ID   SYI_METJA               Reviewed;        1039 AA.
AC   Q58357;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=MJ0947;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB98949.1; -; Genomic_DNA.
DR   PIR; C64418; C64418.
DR   RefSeq; WP_010870461.1; NC_000909.1.
DR   AlphaFoldDB; Q58357; -.
DR   SMR; Q58357; -.
DR   STRING; 243232.MJ_0947; -.
DR   PRIDE; Q58357; -.
DR   EnsemblBacteria; AAB98949; AAB98949; MJ_0947.
DR   GeneID; 1451844; -.
DR   KEGG; mja:MJ_0947; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   InParanoid; Q58357; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; Q58357; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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..1039
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098580"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           600..604
FT                   /note="'KMSKS' region"
FT   BINDING         603
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1039 AA;  122234 MW;  7163C46B4AE08AC0 CRC64;
     MKKVEPVNFR ELDKKIKKFW EENDIYQKVK KKNERNKEFY FVDGPPYCSG AIHLGTAWNK
     IIKDTYLRFK RMQGYNVLDK AGWDMHGLPI EVKVENEFGI KNKKEIETKI GVKQFIEKCK
     EFALKHKEIM EKQFKNLGVW LDWENAYMPI TKEYMEIGWW TLKVAHEKGL LTRDLRVVYW
     CPRCETALAE HEVRGEYKEV YDPSVYVKFR LANEENTYIV IWTTTPWTLV ANLAVTVHPD
     YDYAYVEVEF DDKKEVWIIA EKLVEEVINK AKKFHNIKNY KIIKKVKGKE LEGIKYIHPL
     LEENERQKEF AELENAHTVI LGEHVTLEGG TGLVHTAPGH GEEDFEVGKK YNLPIYSPID
     DEGKYVEGKW KGVFVKDADA EIIETLKNKG LLVYAGKIKH SYPHCWRCKT PLLFRATEQW
     FLEISKIKDN IIEHAKTVQW IPHWVETRYI NGVKFVGDWN ISRQRYWGIP IPVWVCEKCG
     KYIVVGSVEE LEEKMINKDE VGEINDLHKP TVDKIKLRCE CGGEMKRVPD VLDVWFDSGL
     APYASIGVKE LKKADFITEG HDQVTKWFYS QHALSAIVFN DIPYKKCLMH GFTLDEHGDK
     MSKSLGNVVN PDDVVEKYGA DLLRFYLLSA NKVWEDLRFV WSEMDDVLSL FNTLWNAYMF
     AVNYMVLDNF KPDEKYFEYL KDEDRWIVSR INSVAKIAIE NLEVPYFHTY TWTLKDFILN
     DLSRWYIRLI RDRTWKEKDD ADKLAAYQTL YYVLLKLATI LAPVAPHTAE AIYQNLKTED
     MEESIFMNKI EVDEEFIDEE LERDMAIVRD VVDAIYRGRD RIKYTLRYPL KEITIAGGEE
     VKKAVERFEY IIKEQGNVKN IKFGEVEGSK YIIKPNYREL GKRYRSEVPK VVEALNKADA
     KELMERLKEG AVILDGYEIK PEYVEIRLEI PEHIAGVEFS KGTVFINTEI TDDLIKEGLM
     REVIRRIQAM RKDMDLDIEE KIKIKVEGID LDEFKEIIER EVRGQFVDEI KADYEKDWEI
     KTPNGEKYNV KIAIERINK