Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Isoleucine--tRNA ligase |
Protein Synonyms/Alias | IleRS |
Gene Name | ileS |
Gene Synonyms/Alias | SPD_1472 |
Created Date | 3-June-2014 |
Organism | Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) |
NCBI Taxa ID | 373153 |
Phosphorylation | Position | Peptide | Code | Type | References | 6 | **MKLKDTLNLGKTE | T | HTP | [1] | 22 | PMRAGLPTKEPVWQK | 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 isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity) |
| |
| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Proteinbiosynthesis; Zinc |
Protein Sequence | MKLKDTLNLG KTEFPMRAGL PTKEPVWQKE WEYAKLYQRR QELNQGKPHF TLHDGPPYAN 60 GNIHVGHAMN KISKDIIVRS KSMSGFYAPF IPGWDTHGLP IEQVLSKQGV KRKEMDLVEY 120 LKLCREYALS QVDKQREDFK RLGVSGDWEN PYVTLTPDYE AAQIRVFGEM ANKGYIYRGA 180 KPVYWSWSSE SALAEAEIEY HDLVSTSLYY ANKVKDGKGV LDTDTYIVVW TTTPFTITAS 240 RGLTVGADID YVLVQPAGEA RKFVVAAELL TSLSEKFGWA DVQVLETYRG QELNHIVTEH 300 PWDTAVEELV ILGDHVTTDS GTGIVHTAPG FGEDDYNVGI ANNLEVAVTV DERGIMMKNA 360 GPEFEGQFYE KVVPTVIEKL GNLLLAQEEI SHSYPFDWRT KKPIIWRAVP QWFASVSKFR 420 QEILDEIEKV KFHSEWGKVR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMVAETI 480 EHVAQLFEEH GSSIWWERDA KDLLPEGFTH PGSPNGEFKK ETDIMDVWFD SGSSWNGVVV 540 NRPELTYPAD LYLEGSDQYR GWFNSSLITS VANHGVAPYK QILSQGFALD GKGEKMSKSL 600 GNTIAPSDVE KQFGAEILRL WVTSVDSSND VRISMDILSQ VSETYRKIRN TLRFLIANTS 660 DFNPAQDTVA YDELRSVDKY MTIRFNQLVK TIRDAYADFE FLTIYKALVN FINVDLSAFY 720 LDFAKDVVYI EGAKSLERRQ MQTVFYDILV KITKLLTPIL PHTAEEIWSY LEFETEDFVQ 780 LSELPEVQTF ANQEEILDTW AAFMDFRGQA QKALEEARNA KVIGKSLEAH LTVYPNEVVK 840 TLLEAVNSNV AQLLIVSELT IAEGPAPEAA LSFEDVAFTV ERATGEVCDR CRRIDPTTAE 900 RSYQAVICDH CASIVEENFA EAVAEGFEEK 930 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0002161 F:aminoacyl-tRNA editing activity IEA:InterPro GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0004822 F:isoleucine-tRNA ligase activity IEA:UniProtKB-HAMAP GO:0008270 F:zinc ion binding IEA:UniProtKB-HAMAP GO:0006428 P:isoleucyl-tRNA aminoacylation IEA:UniProtKB-HAMAP |
| |
| |
| |
| |
| |