ID A0A2E8MY86_9RICK Unreviewed; 382 AA. AC A0A2E8MY86; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 14-DEC-2022, entry version 14. DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165}; DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165}; DE Flags: Fragment; GN ORFNames=CMP48_08980 {ECO:0000313|EMBL:MBR07809.1}; OS Rickettsiales bacterium. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales. OX NCBI_TaxID=2026788 {ECO:0000313|EMBL:MBR07809.1, ECO:0000313|Proteomes:UP000230568}; RN [1] {ECO:0000313|Proteomes:UP000230568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS CC can inadvertently accommodate and process structurally similar amino CC acids such as valine, to avoid such errors it has two additional CC distinct tRNA(Ile)-dependent editing activities. One activity is CC designated as 'pretransfer' editing and involves the hydrolysis of CC activated Val-AMP. The other activity is designated 'posttransfer' CC editing and involves deacylation of mischarged Val-tRNA(Ile). CC {ECO:0000256|ARBA:ARBA00025217}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L- CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, CC ChEBI:CHEBI:456215; EC=6.1.1.5; CC Evidence={ECO:0000256|ARBA:ARBA00000114}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBR07809.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PBTY01000026; MBR07809.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2E8MY86; -. DR Proteomes; UP000230568; Unassembled WGS sequence. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.90.740.10; -; 1. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023586; Ile-tRNA-ligase_type2. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. PE 4: Predicted; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:MBR07809.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}. FT DOMAIN 19..380 FT /note="tRNA-synt_1" FT /evidence="ECO:0000259|Pfam:PF00133" FT NON_TER 382 FT /evidence="ECO:0000313|EMBL:MBR07809.1" SQ SEQUENCE 382 AA; 43464 MW; 60A813E8E54BB2C4 CRC64; MAKYPEYKQV SYPQIAEEVL KFWADQQIFE KSVTEREGAE TFTFYEGPPS ANGTPGIHHV MARTVKDIFC RYKTQKGYQV KRKGGWDTHG LPVELQVEKE LGIKKDDIGK TISVAEYNQK CKETVMRFKD EWDRLTQQMG YWVDLDDPYI TFDQKYMESL WHLLKKLYEK GLLYKGYTVQ PYSPAAGTGL SSHELNQPGT YKDVKDTSIV AQFKVKKDDR SSFLFESDDE DVRILAWTTT PWTLPSNCAL AVGEKITYVK VKSYNQYTGT AISVVLAKDL VGKFFSDKAK EVAFGDYKLG DKLIPFEIVS EFTGKDILEV RYEQLMPYVT NEDLEKNAFR VIPGDFVSTE DGTGVVHTAS VFGADDFRVA QQAGVPAVMV KD //