P44868 (TRML_HAEIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 80.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: tRNA (cytidine(34)-2'-O)-methyltransferase EC=2.1.1.207 Alternative name(s): tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmL | ||||
| Gene names |
| ||||
| Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) | ||||
| Taxonomic identifier | 71421 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 160 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide By similarity. HAMAP MF_01885 |
| Catalytic activity | S-adenosyl-L-methionine + cytidine(34) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(34) in tRNA. HAMAP MF_01885 S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) = S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu). HAMAP MF_01885 |
| Subunit structure | Homodimer. Ref.2 |
| Subcellular location | Cytoplasm Potential HAMAP MF_01885. |
| Sequence similarities | Belongs to the RNA methyltransferase TrmH family. TrmL subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | tRNA processing |
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | RNA binding Inferred from electronic annotation. Source: InterPro RNA methyltransferase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 160 | 160 | tRNA (cytidine(34)-2'-O)-methyltransferase HAMAP MF_01885 | PRO_0000159819 | ||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||
| Binding site | 78 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen | |||||||||||||||||||||||||||||||||||
| Binding site | 100 | 1 | S-adenosyl-L-methionine; via amide nitrogen | |||||||||||||||||||||||||||||||||||
| Binding site | 122 | 1 | S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen | |||||||||||||||||||||||||||||||||||
| Binding site | 130 | 1 | S-adenosyl-L-methionine | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 3 – 8 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 12 – 25 | 14 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 28 – 33 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 42 – 45 | 4 | ||||||||||||||||||||||||||||||||||||
| Turn | 46 – 48 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 51 – 53 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 54 – 56 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 58 – 62 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 63 – 70 | 8 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 73 – 78 | 6 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 83 – 85 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 95 – 99 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 108 – 111 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 116 – 118 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 121 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 133 – 147 | 15 | ||||||||||||||||||||||||||||||||||||
| Turn | 148 – 152 | 5 | ||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
| [2] | "Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): a cofactor bound at a site formed by a knot." Lim K., Zhang H., Tempczyk A., Krajewski W., Bonander N., Toedt J., Howard A., Eisenstein E., Herzberg O. Proteins 51:56-67(2003) [PubMed: 12596263] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE, SUBUNIT. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L42023 Genomic DNA. Translation: AAC22424.1. | ||||||||||||||||||
| PIR | E64158. | ||||||||||||||||||
| RefSeq | NP_438925.1. NC_000907.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | P44868. | ||||||||||||||||||
| SMR | P44868. Positions 1-156. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-29173N. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 949782. | ||||||||||||||||||
| GenomeReviews | Gene locus HI_0766 in contig L42023_GR. | ||||||||||||||||||
| KEGG | hin:HI0766. | ||||||||||||||||||
| NMPDR | fig|71421.1.peg.734. | ||||||||||||||||||
| PATRIC | 20190183. VBIHaeInf48452_0805. | ||||||||||||||||||
| TIGR | HI_0766. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | HBG309728. | ||||||||||||||||||
| OMA | EAWRQNG. | ||||||||||||||||||
| ProtClustDB | CLSK870515. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | HINF71421:HI_0766-MONOMER. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| HAMAP | MF_01885. tRNA_methyltr_TrmL. [Tree] | ||||||||||||||||||
| InterPro | IPR001537. SpoU_MeTrfase. IPR016914. tRNA_cyt/urid_MeTfrase. [Graphical view] | ||||||||||||||||||
| KO | K03216. | ||||||||||||||||||
| PANTHER | PTHR12029:SF26. PTHR12029:SF26. 1 hit. | ||||||||||||||||||
| Pfam | PF00588. SpoU_methylase. 1 hit. [Graphical view] | ||||||||||||||||||
| PIRSF | PIRSF029256. SpoU_TrmH_prd. 1 hit. | ||||||||||||||||||
| TIGRFAMs | TIGR00185. RRNA_methyl_2. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | TRML_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P44868 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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