TRMI_MYCTU
ID TRMI_MYCTU Reviewed; 280 AA.
AC P9WFZ1; L0TA90; O33253; Q7D7H7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase TrmI;
DE EC=2.1.1.220;
DE AltName: Full=tRNA(m1A58)-methyltransferase;
DE Short=tRNA(m1A58)MTase;
GN Name=trmI; OrderedLocusNames=Rv2118c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14960715; DOI=10.1093/nar/gkh207;
RA Varshney U., Ramesh V., Madabushi A., Gaur R., Subramanya H.S.,
RA RajBhandary U.L.;
RT "Mycobacterium tuberculosis Rv2118c codes for a single-component
RT homotetrameric m1A58 tRNA methyltransferase.";
RL Nucleic Acids Res. 32:1018-1027(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, SUBUNIT, AND DOMAIN.
RX PubMed=11554794; DOI=10.1006/jmbi.2001.4935;
RA Gupta A., Kumar P.H., Dineshkumar T.K., Varshney U., Subramanya H.S.;
RT "Crystal structure of Rv2118c: an AdoMet-dependent methyltransferase from
RT Mycobacterium tuberculosis H37Rv.";
RL J. Mol. Biol. 312:381-391(2001).
CC -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of
CC N(1)-methyladenine at position 58 (m1A58) in tRNA.
CC {ECO:0000269|PubMed:14960715}.
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:14960715};
CC -!- ACTIVITY REGULATION: Inhibited by Mg(2+).
CC {ECO:0000269|PubMed:14960715}.
CC -!- SUBUNIT: Homotetramer composed of a dimer of dimers.
CC {ECO:0000269|PubMed:11554794, ECO:0000269|PubMed:14960715}.
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:11554794}.
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; AL123456; CCP44893.1; -; Genomic_DNA.
DR PIR; A70513; A70513.
DR RefSeq; NP_216634.1; NC_000962.3.
DR RefSeq; WP_003411041.1; NZ_NVQJ01000058.1.
DR PDB; 1I9G; X-ray; 1.98 A; A=1-280.
DR PDBsum; 1I9G; -.
DR AlphaFoldDB; P9WFZ1; -.
DR SMR; P9WFZ1; -.
DR STRING; 83332.Rv2118c; -.
DR PaxDb; P9WFZ1; -.
DR DNASU; 887374; -.
DR GeneID; 45426093; -.
DR GeneID; 887374; -.
DR KEGG; mtu:Rv2118c; -.
DR TubercuList; Rv2118c; -.
DR eggNOG; COG2519; Bacteria.
DR OMA; VVYPKDA; -.
DR PhylomeDB; P9WFZ1; -.
DR BRENDA; 2.1.1.220; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:MTBBASE.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IDA:MTBBASE.
DR GO; GO:0030488; P:tRNA methylation; IDA:MTBBASE.
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; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..280
FT /note="tRNA (adenine(58)-N(1))-methyltransferase TrmI"
FT /id="PRO_0000407309"
FT BINDING 110..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|PubMed:11554794"
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|PubMed:11554794"
FT BINDING 161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|PubMed:11554794"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|PubMed:11554794"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 193..205
FT /evidence="ECO:0007829|PDB:1I9G"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1I9G"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:1I9G"
SQ SEQUENCE 280 AA; 30123 MW; D09F0CEFC6778935 CRC64;
MSATGPFSIG ERVQLTDAKG RRYTMSLTPG AEFHTHRGSI AHDAVIGLEQ GSVVKSSNGA
LFLVLRPLLV DYVMSMPRGP QVIYPKDAAQ IVHEGDIFPG ARVLEAGAGS GALTLSLLRA
VGPAGQVISY EQRADHAEHA RRNVSGCYGQ PPDNWRLVVS DLADSELPDG SVDRAVLDML
APWEVLDAVS RLLVAGGVLM VYVATVTQLS RIVEALRAKQ CWTEPRAWET LQRGWNVVGL
AVRPQHSMRG HTAFLVATRR LAPGAVAPAP LGRKREGRDG
