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Q732K6

- RLMN_BACC1

UniProt

Q732K6 - RLMN_BACC1

Protein

Probable dual-specificity RNA methyltransferase RlmN

Gene

rlmN

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    • Comment

    Functioni

    Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.UniRule annotation

    Catalytic activityi

    2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA.UniRule annotation
    2 S-adenosyl-L-methionine + adenine(37) in tRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA.UniRule annotation

    Cofactori

    Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei105 – 1051Proton acceptorUniRule annotation
    Metal bindingi125 – 1251Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi129 – 1291Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi132 – 1321Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
    Binding sitei207 – 2071S-adenosyl-L-methionineUniRule annotation
    Binding sitei306 – 3061S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation
    Active sitei349 – 3491S-methylcysteine intermediateUniRule annotation

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-KW
    3. rRNA (adenine-C2-)-methyltransferase activity Source: UniProtKB-HAMAP
    4. rRNA binding Source: UniProtKB-HAMAP
    5. tRNA (adenine-C2-)-methyltransferase activity Source: UniProtKB-HAMAP
    6. tRNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. rRNA base methylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    rRNA processing, tRNA processing

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable dual-specificity RNA methyltransferase RlmNUniRule annotation (EC:2.1.1.-UniRule annotation, EC:2.1.1.192UniRule annotation)
    Alternative name(s):
    23S rRNA (adenine(2503)-C(2))-methyltransferaseUniRule annotation
    23S rRNA m2A2503 methyltransferaseUniRule annotation
    Ribosomal RNA large subunit methyltransferase NUniRule annotation
    tRNA (adenine(37)-C(2))-methyltransferaseUniRule annotation
    tRNA m2A37 methyltransferaseUniRule annotation
    Gene namesi
    Name:rlmNUniRule annotation
    Ordered Locus Names:BCE_3906
    OrganismiBacillus cereus (strain ATCC 10987)
    Taxonomic identifieri222523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000002527: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 362362Probable dual-specificity RNA methyltransferase RlmNPRO_0000350028Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi118 ↔ 349(transient)UniRule annotation

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi222523.BCE_3906.

    Structurei

    3D structure databases

    ProteinModelPortaliQ732K6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 1762S-adenosyl-L-methionine bindingUniRule annotation
    Regioni230 – 2323S-adenosyl-L-methionine bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the radical SAM superfamily. RlmN family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0820.
    HOGENOMiHOG000217991.
    KOiK06941.
    OMAiHLIYKRK.
    OrthoDBiEOG6DJZ2N.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01849. RNA_methyltr_RlmN.
    InterProiIPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR027492. RNA_MTrfase_RlmN.
    IPR004383. rRNA_lsu_MTrfase_RlmN/Cfr.
    IPR007197. rSAM.
    [Graphical view]
    PANTHERiPTHR30544. PTHR30544. 1 hit.
    PfamiPF04055. Radical_SAM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006004. CHP00048. 1 hit.
    SMARTiSM00729. Elp3. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00048. TIGR00048. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q732K6-1 [UniParc]FASTAAdd to Basket

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    METTVRKQKK NLETKKPSIY SLQLHEMQDW LKEQGEPKFR AGQIFDWLYK    50
    KRVKNYEDMS NLSKGLREKL SNSFDITTLN TLVKQTSSDG TIKFLFQLYD 100
    GYSIETVLMR HEYGNSICVT TQVGCRIGCT FCASTLGGLK RNLEAGEIVA 150
    QVVEVQRALD ESEERVSSLV VMGIGEPFDN YDNLMGFLRI INHEKGLHIG 200
    ARHMTVSTSG IIPKIYKFAE EDLQINFAIS LHAPNSELRS KLMPINRAYK 250
    LPDLMEAIKY YVNRTGRRIT FEYGLFGGEN DQVEHAEELA ALLKGVKCHV 300
    NLIPVNYVPE RDYVRTPREQ IFLFEKTLKD RGVNVTIRRE QGHDIDAACG 350
    QLRAKERKEE TR 362
    Length:362
    Mass (Da):41,553
    Last modified:July 5, 2004 - v1
    Checksum:i5D1D0D3E937245BD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS42811.1.
    RefSeqiNP_980203.1. NC_003909.8.

    Genome annotation databases

    EnsemblBacteriaiAAS42811; AAS42811; BCE_3906.
    GeneIDi2748697.
    KEGGibca:BCE_3906.
    PATRICi18856468. VBIBacCer118379_3733.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS42811.1 .
    RefSeqi NP_980203.1. NC_003909.8.

    3D structure databases

    ProteinModelPortali Q732K6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 222523.BCE_3906.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS42811 ; AAS42811 ; BCE_3906 .
    GeneIDi 2748697.
    KEGGi bca:BCE_3906.
    PATRICi 18856468. VBIBacCer118379_3733.

    Phylogenomic databases

    eggNOGi COG0820.
    HOGENOMi HOG000217991.
    KOi K06941.
    OMAi HLIYKRK.
    OrthoDBi EOG6DJZ2N.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01849. RNA_methyltr_RlmN.
    InterProi IPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR027492. RNA_MTrfase_RlmN.
    IPR004383. rRNA_lsu_MTrfase_RlmN/Cfr.
    IPR007197. rSAM.
    [Graphical view ]
    PANTHERi PTHR30544. PTHR30544. 1 hit.
    Pfami PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006004. CHP00048. 1 hit.
    SMARTi SM00729. Elp3. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00048. TIGR00048. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
      Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
      Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10987.

    Entry informationi

    Entry nameiRLMN_BACC1
    AccessioniPrimary (citable) accession number: Q732K6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.UniRule annotation

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3