Q2GIL5 (TRMD_ANAPZ) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 43.
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 (guanine-N(1)-)-methyltransferase EC=2.1.1.228 Alternative name(s): M1G-methyltransferase tRNA [GM37] methyltransferase | ||||
| Gene names |
| ||||
| Organism | Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 212042 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group |
Protein attributes
| Sequence length | 232 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Specifically methylates guanosine-37 in various tRNAs By similarity. HAMAP MF_00605 |
| Catalytic activity | S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA. HAMAP MF_00605 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00605 |
| Subcellular location | Cytoplasm Potential HAMAP MF_00605. |
| Sequence similarities | Belongs to the RNA methyltransferase TrmD family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | tRNA processing |
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | RNA binding Inferred from electronic annotation. Source: InterPro tRNA (guanine-N1-)-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 – 232 | 232 | tRNA (guanine-N(1)-)-methyltransferase HAMAP MF_00605 | PRO_0000257389 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Region | 132 – 137 | 6 | S-adenosyl-L-methionine binding By similarity | ||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Binding site | 112 | 1 | S-adenosyl-L-methionine; via amide nitrogen By similarity | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 1 – 8 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 10 – 12 | 3 | |||||||||||||||||||||||||||||||||||
| Turn | 25 – 27 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 31 – 37 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 38 – 41 | 4 | |||||||||||||||||||||||||||||||||||
| Turn | 64 – 66 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 70 – 77 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 82 – 89 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 95 – 102 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 105 – 110 | 6 | |||||||||||||||||||||||||||||||||||
| Helix | 119 – 125 | 7 | |||||||||||||||||||||||||||||||||||
| Beta strand | 128 – 131 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 142 – 152 | 11 | |||||||||||||||||||||||||||||||||||
| Helix | 192 – 195 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 202 – 209 | 8 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. Tettelin H.PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HZ. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | CP000235 Genomic DNA. Translation: ABD43497.1. | ||||||||||||
| RefSeq | YP_505786.1. NC_007797.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q2GIL5. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | Q2GIL5. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 3930029. | ||||||||||||
| GenomeReviews | Gene locus APH_1267 in contig CP000235_GR. | ||||||||||||
| KEGG | aph:APH_1267. | ||||||||||||
| NMPDR | fig|212042.5.peg.1214. | ||||||||||||
| PATRIC | 20951324. VBIAnaPha602_1358. | ||||||||||||
| TIGR | APH_1267. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0336. | ||||||||||||
| HOGENOM | HBG285805. | ||||||||||||
| OMA | VCGRFEG. | ||||||||||||
| PhylomeDB | Q2GIL5. | ||||||||||||
| ProtClustDB | PRK00026. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | APHA212042:APH_1267-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00605. TrmD. [Tree] | ||||||||||||
| InterPro | IPR016009. tRNA_m1G_MeTrfase. IPR002649. tRNA_m1G_MeTrfase_bac. IPR023148. tRNA_m1G_MeTrfase_C. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.1270.20. tRNA_m1G_MeTrfase_C. 1 hit. | ||||||||||||
| KO | K00554. | ||||||||||||
| PANTHER | PTHR10056. PTHR10056. 1 hit. | ||||||||||||
| Pfam | PF01746. tRNA_m1G_MT. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF000386. tRNA_mtase. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR00088. TrmD. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | TRMD_ANAPZ | ||||||||
| Accession | Primary (citable) accession number: Q2GIL5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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