ID   MRM1_LACK1              Reviewed;         138 AA.
AC   Q02997;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=rRNA methyltransferase 1, mitochondrial {ECO:0000250|UniProtKB:P25270};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:P25270};
DE   AltName: Full=21S rRNA (guanosine-2'O)-methyltransferase {ECO:0000250|UniProtKB:P25270};
DE   AltName: Full=Mitochondrial large ribosomal RNA ribose methylase {ECO:0000250|UniProtKB:P25270};
DE   Flags: Precursor; Fragment;
GN   Name=MRM1 {ECO:0000250|UniProtKB:P25270};
GN   Synonyms=PET56 {ECO:0000312|EMBL:CAA78498.1};
OS   Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS   JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=226302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC   / NRRL Y-12651;
RX   PubMed=8511965; DOI=10.1002/yea.320090405;
RA   Weinstock K.G., Strathern J.N.;
RT   "Molecular genetics in Saccharomyces kluyveri: the HIS3 homolog and its use
RT   as a selectable marker gene in S. kluyveri and Saccharomyces cerevisiae.";
RL   Yeast 9:351-361(1993).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC       methyltransferase that catalyzes the formation of the 2'-O-
CC       methylguanosine corresponding to position 2270 in S.cerevisiae 21S
CC       mitochondrial large ribosomal RNA, a universally conserved modification
CC       in the peptidyl transferase domain of the 21S rRNA.
CC       {ECO:0000250|UniProtKB:P25270}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a guanosine in 21S rRNA + S-adenosyl-L-methionine = a 2'-O-
CC         methylguanosine in 21S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:47772, Rhea:RHEA-COMP:11907, Rhea:RHEA-COMP:11908,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74445;
CC         Evidence={ECO:0000250|UniProtKB:P25270};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P25270}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z14125; CAA78498.1; -; Genomic_DNA.
DR   PIR; S31234; S31234.
DR   AlphaFoldDB; Q02997; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Methyltransferase; Mitochondrion; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..>138
FT                   /note="rRNA methyltransferase 1, mitochondrial"
FT                   /id="PRO_0000058320"
FT   REGION          92..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         138
SQ   SEQUENCE   138 AA;  16188 MW;  2E5427F1AE745ED6 CRC64;
     MNNQPCSIVW RRFLTSKVKP AVRIPNENLK ANKPTNFTKN FPLNERTKAW ERAGEDKESW
     FKRKYAHVHA KQKSQPQVDL YGKKEAHYSR LKQDILSSKR QQEEHKSKYS RKSVTLGLRP
     NPLMEYIYGT NSVIAALN