(data stored in SCRATCH zone)

SWISSPROT: Q3IID9_PSEHT

ID   Q3IID9_PSEHT            Unreviewed;       154 AA.
AC   Q3IID9;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 77.
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=PSHAa0371 {ECO:0000313|EMBL:CAI85469.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85469.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85469.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: S-adenosyl-L-methionine + 5-
CC       carboxymethylaminomethyluridine(34) in tRNA(Leu) = S-adenosyl-L-
CC       homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine(34)
CC       in tRNA(Leu). {ECO:0000256|HAMAP-Rule:MF_01885}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(34) in tRNA
CC       = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(34) in tRNA.
CC       {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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01885}.
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DR   EMBL; CR954246; CAI85469.1; -; Genomic_DNA.
DR   RefSeq; WP_011327082.1; NC_007481.1.
DR   ProteinModelPortal; Q3IID9; -.
DR   STRING; 326442.PSHAa0371; -.
DR   EnsemblBacteria; CAI85469; CAI85469; PSHAa0371.
DR   GeneID; 32568172; -.
DR   KEGG; pha:PSHAa0371; -.
DR   eggNOG; ENOG4108UIQ; Bacteria.
DR   eggNOG; COG0219; LUCA.
DR   HOGENOM; HOG000272756; -.
DR   KO; K03216; -.
DR   OMA; AGLDYWH; -.
DR   OrthoDB; POG091H02BS; -.
DR   Proteomes; UP000006843; Chromosome I.
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-HAMAP.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-HAMAP.
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; Q3IID9.
DR   SWISS-2DPAGE; Q3IID9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885,
KW   ECO:0000256|SAAS:SAAS00120900, ECO:0000313|EMBL:CAI85469.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
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:SAAS00121476, ECO:0000313|EMBL:CAI85469.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01885}.
FT   DOMAIN        2    142       SpoU_methylase. {ECO:0000259|Pfam:
FT                                PF00588}.
FT   BINDING     100    100       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01885, ECO:0000256|PIRSR:PIRSR029256-
FT                                1}.
FT   BINDING     122    122       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     130    130       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01885,
FT                                ECO:0000256|PIRSR:PIRSR029256-1}.
SQ   SEQUENCE   154 AA;  17496 MW;  C3A00F8F6C488C01 CRC64;
     MLDIVLYQPE IPPNTGNIIR LCANTGYSLH LIEPLGFAWD DKRIKRAGLD YHEFSHVQRH
     ASFEAYLEAC KPKKIYACTT KGSQFHHQAQ YEAGDCLVFG PETRGLPDEL IQSLPNEQRV
     RIPMQANSRS MNLSNAVSVF VYESWRQLGF PGAK
//

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