ID   MRM3_XENTR              Reviewed;         415 AA.
AC   A4QNL8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) 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; BC135861; AAI35862.1; -; mRNA.
DR   AlphaFoldDB; A4QNL8; -.
DR   SMR; A4QNL8; -.
DR   STRING; 8364.ENSXETP00000048602; -.
DR   PaxDb; A4QNL8; -.
DR   Ensembl; ENSXETT00000048602; ENSXETP00000048602; ENSXETG00000022451.
DR   eggNOG; KOG2506; Eukaryota.
DR   HOGENOM; CLU_021322_1_0_1; -.
DR   InParanoid; A4QNL8; -.
DR   OMA; FAKPDHE; -.
DR   TreeFam; TF323420; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000022451; Expressed in egg cell and 15 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..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..415
FT                   /note="rRNA methyltransferase 3, mitochondrial"
FT                   /id="PRO_0000311306"
FT   REGION          41..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Polar 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   415 AA;  46212 MW;  B1F74A6F19D309B4 CRC64;
     MAALCRGTVR ACILKPLGLS VSLQVKRNVR ALRRTPVRVL PAAEKGRERK EVEARRPQQP
     RQSEYQTRTS QGVRQASALT EAPALEFRYE RALPGDKRLS KVVTIAKSKK FRDRHGQVLL
     EGRRLLTDAL ESGAVLQTLF FSRVDYLKLF PPDKLRKANL IKVNFDNIKI WSDVVAPQGL
     MGIFAKPDHE KISYPTTQTK HTLPLSLICD NIRDPGNLGT ILRCAAGAGC NKVLLTKGCV
     DAWEPKVLRA GMGAHFRLPV ISSLDWDIVP NYLSAGTKVF LADNFRPDMK HKTGDVSEKA
     SDYGWVSTNP RRILITEEGY ESSSDEEDNA DKLYIPGLEV QSYFESWAQS PCAIVIGGET
     HGLSIESLLL AEKSNGKRLY IPVVPDIDSL NSAMAASILL FEGKRQIENT MKRKS