MRM1_SCHPO
ID MRM1_SCHPO Reviewed; 301 AA.
AC O94631;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
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;
GN Name=mrm1 {ECO:0000250|UniProtKB:P25270};
GN ORFNames=SPBC1347.13c {ECO:0000312|PomBase:SPBC1347.13c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 subunit ribosomal RNA (mtLSU rRNA), a universally
CC conserved modification in the peptidyl transferase domain of the mtLSU
CC rRNA. {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}.
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DR EMBL; CU329671; CAB37444.1; -; Genomic_DNA.
DR PIR; T39401; T39401.
DR RefSeq; NP_596705.1; NM_001022629.2.
DR AlphaFoldDB; O94631; -.
DR SMR; O94631; -.
DR BioGRID; 276350; 9.
DR STRING; 4896.SPBC1347.13c.1; -.
DR MaxQB; O94631; -.
DR PaxDb; O94631; -.
DR PRIDE; O94631; -.
DR EnsemblFungi; SPBC1347.13c.1; SPBC1347.13c.1:pep; SPBC1347.13c.
DR GeneID; 2539800; -.
DR KEGG; spo:SPBC1347.13c; -.
DR PomBase; SPBC1347.13c; mrm1.
DR VEuPathDB; FungiDB:SPBC1347.13c; -.
DR eggNOG; KOG0838; Eukaryota.
DR HOGENOM; CLU_021322_5_1_1; -.
DR InParanoid; O94631; -.
DR OMA; VMSRRNC; -.
DR PhylomeDB; O94631; -.
DR PRO; PR:O94631; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008989; F:rRNA (guanine-N1-)-methyltransferase activity; ISS:PomBase.
DR GO; GO:0000963; P:mitochondrial RNA processing; ISS:PomBase.
DR GO; GO:0031167; P:rRNA methylation; ISS:PomBase.
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; IPR004441; rRNA_MeTrfase_TrmH.
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.
DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..11
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 12..301
FT /note="rRNA methyltransferase 1, mitochondrial"
FT /id="PRO_0000337261"
FT REGION 121..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 33402 MW; 437087BC3A2D7E5B CRC64;
MIRSRVNLAR EVPKKAKAHL SKERRLIKED SEFVFGTHSV KNALATRKRE CRALYVQNAD
IHSEFEEFLN KLQYKIPIKS VNKEHLNQIT ACRPHNGVVL EASSLNVPTI SDLLFPAGEE
YNNKNGQDSP HNDLNEGKSS SSDNYPPLYV YVDGITDPQN MGAVIRSAYI LGAKGILLSK
KHNTFLSPVV SKASAGALEV FNISHVKNPM VFLRNSVLKG WKVIGTKPAL PDNKDQIYTP
HKIKTELMNE PKILVLGSEK GLRTNILTQC SHYVSIPGGD KYVDSLNVSV AAGILLYSLV
N
