A0A9W5T935 · A0A9W5T935_BABOV
- ProteinPutative rRNA methyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids876 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Probable methyltransferase involved in the maturation of rRNA and in the biogenesis of ribosomal subunits.
Catalytic activity
- a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-methylribonucleotide in rRNA + H+ + S-adenosyl-L-homocysteine
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 56 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 58 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 76 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 117 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 157 | Proton acceptor | ||||
Sequence: K |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleolus | |
Cellular Component | preribosome, large subunit precursor | |
Cellular Component | ribosome | |
Molecular Function | rRNA (guanine) methyltransferase activity | |
Molecular Function | rRNA (uridine-2'-O-)-methyltransferase activity | |
Biological Process | maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) | |
Biological Process | maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutative rRNA methyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia
Accessions
- Primary accessionA0A9W5T935
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-213 | Ribosomal RNA methyltransferase FtsJ | ||||
Sequence: YRARSAFKIIQLAKKFNIFENCNVLVDLCAAPGGWLQVAAKHLPISSIIVGVDLVPIRPIKGVVTIQADIRTQRCRNLISQQLRGAEVDVVLHDGAPNVGANWNLDAFNQNVLVLEAAKLASQVLRKGGIFVTKIFRYLSLCINHIMLYRSADYNSLIWTLGKCFERVKVTKPSSSRNVSAEIFAVCIGF | ||||||
Domain | 256-415 | DUF3381 | ||||
Sequence: QRKKVNKEGYEEGDDFREYNILDFVTTDNPPQMLVSSNRFVFRPRDKPETLEKDNELLKQILSHPLTTEEVRLLCSDLKVAGRSDLHHLLKWRHKICKDLFPVDKKPKVENEVAAYPEQVEEPEEDTLKRQELEVADRVRKELRRTERKQRRAMMKHKKA | ||||||
Region | 396-415 | Disordered | ||||
Sequence: KELRRTERKQRRAMMKHKKA | ||||||
Region | 466-661 | Disordered | ||||
Sequence: ILYAGSDDNTSEADSMDLQFETDSEDDDKIAKMEVDLEVQHEMSKLTEETRPKSTKKLTRRQRVNEERGAELSSLLENMQYEARLKAQQEMQDSDDELDDSEDDDTGASGDVTDVEVIDDSQGGDDTNQIISEESPGETKATKTSGPTKDDRDTKRALEDAMIDRWFDQDVFHDQPRETARKQKTRENKNAKAKNK | ||||||
Compositional bias | 490-535 | Basic and acidic residues | ||||
Sequence: EDDDKIAKMEVDLEVQHEMSKLTEETRPKSTKKLTRRQRVNEERGA | ||||||
Compositional bias | 558-575 | Acidic residues | ||||
Sequence: DSDDELDDSEDDDTGASG | ||||||
Compositional bias | 587-608 | Polar residues | ||||
Sequence: QGGDDTNQIISEESPGETKATK | ||||||
Compositional bias | 609-659 | Basic and acidic residues | ||||
Sequence: TSGPTKDDRDTKRALEDAMIDRWFDQDVFHDQPRETARKQKTRENKNAKAK | ||||||
Domain | 661-866 | Ribosomal RNA methyltransferase SPB1-like C-terminal | ||||
Sequence: KEPTFTVVPAISDADAVERARDAIELELSRNKETIAEVQAMGSLLVNKDTRMALIDGAYNKRTFDDGELPSWFEEDEKKHSNYELPVTKELMKRYKAKLHELKNRPIRKVLEARGRRKLRVERKLKSVLPRVEALQNSDTGGARTAKKLLRKVQNTASNKREKVYVVSRRGGTTTTAPTGGKGSRKVTKAVDKRMKKDNVRQKRKP | ||||||
Region | 830-876 | Disordered | ||||
Sequence: RGGTTTTAPTGGKGSRKVTKAVDKRMKKDNVRQKRKPKSRSRKARIH | ||||||
Compositional bias | 858-876 | Basic residues | ||||
Sequence: DNVRQKRKPKSRSRKARIH |
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length876
- Mass (Da)99,817
- Last updated2023-11-08 v1
- ChecksumF4DF4670341615E3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 490-535 | Basic and acidic residues | ||||
Sequence: EDDDKIAKMEVDLEVQHEMSKLTEETRPKSTKKLTRRQRVNEERGA | ||||||
Compositional bias | 558-575 | Acidic residues | ||||
Sequence: DSDDELDDSEDDDTGASG | ||||||
Compositional bias | 587-608 | Polar residues | ||||
Sequence: QGGDDTNQIISEESPGETKATK | ||||||
Compositional bias | 609-659 | Basic and acidic residues | ||||
Sequence: TSGPTKDDRDTKRALEDAMIDRWFDQDVFHDQPRETARKQKTRENKNAKAK | ||||||
Compositional bias | 858-876 | Basic residues | ||||
Sequence: DNVRQKRKPKSRSRKARIH |
Keywords
- Technical term