(data stored in ACNUC1104 zone)

SWISSPROT: D3VGD7_XENNA

ID   D3VGD7_XENNA            Unreviewed;       167 AA.
AC   D3VGD7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   RecName: Full=tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885};
DE            EC=2.1.1.207 {ECO:0000256|HAMAP-Rule:MF_01885};
DE   AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmL {ECO:0000256|HAMAP-Rule:MF_01885};
GN   Name=yibK {ECO:0000313|EMBL:CBJ88227.1};
GN   Synonyms=trmL {ECO:0000256|HAMAP-Rule:MF_01885};
GN   OrderedLocusNames=XNC1_0139 {ECO:0000313|EMBL:CBJ88227.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88227.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88227.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble
CC       position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and
CC       tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-
CC       adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.
CC       {ECO:0000256|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-
CC         homocysteine; Xref=Rhea:RHEA:43088, Rhea:RHEA-COMP:10333,
CC         Rhea:RHEA-COMP:10334, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74508, ChEBI:CHEBI:74511;
CC         EC=2.1.1.207; Evidence={ECO:0000256|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-
CC         COMP:10332, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC         EC=2.1.1.207; Evidence={ECO:0000256|HAMAP-Rule:MF_01885};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01885}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase TrmH family.
CC       TrmL subfamily. {ECO:0000256|HAMAP-Rule:MF_01885}.
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DR   EMBL; FN667742; CBJ88227.1; -; Genomic_DNA.
DR   RefSeq; WP_010847601.1; NC_014228.1.
DR   STRING; 406817.XNC1_0139; -.
DR   EnsemblBacteria; CBJ88227; CBJ88227; XNC1_0139.
DR   KEGG; xne:XNC1_0139; -.
DR   eggNOG; ENOG4108UIQ; Bacteria.
DR   eggNOG; COG0219; LUCA.
DR   HOGENOM; HOG000272757; -.
DR   KO; K03216; -.
DR   OMA; AGLDYWH; -.
DR   Proteomes; UP000008075; 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; D3VGD7.
DR   SWISS-2DPAGE; D3VGD7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885,
KW   ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:CBJ88227.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01885,
KW   ECO:0000256|PIRSR:PIRSR029256-1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01885,
KW   ECO:0000256|SAAS:SAAS00477754, ECO:0000313|EMBL:CBJ88227.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT   DOMAIN        2    151       SpoU_methylase. {ECO:0000259|Pfam:
FT                                PF00588}.
FT   BINDING      88     88       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_01885,
FT                                ECO:0000256|PIRSR:PIRSR029256-1}.
FT   BINDING     110    110       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01885, ECO:0000256|PIRSR:PIRSR029256-
FT                                1}.
FT   BINDING     132    132       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01885,
FT                                ECO:0000256|PIRSR:PIRSR029256-1}.
FT   BINDING     140    140       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01885,
FT                                ECO:0000256|PIRSR:PIRSR029256-1}.
SQ   SEQUENCE   167 AA;  18774 MW;  F80EBD8A9C3F753D CRC64;
     MLNIVLFEPE IPPNTGNIIR LCANTGCQLH LIQPLGFTWD DKRLRRAGLD YHEFANIKQH
     HDYNAFLESE GLSSVNSQSH SGARLFALTT KGTPAHSNVS YRDGDYLMFG PETRGLPSYV
     LDNMPPEQKI RIPMLSDSRS MNLSNTVAVV VFEAWRQLGY PGALLRD
//

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