MRM3B_DANRE
ID MRM3B_DANRE Reviewed; 445 AA.
AC A1L2E4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=rRNA methyltransferase 3B, mitochondrial {ECO:0000250|UniProtKB:Q9HC36};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=RNA methyltransferase-like protein 1B {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=rRNA (guanosine-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q9HC36};
DE Flags: Precursor;
GN Name=rnmtl1b {ECO:0000250|UniProtKB:Q9HC36};
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=Testis;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI29485.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC129484; AAI29485.1; ALT_INIT; mRNA.
DR AlphaFoldDB; A1L2E4; -.
DR SMR; A1L2E4; -.
DR STRING; 7955.ENSDARP00000091013; -.
DR PaxDb; A1L2E4; -.
DR PeptideAtlas; A1L2E4; -.
DR ZFIN; ZDB-GENE-030131-158; mrm3b.
DR eggNOG; KOG2506; Eukaryota.
DR InParanoid; A1L2E4; -.
DR PhylomeDB; A1L2E4; -.
DR PRO; PR:A1L2E4; -.
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..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..445
FT /note="rRNA methyltransferase 3B, mitochondrial"
FT /id="PRO_0000311304"
FT REGION 52..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 387
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 445 AA; 49495 MW; DC62A5B8C74F6BE2 CRC64;
MATRIASMRF RCALFQSALT LGRNEVNIKR YVRRRRAVSG VVSVNEPTEI SEGVISQTSE
RSSQHNNDIT RNTDKSSIEN PVSPNNSQPV QFSHINRQKV INLTSRTRFG EVDGLLYEKL
HPGDKSLAKL ARIAGSKKLR EHQVVLEGKH LVCSALDAGA EAQTLYFSSV DALRELPLDK
LRQTNVVKVK MEDAQVWSEL DTSQEIIAIF KRPEASRLTF SEEKYGRAVP LTLICDTVRD
PGNLGSVLRS AAAAGCHSVL LTKGCVDIWE LKVLRAAMGA HFRLPIIPNL TWTDISNHLP
KTSTVHVADN HSTTMGKHND NTTPQKHRRP SDYGWVKGHQ YQSKAHDDDD ANDLCSLEDY
CDENSKSLET QLYYTDWVAG HTSLIIGGET HGLSREALQL AERTSGRRLL IPMVDGVDSL
NSAIAAGVLL FEGRKQLLSL EKIRV
