TRMI_THET2
ID TRMI_THET2 Reviewed; 255 AA.
AC Q8GBB2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase TrmI;
DE EC=2.1.1.220 {ECO:0000269|PubMed:12682365};
DE AltName: Full=tRNA(m1A58)-methyltransferase;
DE Short=tRNA(m1A58)MTase;
GN Name=trmI; OrderedLocusNames=TT_C0244;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=12682365; DOI=10.1093/nar/gkg314;
RA Droogmans L., Roovers M., Bujnicki J.M., Tricot C., Hartsch T., Stalon V.,
RA Grosjean H.;
RT "Cloning and characterization of tRNA (m1A58) methyltransferase (TrmI) from
RT Thermus thermophilus HB27, a protein required for cell growth at extreme
RT temperatures.";
RL Nucleic Acids Res. 31:2148-2156(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-253 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN,
RP AND MUTAGENESIS OF TYR-78; ASP-170 AND TYR-194.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=18262540; DOI=10.1016/j.jmb.2008.01.041;
RA Barraud P., Golinelli-Pimpaneau B., Atmanene C., Sanglier S.,
RA Van Dorsselaer A., Droogmans L., Dardel F., Tisne C.;
RT "Crystal structure of Thermus thermophilus tRNA m1A58 methyltransferase and
RT biophysical characterization of its interaction with tRNA.";
RL J. Mol. Biol. 377:535-550(2008).
CC -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of
CC N(1)-methyladenine at position 58 (m1A58) in tRNA. Is required for cell
CC growth at extreme temperatures. {ECO:0000269|PubMed:12682365}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00952,
CC ECO:0000269|PubMed:12682365};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18262540};
CC KM=2.7 uM for tRNA(Met) {ECO:0000269|PubMed:18262540};
CC -!- SUBUNIT: Homotetramer composed of a dimer of dimers.
CC {ECO:0000269|PubMed:12682365, ECO:0000269|PubMed:18262540}.
CC -!- DOMAIN: Contains a large catalytic C-terminal domain that binds S-
CC adenosyl-L-methionine and a smaller N-terminal domain that may play a
CC role in tRNA recognition. Domains are connected by a linker region.
CC {ECO:0000269|PubMed:18262540}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
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DR EMBL; AJ516007; CAD56705.2; -; Genomic_DNA.
DR EMBL; AE017221; AAS80592.1; -; Genomic_DNA.
DR RefSeq; WP_011172697.1; NC_005835.1.
DR PDB; 2PWY; X-ray; 1.70 A; A/B=1-253.
DR PDB; 5C0O; X-ray; 2.62 A; E/F/G/H=1-255.
DR PDB; 5C1I; X-ray; 3.10 A; A/B/C/D=5-253.
DR PDBsum; 2PWY; -.
DR PDBsum; 5C0O; -.
DR PDBsum; 5C1I; -.
DR AlphaFoldDB; Q8GBB2; -.
DR SMR; Q8GBB2; -.
DR STRING; 262724.TT_C0244; -.
DR EnsemblBacteria; AAS80592; AAS80592; TT_C0244.
DR KEGG; tth:TT_C0244; -.
DR eggNOG; COG2519; Bacteria.
DR HOGENOM; CLU_025402_0_1_0; -.
DR OMA; VVYPKDA; -.
DR OrthoDB; 944891at2; -.
DR BRENDA; 2.1.1.220; 2305.
DR SABIO-RK; Q8GBB2; -.
DR EvolutionaryTrace; Q8GBB2; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR PANTHER; PTHR12133; PTHR12133; 1.
DR Pfam; PF08704; GCD14; 1.
DR PIRSF; PIRSF017269; GCD14; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51620; SAM_TRM61; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..255
FT /note="tRNA (adenine(58)-N(1))-methyltransferase TrmI"
FT /id="PRO_0000204467"
FT BINDING 104..107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT MUTAGEN 78
FT /note="Y->A: 20-fold decrease in catalytic efficiency. No
FT change in Km for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:18262540"
FT MUTAGEN 170
FT /note="D->A: 300-fold decrease in catalytic efficiency.
FT Increase in Km for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:18262540"
FT MUTAGEN 194
FT /note="Y->A: 3-fold decrease in catalytic efficiency.
FT Increase in Km for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:18262540"
FT CONFLICT 254
FT /note="A -> G (in Ref. 1; CAD56705)"
FT /evidence="ECO:0000305"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:5C1I"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5C1I"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2PWY"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:2PWY"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5C1I"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:2PWY"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:5C0O"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2PWY"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2PWY"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:2PWY"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2PWY"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 185..196
FT /evidence="ECO:0007829|PDB:2PWY"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:2PWY"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 213..229
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2PWY"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5C0O"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:2PWY"
SQ SEQUENCE 255 AA; 28596 MW; D56E4CB77232AEC3 CRC64;
MAWPGPLLLK DRKGRAYLVF PKEGGVFHHH KGSVPHEALL EAGPGGVVRT HLGEELSVHR
PTLEEYLLHM KRSATPTYPK DASAMVTLLD LAPGMRVLEA GTGSGGLTLF LARAVGEKGL
VESYEARPHH LAQAERNVRA FWQVENVRFH LGKLEEAELE EAAYDGVALD LMEPWKVLEK
AALALKPDRF LVAYLPNITQ VLELVRAAEA HPFRLERVLE VGWREWEVRL PVAHPRFQQV
GHTAFLVALR RWKAS
