ID SYI_STRA5 Reviewed; 930 AA. AC Q8E177; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002}; DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002}; DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002}; DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002}; GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; GN OrderedLocusNames=SAG0485; OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=208435; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-611 / 2603 V/R; RX PubMed=12200547; DOI=10.1073/pnas.182380799; RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N., RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D., RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D., RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A., RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T., RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.; RT "Complete genome sequence and comparative genomic analysis of an emerging RT human pathogen, serotype V Streptococcus agalactiae."; RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002). 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:0000255|HAMAP-Rule:MF_02002}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_02002}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and CC one for editing. The misactivated valine is translocated from the CC active site to the editing site, which sterically excludes the CC correctly activated isoleucine. The single editing site contains two CC valyl binding pockets, one specific for each substrate (Val-AMP or Val- CC tRNA(Ile)). {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}. 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; AE009948; AAM99387.1; -; Genomic_DNA. DR RefSeq; NP_687515.1; NC_004116.1. DR RefSeq; WP_000768163.1; NC_004116.1. DR AlphaFoldDB; Q8E177; -. DR SMR; Q8E177; -. DR STRING; 208435.SAG0485; -. DR KEGG; sag:SAG0485; -. DR PATRIC; fig|208435.3.peg.483; -. DR HOGENOM; CLU_001493_7_0_9; -. DR OrthoDB; 9810365at2; -. DR Proteomes; UP000000821; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1. DR CDD; cd00818; IleRS_core; 1. DR Gene3D; 1.10.730.20; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1. DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR033708; Anticodon_Ile_BEm. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023585; Ile-tRNA-ligase_type1. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR NCBIfam; TIGR00392; ileS; 1. DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..930 FT /note="Isoleucine--tRNA ligase" FT /id="PRO_0000098477" FT MOTIF 57..67 FT /note="'HIGH' region" FT MOTIF 595..599 FT /note="'KMSKS' region" FT BINDING 554 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT BINDING 598 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" SQ SEQUENCE 930 AA; 104897 MW; C77646FA00A10CDE CRC64; MKLKETLNLG QTAFPMRAGL PNKEPQWQEA WDQADIYKKR QALNEGKPAF HLHDGPPYAN GNIHVGHALN KISKDIIVRS KSMSGFRAPY VPGWDTHGLP IEQVLAKKGV KRKEMDLAEY LEMCRDYALS QVDKQRDDFK RLGVSADWEN PYITLTPDYE ADQVRVFGAM ADKGYIYRGA KPVYWSWSSE SALAEAEIEY HDIDSTSLYY ANKVKDGKGI LDTDTYIVVW TTTPFTVTAS RGLTVGPDME YVVVVPVGSE RKYLLAEVLV DSLAAKFGWE NFEIVTHHTG KELNHIVTEH PWDTEVEELV ILGDHVTTDS GTGIVHTAPG FGEDDYNVGI ANGLDVVVTV DSRGLMMENA GPDFEGQFYD KVTPLVKEKL GDLLLASEVI NHSYPFDWRT KKPIIWRAVP QWFASVSKFR QEILDEIEKT NFQPEWGKKR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMTKEVT DHVADLFAEY GSIVWWQRDA KDLLPAGYTH PGSPNGLFEK ETDIMDVWFD SGSSWNGVMN ARENLSYPAD LYLEGSDQYR GWFNSSLITS VAVNGHAPYK AVLSQGFVLD GKGEKMSKSL GNTILPSDVE KQFGAEILRL WVTSVDSSND VRISMDILKQ TSETYRKIRN TLRFLIANTS DFNPKQDAVA YENLGAVDRY MTIKFNQVVD TINKAYAAYD FMAIYKAVVN FVTVDLSAFY LDFAKDVVYI EAANSPERRR MQTVFYDILV KLTKLLTPIL PHTAEEIWSY LEHEEEEFVQ LAEMPVAQTF SGQEEILEEW SAFMTLRTQA QKALEEARNA KVIGKSLEAH LTIYASQEVK TLLTALNSDI ALLMIVSQLT IADEADKPAD SVSFEGVAFT VEHAEGEVCE RSRRIDPTTK MRSYGVAVCD ASAAIIEQYY PEAVAQGFEA //