SYI_CORJK
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 03-AUG-2022, entry version 104.
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; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC 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;
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; CR931997; CAI36922.1; -; Genomic_DNA.
DR RefSeq; WP_011273371.1; NC_007164.1.
DR AlphaFoldDB; Q4JW85; -.
DR SMR; Q4JW85; -.
DR STRING; 306537.jk0760; -.
DR PRIDE; Q4JW85; -.
DR EnsemblBacteria; CAI36922; CAI36922; jk0760.
DR KEGG; cjk:jk0760; -.
DR PATRIC; fig|306537.10.peg.768; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_11; -.
DR OMA; KMMAPFT; -.
DR OrthoDB; 32262at2; -.
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 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; 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..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
