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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)DescriptionActionsGraphical viewLength
    Binding sitei125S-adenosyl-L-methionine1
    Binding sitei130S-adenosyl-L-methionine1
    Binding sitei155S-adenosyl-L-methionine1
    Binding sitei170S-adenosyl-L-methionine1

    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

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi78Y → A: 20-fold decrease in catalytic efficiency. No change in Km for S-adenosyl-L-methionine. 1 Publication1
    Mutagenesisi170D → A: 300-fold decrease in catalytic efficiency. Increase in Km for S-adenosyl-L-methionine. 1 Publication1
    Mutagenesisi194Y → A: 3-fold decrease in catalytic efficiency. Increase in Km for S-adenosyl-L-methionine. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002044671 – 255tRNA (adenine(58)-N(1))-methyltransferase TrmIAdd BLAST255

    Interactioni

    Subunit structurei

    Homotetramer composed of a dimer of dimers.2 Publications

    Protein-protein interaction databases

    STRINGi262724.TTC0244.

    Structurei

    Secondary structure

    1255
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 10Combined sources4
    Beta strandi16 – 19Combined sources4
    Beta strandi26 – 31Combined sources6
    Beta strandi33 – 35Combined sources3
    Helixi36 – 42Combined sources7
    Beta strandi47 – 49Combined sources3
    Beta strandi55 – 59Combined sources5
    Helixi63 – 69Combined sources7
    Helixi79 – 88Combined sources10
    Beta strandi96 – 100Combined sources5
    Beta strandi103 – 105Combined sources3
    Helixi106 – 115Combined sources10
    Turni116 – 118Combined sources3
    Beta strandi119 – 126Combined sources8
    Helixi128 – 141Combined sources14
    Beta strandi147 – 152Combined sources6
    Helixi154 – 156Combined sources3
    Beta strandi164 – 172Combined sources9
    Helixi174 – 177Combined sources4
    Helixi178 – 184Combined sources7
    Beta strandi185 – 196Combined sources12
    Helixi198 – 208Combined sources11
    Turni209 – 212Combined sources4
    Beta strandi213 – 229Combined sources17
    Beta strandi232 – 235Combined sources4
    Beta strandi237 – 240Combined sources4
    Beta strandi245 – 251Combined sources7

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ8GBB2.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni104 – 107S-adenosyl-L-methionine binding4

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti254A → G in CAD56705 (PubMed:12682365).Curated1

    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:TT_C0244.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2PWYX-ray1.70A/B1-253[»]
    5C0OX-ray2.62E/F/G/H1-255[»]
    5C1IX-ray3.10A/B/C/D5-253[»]
    ProteinModelPortaliQ8GBB2.
    SMRiQ8GBB2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi262724.TTC0244.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

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

    Enzyme and pathway databases

    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: November 2, 2016
    This is version 87 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.