ID   SYI_LEIXX               Reviewed;        1119 AA.
AC   Q6AFZ0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=Lxx07970;
OS   Leifsonia xyli subsp. xyli (strain CTCB07).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=281090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07;
RX   PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA   Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA   de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA   Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA   El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT   subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(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_02003}.
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_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02003}.
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_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; AE016822; AAT88705.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6AFZ0; -.
DR   SMR; Q6AFZ0; -.
DR   STRING; 281090.Lxx07970; -.
DR   PRIDE; Q6AFZ0; -.
DR   EnsemblBacteria; AAT88705; AAT88705; Lxx07970.
DR   KEGG; lxx:Lxx07970; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OMA; KMMAPFT; -.
DR   Proteomes; UP000001306; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033709; Anticodon_Ile_ABEc.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
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   PANTHER; PTHR42780; PTHR42780; 1.
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; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1119
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098546"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           84..94
FT                   /note="'HIGH' region"
FT   MOTIF           676..680
FT                   /note="'KMSKS' region"
FT   COMPBIAS        29..43
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         679
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1119 AA;  124049 MW;  7576194652881F39 CRC64;
     MVPRRSRQRP ASSCRTAKTA RREMPYPLPA PDGQEPEAQP VTPSPVFPEI EEDVLAFWDR
     DGTFHASIDN RDGAPEWVFY DGPPFANGLP HYGHLMTGYA KDVFPRYQTM RGKKVERRFG
     WDTHGLPAEL EAERQLGITD KSQIEEMGLA AFNQAAKDSV LKYTREWQQY VTRQARWVDF
     DNGYKTLDTT YMESVIWAFK QLHEKGLAYE GYRVLPYCWR DQTPLSNHEL RMDDDVYKMR
     QDQTVTVTFP LTGAKAESLG LTGVRVLAWT TTPWTLPTNL ALVVGPDIQY AVVPAGPNGA
     ADAHGRPDDE VLSGEYLLAI DLVGNYAKDL GYGSPEAARA AVTRTIPGRE LEGVTYDRLW
     DYYADAATWG TQNAWQILVD GYVTTEDGTG IVHQAPAYGE DDQRVCEAAG IPVIISVDDG
     ARFLPAVQDV AGLQVFEAGK PLIKLLREEG RLLRQASYEH SYPHCWRCRN PLIYKAVSSW
     FVRVTDFRDR MVALNQEITW VPENVKDGQF GKWLAGARDW SISRNRYFGS PIPVWKSDDP
     DYPRVDVYGS LAELERDFGR LPLNAAGEPD LHRPFVDDLT RPNPDDPTGR STMRRIPDVL
     DVWFDSGSMP FAQVHYPFEN SDWFDSHNPA DFIVEYIGQA RGWFYLLHAL STALFDRPAF
     TNVISHGIVL GNDGQKVSKS LRNYPDVNDV FDRDGSDAMR WFLMSSPVLR GGNLVVTEEG
     VREGVRQVLL PLWNTWYFFS LYANATGYEA KRSTASAAVL DRYLLAKTRD LVEAVTADLD
     ALDSTLASAK LRDFADLLTN WYVRRSRDRF WAGVDGEGAG AEAFDTLYTV LETLTRVAAP
     LLPLVTERIW KDLTGGRSVH LTDWPDAAEL PADDALVAAM DRVRAISSTA LSLRKQAGLR
     VRLPLASLTV VAEGAAALAP FEAILRDELN VKAVCLVEGE HSGVDRALTV KARQLGPRIG
     KRVQEVIRAA KSGDWSEADG VVTAGGVELE PGEYELAVVI SAPTARFENG VYIELDTALT
     PELEAEGLAR DIIRAVQDTR KAAGLGVSDR IALTLAFENG GDARVLGLAT EVDIASETLA
     RTVQVAAAAG AFVKTFGAGQ FANVGDFTVG ITKIEEADE