ID   SYI_RICFE               Reviewed;        1094 AA.
AC   Q4UMD8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=RF_0423;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61274.1; -; Genomic_DNA.
DR   RefSeq; WP_011270758.1; NC_007109.1.
DR   AlphaFoldDB; Q4UMD8; -.
DR   SMR; Q4UMD8; -.
DR   STRING; 315456.RF_0423; -.
DR   PRIDE; Q4UMD8; -.
DR   EnsemblBacteria; AAY61274; AAY61274; RF_0423.
DR   KEGG; rfe:RF_0423; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   OMA; KMMAPFT; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008548; 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..1094
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098559"
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   1094 AA;  125428 MW;  8C4804C46D115EB6 CRC64;
     MTNTKYYPEV SSNADFAAIE REILKFWQDN NIFQKSIDDR NGESEFIFYD GPPFANGLPH
     YGHLLTGFIK DVYARYQTVK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAITNFGIEK
     FNSHCRASVM KYASDWEEYV TRQARWVDFK NSYKTMDKNF MESVIWAFKE LYNKGLLYES
     MRVMPYSWAC ETPLSNFETR LDNSYRERAD KAVTVSFVLN EIPAINGMTS RESGTTSSGD
     YKEYRILAWT TTPWTLPSNL ALAVGSDIDY ASIPKEDICY IIAASSVSKY AKELGLSGEE
     NFEIIKGSAL QGLSYKPLFD YFANHPNSFK IFAGDFVVEG DGTGIVHMAP GFGEDDQILC
     ESKGISLVCP VDNSGKFTKE IPDLEGVQVF DANDKIIIKL KEQGNWLKTE QYIHNYPHCW
     RTDTPLIYKA VPSWYVKVTQ FKDRMVELNQ QINWIPFHVK DNLFGKWLEN ARDWSISRNR
     FWGTPLPVWK SDDPKYPRID VYGSIEELEK DFGVKVTDLH RPFIDELARP NPNDPTGKST
     MRRIEDVFDC WFESGSMPYG QAHYPFENKK WFEDHFPADF IVEYSAQTRG WFYTLMVLST
     ALFDRPPFLN CICHGVILDA TGQKLSKRLN NYADPLELFD KYGSDALRVT MLSSNVVKGQ
     ELLIDKDGKM VFDTLRLFIK PIWNAYHFFT MYANADSLKG ELNFASQNVL DIYILSKLKI
     AVNKIEESLD NFDTQTAYHA VSEFFEVLNN WYIRRSRARF WKSEKDADKQ NAYNTLYSCL
     ETMAIAMSAL VPMISEAIYL GLCHKRPDVI ARKDLSLDEA ISGNSHEIAT ALSVPRNDGS
     ISVHLCNYPN LSSFEINHEL VATMDNVLDI CSNSLFIRST ENIRVRQPLA TITIISKHND
     KLKSFEDLIK DEINVKSVIY RDDLENYASK KLSINFPMLG KRLPAKMKEI IAASKKGEWE
     AIGGGLAICD ETLNSDEYKL VLEPHVHIKG AASFENNSSL LILDLELTAE LIEEGYARDI
     VRFIQQARKD ADFSITDRIL IEIISEFDLS KIIDNYGDFI KEQTLGEFSK NFTPDYVSKV
     ELENHQIQLK VKRS