(data stored in SCRATCH zone)

SWISSPROT: A8FPV5_SHESH

ID   A8FPV5_SHESH            Unreviewed;       154 AA.
AC   A8FPV5;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 59.
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=Ssed_0265 {ECO:0000313|EMBL:ABV34878.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34878.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34878.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34878.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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: 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; CP000821; ABV34878.1; -; Genomic_DNA.
DR   RefSeq; WP_012004404.1; NC_009831.1.
DR   ProteinModelPortal; A8FPV5; -.
DR   STRING; 425104.Ssed_0265; -.
DR   EnsemblBacteria; ABV34878; ABV34878; Ssed_0265.
DR   KEGG; sse:Ssed_0265; -.
DR   eggNOG; ENOG4108UIQ; Bacteria.
DR   eggNOG; COG0219; LUCA.
DR   HOGENOM; HOG000272756; -.
DR   KO; K03216; -.
DR   OMA; AGLDYWH; -.
DR   OrthoDB; POG091H02BS; -.
DR   Proteomes; UP000002015; 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-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; A8FPV5.
DR   SWISS-2DPAGE; A8FPV5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885,
KW   ECO:0000256|SAAS:SAAS00120900, ECO:0000313|EMBL:ABV34878.1};
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:SAAS00121476, ECO:0000313|EMBL:ABV34878.1};
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;  17305 MW;  F35E361F3786C844 CRC64;
     MFHIALFEPE IAPNTGNIIR LCANNGCQLH LIEPMGFDLE EKKLRRAGLD YSDLTRVTRH
     KDFESFLAAM DGKRIMACTT KGSRPHTELA YEKEDVLLFG PETRGLPIEI IESLPTTQRL
     KIPMTANSRS LNLSNAVAII SYEAWRQIGF EGAV
//

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