TRML_HAEIN
ID TRML_HAEIN Reviewed; 160 AA.
AC P44868;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885};
DE EC=2.1.1.207 {ECO:0000255|HAMAP-Rule:MF_01885};
DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmL {ECO:0000255|HAMAP-Rule:MF_01885};
GN Name=trmL {ECO:0000255|HAMAP-Rule:MF_01885}; OrderedLocusNames=HI_0766;
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 (1.7 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
RX PubMed=12596263; DOI=10.1002/prot.10323;
RA Lim K., Zhang H., Tempczyk A., Krajewski W., Bonander N., Toedt J.,
RA Howard A., Eisenstein E., Herzberg O.;
RT "Structure of the YibK methyltransferase from Haemophilus influenzae
RT (HI0766): a cofactor bound at a site formed by a knot.";
RL Proteins 51:56-67(2003).
CC -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble position in
CC the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA).
CC Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH
CC of the wobble nucleotide. {ECO:0000255|HAMAP-Rule:MF_01885}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43084, Rhea:RHEA-COMP:10331, Rhea:RHEA-COMP:10332,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.207;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01885};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-
CC adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-
CC methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43088, Rhea:RHEA-COMP:10333, Rhea:RHEA-COMP:10334,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74508, ChEBI:CHEBI:74511; EC=2.1.1.207;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01885};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01885,
CC ECO:0000269|PubMed:12596263}.
CC -!- INTERACTION:
CC P44868; P44868: trmL; NbExp=4; IntAct=EBI-15618808, EBI-15618808;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01885}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01885}.
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DR EMBL; L42023; AAC22424.1; -; Genomic_DNA.
DR PIR; E64158; E64158.
DR RefSeq; NP_438925.1; NC_000907.1.
DR RefSeq; WP_005652354.1; NC_000907.1.
DR PDB; 1J85; X-ray; 2.00 A; A=1-160.
DR PDB; 1MXI; X-ray; 1.70 A; A=1-160.
DR PDB; 6AHW; X-ray; 1.56 A; A/B=1-160.
DR PDB; 7D51; X-ray; 2.68 A; A/B=1-160.
DR PDBsum; 1J85; -.
DR PDBsum; 1MXI; -.
DR PDBsum; 6AHW; -.
DR PDBsum; 7D51; -.
DR AlphaFoldDB; P44868; -.
DR SMR; P44868; -.
DR DIP; DIP-29173N; -.
DR STRING; 71421.HI_0766; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR EnsemblBacteria; AAC22424; AAC22424; HI_0766.
DR KEGG; hin:HI_0766; -.
DR PATRIC; fig|71421.8.peg.805; -.
DR eggNOG; COG0219; Bacteria.
DR HOGENOM; CLU_110125_1_0_6; -.
DR OMA; AGLDYWH; -.
DR PhylomeDB; P44868; -.
DR BioCyc; HINF71421:G1GJ1-806-MON; -.
DR EvolutionaryTrace; P44868; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002131; P:wobble position cytosine ribose methylation; IBA:GO_Central.
DR GO; GO:0002132; P:wobble position uridine ribose methylation; IBA:GO_Central.
DR CDD; cd18094; SpoU-like_TrmL; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_01885; tRNA_methyltr_TrmL; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR016914; tRNA_cyt/urid_MeTfrase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR42971; PTHR42971; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00185; tRNA_yibK_trmL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..160
FT /note="tRNA (cytidine(34)-2'-O)-methyltransferase"
FT /id="PRO_0000159819"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885,
FT ECO:0000269|PubMed:12596263"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885,
FT ECO:0000269|PubMed:12596263"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885,
FT ECO:0000269|PubMed:12596263"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885,
FT ECO:0000269|PubMed:12596263"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6AHW"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:6AHW"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:6AHW"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:6AHW"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:6AHW"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6AHW"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:6AHW"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6AHW"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1MXI"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1MXI"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1MXI"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1MXI"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:1MXI"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1MXI"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1MXI"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:1MXI"
FT TURN 148..152
FT /evidence="ECO:0007829|PDB:1MXI"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:7D51"
SQ SEQUENCE 160 AA; 18401 MW; 0E09ADB31E575026 CRC64;
MLDIVLYEPE IPQNTGNIIR LCANTGFRLH LIEPLGFTWD DKRLRRSGLD YHEFAEIKRH
KTFEAFLESE KPKRLFALTT KGCPAHSQVK FKLGDYLMFG PETRGIPMSI LNEMPMEQKI
RIPMTANSRS MNLSNSVAVT VYEAWRQLGY KGAVNLPEVK
