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Q9WYV8

- PRMC_THEMA

UniProt

Q9WYV8 - PRMC_THEMA

Protein

Release factor glutamine methyltransferase

Gene

prmC

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.Curated

    Catalytic activityi

    S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei151 – 1511S-adenosyl-L-methionine2 Publications
    Binding sitei180 – 1801S-adenosyl-L-methionine2 Publications
    Binding sitei197 – 1971S-adenosyl-L-methionine2 Publications

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro
    2. protein-glutamine N-methyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. peptidyl-glutamine methylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Release factor glutamine methyltransferase (EC:2.1.1.297)
    Short name:
    RF MTase
    Alternative name(s):
    N5-glutamine methyltransferase PrmC
    Protein-(glutamine-N5) MTase PrmC
    Protein-glutamine N-methyltransferase PrmC
    Gene namesi
    Name:prmC
    Ordered Locus Names:TM_0488
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 282282Release factor glutamine methyltransferasePRO_0000414548Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer and homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi243274.TM0488.

    Structurei

    Secondary structure

    1
    282
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 2411
    Turni25 – 284
    Helixi32 – 4413
    Helixi48 – 514
    Beta strandi53 – 553
    Helixi60 – 7415
    Helixi79 – 835
    Beta strandi85 – 884
    Beta strandi91 – 944
    Helixi106 – 12015
    Beta strandi124 – 1296
    Helixi134 – 1429
    Beta strandi146 – 1527
    Helixi154 – 16613
    Beta strandi172 – 1798
    Helixi182 – 1876
    Turni188 – 1903
    Beta strandi193 – 1964
    Helixi203 – 2053
    Helixi211 – 2133
    Helixi216 – 2194
    Turni222 – 2243
    Helixi227 – 2359
    Beta strandi242 – 2465
    Helixi249 – 2513
    Helixi252 – 2554
    Turni256 – 2583
    Beta strandi259 – 2613
    Beta strandi263 – 2664
    Beta strandi270 – 2789

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NV8X-ray2.20A/B1-282[»]
    1NV9X-ray2.36A1-282[»]
    1SG9X-ray2.30A/B/C1-282[»]
    1VQ1X-ray2.80A/B1-282[»]
    ProteinModelPortaliQ9WYV8.
    SMRiQ9WYV8. Positions 8-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WYV8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 1335S-adenosyl-L-methionine binding
    Regioni197 – 2004Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    KOiK02493.
    OMAiLFEPPEA.
    OrthoDBiEOG68Q0SZ.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    HAMAPiMF_02126. RF_methyltr_PrmC.
    InterProiIPR002052. DNA_methylase_N6_adenine_CS.
    IPR004556. Modification_methylase_HemK.
    IPR019874. Release_fac_Glu-N5_MeTfrase.
    IPR029063. SAM-dependent_MTases-like.
    IPR007848. Small_mtfrase_dom.
    [Graphical view]
    PfamiPF05175. MTS. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    TIGRFAMsiTIGR00536. hemK_fam. 1 hit.
    TIGR03534. RF_mod_PrmC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9WYV8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTRKNVSGA ERKIWSLIRD CSGKLEGVTE TSVLEVLLIV SRVLGIRKED    50
    LFLKDLGVSP TEEKRILELV EKRASGYPLH YILGEKEFMG LSFLVEEGVF 100
    VPRPETEELV ELALELIRKY GIKTVADIGT GSGAIGVSVA KFSDAIVFAT 150
    DVSSKAVEIA RKNAERHGVS DRFFVRKGEF LEPFKEKFAS IEMILSNPPY 200
    VKSSAHLPKD VLFEPPEALF GGEDGLDFYR EFFGRYDTSG KIVLMEIGED 250
    QVEELKKIVS DTVFLKDSAG KYRFLLLNRR SS 282
    Length:282
    Mass (Da):31,609
    Last modified:November 1, 1999 - v1
    Checksum:i68130302E620181B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35573.1.
    PIRiG72369.
    RefSeqiNP_228298.1. NC_000853.1.
    YP_008990542.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35573; AAD35573; TM_0488.
    GeneIDi897528.
    KEGGitma:TM0488.
    tmi:THEMA_02230.
    PATRICi23935881. VBITheMar51294_0495.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35573.1 .
    PIRi G72369.
    RefSeqi NP_228298.1. NC_000853.1.
    YP_008990542.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NV8 X-ray 2.20 A/B 1-282 [» ]
    1NV9 X-ray 2.36 A 1-282 [» ]
    1SG9 X-ray 2.30 A/B/C 1-282 [» ]
    1VQ1 X-ray 2.80 A/B 1-282 [» ]
    ProteinModelPortali Q9WYV8.
    SMRi Q9WYV8. Positions 8-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM0488.

    Protocols and materials databases

    DNASUi 897528.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD35573 ; AAD35573 ; TM_0488 .
    GeneIDi 897528.
    KEGGi tma:TM0488.
    tmi:THEMA_02230.
    PATRICi 23935881. VBITheMar51294_0495.

    Phylogenomic databases

    KOi K02493.
    OMAi LFEPPEA.
    OrthoDBi EOG68Q0SZ.

    Miscellaneous databases

    EvolutionaryTracei Q9WYV8.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    HAMAPi MF_02126. RF_methyltr_PrmC.
    InterProi IPR002052. DNA_methylase_N6_adenine_CS.
    IPR004556. Modification_methylase_HemK.
    IPR019874. Release_fac_Glu-N5_MeTfrase.
    IPR029063. SAM-dependent_MTases-like.
    IPR007848. Small_mtfrase_dom.
    [Graphical view ]
    Pfami PF05175. MTS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    TIGRFAMsi TIGR00536. hemK_fam. 1 hit.
    TIGR03534. RF_mod_PrmC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase."
      Yoon H.J., Kang K.Y., Ahn H.J., Shim S.M., Ha J.Y., Lee S.K., Mikami B., Suh S.W.
      Mol. Cells 16:266-269(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    3. "Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase."
      Schubert H.L., Phillips J.D., Hill C.P.
      Biochemistry 42:5592-5599(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-HOMOCYSTEINE; S-ADENOSYL-L-METHIONINE AND GLUTAMINE.
    4. "A novel mode of dimerization via formation of a glutamate anhydride crosslink in a protein crystal structure."
      Agarwal R., Burley S.K., Swaminathan S.
      Proteins 71:1038-1041(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND GLUTAMINE, SUBUNIT, GLUTAMATE ANHYDRIDE CROSS-LINK.
    5. "Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution."
      Joint Center for Structural Genomics (JCSG)
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

    Entry informationi

    Entry nameiPRMC_THEMA
    AccessioniPrimary (citable) accession number: Q9WYV8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 14, 2011
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The crystal structure corresponding to PDB 1SG9 shows a glutamate anhydride cross-link formed between the Glu-97 side chains from two molecules, but this has not been observed in other PrmC structures from T.maritima. This cross-link is suggested being an artifact of concentration during crystallization (PubMed:18247349).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3