ID   SYI_THEVO               Reviewed;        1028 AA.
AC   Q97AG7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=TV0843;
GN   ORFNames=TVG0867938;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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}.
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DR   EMBL; BA000011; BAB59985.1; -; Genomic_DNA.
DR   RefSeq; WP_010917087.1; NC_002689.2.
DR   AlphaFoldDB; Q97AG7; -.
DR   SMR; Q97AG7; -.
DR   STRING; 273116.gene:9381635; -.
DR   PaxDb; 273116-14325060; -.
DR   GeneID; 1441935; -.
DR   KEGG; tvo:TVG0867938; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OrthoDB; 30823at2157; -.
DR   PhylomeDB; Q97AG7; -.
DR   Proteomes; UP000001017; 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; Zinc.
FT   CHAIN           1..1028
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098596"
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   1028 AA;  119494 MW;  ABBBCD972B46641F CRC64;
     MQAQRYRLIE QGNTIMDIDN EILRYWNDHA INEKIFKKEG TKKFVFLEGP PTANGRPHIG
     HAMTRTIKDI VLRYNTMTGH KIYRRYGGWD CHGLPVELEA EKYFGFKTKS DIINYGVEKF
     NSYCRDSVFR YIDEWKTVDQ IIGFSIDHSG DYITLRNEYI ESEWYVLKYI YENGLLYKDY
     TVVPYCPRCE TSLSSHEVAQ GYKDVKDPSV YVRFKEKGSE NTYFVAWTTT PWTLPSNEFL
     VVNPDIEYSL IEYNNAKYYV ASSRAQYIFK DFKVLKKMKG FELAGKGYEQ LLPFLDPPAG
     ALRVVTGDFV TDIDGSGIVH AAPAFGSDDY QIGKRENVPI LNPVDKNGRF SDERLPWYGK
     KVREANEDII VYLKNNGLLI KSEKYEHSYP FCYRCDTPLL YYPLDAWFIR VSSVRDKLVE
     NNEKIRWKPD YLKHGRFGNF LDEAKDWNLS RDRFWGTPLP VWRCRNNHVR FIGSRKEIEE
     MGATVPQDLH RPYIDEVKFV CPDCGEEMRR EPYVIDTWFD SGSATYAAMH YPFEDNFDPS
     SDLPVSFITE AIDQTRGWFY VLHVISTIMF NKNAYDSALS ISFILDEQGR KMSKSKGNSV
     FALDYLKQVA PDSLRLFFLY GAPWKSKNLD RKIIDEVSRR VISTLLNVYS FFAYNANIDG
     FEFKGILEAK DTLDKWLISK INTFIIESRR AYDDLDFHEV VRLSMDFVDN LSNFYLRLSR
     RRFWAEDVTE DKLAAYSTLY TAIMTCSKVL APIVPFVSDY LYLSLHGPYE SIHLDSFPEP
     DTSKIDHDLE KRMDQAYSVI ETVRRIRQEI NIKGRQPVKE ILLSGNIDPE IIPVVSQEVN
     AKEIRIVSSE QRPLKYTVDL KMETAAPILR SSVNSVREAL KSIDGKAAFD AVQNGGKLRV
     LDHELTGEML NISTIPDPDY GYSRDEKNGI DVFVNKRIDR NEYLEGLARE IVRRIQLMRK
     EMNLDYTDRI NVWIDPVGDF SDAIDKFESY IKAETQCDSL NVGHTDDLRK WEIGDETIGI
     RIEKVVPK
//