ID   SYI_PICTO               Reviewed;        1024 AA.
AC   Q6L206;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=PTO0411;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT42996.1; -; Genomic_DNA.
DR   RefSeq; WP_011177212.1; NC_005877.1.
DR   AlphaFoldDB; Q6L206; -.
DR   SMR; Q6L206; -.
DR   STRING; 263820.PTO0411; -.
DR   EnsemblBacteria; AAT42996; AAT42996; PTO0411.
DR   GeneID; 2844251; -.
DR   KEGG; pto:PTO0411; -.
DR   PATRIC; fig|263820.9.peg.436; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000000438; 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   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..1024
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098586"
FT   MOTIF           52..62
FT                   /note="'HIGH' region"
FT   MOTIF           590..594
FT                   /note="'KMSKS' region"
FT   BINDING         593
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1024 AA;  120191 MW;  6B23F804B7AAFF9F CRC64;
     MKATLYENIN VNKSMIDINN EILNYWKENH IDENIIKSNR NLKPFAFLEG PPTANGRPHV
     GHLMTRAVKD TVMRYKYMTG HDILRRTGGW DCHGLPVELE AEKHFGFKNK KDIENFGIEK
     FNQYCRDSVF RYIDEWNIVD DLVGFWVDKE NSYITLKNDY MESEWWALKT LYENNLLVKD
     YKIVPYCPRC GTSLSSHEVA QGYKNVDDPS VFVKFAEKGR KNRYFIAWTT TPWTLPSNEF
     LVVNPDMDYS LIESDGFEYY LLSSKVESLF NDYKLIKTFK GRDLEGIEYE QLMPFLEKPE
     NAFRVVAASF VTAEDGTGIV HAAPAFGADD FEIGKRFSVE ILNPVDQDGR FNEKLPWSGL
     FVTDANKSII NYLKENNLLF KAETMKHDYP FCYRCGTRLL YYPLDTWFIK VSLIRKKLLE
     NNEKINWVPD YLKNGRFGNF LEEAKDWALS RDRYWGTPLP IWRCNKNHYL AIGSRDDLLK
     YGGYIPEDLH RPYIDDVVLK CPECGSEMHR ESYVIDTWFD SGSASYAAMH YPFSKDFTKS
     HFPVDFITEA IDQTRGWFYT LHVVASLLFD ENAYKNVVSI SHILDENGQK MSKSKGNFIA
     AIDFLNDYGA DAARMFFFTG APWNSKSVNK KLIGEITRKN LSTLLNVYSF FASNANIDEY
     RFTEIKEPEN LLDRWMLSRL NTTIIKVREN MDNYNIHTAL RYIEDLISEL SNVYLRLSRK
     RFWEGNLDDS KERAYSTLYY TLRETIKMMA PITPFFSEYL YQKLSPGMPS VHMESYPEAI
     ERFIDNDLEN EMEHAIEIME LSRRTRQELN IKGRQPVKEI LIYSDIKLRD DIIDIISPEL
     NAESIRFIKS DEMPLKITVR ADISKVAKLL KSRINDFNLY LERNNDLVYR ELKSKGKINF
     DGIYLTDDMF IMNEEVNGNY GFNKDERSGI YLFINREIDN DLLLEGYARE IIRRIQVMRK
     DLNLEYSEKI KTYIDADEDI RSAVERYMEK IKNETLSSEI LFKNDPEARA WDIDDKTVYI
     KIVK