ID   SYI_EHRCJ               Reviewed;        1120 AA.
AC   Q3YRX3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Ecaj_0495;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake;
RX   PubMed=16707693; DOI=10.1128/jb.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68532.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3YRX3; -.
DR   SMR; Q3YRX3; -.
DR   STRING; 269484.Ecaj_0495; -.
DR   EnsemblBacteria; AAZ68532; AAZ68532; Ecaj_0495.
DR   KEGG; ecn:Ecaj_0495; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   OMA; KMMAPFT; -.
DR   Proteomes; UP000000435; 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   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; 2.
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..1120
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098543"
FT   MOTIF           64..74
FT                   /note="'HIGH' region"
FT   MOTIF           647..651
FT                   /note="'KMSKS' region"
FT   BINDING         650
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1120 AA;  131115 MW;  E982615B4B75549D CRC64;
     MCIVKYLSLI INTMTEHYSQ LTGEPDFPSI EENVLKFWQE NNIFKKSVDN RDENKRFIFY
     DGPPFANGLP HYGHLLTGFI KDTVARYKTM AGFKVERRFG WDCHGLPAEM LSEKELGISG
     KLAIEKFGIE KFNNHCRNSV MKFSKEWKQY VDRQARWVDF ENDYKTMNSS FMESIIWSFH
     ELWNKGLIYE SIKIVPYSWA CQTPLSNFET RMDNAYREKT SKTVTVAFEL LESPKFITVE
     NVKTYKILVW TTTPWTLPCN LALAISKNIK YCGAIIKHEM LIFATGYLKI FQEHCKKNNI
     EYQLYNQDIS SVNLEDLHYK PLFKYFADVK NAFKILTADF VVEGEGTGIV HIAPGFGEDD
     FILCKMQDIP HIEGDTSNLL SIICPIDDGA KFTDKISDFK NMHVFDTNDQ IINILKQKNL
     CFKIDQYLHN YPHCWRTDTP LIYRAMSSWY VEVTKIKDKM IELNKTVNWI PNHICNGQFG
     KWLENAKDWA ISRNRFWGTP LPVWKSDNPN YPRIDVYGSI RKVFNNVKAL EEDFDISSIN
     DLHRPYIDNL VRPNPDDPTG KSMMRRVSDV FDCWFESGSM PYAQLHYPFE NKEFFENYFP
     ADFITEYIAQ TRGWFYTLFI LSTALFNKPP FINCICHGVV LDTQGQKLSK RLNNYADPME
     IFNQYGSDAM RFLMLSHTVL YGGDLLLDKE GVMIKDVLRN VIKPIWNSYN FFTIYANIDH
     ITAEIITELN ELSNIMDRYI ICECINTIHS IFNAMEELDQ CSNNLGYNIK LACNNITKFF
     EILNNWYIRR CRSRFWSSEI TQDKQDAYNT LYTVIYYMIK VSAPFLPIIT EAIWQRLNFQ
     KEESVHLSSL PNISNFILNN EDKQNIQYMK LITCICNYVL SIRSTHNIRI RQPLNKIVIY
     SHNCPDLLNL PAEYQNILLE EVNVKSISFK SDISDIASFQ LKLNFPELGK RIPDKVKRLI
     FLLKNDQWKI LENDKLLLGT IEAEHYVINN NEYTLALKVH NDFACTINLD QHLLGVVLLD
     NELSNELIME GIARDIIRTI QHSRKDNKFN ISDKIDVIIH TKDNIVKDSI KTWSQYIIQQ
     TLSTSFAIHE EISDIQDINE YYKTTMKDKE VSVFLKKSHT