ID   SYI_PARUW               Reviewed;        1038 AA.
AC   Q6MDY1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=pc0494;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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; BX908798; CAF23218.1; -; Genomic_DNA.
DR   RefSeq; WP_011175044.1; NC_005861.1.
DR   AlphaFoldDB; Q6MDY1; -.
DR   SMR; Q6MDY1; -.
DR   STRING; 264201.pc0494; -.
DR   EnsemblBacteria; CAF23218; CAF23218; PC_RS02405.
DR   KEGG; pcu:PC_RS02405; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_0; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000529; 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   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; 1.
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..1038
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098553"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           591..595
FT                   /note="'KMSKS' region"
FT   BINDING         594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1038 AA;  120225 MW;  9A85E181CB977895 CRC64;
     MFEEVLQESF DEREKKVLKF WQEGQLFERS VENRKGQPLF TFYDGPPFAT GLPHYGHILA
     GTIKDVVLRY KTMKGFCAPR RFGWDCHGLP VENEIEKTFG LSGAKSIEEF GIAKFNEECR
     NIVLRYTEEW KFTVNRMGRW VDFNQTYRTM DLPFMESVWW VFKQLYAKGL VYEGLKVMPF
     SAKLGTPLSN FEASENYKEV DDPSLTVAFQ SRDNSNTYFL AWTTTPWTLV SNLALMVSPM
     IEYAEVQDHV SKRNYILATE RLKGYYKDSG EYTIVRKFPG SELEGQHYIP LFDYFNDRAH
     SGAFKIILED SISVEEGTGI VQTAPAFGEI DFYACQKAGI DPVCPVDNNG QFTDEIPEYK
     GIFVKEADKD IIKRLKQQAK VIHQGTCHHR YPFCPRSDTP LIYKTVRTWF VAVEKIKDRL
     LAANSQIHWT PEHIQYGRFG KWLEGARDWA ISRNRYWGTP IPLWRAQDGE IHVVGSIEEL
     KQLTGNPLTD LHRHFIDEMS FEKNGKTFKR IPEVFDCWFE SGSMPYAQNH YPFENRELFE
     QNFPADFIAE GLDQTRGWFY TLTVLSAALF DQPAMKNVIV NGLILAENGA KMSKRLKNYP
     DPAEVIQQYG ADAIRLYMLH SPAVKADDLS FSKSGVELVL RQILLPLWNA YTFFLTYARI
     YNWKPGKLVQ KPELAIDQWI ISLLNKLVHE VEQGMDDYDL SRSVEPFVNF VDQLTNWYIR
     RSRRRFWDDK ESPNRTQAFE TLYYVLIELT KISAPYVPFI SEAIYQNLRS CDMPESVHLC
     DFPHYQQLSR HEKLEAEMEA VQVTVSLGHA LRKEHKLKVR QPLATAQLAS ADPKVLDFLK
     EQQHLISEEL NVKEITFSSN EKDFVSLKAK PNFRVLGKKV GKLMKLAQLT IEQFGQKELT
     ELLNHRSVEI ILEGHPVLLT SEDVQVERIV REGIIAANQG TITIALNTNL NKELLLEGLA
     REIVNKVNTM RREANFAVTD RIQLYMQTTT RVIECFDQYK NYICQEVLAT DVQFGPYEGT
     DWDLNGEPTK IIIKKSEY