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 | Saci_0599 |
Created Date | 3-June-2014 |
Organism | Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) |
NCBI Taxa ID | 330779 |
Phosphorylation | Position | Peptide | Code | Type | References | 24 | YWDDNNIYKKLKEIN | Y | HTP | [1] | 1050 | SKADVSVSMTSKFDP | S | HTP | [1] | 375 | SASEEIISDLKQRSA | S | HTP | [1] | |
Reference | [1]Archaeal signal transduction: impact of protein phosphatase deletions on cell size, motility, and energy metabolism in Sulfolobus acidocaldarius. Reimann J,Esser D,Orell A,Amman F,Pham TK,Noirel J,Lindås AC,Bernander R,Wright PC,Siebers B,Albers SV Mol. Cell Proteomics 2013, Dec;12(12):3908-23. [ PMID:24078887] |
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; Zinc |
Protein Sequence | MTSKFDPLKF EEEVLKYWDD NNIYKKLKEI NEKNHKKFLF IDGPPYPSSP IPHIGTVWNK 60 TIKDCILRYE RLMGYSVKDQ PGYDTHGLPI EVETEKRLGI KSKAEIIEKV GVDNFISKCK 120 EFAVNNSKSL TQNFRNLGIF MDWENPYFTF NNDYISNSWA VIKKAYERGL LYKGVHVLHW 180 CSRCETTLAD YEVSEYRDLE DPSIYVKFRV KGEPNRYLVI WTTTPWTLPA NVFVMINKDF 240 EYADVRVGDE ILVIAKDRVK ELMKEARIKE YKILRVYKGE ELLGLEYEHP LADIVSAQSK 300 INNHHKVLDG GEAVTLQEGT GLVHSAPGHG DVDFEIGKKY DMPVVMLVND KGEFTQDSGK 360 YAGKYVRSAS EEIISDLKQR SALLHASKIV HRYPVCWRCK TPLILRAIEQ WFIAVSKLKD 420 HLMGEIDRVR WIPDWGKTRI GNMVKEVRDW VISRQRFWGT PLPIWVCSNC QNIIVVGGVD 480 ELSKISINQV PQDLHRPWID SVVVRCEKCG GEARRISDVA DVWFDSGVAF FASLGQDWRK 540 RWSELGPVDL VLEGHDQLRG WFFSLLRTGV ILMDKAPYEA VLVHGFMLDE QGREMHKSSG 600 NYVEPSQVVS KYGRDTLRLW LLRNTTWEDA KFSWKSLDMT RRDLNIIWNV YVFANTYMSL 660 DEFKYSKYSY NDIKDYLKLE DIWLLSRYYR MLKEVIEAMK EYKVHELANK VTAFIIDDIS 720 RFYLRVTRKR AWNEANDPDK IAMYYVLYHV LKGSLILLST VIPFTAEKIY LDFVQERLES 780 ISMEKIPEIK EEFINSEIEE AFEVAKEIID AGLNARAKAG IKLRWPLKEV YVFLVSDKDR 840 RSIEKITDVL SSLLNSKSII IEGIDGYKRF SKIRATPNTG SIGPTFKRLS VKVAEYIQNN 900 SDKVAQDIVS KGYHEFNVDS ENLRLDISHV NLVEEVEKGY VSARFSKGVV LLKQEMSKEE 960 EEEGIIRDLI RRIQFMRKQL SLNVNEYILL SIRAPDDKVD LIKKWEQYIK NETRAKELRI 1020 GDVSGDLIQD WDVEEETYTI GVSKADVSVS 1050 |
| 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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