ID   SYI_CHLAB               Reviewed;        1043 AA.
AC   Q5L5L0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
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=CAB634;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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; CR848038; CAH64081.1; -; Genomic_DNA.
DR   RefSeq; WP_011097220.1; NC_004552.2.
DR   AlphaFoldDB; Q5L5L0; -.
DR   SMR; Q5L5L0; -.
DR   KEGG; cab:CAB634; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_0; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001012; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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.
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..1043
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098530"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           592..596
FT                   /note="'KMSKS' region"
FT   BINDING         595
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1043 AA;  119728 MW;  331B040D1C6F5114 CRC64;
     MHTEGEGSKE SLASREERIL NFWKTQEIFQ KSLKNREGRT LYSFYDGPPF ATGLPHYGHL
     LAGTIKDVVG RFATMDGYYV PRRFGWDCHG VPVEYEVEKS LNLTTPGAIE DFGVAKFNEE
     CRKIVFRYVD EWEHYIYRVG RWVDFSATWK TMDASFMESV WWVFRSLYDQ GLVYEGVKVV
     PFSTKLGTPL SNFEAGQNYK EVDDPSVVIK FALHGDPGSL LVWTTTPWTL VSNMAVAVGP
     EITYVRVADK VSGEQWILGQ GCLSRWFSDP DTYEVIESFP GTALIGKSYE PPFNFFEQKR
     AEGAYTILPG SFVEESEGTG VVHMAPAFGE ADFFVCKEHH VPMVCPVDNH GCFTEEIPEY
     QGQYIKSCDK GIIKSLKNQG KVFYHGTVVH RYPFCWRTDT PLIYKTVNSW FISVEKIKDK
     MLQANKKIHW VPEHIKEGRF GKWLEGARDW AISRNRYWGT PIPVWKSKDG DILVIGSVEE
     LEKLTGEKVS DLHCHFVDQL KIEKDGKSFH RVPYVFDCWF DSGAMPYAQN HYPFENQKET
     ESGFPADFIA EGLDQTRGWF YTLTVISAAL FDQPVFKNAI VNGIVLAEDG NKMSKRLNNY
     PSPMSIMNTY GADALRLYLL DSVVVKAEDL RFSDKGVESV LKQVLLPLTN VLSFFKTYTD
     LYGFDANNYD KEEISYSEID RWILSNLYTV VGKVRESMSS YNLNTAVNPF VTFIDDLTNW
     YIRRCRRRFW ESADTPDRRA AFATLYEVLT VFCRVIAPFI PFISEDIYQQ IKTENSLESV
     HLCDFPYIDL AKVFPDLEQR MGDAREIVGL GHSLRKEHKL KVRQPLANFY VVGPKDRLDQ
     LDSFKQLISE ELNVKNIVFY KEAPSFVKTT VKPNFRSLGR RVGEKIKDIQ KALASLSQAQ
     IQQLLTQEYL SLNLGSEEIV LHMEDVLISW ETDPGYVARS SSLFTVVLDC QLTEELVVEA
     ISRELVNKIN TMRRNQKLHV SDRIVLRMQT SEEVRKAFLH YADYICEETL TTQSEFADVL
     EGEEWDINGH PTVIAIEVAA RPH
//