SYI_THEKO
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 03-AUG-2022, entry version 108.
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;
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; AP006878; BAD85937.1; -; Genomic_DNA.
DR RefSeq; WP_011250699.1; NC_006624.1.
DR AlphaFoldDB; Q5JJ31; -.
DR SMR; Q5JJ31; -.
DR STRING; 69014.TK1748; -.
DR PRIDE; Q5JJ31; -.
DR EnsemblBacteria; BAD85937; BAD85937; TK1748.
DR GeneID; 3235480; -.
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 OMA; HLGTAWN; -.
DR OrthoDB; 4914at2157; -.
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 Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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 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; 2.
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..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