ID   SYI_CHLCV               Reviewed;        1043 AA.
AC   Q822L8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=CCA_00664;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
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; AE015925; AAP05406.1; -; Genomic_DNA.
DR   RefSeq; WP_011006621.1; NC_003361.3.
DR   AlphaFoldDB; Q822L8; -.
DR   SMR; Q822L8; -.
DR   STRING; 227941.CCA_00664; -.
DR   KEGG; cca:CCA_00664; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_0_0; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002193; 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_0000098531"
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;  119911 MW;  39606F73FF6A6635 CRC64;
     MNTEGESSKE SLANREERIL DFWKTHDIFQ KSLKNREGKT LYSFYDGPPF ATGLPHYGHL
     LAGTIKDVVG RFATMDGYYV PRRFGWDCHG VPVEYEVEKS LDLTTPGAIE DFGVAKFNEE
     CRKIVFRYVD EWERYVHRLG RWVDFSVTWK TMDASFMESV WWVFRSLYDQ GLVYEGVKVV
     PFSTKLGTPL SNFEAGQNYK EVDDPSVVIK FALHGDPASL LVWTTTPWTL VSNMAAAVGP
     EITYVRVADK VSGEQWILGQ GCLSRWFSDP DSYEILESFL GTALVGKSYE PPFSFFEHKR
     AEGAYKILSG SFVEESEGTG VVHMAPAFGE ADFFVCKEHH VPIVCPVDNH GCFTEEIPEY
     QGQYIKSCDK GIIKSLKNLG KVFYHGTVMH RYPFCWRTDT PLIYKTVNSW FVSVEKIKDK
     MLRANQKIHW VPEHIKEGRF GKWLDGARDW AISRNRYWGT PIPIWKSKEG EILVIGSVKE
     LEELTGEKIS DLHCHFIDQL KVEKEGKTFQ RVPYVFDCWF DSGAMPYAQN HYPFENQKET
     EAGFPADFIA EGLDQTRGWF YTLTVISSAL FDQTAFKNAI VNGIVLAEDG NKMSKRLNNY
     PSPMGIMNTY GADALRLYLL DSVVVKAEDL RFSDKGVESI LKQILLPLTN VLSFFKTYTD
     LYGFDADNYD KEEITYSEID RWILSNLYTV VGKVRESMSS YNLNTAVNPF VTFIDDLTNW
     YIRRCRRRFW ESEDTPDRRA AFATLYEVLT VFCRVIAPFI PFISEDIYQQ IKTEHSAESV
     HLCDFPHIDL AKVFPDLEQR MSDAREIVGL GHSLRKEHKL KVRQPLANFY IVGPKDRLDE
     LTSFEQLIAE ELNVKNIVFY KETPSFVKTT VKPNFRSLGR KVGEKIKDVQ RALSNLSQDQ
     IQQLLKQQYL LLNLGFEEIT LGIDDVVISW ETDPGYVARS SSLFTVVLDC QLTEDLIVEA
     ISRELVNKIN TMRRNHKLHV SDRILLQIHS SEDVEKAFLH YEDYICEETL TVQFEFKDSV
     EGEEWDINGH PTVIALTVAS KAN
//