.
DR CTD; 63899; -.
DR VEuPathDB; HostDB:ENSBTAG00000015728; -.
DR VGNC; VGNC:32286; NSUN3.
DR eggNOG; KOG2198; Eukaryota.
DR GeneTree; ENSGT00940000153665; -.
DR HOGENOM; CLU_041061_1_0_1; -.
DR InParanoid; Q0P5D8; -.
DR OMA; KAWGPMF; -.
DR OrthoDB; 1239772at2759; -.
DR TreeFam; TF321304; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000015728; Expressed in oocyte and 108 other tissues.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070129; P:regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR GO; GO:0002127; P:tRNA wobble base cytosine methylation; ISS:UniProtKB.
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 S-adenosyl-L-methionine; Transferase; tRNA-binding.
FT CHAIN 1..338
FT /note="tRNA (cytosine(34)-C(5))-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000289229"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 140..146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 338 AA; 38384 MW; AF20AF5295967D89 CRC64;
MVLTLLKAKP ERKLAKQICK VVLDHFEKQY SKELGDAWNT VRDILTSPSC WQYAVLLNRF
NYPFELEKDL HLKGYHSLLQ GSLPYYPKSM KCYLSRTPHR MPSERHQTGN LKKYYLLNAA
SLLPVLALEL RDGEKVLDLC AAPGGKSLAL LQCAYPGYLH CNEYDSLRLR WLRQTLESFI
PQPLVNVIKV SELDGREMGD AQPETFDKVL VDAPCSNDRS WLFSSDSQKA ACRISQRRNL
PLLQMELLRS AIKALRPGGL LVYSTCTLSK AENQDVISEV LNSYSNIMPV DIKEMARTCS
RDFTFAPTGQ ECGLLVIPDK GKAWGPMYVA KLKKSWTT
