ID   SYI_RICPR               Reviewed;        1086 AA.
AC   Q9ZCU4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   28-JAN-2026, entry version 128.
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=RP617;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC         COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC         Evidence={ECO:0000255|HAMAP-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; AJ235272; CAA15060.1; -; Genomic_DNA.
DR   PIR; B71667; B71667.
DR   RefSeq; WP_004596290.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCU4; -.
DR   SMR; Q9ZCU4; -.
DR   STRING; 272947.gene:17555696; -.
DR   EnsemblBacteria; CAA15060; CAA15060; CAA15060.
DR   GeneID; 57569742; -.
DR   KEGG; rpr:RP617; -.
DR   PATRIC; fig|272947.5.peg.636; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase 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   FunFam; 3.40.50.620:FF:000075; Isoleucine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000241; Isoleucine--tRNA ligase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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; Reference proteome; Zinc.
FT   CHAIN           1..1086
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098560"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1086 AA;  125637 MW;  DEC857A0D81E5963 CRC64;
     MTNTKYYPDV SANVDFAAIE QEILKFWQNN NIFQKSIDYR NGESEFIFYD GPPFANGLPH
     YGHLLTGFIK DVYARYKTIK GKKVERRFGW DCHGLPAEMQ SEKELGISGR IAITNFGIEK
     FNNHCRASVM QYASEWEQYV TRQARWVAFK NAYKTMDKNF MESVLWAFKE LYNKDLLYES
     MRVMPYSWAC ETPLSNFETR LDNAYRERTD KAITVSFVLN EVTLINGIIS QKSDMKEGDN
     FKEYRILAWT TTPWTLPANL ALAVGSDIDY AFVDKNEVCY IIAASSVAKY AKELGLSGKE
     NFEIIKGLKL QGLSYKPLFN YFENHPNSFK IFASDFVVEG DGTGIVHMAP GFGEDDQILC
     ESKGIELVCP VDNSGKFTKE IPDLEGVQVF DANDKIIIKL KEQGNWIKTE QYIHNYPHCW
     RTDTPLIYKA VPSWYVRVTK FKDRMVELNQ QINWIPHNVK DNLFGKWLEN ARDWSISRNR
     FWGTPLPVWK SDDPKYPRID VYGSIEEIEK DFGVKINDLH RPFIDELTRT NPDDPTGKST
     MRRIDDVFDC WFESGSMPYG QVHYPFENKK WFVEHFPADF IVEYSSQTRG WFYTLMVLST
     ALFDRPPFLN CICHGVILDA TGQKLSKRLN NYADPLELFD KYGSDALRVT MLSSNVVKGQ
     ELLIDKDGKM VFDTLRLFIK PIWNAYHFFT IYANADSLKG TLNFASQNVL DVYILSKLKI
     AVNKIEESLD NFDTQTAYHA VSEFFEVLNN WYIRRSRARF WKNEKDTDKQ NAYNTLYSCL
     KIMTIAMSAL IPMISETIYQ GLHNTAITQL NCLLSEGKHI VQNPMSDTQD YNTSVHLCNY
     PTLSDFEINY ELVSTMDNVL DICSNSLFIR STENIRVRQP LACITIISKH NNNLKDFEDL
     IKDEINVKTV IYRDDLENYA RKKLSLNFAI LGKRLPHKMK AIIDAAKKGE WEATTLGLAI
     CGEILNSDEY TLILEPYSHI KGTANFDNNS SLLILNLELT SELIEEGYAR DIVRFIQYAR
     KEADFSITDR ILIEIISEFD LSKIIDHYGD FIKEQTLGEF AKNFTPDYVS KVALENNQIQ
     LKVKRL
//