ID   SYI_CORJK               Reviewed;        1092 AA.
AC   Q4JW85;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=jk0760;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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; Evidence={ECO:0000255|HAMAP-
CC         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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR931997; CAI36922.1; -; Genomic_DNA.
DR   RefSeq; WP_011273371.1; NC_007164.1.
DR   AlphaFoldDB; Q4JW85; -.
DR   SMR; Q4JW85; -.
DR   STRING; 306537.jk0760; -.
DR   GeneID; 3432445; -.
DR   KEGG; cjk:jk0760; -.
DR   PATRIC; fig|306537.10.peg.768; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000545; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF19302; DUF5915; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..1092
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098539"
FT   REGION          554..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           61..71
FT                   /note="'HIGH' region"
FT   MOTIF           662..666
FT                   /note="'KMSKS' region"
FT   COMPBIAS        554..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         665
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1092 AA;  121234 MW;  E9C5389841FBAAD6 CRC64;
     MSEATPAGGA YPRVDMSNGG STAFPALEEN VLKYWEKDGT FNESVASREG NEEYVFYDGP
     PFANGLPHYG HLLTGYVKDI VPRYQTMQGK KVARVFGWDC HGLPAELEAE KQLGIKDRAG
     IEEMGMRSFN EYCATSVLRY TDEWKEYVTR QARWVDFDNG YKTMDPGFME SVMWAFKTLY
     DKGLIYQGFR VLPYSWAEHT PLSNQETRLD DSYKMRQDPT ITVTFPITGA TEGTASVKTL
     AEHPELADAA FIGWTTTPWT TPANLALAVN PEVTYAAVRI GDDAAGADGA EGMYGKTVVL
     ADDLRGAYAK ELGEKAEVLG TFTGAELEGM TYEPLFGYFA ERAGEKASAG EGSEGGEGNQ
     RKPGAFRVLC ADYVTTADGT GVVHQAPAFG EDDMFTCEAA GIDLEIPVDM DGKFTSLAPE
     YQGQLVFDAN KAIIKDLKAA GRVLRHQTIE HSYPHSWRSG EPLIYMALPS WFVAVTKFRD
     RMVELNHEQI EWMPSHIRDG QFGKWLEGAR DWNISRNRYW GAPIPVWVSD SEEYPRMDVY
     GSLEELERDF GRKPASLHRP DIDELTRPNP DDPTGKSTMR RVPEVLDCWF ESGSMPFAQK
     HYPFENKEWF DTHSPADFIV EYSGQTRGWF YTMHVLSTAL FDRPAFKKVV AHGIVLGDDG
     LKMSKSKGNY PNVNEVFDRD GSDAMRWFLM SSPILRGGNL IVTEQGIREG VRQAMLPMWN
     AYSFLRLYAS QPAQYDTSST NVLDRYILAK LRDTVQGVSD ALDNTDIATA CDEIRWFCDA
     LTNWYVRRSR DRFWAGDAVH PEAFNTLYTV LETLCRAAAP LLPMTTEVIW RGLTGERSVH
     LADFPKSENL PADAELVTAM DAVRAVSSAT SSLRKAHKLR NRLPLPKLTV ALPNASALED
     FTKIIADEVN VKQVELTEDV AQVGGFEVVV NARVAGPRLG KDVQRVIKAV KSGNYTVDDA
     GVVTADGIEL QDGEFTRKLV AAEPEHTAEV SGQDGLVVLD TQTTPELEAE GWAADRVRGL
     QEARKAADLQ ISDRIHLTLS VPAEKEEWAR THADSIAKEV LATDVKVVVG EQLSHDVADD
     CSADIVVASV AS
//