SYI_STRA3
ID SYI_STRA3 Reviewed; 930 AA.
AC Q8E6N1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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}; OrderedLocusNames=gbs0532;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(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}.
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DR EMBL; AL766845; CAD46176.1; -; Genomic_DNA.
DR RefSeq; WP_000768154.1; NC_004368.1.
DR AlphaFoldDB; Q8E6N1; -.
DR SMR; Q8E6N1; -.
DR STRING; 211110.gbs0532; -.
DR EnsemblBacteria; CAD46176; CAD46176; CAD46176.
DR KEGG; san:gbs0532; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_0_9; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000000823; 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 Gene3D; 3.40.50.620; -; 2.
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 Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 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..930
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098476"
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; 104909 MW; 755EEF3B81F805BE 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 YVVVAPVGSE 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 TSEIYRKIRN TLRFLIANTS
DFNPKQDAVA YENLGAVDRY MTIKFNQVVD TINKAYAAYD FMAIYKAVVN FVTVDLSAFY
LDFAKDVVYI EAANSPERRR MQTVFYDILV KLTKLLTPIL PHTAEEIWSY LEHEEEEFVQ
LAEMPVAQTF SGQEEILEEW SAFMTLRTQA QKALEEARNA KVIGKSLEAH LTIYASQEVK
TLLTALNSDI ALLMIVSQLT IADEADKPAD SVSFEGVAFT VEHAEGEVCE RSRRIDPTTR
MRSYGVAVCD ASAAIIEQYY PEAVAQGFEA
