ID   SYI_RICBR               Reviewed;        1108 AA.
AC   Q1RIY1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=RBE_0602;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04683.1; -; Genomic_DNA.
DR   RefSeq; WP_011477271.1; NC_007940.1.
DR   AlphaFoldDB; Q1RIY1; -.
DR   SMR; Q1RIY1; -.
DR   STRING; 336407.RBE_0602; -.
DR   EnsemblBacteria; ABE04683; ABE04683; RBE_0602.
DR   KEGG; rbe:RBE_0602; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   OMA; KMMAPFT; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001951; 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; IPR022439; RPE4.
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   TIGRFAMs; TIGR03777; RPE4; 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..1108
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000273379"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           654..658
FT                   /note="'KMSKS' region"
FT   BINDING         657
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1108 AA;  127566 MW;  E75F20C1644FE1CF CRC64;
     MTNTKYYPEV SSNADFATIE KEILKFWQDN NIFQKSIDIR EGDAEFIFYD GPPFANGLPH
     YGHLLTGFIK DVYARYQTVR GKKVERRFGW DCHGLPAEMQ SEKELGISGH LAITNFGIEK
     FNAHCRDSVM KYAGEWEQYV TRQARWVDFK NSYKTMDKNF MESVLWAFKE LYNKGLLYES
     MRVMPYSWAC ETPLSNFETR LDNSYRERAD KAVTVSFVLC HPVSKSTLDV IPWLDHGIQK
     TINNDSANCS MDPVDKPRYD TENFLGITAN YKEYRILAWT TTTWTLPSNL ALAVGSDIDY
     ALVPKGDVCY IIAASSVSKY AKELELKGDE QFTIIKGSEL QGLSYKPLFD YFKNHPNSFK
     IFAGDFVVEG DGTGVVHMAP GFGEDDQILC ESKGIKLVCP VDNSGKFTKE IPDLEGLQVF
     DANDKIIIKL KEQGNWLKTE QYIHNYPHCW RTDTPLIYKA VPSWYVKVTE FKDRMVELNQ
     QINWIPTHVK DNLFGKWLEN ARDWSISRNR FWGTPLPVWK SDDPKYPRID VYGSIEELEK
     DFGVKITDLH RPFIDELTRA NPDDPTGKST MRRIEDVFDC WFESGSMPYG QAHYPFENKQ
     WFEEHFPADF IVEYSAQTRG WFYTLMVLST ALFDRPPFLN CICHGVILDA TGQKLSKRLN
     NYADPLELFD KYGSDALRVT MLSSNVVKGQ ELLIDKDGKM VFDTLRLFIK PIWNAYHFFT
     MYVNADHIKG ELNFTSENVL DVYILSKLKI AVEKIKESLD SFDTGTAYHA VSEFFEVLNN
     WYIRRSRARF WKSEKDADKQ SAYNTLYTCL ETMAIAMSSL VPLISEAIYL GLYCHPRKSG
     DPEKPECLDS RLCGNDNLSV HLCDYPDLSK FKINSELVDT MDTVLDICSH SLFIRSSENA
     RVRQPLSSIT IISKNNDKLK SFEDLIKDEI NVKSVIYRDD LENYAVKKLS INFPLLGKRL
     PAKMKDIIAA SKKNEWEVTS GSLIICNETL NSDEYKLILE PHSHIKGASS FAHNSSLLIL
     DLELTPELID EGIARDIVRF IQQARKNADF AITDRILIDI NLPKITDIYG EFIKEQTLGE
     FAKDFIPDHI SEIELDNHKL QLKIKKVN