MET15_BOVIN
ID MET15_BOVIN Reviewed; 407 AA.
AC A0JN95;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=12S rRNA N4-methylcytidine methyltransferase;
DE Short=12S rRNA m4C methyltransferase;
DE EC=2.1.1.-;
DE AltName: Full=Methyltransferase 5 domain-containing protein 1;
DE AltName: Full=Methyltransferase-like protein 15;
DE Flags: Precursor;
GN Name=METTL15; Synonyms=METT5D1;
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=Placenta;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: N4-methylcytidine (m4C) methyltransferase responsible for the
CC methylation of position C839 in mitochondrial 12S rRNA. Involved in the
CC stabilization of 12S rRNA folding, therefore facilitating the assembly
CC of the mitochondrial small ribosomal subunits.
CC {ECO:0000250|UniProtKB:A6NJ78}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(839) in 12S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(4)-methylcytidine(839) in 12S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:62524, Rhea:RHEA-COMP:16109, Rhea:RHEA-COMP:16110,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74506, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:A6NJ78};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62525;
CC Evidence={ECO:0000250|UniProtKB:A6NJ78};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:A6NJ78}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000305}.
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DR EMBL; BC126575; AAI26576.1; -; mRNA.
DR RefSeq; NP_001073250.1; NM_001079782.2.
DR RefSeq; XP_005216340.1; XM_005216283.3.
DR RefSeq; XP_005216342.1; XM_005216285.3.
DR RefSeq; XP_010811027.1; XM_010812725.2.
DR AlphaFoldDB; A0JN95; -.
DR SMR; A0JN95; -.
DR STRING; 9913.ENSBTAP00000042150; -.
DR PaxDb; A0JN95; -.
DR PRIDE; A0JN95; -.
DR Ensembl; ENSBTAT00000044672; ENSBTAP00000042150; ENSBTAG00000003361.
DR GeneID; 533987; -.
DR KEGG; bta:533987; -.
DR CTD; 196074; -.
DR VEuPathDB; HostDB:ENSBTAG00000003361; -.
DR VGNC; VGNC:54885; METTL15.
DR eggNOG; KOG2782; Eukaryota.
DR GeneTree; ENSGT00390000014756; -.
DR HOGENOM; CLU_038422_1_0_1; -.
DR InParanoid; A0JN95; -.
DR OMA; NPAKRTF; -.
DR OrthoDB; 809593at2759; -.
DR TreeFam; TF106425; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000003361; Expressed in cardiac ventricle and 104 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 1.10.150.170; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1.
DR InterPro; IPR002903; RsmH.
DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11265; PTHR11265; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF81799; SSF81799; 1.
DR TIGRFAMs; TIGR00006; TIGR00006; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Mitochondrion; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..407
FT /note="12S rRNA N4-methylcytidine methyltransferase"
FT /id="PRO_0000308331"
FT REGION 44..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9WZX6"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NJ78"
SQ SEQUENCE 407 AA; 45768 MW; 2EDDB045E7FC8DC7 CRC64;
MLRYPYFCRI HKNFLSCWLE SGIYNLGVWP KKIHATAERY NEYEAQEETD QTGIQELHRS
QDRDSGVMTK LHIPVMVDEV VRCLAPQKGQ VFLDMTFGSG GHTRAILQKE PDITLYALDR
DPTAYAIAEQ LSELYPKQIR AILGQFSQAE ALLMKAGVQP GTLDGVLLDL GCSSMQLDTP
ERGFSLRKDG PLDMRMDGDR YPDMPTAADV VNALDQQALA SILRAYGEEK HAKKIASAII
QARGLYPITR TQQLASIVAG AFPPSALYAR KDLLQRPTHI ATKTFQAFRI FVNNELNELY
TGLKTAQKFL RPGGHLVALS FHSLEDRIIK RFLLGISMTE RFNLSARQKV IQKSQLDSDQ
ENKEGVSTGK APLMWKLIHK KVLTPEDEDV QDNPRGRSAK LRAAIKL
