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Protein

Ribosomal RNA small subunit methyltransferase mra1

Gene

mra1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates the pseudouridine corresponding to position 1189 (Psi1189) in S.cerevisiae 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity). Essential for cell growth. It also has a key role in promoting the mating function (PubMed:9133664).By similarity1 Publication

Catalytic activityi

S-adenosyl-L-methionine + a pseudouridine in 18S rRNA = S-adenosyl-L-homocysteine + a N(1)-methylpseudouridine in 18S rRNA.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei197 – 1971Stabilizes Arg-195By similarity
Binding sitei287 – 2871S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei314 – 3141S-adenosyl-L-methionine; via amide nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Pheromone response, Ribosome biogenesis, rRNA processing

Keywords - Ligandi

RNA-binding, rRNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal RNA small subunit methyltransferase mra1Curated (EC:2.1.1.-By similarity)
Alternative name(s):
18S rRNA (pseudouridine-N1)-methyltransferaseBy similarity
Multicopy suppressor of ras1-deficiency protein1 Publication
Gene namesi
Name:mra11 Publication
ORF Names:SPAC18G6.07cImported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC18G6.07c.
PomBaseiSPAC18G6.07c. mra1.

Subcellular locationi

  • Nucleusnucleolus By similarity

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleolus Source: UniProtKB-SubCell
  • nucleus Source: PomBase
  • small-subunit processome Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Ribosomal RNA small subunit methyltransferase mra1PRO_0000158613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine1 Publication
Modified residuei33 – 331Phosphothreonine1 Publication
Modified residuei100 – 1001Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ10107.

PTM databases

iPTMnetiQ10107.

Interactioni

Subunit structurei

Homodimer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei195 – 1951Interaction with substrate rRNABy similarity
Sitei236 – 2361Interaction with substrate rRNABy similarity
Sitei239 – 2391Interaction with substrate rRNABy similarity
Sitei243 – 2431Interaction with substrate rRNABy similarity

Protein-protein interaction databases

BioGridi278615. 4 interactions.
MINTiMINT-4696973.

Structurei

3D structure databases

ProteinModelPortaliQ10107.
SMRiQ10107. Positions 142-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni319 – 3213S-adenosyl-L-methionine bindingBy similarity
Regioni334 – 3396S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000193819.
InParanoidiQ10107.
KOiK14568.
OMAiCICCSED.
OrthoDBiEOG7FV415.
PhylomeDBiQ10107.

Family and domain databases

InterProiIPR029028. Alpha/beta_knot_MTases.
IPR005304. Rbsml_bgen_MeTrfase_EMG1/NEP1.
[Graphical view]
PANTHERiPTHR12636. PTHR12636. 1 hit.
PfamiPF03587. EMG1. 1 hit.
[Graphical view]
SUPFAMiSSF75217. SSF75217. 1 hit.

Sequencei

Sequence statusi: Complete.

Q10107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTYSKRKSR GSLEVSEKTN QPKFIKRSQS SETITSGETA SELMQDEKEQ
60 70 80 90 100
SNGAVGSIED EELQRLRENQ ASVEALSKKP ESIDRELGVE ALEIDNVVKS
110 120 130 140 150
DEEKEDPNGA SSKTVKARPL PAGSVHRVTT HMAPIPARSI GSHDTTTQRL
160 170 180 190 200
IVVLDQACLE IYKVGKAKDA KYQLLNCDDH QGILKKLNRN IAQARPDITH
210 220 230 240 250
QCLLTLLDSP LNKAGRLQVY IHTAKKVLIE VNPSVRIPRT FKRFSGLMVQ
260 270 280 290 300
LLHKLSIRSV NGNEKLLKVI KNPVTDYLPP NCRKATLSFD APTVPPRKYL
310 320 330 340 350
ETLQPNQSVC IAIGAMAHGP DDFSDGWVDE KISISDYPLS ASIACSKFLH

SMEDFLGIV
Length:359
Mass (Da):39,775
Last modified:December 15, 1998 - v2
Checksum:iD7753DD546E2E3EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78582 Genomic DNA. Translation: BAA24497.1.
CU329670 Genomic DNA. Translation: CAA92394.1.
PIRiT37921.
RefSeqiNP_593671.1. NM_001019103.2.

Genome annotation databases

EnsemblFungiiSPAC18G6.07c.1; SPAC18G6.07c.1:pep; SPAC18G6.07c.
GeneIDi2542139.
KEGGispo:SPAC18G6.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78582 Genomic DNA. Translation: BAA24497.1.
CU329670 Genomic DNA. Translation: CAA92394.1.
PIRiT37921.
RefSeqiNP_593671.1. NM_001019103.2.

3D structure databases

ProteinModelPortaliQ10107.
SMRiQ10107. Positions 142-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278615. 4 interactions.
MINTiMINT-4696973.

PTM databases

iPTMnetiQ10107.

Proteomic databases

MaxQBiQ10107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC18G6.07c.1; SPAC18G6.07c.1:pep; SPAC18G6.07c.
GeneIDi2542139.
KEGGispo:SPAC18G6.07c.

Organism-specific databases

EuPathDBiFungiDB:SPAC18G6.07c.
PomBaseiSPAC18G6.07c. mra1.

Phylogenomic databases

HOGENOMiHOG000193819.
InParanoidiQ10107.
KOiK14568.
OMAiCICCSED.
OrthoDBiEOG7FV415.
PhylomeDBiQ10107.

Miscellaneous databases

NextBioi20803211.
PROiQ10107.

Family and domain databases

InterProiIPR029028. Alpha/beta_knot_MTases.
IPR005304. Rbsml_bgen_MeTrfase_EMG1/NEP1.
[Graphical view]
PANTHERiPTHR12636. PTHR12636. 1 hit.
PfamiPF03587. EMG1. 1 hit.
[Graphical view]
SUPFAMiSSF75217. SSF75217. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Schizosaccharomyces pombe mra1 gene, which is required for cell growth and mating, can suppress the mating inefficiency caused by a deficit in the Ras1 activity."
    Hakuno F., Hughes D.A., Yamamoto M.
    Genes Cells 1:303-315(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: JY450.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-33 AND SER-100, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNEP1_SCHPO
AccessioniPrimary (citable) accession number: Q10107
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 15, 1998
Last modified: May 11, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.