ID   SYI_SULTO               Reviewed;        1047 AA.
AC   Q975H9; F9VMY3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 111.
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=STK_04310;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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; BA000023; BAK54280.1; -; Genomic_DNA.
DR   RefSeq; WP_010978404.1; NC_003106.2.
DR   AlphaFoldDB; Q975H9; -.
DR   SMR; Q975H9; -.
DR   STRING; 273063.STK_04310; -.
DR   PRIDE; Q975H9; -.
DR   EnsemblBacteria; BAK54280; BAK54280; STK_04310.
DR   GeneID; 1458368; -.
DR   KEGG; sto:STK_04310; -.
DR   PATRIC; fig|273063.9.peg.502; -.
DR   eggNOG; arCOG00807; Archaea.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000001015; 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   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; 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..1047
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098594"
FT   MOTIF           45..56
FT                   /note="'HIGH' region"
FT   MOTIF           594..598
FT                   /note="'KMSKS' region"
FT   BINDING         597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1047 AA;  121455 MW;  7CE78F48A73547B2 CRC64;
     MPSKFDPLST EKEILKFWEQ NKIYEKLKEY NSKFEKKFLF IDGPPYPSSP IPHIGTVWNK
     VIKDCILRYE RLAGFRTYDQ PGYDTHGLPI EVAIEKQLGI QKKSDIIEKI GVDNFVNKCK
     EFALNNASSL TANFKNIGIF MDWNNPYMTL HNDYISNSWM LIKKAYERGL LYKGVHVLHW
     CPRCETTLAD YEVSEYKEIE DPSIYVKFKV KGSENRYLVI WTTTPWTLPA NVFVMINKDY
     EYAEVEVNNE ILIMAKDRVS DVMKEAGIKN YKIVRTFKGV ELVGLQYIHP LADIVTAQKG
     LDNYHIVVDA GEEVTLTEGT GLVHSAPGHG DIDFEIGKKI GAPVVMLVND RGEFLPEAGK
     YVGKNVRSAA EEIINDLKQR NALLHSGKVV HRYPVCWRCK TPLILRAIEQ WFIGVSKLKE
     ELLKEIDNVK WVPDWGKTRI GNMVREIRDW VISRQRFWGT PLPIWICKNC GNIIVIGSRD
     ELEKVAITKV PEDLHRPWID KVVVRCNKCG GEAHRVPDVA DVWFDSGVAF FASLGKDWEK
     KWKEIGPVDL VLEGHDQLRG WFFSLLRAGV ILLDRAPYNA VLVHGFMLDE QGREMHKSLG
     NYVEPSQVTE NEKYGRDVLR LWLLRNTTWE DAKFSWKALD QTKRDLNIIW NVYVFASTYM
     NLDNFDPRIY NLDNLKQYLR IEDLWLLSRY NRVVKEVKES MNDFKVHELA NKMTSFIIDD
     ISRFYLRLVR KRAWNESNDP DKIAMYYVLY EVLKGSLVLL SPVIPFTTER IYQDFVVDKK
     DSVSMESLPE VKEEFINDKI EKEFELSKEI AEAGLNARAK AGIKLRWPIK NAYVFLVSDI
     DVEMANNVKE VIKFLLNTKD VEIGGIEGYR RFSKIKATPN RGTIGPDFKR LTNKIVEYIE
     NNSEKVASDI IAKGYHEVVI EGEPVQIKVN HVNILEETEE GYISARFNKG VVVLKKEISK
     EEEEEGIVRD IIRRIQFMRK QLNVQINDYI LLYIKAPEER TEMLKKWTDY IKSETRAKEV
     IIGEVKGDLI LPWEIEDEEY IIGVSKS