ID   SYI_MYCBO               Reviewed;        1041 AA.
AC   Q7VEZ0; A0A1R3XZ02; X2BI93;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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};
GN   OrderedLocusNames=BQ2027_MB1563;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00166.1; -; Genomic_DNA.
DR   RefSeq; NP_855215.1; NC_002945.3.
DR   RefSeq; WP_010950555.1; NC_002945.4.
DR   AlphaFoldDB; Q7VEZ0; -.
DR   SMR; Q7VEZ0; -.
DR   EnsemblBacteria; SIU00166; SIU00166; BQ2027_MB1563.
DR   PATRIC; fig|233413.5.peg.1709; -.
DR   OMA; KMMAPFT; -.
DR   Proteomes; UP000001419; 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; 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; Zinc.
FT   CHAIN           1..1041
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098547"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1041 AA;  117314 MW;  4513382E3248D3AB CRC64;
     MTDNAYPKLA GGAPDLPALE LEVLDYWSRD DTFRASIARR DGAPEYVFYD GPPFANGLPH
     YGHLLTGYVK DIVPRYRTMR GYKVERRFGW DTHGLPAELE VERQLGITDK SQIEAMGIAA
     FNDACRASVL RYTDEWQAYV TRQARWVDFD NDYKTLDLAY MESVIWAFKQ LWDKGLAYEG
     YRVLPYCWRD ETPLSNHELR MDDDVYQSRQ DPAVTVGFKV VGGQPDNGLD GAYLLVWTTT
     PWTLPSNLAV AVSPDITYVQ VQAGDRRFVL AEARLAAYAR ELGEEPVVLG TYRGAELLGT
     RYLPPFAYFM DWPNAFQVLA GDFVTTDDGT GIVHMAPAYG EDDMVVAEAV GIAPVTPVDS
     KGRFDVTVAD YQGQHVFDAN AQIVRDLKTQ SGPAAVNGPV LIRHETYEHP YPHCWRCRNP
     LIYRSVSSWF VRVTDFRDRM VELNQQITWY PEHVKDGQFG KWLQGARDWS ISRNRYWGTP
     IPVWKSDDPA YPRIDVYGSL DELERDFGVR PANLHRPYID ELTRPNPDDP TGRSTMRRIP
     DVLDVWFDSG SMPYAQVHYP FENLDWFQGH YPGDFIVEYI GQTRGWFYTL HVLATALFDR
     PAFKTCVAHG IVLGFDGQKM SKSLRNYPDV TEVFDRDGSD AMRWFLMASP ILRGGNLIVT
     EQGIRDGVRQ VLLPLWNTYS FLALYAPKVG TWRVDSVHVL DRYILAKLAV LRDDLSESME
     VYDIPGACEH LRQFTEALTN WYVRRSRSRF WAEDADAIDT LHTVLEVTTR LAAPLLPLIT
     EIIWRGLTRE RSVHLTDWPA PDLLPSDADL VAAMDQVRDV CSAASSLRKA KKLRVRLPLP
     KLIVAVENPQ LLRPFVDLIG DELNVKQVEL TDAIDTYGRF ELTVNARVAG PRLGKDVQAA
     IKAVKAGDGV INPDGTLLAG PAVLTADEYN SRLVAADPES TAALPDGAGL VVLDGTVTAE
     LEAEGWAKDR IRELQELRKS TGLDVSDRIR VVMSVPAERE DWARTHRDLI AGEILATDFE
     FADLADGVAI GDGVRVSIEK T