ID   SYI_RICAE               Reviewed;        1092 AA.
AC   C3PP60;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
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};
GN   OrderedLocusNames=RAF_ORF0859;
OS   Rickettsia africae (strain ESF-5).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=347255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESF-5;
RX   PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA   Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA   Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT   "Analysis of the Rickettsia africae genome reveals that virulence
RT   acquisition in Rickettsia species may be explained by genome reduction.";
RL   BMC Genomics 10:166-166(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; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001612; ACP53720.1; -; Genomic_DNA.
DR   RefSeq; WP_012719895.1; NC_012633.1.
DR   AlphaFoldDB; C3PP60; -.
DR   SMR; C3PP60; -.
DR   KEGG; raf:RAF_ORF0859; -.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   Proteomes; UP000002305; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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; Zinc.
FT   CHAIN           1..1092
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000216256"
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;  125494 MW;  15ACF54252DACEDC CRC64;
     MTNTKYYPEV NSNADFAGLE REILKFWQDN NIFQKSIDDR NGELEFIFYD GPPFANGLPH
     YGHLLTGFIK DVYARYQTIK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAIANFGIEK
     FNAHCRASVM KYANDWEEYV TRQARWVNFK NSYKTMDKNF MESVLWAFKE LYNKGLLYES
     MRVMPYSWAC ETPLSNFETR LDNSYRERAD KAVTVSFVLS HPVATTTGSF KEYRILAWTT
     TPWTLPSNLA LAVGSDIDYA LVPKNDVCYI IAAYSVSKYA KELGLSGEEN FEIIKGSALQ
     GLNYKSLFDY FENHPNSFKI FAGDFVVEGD GTGVVHMAPG FGEDDQILCE SKGIELVCPV
     DNSGKFTKEI PDLEGLQVFD ANDKIIIKLK EQGNWLKTEQ YIHNYPHCWR TDTPLIYKAV
     PSWYVKVTQF KDRMVELNQQ INWIPFHVKD NLFGKWLENA RDWSISRNRF WGTPLPVWKS
     DDPKYPRIDV YGSIEELEKD FGVKVTDLHR PFIDELTRPN PDDPTGKSTM RRIEDVFDCW
     FESGSMPYGQ AHYPFENKEW FEDHFPADFI VEYSAQTRGW FYTLMVLSTA LFDRPPFLNC
     ICHGIILDST GQKLSKRLNN YADPLELFDK YGSDALRVTM LSSNVVKGQE LLIDKDGKMV
     FDTLRLFIKP IWNAYHFFTM YANTDSLKGK LNFSSKNVLD VYILSKLKIA VQKIEESLDN
     FDTQTAYHAV SEFFEVLNNW YIRRSRARFW KSEKDTDKQN AYNTLYSCLD TMAIAMSALV
     PMISEAIYKG LHHCEERNDT ALSGKSNVIV RKDTSLDKAI SGVSHKIATA LSVPCNDAIS
     VHLCNYPTLS DFEINHELVA TMDNVLDICS NSLFIRSTEN IRVRQPLASI AIISKHNNNL
     KDFEDLIKDE INVKAVIYRD DLENYASKKL SINFPMLGKR LPHKMKEIIA ASKKGEWEAI
     AGGLAICGET LNSDEYKLVL EPYSHIKGAA SFENNSSLLI LDLELTPELI EEGYARDIVR
     FIQQARKDAD FSITDRILIE IISEFNLSKI IDNYGDFIKE QTLGEFAKNF TPDYVSKVEL
     ENHQIQLKVK KS
//