(data stored in ACNUC7421 zone)

SWISSPROT: B4SSI6_STRM5

ID   B4SSI6_STRM5            Unreviewed;       159 AA.
AC   B4SSI6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=trmL {ECO:0000256|HAMAP-Rule:MF_01885};
GN   OrderedLocusNames=Smal_0163 {ECO:0000313|EMBL:ACF49868.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49868.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49868.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49868.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF49868.1; -; Genomic_DNA.
DR   RefSeq; WP_012509719.1; NC_011071.1.
DR   STRING; 391008.Smal_0163; -.
DR   EnsemblBacteria; ACF49868; ACF49868; Smal_0163.
DR   KEGG; smt:Smal_0163; -.
DR   eggNOG; ENOG4108UIQ; Bacteria.
DR   eggNOG; COG0219; LUCA.
DR   HOGENOM; HOG000272756; -.
DR   KO; K03216; -.
DR   OMA; AGLDYWH; -.
DR   OrthoDB; 1578095at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00820-MONOMER; -.
DR   Proteomes; UP000001867; 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.
PE   3: Inferred from homology;
DR   PRODOM; B4SSI6.
DR   SWISS-2DPAGE; B4SSI6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885,
KW   ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:ACF49868.1};
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:ACF49868.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT   DOMAIN        7    147       SpoU_methylase. {ECO:0000259|Pfam:
FT                                PF00588}.
FT   BINDING      83     83       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:MF_01885,
FT                                ECO:0000256|PIRSR:PIRSR029256-1}.
FT   BINDING     105    105       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01885, ECO:0000256|PIRSR:PIRSR029256-
FT                                1}.
FT   BINDING     127    127       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     135    135       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01885,
FT                                ECO:0000256|PIRSR:PIRSR029256-1}.
SQ   SEQUENCE   159 AA;  17685 MW;  2CE18D2F5F6C4802 CRC64;
     MNAAPQFHVI LFQPEIPPNT GNVIRLCANT GAQLHLVEPL GFALEDKQLK RAGLDYHEYS
     RLQVHPDLDT ALARIAPKRL FALSTRASVR YDSVAFDDGD AFLFGPESRG LPQDVLDALP
     DGHRLRLPMR PDNRSLNLSN TVAVVMYEAW RQHGFAGGQ
//

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