SYI_STRCO
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 03-AUG-2022, entry version 117.
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=SCO2076;
GN ORFNames=SC4A10.09;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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;
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; 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.SCO2076; -.
DR PRIDE; Q9S2X5; -.
DR GeneID; 1097510; -.
DR KEGG; sco:SCO2076; -.
DR PATRIC; fig|100226.15.peg.2109; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_11; -.
DR InParanoid; Q9S2X5; -.
DR OMA; PSWYIRT; -.
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 Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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 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.
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