ID   SYI_STRCO               Reviewed;        1047 AA.
AC   Q9S2X5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=SCO2076; ORFNames=SC4A10.09;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AL939111; CAB51985.1; -; Genomic_DNA.
DR   PIR; T34946; T34946.
DR   RefSeq; NP_626335.1; NC_003888.3.
DR   RefSeq; WP_003976739.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; Q9S2X5; -.
DR   SMR; Q9S2X5; -.
DR   STRING; 100226.gene:17759674; -.
DR   PaxDb; 100226-SCO2076; -.
DR   PATRIC; fig|100226.15.peg.2109; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   InParanoid; Q9S2X5; -.
DR   OrthoDB; 9810365at2; -.
DR   PhylomeDB; Q9S2X5; -.
DR   Proteomes; UP000001973; 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; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF19302; DUF5915; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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_0000098564"
FT   MOTIF           52..62
FT                   /note="'HIGH' region"
FT   MOTIF           600..604
FT                   /note="'KMSKS' region"
FT   BINDING         603
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1047 AA;  116886 MW;  288C99247ADA7666 CRC64;
     MTTPQYRQVP AQVDLPALEH AVLDFWREQK IFAKSLEQSE GRPEWVFYEG PPTANGMPGA
     HHIEARVFKD VFPRFRTMRG YHVGRKAGWD CHGLPVELAV EKELGFSGKQ DIEAYGIAEF
     NAKCRESVTR HTDAFEELTT RMGYWADLQD PYRTMDPEYI ESVWWSLKEI FNKGLLVQDH
     RVAPWCPRCG TGLSDHELAQ GYETVVDPSV YVRFPLTSGP LAGEAALVVW TTTPWTLVSN
     TAVAAHPDVT YVVATDGEEK LVVAEPLLAK ALGEGWETTG QSFTGAEMER WTYQRPFELV
     EFPEPAHYVV NADYVTTEDG TGLVHQSPAF GEDDLKVCRA YGLPVVNPVR PDGTFEEDVP
     LVGGVFFKKA DEKLTEDLET RGLLFKHIPY EHSYPHCWRC HTALLYYAQP SWYIRTTAIK
     DRLLQENEKT NWFPDAVKHG RYGDWLNNNI DWALSRNRYW GTPLPIWRCA EDHLTVVGSR
     AELTELSGTD QSSLDPHRPF IDDVTFTCAQ EGCSLEAVRV PEVIDAWYDS GSMPFAQWGY
     PYKNKELFES RYPAQFISEA IDQTRGWFYT LMAVGTLVFD KSSYENVVCL GHILAEDGRK
     MSKHLGNILQ PIPLMDQHGA DAVRWFMAAG GSPWAARRVG HGTIQEVVRK TLLTYWNTVA
     FQALYARTTG WAPSEADPAP ADRPVLDRWL LSELHALTDQ VTQALDAYDT QRAGKLLSAF
     VDDLSNWYVR RSRRRFWQGD KAALRTLHEV VETVTKLMAP LTPFITERVW QDLVVPVTPG
     APESVHLSSW PEADLTAIDP ELSKQMVLVR RLVELGRATR AESGVKTRQP LSRALIAVAG
     FDTLSPELHS QITEELNVAS LASLSEVGGS LVDTTAKANF RALGKRFGKR VQDVAKAVAA
     ADAAALSLAL REGTASVEVD GETVTLAPDE VIITETPREG WSVASDSGAT VALDLELTEE
     LRRAGLARDA IRLIQEARKN SGLDVADRIA LRWTATDPAT IAALTDHSGL ISDEVLATDF
     AQGEADDSYG APFTDEGLSL VFRLRKQ
//