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Protein

tRNA (adenine(58)-N(1))-methyltransferase TrmI

Gene

trmI

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA. Is required for cell growth at extreme temperatures.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + adenine(58) in tRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(58) in tRNA.PROSITE-ProRule annotation1 Publication

Kineticsi

  1. KM=2.1 µM for S-adenosyl-L-methionine1 Publication
  2. KM=2.7 µM for tRNA(Met)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei125 – 1251S-adenosyl-L-methionine
    Binding sitei130 – 1301S-adenosyl-L-methionine
    Binding sitei155 – 1551S-adenosyl-L-methionine
    Binding sitei170 – 1701S-adenosyl-L-methionine

    GO - Molecular functioni

    • tRNA (adenine-N1-)-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    • tRNA methylation Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciTTHE262724:GCAT-248-MONOMER.
    BRENDAi2.1.1.220. 2305.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA (adenine(58)-N(1))-methyltransferase TrmI (EC:2.1.1.220)
    Alternative name(s):
    tRNA(m1A58)-methyltransferase
    Short name:
    tRNA(m1A58)MTase
    Gene namesi
    Name:trmI
    Ordered Locus Names:TT_C0244
    OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
    Taxonomic identifieri262724 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    Proteomesi
    • UP000000592 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781Y → A: 20-fold decrease in catalytic efficiency. No change in Km for S-adenosyl-L-methionine. 1 Publication
    Mutagenesisi170 – 1701D → A: 300-fold decrease in catalytic efficiency. Increase in Km for S-adenosyl-L-methionine. 1 Publication
    Mutagenesisi194 – 1941Y → A: 3-fold decrease in catalytic efficiency. Increase in Km for S-adenosyl-L-methionine. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 255255tRNA (adenine(58)-N(1))-methyltransferase TrmIPRO_0000204467Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer composed of a dimer of dimers.2 Publications

    Protein-protein interaction databases

    STRINGi262724.TTC0244.

    Structurei

    Secondary structure

    1
    255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104Combined sources
    Beta strandi16 – 194Combined sources
    Beta strandi26 – 316Combined sources
    Beta strandi33 – 353Combined sources
    Helixi36 – 427Combined sources
    Beta strandi47 – 493Combined sources
    Beta strandi55 – 595Combined sources
    Helixi63 – 697Combined sources
    Helixi79 – 8810Combined sources
    Beta strandi96 – 1005Combined sources
    Beta strandi103 – 1053Combined sources
    Helixi106 – 11510Combined sources
    Turni116 – 1183Combined sources
    Beta strandi119 – 1268Combined sources
    Helixi128 – 14114Combined sources
    Beta strandi147 – 1526Combined sources
    Helixi154 – 1563Combined sources
    Beta strandi164 – 1729Combined sources
    Helixi174 – 1774Combined sources
    Helixi178 – 1847Combined sources
    Beta strandi185 – 19612Combined sources
    Helixi198 – 20811Combined sources
    Turni209 – 2124Combined sources
    Beta strandi213 – 22917Combined sources
    Beta strandi232 – 2354Combined sources
    Beta strandi237 – 2404Combined sources
    Beta strandi245 – 2517Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PWYX-ray1.70A/B1-253[»]
    5C0OX-ray2.62E/F/G/H1-255[»]
    5C1IX-ray3.10A/B/C/D5-253[»]
    ProteinModelPortaliQ8GBB2.
    SMRiQ8GBB2. Positions 5-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8GBB2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni104 – 1074S-adenosyl-L-methionine binding

    Domaini

    Contains a large catalytic C-terminal domain that binds S-adenosyl-L-methionine and a smaller N-terminal domain that may play a role in tRNA recognition. Domains are connected by a linker region.1 Publication

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG41066UU. Bacteria.
    COG2519. LUCA.
    KOiK07442.
    OMAiRPDHRMI.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR029063. SAM-dependent_MTases.
    IPR014816. tRNA_MeTrfase_Gcd14.
    [Graphical view]
    PfamiPF08704. GCD14. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017269. GCD14. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51620. SAM_TRM61. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8GBB2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAWPGPLLLK DRKGRAYLVF PKEGGVFHHH KGSVPHEALL EAGPGGVVRT
    60 70 80 90 100
    HLGEELSVHR PTLEEYLLHM KRSATPTYPK DASAMVTLLD LAPGMRVLEA
    110 120 130 140 150
    GTGSGGLTLF LARAVGEKGL VESYEARPHH LAQAERNVRA FWQVENVRFH
    160 170 180 190 200
    LGKLEEAELE EAAYDGVALD LMEPWKVLEK AALALKPDRF LVAYLPNITQ
    210 220 230 240 250
    VLELVRAAEA HPFRLERVLE VGWREWEVRL PVAHPRFQQV GHTAFLVALR

    RWKAS
    Length:255
    Mass (Da):28,596
    Last modified:May 24, 2004 - v2
    Checksum:iD56E4CB77232AEC3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti254 – 2541A → G in CAD56705 (PubMed:12682365).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ516007 Genomic DNA. Translation: CAD56705.2.
    AE017221 Genomic DNA. Translation: AAS80592.1.
    RefSeqiWP_011172697.1. NC_005835.1.

    Genome annotation databases

    EnsemblBacteriaiAAS80592; AAS80592; TT_C0244.
    KEGGitth:TTC0244.
    PATRICi23950881. VBITheThe54392_0245.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ516007 Genomic DNA. Translation: CAD56705.2.
    AE017221 Genomic DNA. Translation: AAS80592.1.
    RefSeqiWP_011172697.1. NC_005835.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PWYX-ray1.70A/B1-253[»]
    5C0OX-ray2.62E/F/G/H1-255[»]
    5C1IX-ray3.10A/B/C/D5-253[»]
    ProteinModelPortaliQ8GBB2.
    SMRiQ8GBB2. Positions 5-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi262724.TTC0244.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAS80592; AAS80592; TT_C0244.
    KEGGitth:TTC0244.
    PATRICi23950881. VBITheThe54392_0245.

    Phylogenomic databases

    eggNOGiENOG41066UU. Bacteria.
    COG2519. LUCA.
    KOiK07442.
    OMAiRPDHRMI.

    Enzyme and pathway databases

    BioCyciTTHE262724:GCAT-248-MONOMER.
    BRENDAi2.1.1.220. 2305.

    Miscellaneous databases

    EvolutionaryTraceiQ8GBB2.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR029063. SAM-dependent_MTases.
    IPR014816. tRNA_MeTrfase_Gcd14.
    [Graphical view]
    PfamiPF08704. GCD14. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017269. GCD14. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51620. SAM_TRM61. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTRMI_THET2
    AccessioniPrimary (citable) accession number: Q8GBB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: May 24, 2004
    Last modified: September 7, 2016
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.