ID   SYI_CHLTR               Reviewed;        1036 AA.
AC   O84022;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=CT_019;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE001273; AAC67609.1; -; Genomic_DNA.
DR   PIR; F71565; F71565.
DR   RefSeq; NP_219521.1; NC_000117.1.
DR   RefSeq; WP_010724987.1; NC_000117.1.
DR   AlphaFoldDB; O84022; -.
DR   SMR; O84022; -.
DR   STRING; 813.O172_00105; -.
DR   EnsemblBacteria; AAC67609; AAC67609; CT_019.
DR   GeneID; 884097; -.
DR   KEGG; ctr:CT_019; -.
DR   PATRIC; fig|272561.5.peg.24; -.
DR   HOGENOM; CLU_001493_1_0_0; -.
DR   InParanoid; O84022; -.
DR   OMA; HLGTAWN; -.
DR   Proteomes; UP000000431; 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   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..1036
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098529"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           589..593
FT                   /note="'KMSKS' region"
FT   BINDING         592
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1036 AA;  118985 MW;  DC4420FD37343EFD CRC64;
     MDNEDKISIS AKEEKILSFW KEQDIFQKTL DNREGCPTFS FYDGPPFATG LPHYGHLLAG
     TIKDVVCRYA SMDGHYVPRR FGWDCHGVPV EYEVEKSLGL TEPGAIERFG VANFNEECRK
     IVFRYADEWK YFVDRIGRWV DFSATWRTMD LSFMESVWWV FRSLYDQGLV YEGTKVVPFS
     TKLGTPLSNF EAGQNYKEVD DPSVVVKFAL QDNQGFLLAW TTTPWTLVSN MALAVHPELT
     YVRIKDKESG DEYILGQESL PRWFPDRESY EWIGQLSGKS LVGQSYEPLF PYFQDKKELE
     AFRILPADFI EESEGTGIVH MAPAFGEADF FACQEHNVPL VCPVDNQGCY TAEVKDFVGE
     YIKSADKGIA RRLKNENKLF YQGTVRHRYP FCWRTDSPLI YKAVNSWFVA VEKVKSKMLK
     ANESIHWTPE HIKQGRFGKW LEGARDWAIS RNRYWGTPIP IWRSDDGELL VIGSIQELEA
     LSGQKIVDLH RHFIDEIEIN QNGKSFRRIP YVFDCWFDSG AMPYAQNHYP FERAEETEAC
     FPADFIAEGL DQTRGWFYTL TVIAAALFDQ PAFKNVIVNG IILAEDGNKM SKRLNNYPSP
     KMIMDAYGAD ALRLYLLNSV VVKAEDLRFS DKGVESVLKQ VLLPLSNALA FYKTYAELYG
     FDPKETDNIE LAEIDRWILS SLYSLVGKTR ESMSQYDLHA AVNPFVDFIE DLTNWYIRRS
     RRRFWDAEDS ADRRAAFSTL YEVLVVFSKV IAPFIPFIAE DMYQQLRGET DPESVHLCDF
     PHVVLEKILP DLERKMQDIR EIVALGHSLR KEHKLKVRQP LQNVYIVGSK ERKEALAQVG
     SLIGEELNVK DVHFCSETPE YVTTLIKPNF RTLGKKVGNR LPEIQRALAG LPQEQIQAFM
     HKGQMVVSLG EETISLDKED ITVSWASAEG FVARSSASFV AVLDCQLTEP LIMEGIAREL
     VNKINTMRRN RKLHVSDRIA IRLHAPVIVQ EAFALHKEYI CEETLTTSVS VIDYKEGEEW
     DINGHAVSFV LERVER