ID   SYI_RICCK               Reviewed;        1079 AA.
AC   A8EY49;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=A1E_01685;
OS   Rickettsia canadensis (strain McKiel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=293613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=McKiel;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia canadensis.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000409; ABV73282.1; -; Genomic_DNA.
DR   RefSeq; WP_012148481.1; NC_009879.1.
DR   AlphaFoldDB; A8EY49; -.
DR   SMR; A8EY49; -.
DR   STRING; 293613.A1E_01685; -.
DR   PRIDE; A8EY49; -.
DR   EnsemblBacteria; ABV73282; ABV73282; A1E_01685.
DR   KEGG; rcm:A1E_01685; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   OMA; KMMAPFT; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000007056; 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; Zinc.
FT   CHAIN           1..1079
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022160"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           611..615
FT                   /note="'KMSKS' region"
FT   BINDING         614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1079 AA;  124622 MW;  10C7C57F24B79612 CRC64;
     MTNTKYYPEV SSNADFAAIE REILKLWQDN NIFQKSIDNR IKDAEFIFYD GPPFANGLPH
     YGHLLTGFIK DVYARYQTIK GKKVERRFGW DCHGLPAEMQ SEQELGISGR LAITNFSIEK
     FNSHCRASVM KYTGEWEQYV TRQARWVDFK NSYKTMDTHF MESVLWAFKE LYNKGLLYES
     MRVMPYSWAC ETPLSHFETR LDNSYRERAD KAVTVSFMLR DKLPHSEYKE YRIFAWTTTP
     WTLPANLALA VGSDIDYALV PKNDICYIIA AASVSKYAKE LELKGDEQFT IIKGSELEGL
     RYKPLFNYFE NHPNSFKIFA CDFVVEGDGT GVVHMAPGFG EDDQILCESK GIELVCPVDN
     SGKFTKEIPD LEGLQVFDAN DKIIIKLKEQ GNWLKTEQYI HNYPHCWRTD TPLIYKAVPS
     WYVKVTNFKD RIVELNQQIN WIPSHVKDNV FGKWLENARD WSISRNRFWG TPLPVWKSDD
     PKYPRIDVYG SIEELEKDFG VKVTDLHRPF IDELTRANPD DPTGKSTMRR IEDVFDCWFE
     SGSMPYSQAH YPFENKKWFE DHFPADFIVE YVAQTRGWFY TLMVLSTALF DRPPFLNCIC
     HGVILDTTGQ KLSKRLNNYA DPLELFDKYG SDALRITMLS SNVVKGQELL IDKDGKMVFD
     TLRLFIKPIW NAYHFFTMYA NADSLKGKSD FASENVLDIY ILSKLKIAVQ KIEKSLDNFD
     TQAAYHQVSE FFEVLNNWYI RRSRARFWKS EKDADKQNAY NTLYSCLETM AIAMSALVPM
     ISEAIYLGLH NTVIPQLDYG ISGDKPGAQD PIIKSQDGIR GCRNDNLSVH LCNYPKLSNF
     EVNHELVATM DTVLDICSNS LFIRSNENVR VRQPLASITI ISKHNDKLKD FEDLIKDEIN
     VKAIIYRDDL ENYATTKLSL NFPMLGKRLP YKMKEIIAAS KKGEWEATAS ALAICGETLK
     SEEYKLVLEP YSHIKGAASF ADNSSLLILD LELTPELIKE GIARDIVRFI QQARKDADCS
     ITDRILIEII SESDLSKIIN IYGDYIKEQT LSEFAKDFTP DYVNEIELEN HKIQLKIKR