ID Q7WRS1_BACCE Unreviewed; 422 AA.
AC Q7WRS1;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE Flags: Fragment;
GN Name=ileS1 {ECO:0000313|EMBL:AAP22279.1};
OS Bacillus cereus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396 {ECO:0000313|EMBL:AAP22279.1};
RN [1] {ECO:0000313|EMBL:AAP22279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GSK-BRL1243 {ECO:0000313|EMBL:AAP22279.1}, and GSK-BRL1244
RC {ECO:0000313|EMBL:AAP22280.1};
RX PubMed=12792655; DOI=10.1038/sj.embor.embor881;
RA Brown J.R., Gentry D., Becker J.A., Ingraham K., Holmes D.J.,
RA Stanhope M.J.;
RT "Horizontal transfer of drug-resistant aminoacyl-transfer-RNA synthetases
RT of anthrax and Gram-positive pathogens.";
RL EMBO Rep. 4:692-698(2003).
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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000256|ARBA:ARBA00006887}.
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DR EMBL; AY282435; AAP22279.1; -; Genomic_DNA.
DR EMBL; AY282436; AAP22280.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7WRS1; -.
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; HUPs; 2.
DR Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:AAP22279.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 2..422
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP22279.1"
FT NON_TER 422
FT /evidence="ECO:0000313|EMBL:AAP22279.1"
SQ SEQUENCE 422 AA; 48082 MW; 9E0263780A617BC5 CRC64;
VAEFRKLCAE YAYEQVERQR EQFKRLGVRA DWDNPYITLE PAYEAQQIKV FGDMAKKGYI
YKGQKPVYWS PTSESALAEA EIEYQDKKSA SIYVAFPVKD GKNVLEGDEK YIIWTTTPWT
LPANLGISVH PELEYSIVKV NDEKYIIASE LFETVAKTLE WENAEVVKTV KGSELEYTVA
KHPFYNRDSL VMLGDHVTTD AGTGCVHTAP GHGEDDFVVG KKYGLEVLCP VDDKGVLTNE
APGFEGLFYD KANKPITEKL EEVGALLKLT FITHSYPHDW RTKKPIIFRA TAQWFASIEA
FRKELIEAVA ETKWVPAWGE TRLHNMVRDR GDWCISRQRA WGVPIPVFYA ENGDPIITDE
TINHVADLFR EHGSNVWFER EAKDLLPEGF THPGSPNGEF RKETDIMDVW FDSGSSHQAV
LE
//
