ID   SYI_CLONN               Reviewed;        1038 AA.
AC   A0Q3B0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=NT01CX_0646;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK60463.1; -; Genomic_DNA.
DR   RefSeq; WP_011723091.1; NC_008593.1.
DR   AlphaFoldDB; A0Q3B0; -.
DR   SMR; A0Q3B0; -.
DR   STRING; 386415.NT01CX_0646; -.
DR   EnsemblBacteria; ABK60463; ABK60463; NT01CX_0646.
DR   KEGG; cno:NT01CX_0646; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_9; -.
DR   OMA; KMMAPFT; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008220; 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..1038
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000070894"
FT   MOTIF           48..58
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   1038 AA;  119727 MW;  C03996885F7BF8F7 CRC64;
     MYNKIETSGN FVNMEEKIAK LWKDKDVIQK SFDRNEDGEY FTFYDGPPTA NGKPHVGHVL
     TRVMKDLIPR YKVMKGYKVL RKAGWDTHGL PVELEIEKKL GISGKPQIEE YGVEKFVKEC
     KDSVFKYTSL WKDMSEKLGF WVDMDNPYVT YHNTYIESVW WALKTMWEKD LLYKGHRVTP
     YCPRCGTALS SHEVAQGYKD VKEATAFVKF KVKGEENKYI LAWTTTPWTL PSNVALAINK
     AYDYVEVEQN GEHLILAKDL AEKVLEGEYK VVKEFKGEEL VGTEYEQLFK FEVPDKKAFY
     VVHADYVTLT DGTGIVHTAP AYGEDDNMTG KKYDLPLINL VDGEGKFVDS VTPWKGMFVK
     KADPKILEFM KENGSLYKSE KFTHSYPHCW RCDTPLLYYP KDSWFVRMTS LRDKLLENNN
     KINWNPDNIR TGRFGKFLEN VIDWGISRDR YWGTPLPIWE CECGHRECIG SIEELKEKGI
     NVPDDIELHK PYIDGVKLTC PHCGKEMTRT NEVIDCWFDS GSMPFAQHHY PFENKEVFEK
     TFPAQFISEA VDQTRGWFYS LLAISTALFD TNSYENCIVL GHVLDKHGLK MSKSKGNVVD
     PFDVLQNEGA DATRWHFYTA SAPWLPTRFS EDDVKETQRK FLSTLWNVYS FYVLYAELDQ
     FNPLEYKDFV SENVMDKWIL SKLNTLIKTV EEDLDNYKIT EAALELEDFV DELSNWYVRR
     NRSRFWSTEL TDDKIGAYKT LYTVLTTIVK VAAPFVPFMA EEIYQNLVVN LDKDAIESVH
     LCTWPEYDLS VVDNELEGQM DLAYKIVKLG RSARNGANIK NRQPLSEMLI STKSLPDYYG
     DIIKEELNIK KVEFGADLSK YVNFEIKPNL PVLGKAYGRY IPAIRKAISS MDQMELAQNI
     NNGKSVFINV DGLDEQIELT ENNLLVAMQG LEGFAFAGSS GVGVILETTI TEELREEGFV
     REILSKVQNL RKESGFEVAD KIKLYFAGNE TLEVVIKKFE EHIKKETLAV LISYNEDREY
     VDSKINGEEL KIAVEKQD