MRM1_MOUSE
ID MRM1_MOUSE Reviewed; 320 AA.
AC Q99J25; Q3TPX8; Q3U0Z5; Q5ND22;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=rRNA methyltransferase 1, mitochondrial {ECO:0000303|PubMed:24036117};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q6IN84};
DE AltName: Full=16S rRNA (guanosine(1145)-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q6IN84};
DE AltName: Full=16S rRNA [Gm1145] 2'-O-methyltransferase {ECO:0000250|UniProtKB:Q6IN84};
DE Flags: Precursor;
GN Name=Mrm1 {ECO:0000250|UniProtKB:Q6IN84};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=24036117; DOI=10.1074/jbc.m113.515692;
RA Lee K.W., Okot-Kotber C., LaComb J.F., Bogenhagen D.F.;
RT "Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are
RT positioned to modify nascent rRNA in foci near the mitochondrial DNA
RT nucleoid.";
RL J. Biol. Chem. 288:31386-31399(2013).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of 2'-O-methylguanosine
CC at position 1145 (Gm1145) in the 16S mitochondrial large subunit
CC ribosomal RNA (mtLSU rRNA), a universally conserved modification in the
CC peptidyl transferase domain of the mtLSU rRNA.
CC {ECO:0000250|UniProtKB:Q6IN84}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1145) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(1145) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47776, Rhea:RHEA-COMP:11909, Rhea:RHEA-COMP:11910,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445;
CC Evidence={ECO:0000250|UniProtKB:Q6IN84};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE33706.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK156416; BAE33706.1; ALT_FRAME; mRNA.
DR EMBL; AK164059; BAE37607.1; -; mRNA.
DR EMBL; AK163986; BAE37571.1; -; mRNA.
DR EMBL; AL596083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005625; AAH05625.2; -; mRNA.
DR CCDS; CCDS36260.1; -.
DR RefSeq; NP_663408.2; NM_145433.1.
DR AlphaFoldDB; Q99J25; -.
DR SMR; Q99J25; -.
DR BioGRID; 229836; 1.
DR STRING; 10090.ENSMUSP00000018549; -.
DR PhosphoSitePlus; Q99J25; -.
DR EPD; Q99J25; -.
DR MaxQB; Q99J25; -.
DR PaxDb; Q99J25; -.
DR PeptideAtlas; Q99J25; -.
DR PRIDE; Q99J25; -.
DR ProteomicsDB; 290318; -.
DR Antibodypedia; 72774; 123 antibodies from 21 providers.
DR DNASU; 217038; -.
DR Ensembl; ENSMUST00000018549; ENSMUSP00000018549; ENSMUSG00000018405.
DR GeneID; 217038; -.
DR KEGG; mmu:217038; -.
DR UCSC; uc007kqr.1; mouse.
DR CTD; 79922; -.
DR MGI; MGI:2443470; Mrm1.
DR VEuPathDB; HostDB:ENSMUSG00000018405; -.
DR eggNOG; KOG0838; Eukaryota.
DR GeneTree; ENSGT00390000018761; -.
DR HOGENOM; CLU_021322_5_1_1; -.
DR InParanoid; Q99J25; -.
DR OMA; QVPPYEY; -.
DR OrthoDB; 1412032at2759; -.
DR PhylomeDB; Q99J25; -.
DR TreeFam; TF315167; -.
DR BioGRID-ORCS; 217038; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Mrm1; mouse.
DR PRO; PR:Q99J25; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99J25; protein.
DR Bgee; ENSMUSG00000018405; Expressed in interventricular septum and 183 other tissues.
DR Genevisible; Q99J25; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0000154; P:rRNA modification; IBA:GO_Central.
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 Pfam; PF08032; SpoU_sub_bind; 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..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..320
FT /note="rRNA methyltransferase 1, mitochondrial"
FT /id="PRO_0000273203"
SQ SEQUENCE 320 AA; 34843 MW; 361D26D155A233D8 CRC64;
MRRLWTVGCF SRLIARHFSS VARRGERPGG EELSRLLLDD LAPAQRLERL FGLSPCLLAL
RAARRRVARL LLQAGKAGLQ GERAELLRVA EARGIPVLRP RRQKLDALCG YQVHQGVCME
VSPLRPRPCD EAADTSSGDD PQQLWLVLEG LQDPRNLGAV MRSAHFLGVD RVITSQRNSC
PLTPVVSKAS AGAMEVMDVF ATPDLPGFLQ AKAQQGWLVV GTVGCPGPEI SQSSKVPITS
CLEFVWDRPT LLVLGSEGSG LSQEVFASCQ LLLTILPRRH LPPGLESLNV SVATGILLHS
ICSQKKGFPV QERGQLLQDS
