ID MRM3_MOUSE Reviewed; 418 AA.
AC Q5ND52; A4FUR4; Q3UGQ7; Q5U5W2; Q8C1J9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 02-NOV-2016, entry version 84.
DE RecName: Full=rRNA methyltransferase 3, mitochondrial {ECO:0000250|UniProtKB:Q9HC36};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=16S rRNA (guanosine(1370)-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=16S rRNA [Gm1370] 2'-O-methyltransferase {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=RNA methyltransferase-like protein 1 {ECO:0000250|UniProtKB:Q9HC36};
DE Flags: Precursor;
GN Name=Mrm3 {ECO:0000250|UniProtKB:Q9HC36};
GN Synonyms=Rnmtl1 {ECO:0000312|MGI:MGI:1914640};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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
RT project: 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
RT are positioned to modify nascent rRNA in foci near the mitochondrial
RT DNA 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-
CC methylguanosine at position 1370 (Gm1370) in the 16S mitochondrial
CC large subunit ribosomal RNA (mtLSU rRNA), a conserved modification
CC in the peptidyl transferase domain of the mtLSU rRNA.
CC {ECO:0000250|UniProtKB:Q9HC36}.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanosine(1370) in
CC 16S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(1370)
CC in 16S rRNA. {ECO:0000250|UniProtKB:Q9HC36}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24036117}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding
CC methyltransferase superfamily. RNA methyltransferase TrmH family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38288.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH90975.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI15623.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI15624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25446.1; Type=Frameshift; Positions=37; Evidence={ECO:0000305};
DR EMBL; AK014739; BAC25446.1; ALT_FRAME; mRNA.
DR EMBL; AK147805; BAE28150.1; -; mRNA.
DR EMBL; AL591129; CAI35103.1; -; Genomic_DNA.
DR EMBL; BC038288; AAH38288.1; ALT_INIT; mRNA.
DR EMBL; BC090975; AAH90975.2; ALT_INIT; mRNA.
DR EMBL; BC115622; AAI15623.1; ALT_INIT; mRNA.
DR EMBL; BC115623; AAI15624.1; ALT_INIT; mRNA.
DR CCDS; CCDS48852.1; -.
DR RefSeq; NP_899086.2; NM_183263.5.
DR UniGene; Mm.24886; -.
DR ProteinModelPortal; Q5ND52; -.
DR SMR; Q5ND52; -.
DR STRING; 10090.ENSMUSP00000042882; -.
DR iPTMnet; Q5ND52; -.
DR PhosphoSitePlus; Q5ND52; -.
DR EPD; Q5ND52; -.
DR MaxQB; Q5ND52; -.
DR PaxDb; Q5ND52; -.
DR PeptideAtlas; Q5ND52; -.
DR PRIDE; Q5ND52; -.
DR Ensembl; ENSMUST00000040577; ENSMUSP00000042882; ENSMUSG00000038046.
DR GeneID; 67390; -.
DR KEGG; mmu:67390; -.
DR UCSC; uc007kfn.2; mouse.
DR CTD; 67390; -.
DR MGI; MGI:1914640; Rnmtl1.
DR eggNOG; KOG2506; Eukaryota.
DR eggNOG; COG0566; LUCA.
DR GeneTree; ENSGT00390000017317; -.
DR HOGENOM; HOG000154151; -.
DR HOVERGEN; HBG108411; -.
DR InParanoid; Q5ND52; -.
DR KO; K20095; -.
DR OMA; RYDKAFP; -.
DR OrthoDB; EOG091G0OPI; -.
DR PhylomeDB; Q5ND52; -.
DR TreeFam; TF323420; -.
DR PRO; PR:Q5ND52; -.
DR Proteomes; UP000000589; Chromosome 11.
DR Bgee; ENSMUSG00000038046; -.
DR CleanEx; MM_RNMTL1; -.
DR Genevisible; Q5ND52; MM.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 2.
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; 2.
PE 2: Evidence at transcript level;
KW Complete proteome; Methyltransferase; Mitochondrion;
KW Reference proteome; rRNA processing; S-adenosyl-L-methionine;
KW Transferase; Transit peptide.
FT TRANSIT 1 40 Mitochondrion. {ECO:0000255}.
FT CHAIN 41 418 rRNA methyltransferase 3, mitochondrial.
FT /FTId=PRO_0000311302.
FT BINDING 354 354 S-adenosyl-L-methionine; via carbonyl
FT oxygen. {ECO:0000250}.
FT BINDING 378 378 S-adenosyl-L-methionine; via amide
FT nitrogen and carbonyl oxygen.
FT {ECO:0000250}.
FT BINDING 387 387 S-adenosyl-L-methionine; via amide
FT nitrogen. {ECO:0000250}.
FT CONFLICT 102 102 R -> K (in Ref. 3; AAH38288/AAI15624/
FT AAI15623). {ECO:0000305}.
FT CONFLICT 203 203 P -> L (in Ref. 3; AAH38288/AAI15624/
FT AAI15623). {ECO:0000305}.
FT CONFLICT 350 350 A -> V (in Ref. 1; BAE28150).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 124 195 ismart:SpoU_sub_bind [T]
FT MYHIT 210 398 ipfam:SpoU_methylase [T]
SQ SEQUENCE 418 AA; 46796 MW; 54E4A589B436141B CRC64;
MAAPAKGMWC SLGSLLRVVQ TRDLNARRWV RALRRSPVRV LSPSGQVEER KRAPDQQPRK
AVPKASSQGQ RQKQPLETSP SQTPHTWEEA GLRYDKAFPG DRRLSSVMTI VKSRPFREKQ
GKILLEGRRL IADALKAGAV PKAFFFSRLE YVKELPVDKL KDVSLIKVKF EDIKDWSDLV
TPQGIMGIFA KPDPVKMTYP ETPLHHTLPL VLICDNLRDP GNLGTILRSA AGAGCSKVLL
TKGCVDAWEP KVLRAGMGAH FQVPIVNNVE WETVPNHLPP DTRVYVADNC GHYAQVQMSD
KTGDRDWACD RRFLKFHKYE EDLDTKTRKD WLPKLEVQSY DLDWTGAPAA VVIGGETHGV
SLESLQLAES TGGKRLLIPV VPGVDSLNSA MAASILLFEG KRQLRIKVED LSRDRSYH
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