ID   SYI_BORRA               Reviewed;        1044 AA.
AC   B5RQH0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=BRE_844;
OS   Borrelia recurrentis (strain A1).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=412418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(2008).
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; CP000993; ACH95054.1; -; Genomic_DNA.
DR   RefSeq; WP_012539206.1; NC_011244.1.
DR   AlphaFoldDB; B5RQH0; -.
DR   SMR; B5RQH0; -.
DR   EnsemblBacteria; ACH95054; ACH95054; BRE_844.
DR   KEGG; bre:BRE_844; -.
DR   HOGENOM; CLU_001493_1_1_12; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000612; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..1044
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000216251"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           594..598
FT                   /note="'KMSKS' region"
FT   BINDING         597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1044 AA;  122975 MW;  C333F3692BF3F771 CRC64;
     MFKKVENKVH FPQLEEKILQ FWNHNKIFEK SMKQREGCEE FTFYDGPPFA TGLPHFGHFV
     PNTIKDIIPR YQTMKGKNVK RYFGWDTHGL PVEYEVEKSL KLSGRYEIEQ YGIDKFNEEC
     RNIVLRYTKE WKKIITRLGR WVDFENNYKT MDLTFMESVW WVFKTLYNKG LIYESYYVLP
     YSPKLATPLS NFEVNLGEYK EIHDPSLTIK FKIKDKNEYL LAWTTTPWTL PTNLGIAVGK
     DIDYSKVVDQ EKNEIYIIGT KRLNHYYQDE NKYVIIEQFK GEHLKGIEYE PLFDYFVNQR
     NKGAFKIHTA EYVTTDDGTG IVHIAPFGEE DYQILKKNTQ TDMITPIDAE CKFTSEVKDF
     EGLFVKDADN KIIEKLKSMN LLFKRENYLH RYPFCYRTNS PLIYRPISSW FVNIEKIKEK
     LIRSNEQINW IPEHLKKGRF GKWLENARDW AISRNRFWGN PIPIWKCSKT GNKICIGSRE
     ELEKLSGQKI IDLHKDKIDK ITWPSKYGGT YVRTSEVLDC WFESGSMPYA SKHYPFKDKD
     KFQNIFPADF IAEGLDQTRG WFYTLTILGT ALFEKTAFKN VIVNGLVLSS DGKKMSKSLK
     NYTDPIQIIN TFGADALRLY LIMSPVIKAD DLKYSDDGVK DVLKNIIIPI WNAYSFFITY
     AIIDKFTPNN YVNLYKTNIL DKWIISEIES LKQILNEEID KYNLTKSIEV LLTFIDKLNN
     WYIRRSRRRF WKSENDNDKI DAYETLYYTL KNLMLMLAPF IPFLTEEIYQ NLKTKNEKES
     IHLNNYPQSI KELINIELEE KMNFTRKVIT IARALRASHN IKIRKPIKTI YIITKNHKEQ
     NTLREMTEII LEEINAKEIK IKSNEEELVT YKAKANFKEL GSKLGTNMKS VALAITKLSN
     EDILEIINGN KHTITINNNT YDITLKDIIL ERHERKNLKV INEDSITIGL DTLITEELYL
     EGLSRELIRK VQNLRKESNF NVTDRIILYT NNDEILTKII NNFENYIKTE TLAITIEINN
     KKALTTLELD EEISVNIGIE KCLN