TRML_YERPE
ID TRML_YERPE Reviewed; 162 AA.
AC Q74Y93;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
GN OrderedLocusNames=YPO0071, YP_0071;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RC STRAIN=CO-92 / Biovar Orientalis;
RA Osipiuk J., Maltseva N., Peterson S., Anderson W.F., Joachimiak A.;
RT "X-ray crystal structure of putative RNA methyltransferase from Yersinia
RT pestis.";
RL Submitted (JUN-2010) to the PDB data bank.
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 -!- 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; AL590842; CAL18760.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60351.1; -; Genomic_DNA.
DR PIR; AG0009; AG0009.
DR RefSeq; WP_002208973.1; NZ_WUCM01000015.1.
DR RefSeq; YP_002345165.1; NC_003143.1.
DR PDB; 3N4J; X-ray; 1.47 A; A=1-162.
DR PDB; 3N4K; X-ray; 1.76 A; A/B=1-162.
DR PDBsum; 3N4J; -.
DR PDBsum; 3N4K; -.
DR AlphaFoldDB; Q74Y93; -.
DR SMR; Q74Y93; -.
DR STRING; 214092.YPO0071; -.
DR PaxDb; Q74Y93; -.
DR EnsemblBacteria; AAS60351; AAS60351; YP_0071.
DR GeneID; 57974521; -.
DR KEGG; ype:YPO0071; -.
DR KEGG; ypm:YP_0071; -.
DR PATRIC; fig|214092.21.peg.293; -.
DR eggNOG; COG0219; Bacteria.
DR HOGENOM; CLU_110125_1_0_6; -.
DR OMA; AGLDYWH; -.
DR EvolutionaryTrace; Q74Y93; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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..162
FT /note="tRNA (cytidine(34)-2'-O)-methyltransferase"
FT /id="PRO_0000401955"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3N4J"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:3N4J"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3N4J"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:3N4J"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:3N4J"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:3N4J"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:3N4J"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3N4J"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3N4J"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3N4J"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3N4J"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:3N4J"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3N4J"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:3N4J"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3N4J"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3N4J"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:3N4J"
SQ SEQUENCE 162 AA; 18234 MW; 3B0EBC1431E8ED60 CRC64;
MLNIVLFEPE IPPNTGNIIR LCANTGCQLH LIKPLGFTWD DKRLRRAGLD YHEFADIKHH
HDYQAFLDSE KLDSTQPARL FALTTKGTPA HSAVSYQAND YLLFGPETRG LPAYILDALP
AQQKIRIPMQ ADSRSMNLSN AVSVVVYEAW RQLGYPGALL KE
