ID   SYI_RICPU               Reviewed;        1092 AA.
AC   C4K2T0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=RPR_07180;
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=562019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rustic;
RX   PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA   Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT   "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT   with virulent Rickettsia rickettsii: identification of virulence factors.";
RL   PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47875.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4K2T0; -.
DR   SMR; C4K2T0; -.
DR   PRIDE; C4K2T0; -.
DR   EnsemblBacteria; ACR47875; ACR47875; RPR_07180.
DR   KEGG; rpk:RPR_07180; -.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   OMA; KMMAPFT; -.
DR   Proteomes; UP000005015; 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..1092
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000216257"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           613..617
FT                   /note="'KMSKS' region"
FT   BINDING         616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1092 AA;  125622 MW;  3B4B4BD68D1C3416 CRC64;
     MTNTKYYPEV SSNADFAGLE REILKFWQDN NIFQKSIDDR NGESEFIFYD GPPFANGLPH
     YGHLLTGFIK DVYARYQTVK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAIANFGIEK
     FNAHCRASVM KYANDWEEYV TRQARWVDFK NSYKTMDKNF MESVLWAFKE LYNKGLLYES
     MRVMPYSWAC ETPLSNFETR LDNSYRERAD KAVTVSFVLS HPVATTTGSF KEYRILAWTT
     TPWTLPSNLA LAVGSDIDYA LVPKNDVCYI IAAYSVSKYA KELGLSGEEN FEIIKGSELQ
     GLHYKSLFDY FENHPNSFKI FAGDFVVEGD GTGVVHMAPG FGEDDQILCE SKGIELVCPV
     DNSGKFTKEI PNLEGLQVFD ANDKIIIKLK EQGNWLKTEQ YIHNYPHCWR TDTPLIYKAV
     PSWYVKVTQF KDRMVELNQQ INWIPFHVKD NLFGKWLENA RDWSISRNRF WGTPLPVWKS
     DDPKYPRIDV YGSIEELEKD FGVKVTDLHR PFIDELTRPN PDDPTGKSTM RRIEDVFDCW
     FESGSMPYGQ AHYPFENKEW FEDHFPADFI VEYSAQTRGW FYTLMVLSTA LFDRPPFLNC
     ICHGVILDST GQKLSKRLNN YADPLELFDK YGSDALRVTM LSSNVVKGQE LLIDKDGKMV
     FDTLRLFIKP IWNAYHFFTM YANADSLKGK LNFSSKNVLD VYILSKLKIA VQKIEESLDN
     FDTQTAYHAV SEFFEVLNNW YIRRSRARFW KSEKDTDKQN AYNTLYSCLD TMAIAMSALV
     PMISEAIYKG LRHCEERNDT ALSGKSNVIA RQDTSLDKAI SGVSHKIATA LSVPRNDAIS
     VHLCNYPTLS DFEINHELVA TMDNVLDICS NSLFIRSTEN IRVRQPLASI AIISKHNNNL
     KDFEDLIKDE INVKAVIYRD DLENYTSKKL SINFPMLGKR LPHKMKEIIV ASKKGEWEAI
     TGGLAICGET LNSDEYKLVL EPYSHIKGAA SFENNSSLLI LDLELTPELI EEGYARDIVR
     FIQQARKDAD FSITDRILIE IISEFNLSKI IDNYGDFIKE QTLGEFAKNF TPDYVSKVEL
     ENYQIQLKVK KS