ID   SYI_ARCFU               Reviewed;        1018 AA.
AC   O29622;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=AF_0633;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB90608.1; -; Genomic_DNA.
DR   PIR; A69329; A69329.
DR   RefSeq; WP_010878137.1; NC_000917.1.
DR   AlphaFoldDB; O29622; -.
DR   SMR; O29622; -.
DR   STRING; 224325.AF_0633; -.
DR   PRIDE; O29622; -.
DR   EnsemblBacteria; AAB90608; AAB90608; AF_0633.
DR   GeneID; 1483851; -.
DR   KEGG; afu:AF_0633; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; O29622; -.
DR   Proteomes; UP000002199; 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; 1.
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..1018
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098575"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           586..590
FT                   /note="'KMSKS' region"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1018 AA;  118885 MW;  58C8BBE472FF1D0F CRC64;
     MLPAKYSPKD VESEIFKFWE DNDIYRKVKE KGGRKFYFVD GPPYTTGRIH LGTAWNKVLK
     DTILRYKRMM GFAPTDTPGW DMHGLPIEVK VEQELGFRTK RDIESFGIDK FIERCMNYAL
     ANKDAMTEQF KSLAVWMDWE NPYMTIKAEY MNAAWFAIKR AHERGLLERK KMVVNWCHRC
     ETALADAEVE YWDEEDPSIY VKFPVKGEKD TYIVIWTTTP WTLPANMAVA VHPSLEYAKF
     RAVKDGKVEY LILAKELADS VLGKGDYDSW EVVETYLGED LEGLEYEHPL ADEVPLQKNW
     KHQVFFADFV TAENTGCVHI APGHGVEDYE LGVEKGLEVF NPVDDRGVYT EEAGKYAGKH
     VKEANDDIID DLYRKDLLLA EERIVHRYGH CWRCKTPIIY RATEQWFIKI SELKDEMLEE
     IDKVMWIPEW AGSARFKDWV SNAKDWCISR QRYWGIPIPV WICEKCGEMK VVGSINEIEW
     ENDLDLHRPK IDAVTFSCQC GGVMRRVPDV FDVWFDSGVA SWGSIAYPLR KDKFEELWPA
     DFITEGHDQT RGWFYSQLGT SVVCFDKAPY KAVLMHGFTL DEQGRKMSKS LGNVVEPEEV
     VGQIGVDGFR LYVLYSAPWE DLRFSWEEAR NINRMLNVVW NAVRFAHTYM SLDNYSFGEK
     GELKIEDRWI LSRLESFIKE ANEAMEGYQV HRVVRAFFDF FVEDFSRWYI QIIRPRVWEE
     RDSPSKLAAY YTMFRVIDRS LRAIAPFAPL IAEWFYQHVV KEFREGEESI FMEEYSTAEV
     EMIDGELEAA MKVAKEIVEA AANARNKAKR KLRWPLRELV IESGSEKVRK AVEMLEETIL
     SQCNVKQVRV VDSFEKEIEI KPNYKYIGPL LKEKAGEFAK YVASLKEIPE KLVFDGVELD
     PKQAIVVDYR LPEGYEYAEF SGGVVYIYKE LDDELVREAF AREVIRRIQE MRKELDLDVE
     EFIETTVEMD AELVKGWEDY IKSETRSQKL VFGKAEGYVR EWNIEGKKVK IGIKRLRG