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Protein

rRNA methyltransferase 1, mitochondrial

Gene

MRM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 2270 (Gm2270) in the 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA. This modification seems to be important for the normal accumulation of the mitochondrial large ribosomal subunit.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + guanosine(2270) in 21S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(2270) in 21S rRNA.1 Publication

GO - Molecular functioni

  • RNA binding Source: InterPro
  • rRNA (guanine-N1-)-methyltransferase activity Source: SGD

GO - Biological processi

  • rRNA methylation Source: GOC
  • rRNA modification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-33707-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
rRNA methyltransferase 1, mitochondrial1 Publication (EC:2.1.1.-1 Publication)
Alternative name(s):
21S rRNA (guanosine(2270)-2'-O)-methyltransferase1 Publication
21S rRNA [Gm2270] 2'-O-methyltransferase1 Publication
Mitochondrial large ribosomal RNA ribose methylase1 Publication
Petite colonies protein 561 Publication
Gene namesi
Name:MRM11 Publication
Synonyms:PET561 Publication
Ordered Locus Names:YOR201CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR201C.
SGDiS000005727. MRM1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020MitochondrionSequence analysisAdd
BLAST
Chaini21 – 412392rRNA methyltransferase 1, mitochondrialPRO_0000058321Add
BLAST

Proteomic databases

MaxQBiP25270.
PeptideAtlasiP25270.
TopDownProteomicsiP25270.

PTM databases

iPTMnetiP25270.

Interactioni

Protein-protein interaction databases

BioGridi34597. 46 interactions.
DIPiDIP-2603N.
IntActiP25270. 11 interactions.
MINTiMINT-425731.

Structurei

3D structure databases

ProteinModelPortaliP25270.
SMRiP25270. Positions 124-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000018761.
HOGENOMiHOG000248090.
InParanoidiP25270.
KOiK15507.
OMAiARNATEW.
OrthoDBiEOG70KH04.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
3.40.1280.10. 1 hit.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR029064. L30e-like.
IPR004441. rRNA_MeTrfase_TrmH.
IPR001537. SpoU_MeTrfase.
IPR013123. SpoU_subst-bd.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamiPF00588. SpoU_methylase. 1 hit.
PF08032. SpoU_sub_bind. 1 hit.
[Graphical view]
SMARTiSM00967. SpoU_sub_bind. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
SSF75217. SSF75217. 1 hit.
TIGRFAMsiTIGR00186. rRNA_methyl_3. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25270-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSLTNAVFK RYLAVTPSAH QALKTRIKKK SSSFDKFFPQ QSNSRKKQWE
60 70 80 90 100
TLNEDKASWF KRKYAHVHAR EQDRAADPYG KKKAHVEKLK EIKNQAKLNQ
110 120 130 140 150
KSHKSKFQNK DIALKLMNDN PIFEYVYGTN SVYAALLNPS RNCHSRLLYH
160 170 180 190 200
GTIPSKFLQI VDELKVTTEL VDKHRLNLLT NYGVHNNIAL ETKPLQPVEI
210 220 230 240 250
AYLGDMDTSS AALSIHELGF NNENIPHELP YGTKTDAKKF PLGLYLDEIT
260 270 280 290 300
DPHNIGAIIR SAYFLGVDFI VMSRRNCSPL TPVVSKTSSG ALELLPIFYV
310 320 330 340 350
DKPLEFFTKS QEMGGWTFIT SHLANATSEK YTVGKTISMH DLNGLCNELP
360 370 380 390 400
VVLVVGNESQ GVRTNLKMRS DFFVEIPFGG IEKGNRAPEP IVDSLNVSVA
410
TALLIDNILT CK
Length:412
Mass (Da):46,387
Last modified:February 1, 1996 - v2
Checksum:iC01B10254C0EDEA8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19947 Genomic DNA. Translation: AAA74564.1.
Z75107 Genomic DNA. Translation: CAA99414.1.
X03245 Genomic DNA. Translation: CAA27002.1.
BK006948 Genomic DNA. Translation: DAA10974.1.
PIRiS48881.
RefSeqiNP_014844.3. NM_001183620.3.

Genome annotation databases

EnsemblFungiiYOR201C; YOR201C; YOR201C.
GeneIDi854376.
KEGGisce:YOR201C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19947 Genomic DNA. Translation: AAA74564.1.
Z75107 Genomic DNA. Translation: CAA99414.1.
X03245 Genomic DNA. Translation: CAA27002.1.
BK006948 Genomic DNA. Translation: DAA10974.1.
PIRiS48881.
RefSeqiNP_014844.3. NM_001183620.3.

3D structure databases

ProteinModelPortaliP25270.
SMRiP25270. Positions 124-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34597. 46 interactions.
DIPiDIP-2603N.
IntActiP25270. 11 interactions.
MINTiMINT-425731.

PTM databases

iPTMnetiP25270.

Proteomic databases

MaxQBiP25270.
PeptideAtlasiP25270.
TopDownProteomicsiP25270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR201C; YOR201C; YOR201C.
GeneIDi854376.
KEGGisce:YOR201C.

Organism-specific databases

EuPathDBiFungiDB:YOR201C.
SGDiS000005727. MRM1.

Phylogenomic databases

GeneTreeiENSGT00390000018761.
HOGENOMiHOG000248090.
InParanoidiP25270.
KOiK15507.
OMAiARNATEW.
OrthoDBiEOG70KH04.

Enzyme and pathway databases

BioCyciYEAST:G3O-33707-MONOMER.

Miscellaneous databases

NextBioi976508.
PROiP25270.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
3.40.1280.10. 1 hit.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR029064. L30e-like.
IPR004441. rRNA_MeTrfase_TrmH.
IPR001537. SpoU_MeTrfase.
IPR013123. SpoU_subst-bd.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamiPF00588. SpoU_methylase. 1 hit.
PF08032. SpoU_sub_bind. 1 hit.
[Graphical view]
SMARTiSM00967. SpoU_sub_bind. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
SSF75217. SSF75217. 1 hit.
TIGRFAMsiTIGR00186. rRNA_methyl_3. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional requirement of a site-specific ribose methylation in ribosomal RNA."
    Sirum-Connolly K., Mason T.L.
    Science 262:1886-1889(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Nucleotide sequence and transcriptional mapping of the yeast pet56-his3-ded1 gene region."
    Struhl K.
    Nucleic Acids Res. 13:8587-8601(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "MRM2 encodes a novel yeast mitochondrial 21S rRNA methyltransferase."
    Pintard L., Bujnicki J.M., Lapeyre B., Bonnerot C.
    EMBO J. 21:1139-1147(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME.

Entry informationi

Entry nameiMRM1_YEAST
AccessioniPrimary (citable) accession number: P25270
Secondary accession number(s): D6W2Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2760 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.