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   04-NOV-2026, entry version 145.
DE   RecName: Full=tRNA (cytidine(34)/5-carboxymethylaminomethyluridine(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(34)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885};
DE   AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885};
GN   Name=trmL {ECO:0000255|HAMAP-Rule:MF_01885};
GN   Synonyms=yibK {ECO:0000303|PubMed:12596263};
GN   OrderedLocusNames=HI_0766;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; 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] {ECO:0007744|PDB:1J85, ECO:0007744|PDB:1MXI}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, AND
RP   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: S-adenosyl-L-methionine-dependent methyltransferase that
CC       specifically methylates the ribose at the nucleotide 34 wobble position
CC       in the two leucyl isoacceptors tRNA(Leu)(CAA) and tRNA(Leu)(UAA). It
CC       leads to the formation of 2'-O-methylcytidine (Cm34) in tRNA(Leu)(CAA)
CC       and 5-carboxymethylaminomethyl-2'-O-methyluridine (cmnm5Um34) in
CC       tRNA(Leu)(UAA). The enzyme requires the presence of 2-methylthio-N6-
CC       isopentenyladenosine at position 37 (ms2i6A37) for activity.
CC       {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 + S-adenosyl-L-homocysteine + H(+);
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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43085;
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) + S-adenosyl-L-homocysteine + H(+);
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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43089;
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   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   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; AAGCHKM; -.
DR   OrthoDB; 9789043at2; -.
DR   PhylomeDB; P44868; -.
DR   BioCyc; HINF71421:G1GJ1-806-MONOMER; -.
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:0141102; F:tRNA (5-carboxymethylaminomethyluridine(34)-2'-O-ribose)-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0141098; F:tRNA (cytidine(34)-2'-O-ribose)-methyltransferase activity; IEA:RHEA.
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   FunFam; 3.40.1280.10:FF:000002; Peptidylprolyl isomerase; 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; TrmL.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   NCBIfam; NF007683; trmL; 1.
DR   NCBIfam; TIGR00185; tRNA_yibK_trmL; 1.
DR   PANTHER; PTHR42971; TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR42971:SF1; TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   PIRSF; PIRSF029256; SpoU_TrmH_prd; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 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)/5-
FT                   carboxymethylaminomethyluridine(34)-2'-O)-
FT                   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:0000305|PubMed:12596263, ECO:0007744|PDB:1MXI"
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:0000305|PubMed:12596263, ECO:0007744|PDB:1MXI"
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:0000305|PubMed:12596263, ECO:0007744|PDB:1MXI"
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:0000305|PubMed:12596263, ECO:0007744|PDB:1MXI"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01885,
FT                   ECO:0000305|PubMed:12596263, ECO:0007744|PDB:1MXI"
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:6AHW"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:6AHW"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:6AHW"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:6AHW"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:1MXI"
FT   HELIX           133..147
FT                   /evidence="ECO:0007829|PDB:6AHW"
FT   TURN            148..152
FT                   /evidence="ECO:0007829|PDB:6AHW"
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
//