TRMO_HAEIN
ID TRMO_HAEIN Reviewed; 239 AA.
AC P44740;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=tRNA (adenine(37)-N6)-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P28634};
DE AltName: Full=tRNA (m6t6A37) methyltransferase;
DE AltName: Full=tRNA methyltransferase O {ECO:0000250|UniProtKB:P28634};
GN Name=trmO {ECO:0000250|UniProtKB:P28634};
GN Synonyms=tsaA {ECO:0000250|UniProtKB:P28634}; OrderedLocusNames=HI_0510;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), AND SUBUNIT.
RG Northeast structural genomics consortium (NESG);
RT "X-ray structure of yaeb from Haemophilus influenzae. Northeast structural
RT genomics research consortium (nesgc) target ir47.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase
CC responsible for the addition of the methyl group in the formation of
CC N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of
CC the tRNA anticodon loop of tRNA(Thr)(GGU). The methyl group of
CC m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA
CC decoding ability. Binds to tRNA. {ECO:0000250|UniProtKB:P28634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-
CC methionine = H(+) + N(6)-methyl,N(6)-L-threonylcarbamoyladenosine(37)
CC in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70027, Rhea:RHEA-
CC COMP:10163, Rhea:RHEA-COMP:17808, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74418,
CC ChEBI:CHEBI:188470; Evidence={ECO:0000250|UniProtKB:P28634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70028;
CC Evidence={ECO:0000250|UniProtKB:P28634};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the tRNA methyltransferase O family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22168.1; -; Genomic_DNA.
DR PIR; I64153; I64153.
DR RefSeq; NP_438668.1; NC_000907.1.
DR RefSeq; WP_005693665.1; NC_000907.1.
DR PDB; 1XQB; X-ray; 2.85 A; A/B=1-239.
DR PDBsum; 1XQB; -.
DR AlphaFoldDB; P44740; -.
DR SMR; P44740; -.
DR STRING; 71421.HI_0510; -.
DR EnsemblBacteria; AAC22168; AAC22168; HI_0510.
DR KEGG; hin:HI_0510; -.
DR PATRIC; fig|71421.8.peg.529; -.
DR eggNOG; COG1720; Bacteria.
DR HOGENOM; CLU_013458_3_0_6; -.
DR OMA; CFKEKFA; -.
DR PhylomeDB; P44740; -.
DR BioCyc; HINF71421:G1GJ1-523-MON; -.
DR EvolutionaryTrace; P44740; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0089715; F:tRNA m6t6A37 methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR CDD; cd09281; UPF0066; 1.
DR Gene3D; 2.40.30.70; -; 1.
DR InterPro; IPR023370; TrmO-like_N.
DR InterPro; IPR041369; TrmO_C.
DR InterPro; IPR023368; UPF0066_cons_site.
DR InterPro; IPR040372; YaeB-like.
DR InterPro; IPR036413; YaeB-like_sf.
DR InterPro; IPR036414; YaeB_N_sf.
DR PANTHER; PTHR12818; PTHR12818; 1.
DR Pfam; PF01980; TrmO; 1.
DR Pfam; PF18389; TrmO_C; 1.
DR SUPFAM; SSF118196; SSF118196; 1.
DR TIGRFAMs; TIGR00104; tRNA_TsaA; 1.
DR PROSITE; PS01318; TSAA_1; 1.
DR PROSITE; PS51668; TSAA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..239
FT /note="tRNA (adenine(37)-N6)-methyltransferase"
FT /id="PRO_0000155619"
FT DOMAIN 6..147
FT /note="TsaA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01003"
FT BINDING 23..25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 64..65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT BINDING 127..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O29998"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1XQB"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1XQB"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1XQB"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1XQB"
FT TURN 45..50
FT /evidence="ECO:0007829|PDB:1XQB"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:1XQB"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 100..113
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1XQB"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1XQB"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:1XQB"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1XQB"
FT TURN 181..186
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1XQB"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1XQB"
SQ SEQUENCE 239 AA; 27214 MW; E63FE78E7706106E CRC64;
MNDLTLSPIA IIHTPYKEKF SVPRQPNLVE DGVGIVELLP PYNSPEAVRG LEQFSHLWLI
FQFDQIQQGK WQPTVRPPRL GGNQRVGVFA SRATHRPNPL GLSKVELRQV ECINGNIFLH
LGAVDLVDGT PIFDIKPYIA YADSEPNAQS SFAQEKLPVK LTVEFTEQAK SAVKKREEKR
PHLSRFIRQV LEQDPRPAYQ QGKPSDRIYG MSLYEFNVKW RIKAGTVNCV EVIEIEKDK
