MRM3A_DANRE
ID MRM3A_DANRE Reviewed; 435 AA.
AC Q566V3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=rRNA methyltransferase 3A, mitochondrial {ECO:0000250|UniProtKB:Q9HC36};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=RNA methyltransferase-like protein 1A {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=rRNA (guanosine-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q9HC36};
DE Flags: Precursor;
GN Name=mrm3a; Synonyms=rnmtl1a; ORFNames=zgc:112452;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP POSITION OF MODIFIED METHYLGUANOSINE IN MTLSU RRNA.
RX PubMed=25009282; DOI=10.1091/mbc.e14-01-0014;
RA Rorbach J., Boesch P., Gammage P.A., Nicholls T.J., Pearce S.F., Patel D.,
RA Hauser A., Perocchi F., Minczuk M.;
RT "MRM2 and MRM3 are involved in biogenesis of the large subunit of the
RT mitochondrial ribosome.";
RL Mol. Biol. Cell 25:2542-2555(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of 2'-O-methylguanosine
CC at position 1485 (Gm1485) in the mitochondrial large subunit ribosomal
CC RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase
CC domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:Q9HC36,
CC ECO:0000305|PubMed:25009282}.
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; BC093318; AAH93318.1; -; mRNA.
DR AlphaFoldDB; Q566V3; -.
DR SMR; Q566V3; -.
DR STRING; 7955.ENSDARP00000119941; -.
DR PaxDb; Q566V3; -.
DR ZFIN; ZDB-GENE-050417-184; mrm3a.
DR eggNOG; KOG2506; Eukaryota.
DR InParanoid; Q566V3; -.
DR PhylomeDB; Q566V3; -.
DR PRO; PR:Q566V3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..435
FT /note="rRNA methyltransferase 3A, mitochondrial"
FT /id="PRO_0000311303"
FT REGION 314..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 48590 MW; 7BC99DA5F4132823 CRC64;
MAALMYNVSR GLVMLGERSL FQRERYQILV NSRRFLRGLR RRPVAVLYPD GERETLIKSK
RATDITSQGF TQKGKARKDV TERAAYKNCS GFVSERAEES SQINKLKLAG LRFEKAPAGD
NRLARVSSVA RSRAFRDKEG KVLLEGRRLI CDALSAGASP QMIFFSLLER LQELPLDKLQ
QAKLIKVKYE DIKLWSDLVT PQGLIAIFSK PDASRLTFPK DARLQSVPLF LICDNVRDAG
NLGTILRCAA AAGGDRVLLS KGCVDAWEPK VLRSAMGAHF RLPVFPNLDW DDISKHLPKN
VIVHVADNYS TSTKQLVSGQ TENVSSDDYS ESDSDDDDDE EEDEDSLPHV KPQVYHECWA
QRSAALVIGG ETHGLSVEAL RLAEETDGKR LFVPMAPGVE SLNSAMAAGI LLFEGRRQLL
MLSDKLRRRA RTKML
