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A5UAC2

- RLMN_HAEIE

UniProt

A5UAC2 - RLMN_HAEIE

Protein

Dual-specificity RNA methyltransferase RlmN

Gene

rlmN

Organism
Haemophilus influenzae (strain PittEE)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      Previous versions | rss
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    Functioni

    Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.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 sitei110 – 1101Proton acceptorUniRule annotation
    Metal bindingi130 – 1301Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi134 – 1341Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi137 – 1371Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
    Binding sitei216 – 2161S-adenosyl-L-methionineUniRule annotation
    Binding sitei317 – 3171S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation
    Active sitei360 – 3601S-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

    Enzyme and pathway databases

    BioCyciHINF374930:GJDD-223-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    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:CGSHiEE_01185
    OrganismiHaemophilus influenzae (strain PittEE)
    Taxonomic identifieri374930 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000006555: 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 – 390390Dual-specificity RNA methyltransferase RlmNPRO_0000350203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi123 ↔ 360(transient)UniRule annotation

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi374930.CGSHiEE_01185.

    Structurei

    3D structure databases

    ProteinModelPortaliA5UAC2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 1852S-adenosyl-L-methionine bindingUniRule annotation
    Regioni238 – 2403S-adenosyl-L-methionine bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0820.
    HOGENOMiHOG000217992.
    KOiK06941.
    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.

    A5UAC2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCNNEAKMSE LLSVQSDAPA KKINLMDLTR QQMREFFKEL GEKPFRADQL    50
    VKWIYHFGED NFDNMTNINK KLREKLKAVA EIKAPEVAVE QRSADGTIKW 100
    AMQVGEQQVE TVYIPEADRA TLCVSSQVGC ALACTFCSTA QQGFNRNLTV 150
    SEIIGQVWRA SKIIGNFGVT GVRPITNVVM MGMGEPLLNV ANVVPAMEIM 200
    LDDFAYGLSK RRVTLSTSGV VPALDNLSKM IDVALAISLH APNDELRDEI 250
    VPINKKYNIK TLIDSVNRYL TVSNANHGKV TIEYVMLDHV NDGVEHAHQL 300
    ADVLKNTPCK INLIPWNPFP EAPYAKSSNT RIDRFQKTLM EYDFTVIIRK 350
    TRGDDIDAAC GQLAGDVIDR TKRTAMKRQF GQNIGVTEVN 390
    Length:390
    Mass (Da):43,570
    Last modified:September 2, 2008 - v2
    Checksum:i85E174CE9CF12465
    GO

    Sequence cautioni

    The sequence ABQ97723.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000671 Genomic DNA. Translation: ABQ97723.1. Different initiation.
    RefSeqiYP_001290106.1. NC_009566.1.

    Genome annotation databases

    EnsemblBacteriaiABQ97723; ABQ97723; CGSHiEE_01185.
    GeneIDi5224754.
    KEGGihip:CGSHiEE_01185.
    PATRICi20276473. VBIHaeInf81350_0235.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000671 Genomic DNA. Translation: ABQ97723.1 . Different initiation.
    RefSeqi YP_001290106.1. NC_009566.1.

    3D structure databases

    ProteinModelPortali A5UAC2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 374930.CGSHiEE_01185.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ97723 ; ABQ97723 ; CGSHiEE_01185 .
    GeneIDi 5224754.
    KEGGi hip:CGSHiEE_01185.
    PATRICi 20276473. VBIHaeInf81350_0235.

    Phylogenomic databases

    eggNOGi COG0820.
    HOGENOMi HOG000217992.
    KOi K06941.
    OrthoDBi EOG6DJZ2N.

    Enzyme and pathway databases

    BioCyci HINF374930:GJDD-223-MONOMER.

    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. "Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
      Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
      Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PittEE.

    Entry informationi

    Entry nameiRLMN_HAEIE
    AccessioniPrimary (citable) accession number: A5UAC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 47 of the entry and version 2 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