ID   MRM3_XENLA              Reviewed;         419 AA.
AC   Q6GPJ4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=rRNA methyltransferase 3, mitochondrial {ECO:0000250|UniProtKB:Q9HC36};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q9HC36};
DE   AltName: Full=RNA methyltransferase-like protein 1 {ECO:0000250|UniProtKB:Q9HC36};
DE   AltName: Full=rRNA (guanosine-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q9HC36};
DE   Flags: Precursor;
GN   Name=mrm3 {ECO:0000250|UniProtKB:Q9HC36};
GN   Synonyms=rnmtl1 {ECO:0000250|UniProtKB:Q9HC36};
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=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC       methyltransferase that catalyzes the formation of a 2'-O-
CC       methylguanosine at position 1370 (Gm1370) in the mitochondrial large
CC       subunit ribosomal RNA (mtLSU rRNA), a conserved modification in the
CC       peptidyl transferase domain of the mtLSU rRNA.
CC       {ECO:0000250|UniProtKB:Q9HC36}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC         methyluridine in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:54152, Rhea:RHEA-COMP:13812, Rhea:RHEA-COMP:13814,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74478;
CC         Evidence={ECO:0000250|UniProtKB:Q9HC36};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9HC36}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR   EMBL; BC073125; AAH73125.1; -; mRNA.
DR   RefSeq; NP_001085673.1; NM_001092204.1.
DR   AlphaFoldDB; Q6GPJ4; -.
DR   SMR; Q6GPJ4; -.
DR   PRIDE; Q6GPJ4; -.
DR   DNASU; 444099; -.
DR   GeneID; 444099; -.
DR   KEGG; xla:444099; -.
DR   CTD; 444099; -.
DR   Xenbase; XB-GENE-951940; mrm3.L.
DR   OMA; ERKRAPG; -.
DR   OrthoDB; 1183644at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 444099; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR013123; SpoU_subst-bd.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase; Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..419
FT                   /note="rRNA methyltransferase 3, mitochondrial"
FT                   /id="PRO_0000311305"
FT   REGION          42..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         357
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   419 AA;  46440 MW;  800DA46E9CAFC92F CRC64;
     MAALCGGMLR GCILKPLGLS GSLQLKRNVR ALRRTPVRVI QADEEGRERK QVEASRQRQP
     RQNESQACKA VGVSPATVDI EAPAHEFRYE RALPGDKRLS KVVTIAKSKK FRDRHGQVLL
     EGQRLLTDAL DSGAVLQTLF FSRVDYLKEF PPDKLRKTNL IKVNFENIKI WSDLVTPQGL
     MGIFAKPDHV KMTYPDTQTK HTLPLSLICD NIRDPGNLGT ILRCAAGAGC SKVLLTKGCV
     DAWEPKVLRA GMGAHFRLPI ITSLDWDIVP NYLPAGTKVF LADNFRPDNQ NKPAEVSEKA
     SDYGWVATDP KRIFITEDGY ESSSDEEDNT DKLYIPGLEV QSYFERWAQG PCAVVIGGET
     HGLSIESLLL AEKSNGKRLN IPVVPGIDSL NSAMAASILL FEGKRQIENT MKRKSCVTE