ID   SYI_STRP6               Reviewed;         933 AA.
AC   Q5XB14;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, 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=M6_Spy1264;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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}.
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DR   EMBL; CP000003; AAT87399.1; -; Genomic_DNA.
DR   RefSeq; WP_011184754.1; NC_006086.1.
DR   AlphaFoldDB; Q5XB14; -.
DR   SMR; Q5XB14; -.
DR   KEGG; spa:M6_Spy1264; -.
DR   HOGENOM; CLU_001493_7_1_9; -.
DR   Proteomes; UP000001167; 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.
FT   CHAIN           1..933
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098485"
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   933 AA;  105134 MW;  E3D722133D520025 CRC64;
     MKLKETLNLG KIAFPMRADL PNKEPQWQAA WEQAELYKKR QELNAGKPAF HLHDGPPYAN
     GNIHVGHALN KISKDIIVRS KSMSGFQAPY VPGWDTHGLP IEQVLAKQGI KRKEMNLAEY
     LEMCRQYALS QVDKQRDDFK RLGVSADWEN PYVTLDPQFE ADQIRVFGAM AEKGYIYRGA
     KPVYWSWSSE SALAEAEIEY HDIDSTSLYY ANKVKDGKGI LDTNTYIVVW TTTPFTVTAS
     RGLTVGPDMD YLVVKPAGSD RQYVVAEGLL DSLAGKFGWE SFETLASHKG ADLEYIVTEH
     PWDTDVEELV ILGDHVTLES GTGIVHTAPG FGEDDYNVGT KYKLEVAVTV DERGLMMENA
     GPDFHGQFYN KVTPIVIDKL GDLLLAQEVI NHSYPFDWRT KKPIIWRAVP QWFASVSDFR
     QDILDEIEKT TFHPSWGETR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMTKEVT
     DHVADLFQEN GSIIWWQKEA KDLLPEGFTH PGSPNGEFTK ETDIMDVWFD SGSSWNGVMN
     ARENLSYPAD LYLEGSDQYR GWFNSSLITS VAVNGHAPYK AILSQGFVLD GKGEKMSKSK
     GNIISPNDVA KQYGADILRL WVASVDTDND VRVSMEILGQ VSETYRKIRN TLRFLIANTS
     DFNPATDTVA YADLGAVDKY MTIVFNQLVA TITDAYERYD FMAIYKAVVN FVTVDLSAFY
     LDFAKDVVYI EAANSLERRR MQTVFYDILV KITKLLTPIL PHTTEEIWSY LEYESEAFVQ
     LAEMPVAETF SAQEDILEAW SAFMTLRTQA QKALEEARNA KIIGKSLEAH LTIYASEEVK
     TLLTALDSDI ALLLIVSQLT IADLADAPAD AVAFEGIAFM VEHAIGEVCE RSRRIDPTTR
     MRSYNAFVCD HSAKIIEENF PEAVAEGFEE SGK
//