ID   MET15_PONAB             Reviewed;         407 AA.
AC   Q5R5T5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860768; CAH92881.1; -; mRNA.
DR   RefSeq; NP_001126687.1; NM_001133215.1.
DR   AlphaFoldDB; Q5R5T5; -.
DR   SMR; Q5R5T5; -.
DR   STRING; 9601.ENSPPYP00000003901; -.
DR   GeneID; 100173687; -.
DR   KEGG; pon:100173687; -.
DR   CTD; 196074; -.
DR   eggNOG; KOG2782; Eukaryota.
DR   InParanoid; Q5R5T5; -.
DR   OrthoDB; 809593at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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_0000308334"
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;  46169 MW;  0193F86F265780B7 CRC64;
     MIRYPYFCRM YKECLSCWLE SGIPNLGVWP KTIHTTAEKY REYEAREQTD QTQAQELHRS
     QDRDFETMAK LHIPVMVDEV LHCLSPQKGQ IFLDMTFGSG GHTKAILQKE SDIVLYALDR
     DPTAYALAEH LSELYPKQIR AMLGQFSQAE TLLMKAGVQP GTFDGVLMDL GCSSMQLDTP
     ERGFSLRKDG PLDMRMDGGR YPDMPTAADV VNAFDQQALA SILRTYGEEK HAKKIASAIV
     QARSIYPITR TQQLASIVAG AFPPSAIYAR KDLLQRSTHI ATKTFQAVRI FVNNELNELY
     MGLKTAQKFL RPGGRLVALS FHSLEDRIIK RFLLGISMTE RFNLSVRQQV MKTSQLGSDH
     ENTEEVSKRR APLMWELIHK KVLSPQDQDV QDNPRARSAK LRAAIKL