(data stored in ACNUC7421 zone)

SWISSPROT: TRML_AERHH

ID   TRML_AERHH              Reviewed;         156 AA.
AC   A0KEQ6;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   11-DEC-2019, entry version 81.
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=AHA_0188;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM
OS   1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK36903.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; CP000462; ABK36903.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_854721.1; NC_008570.1.
DR   SMR; A0KEQ6; -.
DR   STRING; 380703.AHA_0188; -.
DR   EnsemblBacteria; ABK36903; ABK36903; AHA_0188.
DR   GeneID; 4486818; -.
DR   KEGG; aha:AHA_0188; -.
DR   PATRIC; fig|380703.7.peg.181; -.
DR   eggNOG; ENOG4108UIQ; Bacteria.
DR   eggNOG; COG0219; LUCA.
DR   HOGENOM; HOG000272756; -.
DR   KO; K03216; -.
DR   Proteomes; UP000000756; 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   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   3: Inferred from homology;
DR   PRODOM; A0KEQ6.
DR   SWISS-2DPAGE; A0KEQ6.
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..156
FT                   /note="tRNA (cytidine(34)-2'-O)-methyltransferase"
FT                   /id="PRO_0000401941"
FT   BINDING         100
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT   BINDING         122
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT   BINDING         130
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
SQ   SEQUENCE   156 AA;  17649 MW;  C682BC49AF63E22F CRC64;
     MLDIVLYQPE IPPNTGNIIR LCANTGYRLH LIEPLGFEWD DKRVKRAGLD YHEFAEVKRW
     PNFEAFLEAV APTRVFACTT KGRTAHSAVQ FAAGDALLFG PESRGLPIEI IESLPFEQRL
     RIPMLPQSRS MNLANAVAVF VYESWRQLGY AGSLQE
//

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