ID   SYI_THEKO               Reviewed;        1065 AA.
AC   Q5JJ31;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=TK1748;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(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}.
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DR   EMBL; AP006878; BAD85937.1; -; Genomic_DNA.
DR   RefSeq; WP_011250699.1; NC_006624.1.
DR   AlphaFoldDB; Q5JJ31; -.
DR   SMR; Q5JJ31; -.
DR   STRING; 69014.TK1748; -.
DR   EnsemblBacteria; BAD85937; BAD85937; TK1748.
DR   GeneID; 78448278; -.
DR   KEGG; tko:TK1748; -.
DR   PATRIC; fig|69014.16.peg.1704; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   InParanoid; Q5JJ31; -.
DR   OrthoDB; 30823at2157; -.
DR   PhylomeDB; Q5JJ31; -.
DR   Proteomes; UP000000536; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.30.720.200; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; 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; 2.
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..1065
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098591"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           625..629
FT                   /note="'KMSKS' region"
FT   BINDING         628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1065 AA;  125512 MW;  2BC6601CFF79D3A6 CRC64;
     MIREPEFREY NPGQLEEKIE AFWKENNTYE KVKKLRENGP KYYFLDGPPY VSGAIHLGTA
     WNKIIKDMII RFRSMQGYNV RRQPGFDMHG LPIEVKVEQA LKLKNKREIE TKIGVDNFIK
     KCKEFALNNL KIMTEQFKQL GVWMDWDNPY MTIKNEYIES GWFTLKRAWE KGLLEKDKRV
     LHWCPRCQTA LAEHEVRGEY KMRKDPSIYV KFPIEWKEKE YLLIWTTTPW TLPANLAVAA
     HPEYEYAKVK VETENGEEYW IMAKALVERV LSEVGVKGEI VETFKGEELE GIRYTHVLLE
     EYPAQKEFRE KYEWAHRVIL GEHVTLEDGT GLVHTAPGHG EEDFEVGQRY GLPVYSPVDD
     AGRYTEGKWK GVYVKDADPE IIEYLKEKGY LVKAGEIEHK YPHCWRCKTP LIFRATDQWF
     LKVSKVKDQI IKENDEKVTW YPEWVKVRYD NGVMNSGDWV ISRQRYWGIP LPIWESEDGE
     YYVVGSFEEL VKLAVAIEVN GERIDLPEGY EEKLKIIEEK LGPEDLHRPY VDAFIIKVNG
     KEMKRVKDVV DVWFDSGIAS WASLDYPRNK ELFEKLWPAD FIVEGEDQVT KWFYSQQAAS
     VIAFDTVPYR AVAMHGYVLD EKGDKMSKSL GNIIRPEEVV QKEGRDPFRF YMLWATNPWE
     NLRFSWKGLE QVKRMLNILW NVYVLSATYM SLDNFNPTKV NPEELPFREE DRWILSRVNS
     LIGEVTDGIE TFRLTRATRG IYNFVVEDLS RWYIRLIRKR MWVEGDDPDK LAAYYTVWKV
     FDVLLRLMAP FTPYIAEEIY QNLIRPFVGV ESVHMLDWPE ADEKAIDEEL EKEMEYARKI
     VEAGSSARQK ARIKLRYPVR RIIIETEDET VKKAVERINR ILRDQLNAKE VVVGKVEREL
     IIKPNFAKVG PEFKGDAKKV IAWISEHGRE LYEKGEMDVE IEGKTFHITR EHVTIEEKLP
     DFFVAEEFDG GRVFVDKTLT RELLAEGLAR EFVRRIQEMR KRLDLDVNDR IVVTIETTDE
     NRELLQENLD YIMRETRAVE VRFEEAKGYV VEWPEVQAKI GIEKV
//