| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tyrosine--tRNA ligase |
Protein Synonyms/Alias | TyrRS |
Gene Name | tyrS |
Gene Synonyms/Alias | SPD_1926 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | | 330 | AGNIKNLSVKELKQG | S | HTP | [1] | | 318 | YKEALNITEQLFAGN | T | 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 | FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (By similarity) |
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| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Nucleotide-binding; Proteinbiosynthesis; RNA-binding |
Protein Sequence | MHIFDELKER GLIFQTTDEE ALRKALEEGQ VSYYTGYDPT ADSLHLGHLV AILTSRRLQL 60
AGHKPYALVG GATGLIGDPS FKDAERSLQT KDTVDGWVKS IQGQLSRFLD FENGENKAVM 120
VNNYDWFGSI SFIDFLRDIG KYFTVNYMMS KESVKKRIET GISYTEFAYQ IMQGYDFFVL 180
NQDHNVTLQI GGSDQWGNMT AGTELLRRKA DKTGHVITVP LITDATGKKF GKSEGNAVWL 240
NPEKTSPYEM YQFWMNVMDA DAVRFLKIFT FLSLDEIEDI RKQFEAAPHE RLAQKVLARE 300
VVTLVHGEEA YKEALNITEQ LFAGNIKNLS VKELKQGLRG VPNYQVQADE NNNIVELLVS 360
SGIVNSKRQA REDVQNGAIY VNGDRIQELD YVLSDADKLE NELTVIRRGK KKYFVLTY 418 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0003723 F:RNA binding IEA:UniProtKB-KW GO:0004831 F:tyrosine-tRNA ligase activity IEA:UniProtKB-HAMAP GO:0006437 P:tyrosyl-tRNA aminoacylation IEA:UniProtKB-HAMAP |
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