| 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 | CA_C3038 |
Created Date | 3-June-2014 |
Organism | Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) |
NCBI Taxa ID | 272562 |
Phosphorylation | Position | Peptide | Code | Type | References | | 564 | FYTLLAISTSIFDKS | S | HTP | [1] | |
Reference | [1]Phosphoproteomic investigation of a solvent producing bacterium Clostridium acetobutylicum. Bai X,Ji Z Appl. Microbiol. Biotechnol. 2012, Jul;95(1):201-11. [ PMID:22627760] |
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) |
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| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome; Zinc |
Protein Sequence | MYKKVDSSKS FVDIERDVLK LWHEKEIVKK SFNSNQDGEY FSFYDGPPTA NGRPHVGHII 60
TRVMKDLIPR YKVMKGYKVP RKAGWDTHGL PVELEIEKKL GISGKPQIEE YGIEKFVKEC 120
KESVFSYVSL WKDMSEKLGY WVDMENPYVT YHNDYIESVW WALKQMWDKD LLYKGHKIVP 180
YCPRCGTALS SHEVAQGYKD VKEATAFVKF KVKGEENKYI LAWTTTPWTL PSNVALAINK 240
AYDYVEVINN GEHLILAKAL LTVLEGEYEV VSEFKGEKLL GMEYEQLFKF ANPDKKAFYV 300
VHGDFVTLSD GTGIVHIAPA YGEDDNMLGK KYDLPLINLV NGEGKFVDEV EPWKGLFVKK 360
ADPKILEYMK ENGTLYKSEK FTHSYPHCWR CDTPLLYYPR DSWFVRMTSL RDKLVENNNK 420
IHWYPDNIRT GRFGKFVENV IDWGISRDRY WGTPLPIWQC ECGHRDCVGS IEELKEKGIN 480
VPENIELHKP YIDEVKLTCP KCGKPMTRTE EVIDCWFDSG SMPFAQLHYP FENKEVFENT 540
FPAQFISEAV DQTRGWFYTL LAISTSIFDK SSFENCIVLG HVLDKHGLKM SKHKGNVVDP 600
FDVLDNQGAD ACRWHFYTSS APWLPTRFSQ EDVAETQRKF LSTLWNVYSF YVLYAEIDKF 660
NPNDYKDFVS GNVMDKWIVS RLNTLTKDVG NYLDSYGITQ AALEIQDFVD DLSNWYVRRN 720
RSRYWTQELT DDKVGAYVTL YRVLVTLSKV AAPFIPFMTE QIYQSLVTSI NEGAEESVHL 780
CKWPEYDESL IDSSLEEEMK LAISIVKLGR SARNGANIKN RQPLYEMRVS TKALPDYYGD 840
IIRDELNVKK VEFGADLSKY VNFEIKPNLP VLGKSYGKLI PKIRKEISSM DQMKLAERVR 900
SGEAVKIDVD GTEIELNSEN LLVTMQGLEG FAFAGIGEIG IVLETTITDE LREEGYLREV 960
LSKVQNMRKE SGFEVADKIE IYVSGNEKLE NVIRKFEDTI KKETLATDII YSENKEAAIY 1020
NINGEELNVF VKKNC 1035 |
| 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 |
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