ID   SYI_EHRRG               Reviewed;        1118 AA.
AC   Q5FH91;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   24-JAN-2024, entry version 120.
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=ERGA_CDS_05000;
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(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; 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   -!- SEQUENCE CAUTION:
CC       Sequence=CAI27952.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR925677; CAI27952.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q5FH91; -.
DR   SMR; Q5FH91; -.
DR   KEGG; erg:ERGA_CDS_05000; -.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   Proteomes; UP000000533; 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..1118
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098544"
FT   MOTIF           64..74
FT                   /note="'HIGH' region"
FT   MOTIF           647..651
FT                   /note="'KMSKS' region"
FT   BINDING         650
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1118 AA;  130722 MW;  1DB03A3249BFB06C CRC64;
     MCIVKTLHLI THVMKEYNSQ FTEGSDFSLI EEQILEFWKE NNIFKKSIEN RDEKRRFVFY
     DGPPFANGLP HYGHLLTGFI KDTVARYKTM AGFRVDRRFG WDCHGLPAEM LAEKELGVSG
     KLAIEEFGIE KFNNYCRNSV MKFSREWKQY IDRQSRWVDF ENDYKTMNLS FMESIMWSFY
     QLWQKGLIYE SIKIVPYSWA CQTPLSNFET RIDNAYRQKT SKTVTLAFEL LDAPKSLIVD
     NITAYKILVW TTTPWTLPCN LALAISPNIK YCGAIINKEM YIFSRAYLKN FEDHCKKNNI
     EYLIHSDDIC YLSLEYLSYK PVFNYFIDIK NAFKVLVADF VVEDEGTGIV HMAPGFGEDD
     FILCKKQGIP DIDDKDTSKL LATICPIDDG GKFTERISDF VNMHVFDTND QIISILKAKN
     LCFKTDQYLH NYPHCWRTDT PLIYRAMSSW YVEVTKIKNR MIDLNKDVNW IPSHIRSGQF
     GKWLENAKDW AISRNRFWGT PLPVWKSDNP NYPRIDVYGS IKKVFDDIKA LEEDFDIPID
     DLHRPYIDNL VRPNPDDPTG KSMMRRVTDV FDCWFESGSM PYAQLHYPFE NKELFENYFP
     ADFITEYVAQ TRGWFYTLFV LSTALFDKPP FKNCICHGVV LDTQGQKLSK RLNNYADPME
     IFKQYGSDAM RFLMLSHTVS YGGDLLLDKD GVMVRDVIRN VIKPMWNSYN FFTIYADIDK
     VSARVISDLD EVDNIMDKYI MCECISTIQS IFNAMEEFDQ SVGNYGYNIK AACNSIVQFF
     EVLNNWYIRR CRSRFWSSEI TKDKVNAYNT LYTVMYYMVK VSAPFLPAIT EAIWQKLNFQ
     EEESVHLSLL PNIEHITLKD EDQKNIQYMK LIINICGCVL SIRNVRNIRV RQPLNKITIY
     SYNNNNDLFN LPVKYQNILL DEINVKSIVF KSNIEDIASF QLKLNFPELG KRIPEKMKNL
     ISLLKSNQWK VLENGQLMLG IREGEYYILE DNEYTLNLKV HSEFASTITL GPNLLGVLVL
     DNTLTDELIM EGIARDIVRI IQQSRKDNKF NVSDKIDVVI CTQDKMVKNS VQAWYEYIVQ
     QTLSLSLVIH ENLDANNVAE YCKTTMKDRN LTLFIKKL
//