ID   SYI_THEAC               Reviewed;        1026 AA.
AC   Q9HJT4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 124.
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=Ta0879;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAC12008.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL445065; CAC12008.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048161849.1; NC_002578.1.
DR   AlphaFoldDB; Q9HJT4; -.
DR   SMR; Q9HJT4; -.
DR   STRING; 273075.gene:9572093; -.
DR   PaxDb; 273075-Ta0879; -.
DR   EnsemblBacteria; CAC12008; CAC12008; CAC12008.
DR   GeneID; 1456418; -.
DR   KEGG; tac:Ta0879; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   InParanoid; Q9HJT4; -.
DR   OrthoDB; 30823at2157; -.
DR   Proteomes; UP000001024; 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   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; 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; 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..1026
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098595"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           591..595
FT                   /note="'KMSKS' region"
FT   BINDING         594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1026 AA;  119169 MW;  0FE6AA2C39E9B50F CRC64;
     MQSLRFRQID PGMTLREIDS EILKYWKDKN ILEKILSKGG SKKFVFLEGP PTANGRPHIG
     HAMTRTIKDI VLRYNTMTDH KIYRRVGGWD CHGLPVELEA EKHFGFHTKS EIVNFGVEKF
     NQYCRESIFR YIDEWKQVDD LIGFSIDHNG DYITLRNDYM ESEWFALKTM YNSGLLYKDY
     TVVPYCPRCE TSLSSHEVAQ GYKDVKDPSV YVRFKSADEE NTYFVAWTTT PWTLPSNEFL
     VVNPDMEYSL VEAQGSRYYV ASSRAGYIFK EYREIRRMHG RDLVGKRYLQ LMPFLDPPSG
     SLKVVAGSFV TSEDGSGIVH AAPAFGADDY QIGKEEGVEI LNPVDKNGRF ADPRIPWNGK
     FVRDANEDII VYLKKNQMLL KSEKYEHSYP FCYRCDTPLL YYPLDAWFIA VSRIRDKLVE
     YNERINWKPD YLKHGRFGNF LGEAKDWNLS RDRFWGTPLP AWRCKNGHLV FVGSRKEIED
     LGGKVPEDLH RPYIDEVRFK CPTCGEEMSR EPYVIDTWFD SGSATYAASH YPFEKNFDPE
     TDVPVSFITE AIDQTRGWFY VLHVIATIMF NKNAYESALS INFILDAQGR KMSKSKGNSV
     YALDFLNEVP PDSLRLFFLY GAPWKSKNLD KKVIDEVSRK TLMTVLNVYS FFAYNANIDN
     FQWNGLQLSG NALDRYMVSK VNSFVRSSRD AYESLDFHEV VRASMEFVDD LSNFYLRLSR
     RRFWAEGFDD DKLSAYSTLY YALKAFSEVM APITPFFSDF IYLNLGGDKE SVHLEAFPEF
     DSTLMDEKLE SEMDRAYSVI ETVRRLRQEN SIKGRQPLRE ILIAGDMEES IIDVVKSELN
     AKDIKLIERD QEPIRLSADL RMDRAAPVLR SRVNAVRHKI RSMDGLEVQR QISEKGFVEI
     DGVRLDPDMV EISRVPDPNY AYSQTEKYGI DVFINKNIDR DGYLEGLARE LVRRIQVMRK
     EMNLNYTDRI ITHLDLSDDF LEALNKHAEY IKNETQSDSI ITDKVEGMKL WEINGEPVRI
     KIDLAR
//