Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phenylalanine--tRNA ligase alpha subunit |
Protein Synonyms/Alias | PheRS |
Gene Name | pheS |
Gene Synonyms/Alias | SPD_0504 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | 229 | LVVGKNISMADLQGT | S | HTP | [1] | |
Reference | [1]Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. Sun X,Ge F,Xiao CL,Yin XF,Ge R,Zhang LH,He QY J. Proteome Res. 2010, Jan;9(1):275-82. [ PMID:19894762] |
Functional Description From UniProt | |
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| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Proteinbiosynthesis |
Protein Sequence | MSTIEEQLKA LREETLTSLK QITAGNEKEM QDLRVSVLGK KGSLTEILKG MKDVSAEMRP 60 IIGKHVNEAR DVLTAAFEET AKLLEEKKVA AQLASESIDV TLPGRPVATG HRHVLTQTSE 120 EIEDIFIGMG YQVVDGFEVE QDYYNFERMN LPKDHPARDM QDTFYITEEI LLRTHTSPVQ 180 ARAMDAHDFS KGPLKMISPG RVFRRDTDDA THSHQFHQIE GLVVGKNISM ADLQGTLQLI 240 VQKMFGEERQ IRLRPSYFPF TEPSVEVDVS CFKCGGEGCN VCKKTGWIEI MGAGMVHPRV 300 LEMSGIDATV YSGFAFGLGQ ERVAMLRYGI NDIRGFYQGD VRFSEQFK 348 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0000287 F:magnesium ion binding IEA:UniProtKB-HAMAP GO:0004826 F:phenylalanine-tRNA ligase activity IEA:UniProtKB-HAMAP GO:0000049 F:tRNA binding IEA:InterPro GO:0006432 P:phenylalanyl-tRNA aminoacylation IEA:UniProtKB-HAMAP |
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