Reviewed,
UniProtKB/Swiss-Prot Q8CGC7 (SYEP_MOUSE)
Last modified
October 13, 2009.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional aminoacyl-tRNA synthetase Including the following 2 domains: 1- Recommended name: Glutamyl-tRNA synthetase EC=6.1.1.17 Alternative name(s): Glutamate--tRNA ligase 2- Recommended name: Prolyl-tRNA synthetase EC=6.1.1.15 Alternative name(s): Proline--tRNA ligase | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1512 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA By similarity. |
| Catalytic activity | ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). |
| Subunit structure | Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L By similarity. |
| Domain | The WHEP-TRS domain is involved in RNA binding By similarity. |
| Sequence similarities | In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family. In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family. Contains 3 WHEP-TRS domains. |
| Sequence caution | The sequence AAH40802.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Coding sequence diversity | Polymorphism |
| Domain | Repeat |
| Ligand | ATP-binding Nucleotide-binding RNA-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro prolyl-tRNA aminoacylationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA bindingInferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activityInferred from electronic annotation. Source: EC proline-tRNA ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1512 | 1512 | Bifunctional aminoacyl-tRNA synthetase | PRO_0000119744 | |||||
Regions | |||||||||
| Domain | 749 – 805 | 57 | WHEP-TRS 1 | ||||||
| Domain | 822 – 878 | 57 | WHEP-TRS 2 | ||||||
| Domain | 900 – 956 | 57 | WHEP-TRS 3 | ||||||
| Nucleotide binding | 432 – 436 | 5 | ATP By similarity | ||||||
| Region | 164 – 759 | 596 | Glutamyl-tRNA synthetase | ||||||
| Region | 760 – 956 | 197 | 3 X 57 AA approximate repeats | ||||||
| Region | 1007 – 1512 | 506 | Prolyl-tRNA synthetase | ||||||
| Motif | 204 – 214 | 11 | "HIGH" region | ||||||
| Motif | 432 – 436 | 5 | "KMSKS" region | ||||||
| Compositional bias | 959 – 991 | 33 | Asp/Glu/Lys-rich | ||||||
Sites | |||||||||
| Binding site | 211 | 1 | ATP By similarity | ||||||
| Binding site | 398 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 300 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 417 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 498 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 535 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 542 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 637 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 788 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 872 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 883 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 885 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1156 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1503 | 1 | N6-acetyllysine By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 871 | 1 | D → E | ||||||
Experimental info | |||||||||
| Sequence conflict | 94 | 1 | R → G in AAH40802. Ref.1 | ||||||
| Sequence conflict | 172 | 1 | N → S in AAH40802. Ref.1 | ||||||
| Sequence conflict | 618 | 1 | S → P in AAH40802. Ref.1 | ||||||
| Sequence conflict | 986 | 1 | G → R in X54327. Ref.3 | ||||||
| Sequence conflict | 1141 | 1 | A → P in AAH94679. Ref.1 | ||||||
| Sequence conflict | 1290 | 1 | N → S in AAH94679. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Eye and Mammary tumor. |
| [2] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962. Strain: C57BL/6J. Tissue: Pancreas. |
| [3] | "M.musculus mRNA for glutamyl-tRNA synthetase." Knippers R. Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 406-1512. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| BC040802 mRNA. Translation: AAH40802.1. Sequence problems. BC094679 mRNA. Translation: AAH94679.1. AK148463 mRNA. Translation: BAE28568.1. X54327 mRNA. No translation available. | |
| IPI | IPI00339916. |
| RefSeq | NP_084011.1. |
| UniGene | Mm.154511 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FYJ based on UniProtKB P07814. |
| SMR | Q8CGC7. Positions 749-804, 826-875. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8CGC7. |
PTM databases | |
| PhosphoSite | Q8CGC7. |
Proteomic databases | |
| PRIDE | Q8CGC7. |
Genome annotation databases | |
| Ensembl | ENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615; Mus musculus. [Genome view] |
| GeneID | 107508. |
| KEGG | mmu:107508. |
| UCSC | uc007dze.1. mouse. uc007dzg.1. mouse. |
Organism-specific databases | |
| CTD | 107508. |
| MGI | MGI:97838. Eprs. |
Phylogenomic databases | |
| HOGENOM | Q8CGC7. |
| HOVERGEN | Q8CGC7. |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.15. 244. 6.1.1.17. 244. |
Gene expression databases | |
| ArrayExpress | Q8CGC7. |
| Bgee | Q8CGC7. |
| CleanEx | MM_EPRS. |
| Genevestigator | Q8CGC7. |
| GermOnline | ENSMUSG00000026615. Mus musculus. |
Family and domain databases | |
| InterPro | IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR001412. aa-tRNA-synth_I_CS. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004154. Anticodon_bd. IPR004526. Glu-tRNA-synth_Ic_arc/euk. IPR000924. Glu/Gln-tRNA-synth_Ic. IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom. IPR020059. Glu/Gln-tRNA-synth_Ic_codon-bd. IPR020060. Glu/Gln-tRNA-synth_Ic_N. IPR010987. Glutathione-S-Trfase_C-like. IPR004499. Pro-tRNA-synth_IIa_pro-type. IPR016061. Pro-tRNA_synth_II_C. IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl. IPR009068. S15_NS1_RNA_bd. IPR000738. WHEP-TRS. [Graphical view] |
| Gene3D | G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:1.20.1050.10. GST_C_like. 1 hit. G3DSA:3.30.110.30. Pro-tRNA-synth_II_C_arc/euk. 1 hit. G3DSA:2.40.240.10. Rbsml_L25/Gln-tRNA_synth_b-brl. 1 hit. G3DSA:1.10.287.10. S15_NS1_RNA_bd. 3 hits. |
| PANTHER | PTHR10119. Glu_tRNA-synt_1c. 1 hit. |
| Pfam | PF03129. HGTP_anticodon. 1 hit. PF09180. ProRS-C_1. 1 hit. PF00749. tRNA-synt_1c. 1 hit. PF03950. tRNA-synt_1c_C. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF00458. WHEP-TRS. 3 hits. [Graphical view] |
| PRINTS | PR00987. TRNASYNTHGLU. |
| TIGRFAMs | TIGR00463. gltX_arch. 1 hit. TIGR00408. proS_fam_I. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. PS50862. AA_TRNA_LIGASE_II. 1 hit. PS00762. WHEP_TRS_1. 2 hits. PS51185. WHEP_TRS_2. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 358934. |
| SOURCE | Search... |
Entry information
| Entry name | SYEP_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8CGC7 Secondary accession number(s): Q3UFJ2, Q4VC16 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


