ID   A0A231VVB5_9MICC        Unreviewed;      1115 AA.
AC   A0A231VVB5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003};
GN   ORFNames=B9K03_03510 {ECO:0000313|EMBL:OXT12203.1};
OS   Rothia sp. Olga.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia.
OX   NCBI_TaxID=1979525 {ECO:0000313|EMBL:OXT12203.1, ECO:0000313|Proteomes:UP000215251};
RN   [1] {ECO:0000313|EMBL:OXT12203.1, ECO:0000313|Proteomes:UP000215251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Olga {ECO:0000313|EMBL:OXT12203.1,
RC   ECO:0000313|Proteomes:UP000215251};
RA   Kim Y., Blasche S., Patil K.R.;
RT   "Kefir bacterial isolates.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00025217, ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000114, ECO:0000256|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000256|ARBA:ARBA00007078,
CC       ECO:0000256|HAMAP-Rule:MF_02003}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXT12203.1}.
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DR   EMBL; NDFM01000002; OXT12203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A231VVB5; -.
DR   EnsemblBacteria; OXT12203; OXT12203; B9K03_03510.
DR   Proteomes; UP000215251; Unassembled WGS sequence.
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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   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; 2.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_02003};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02003};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02003};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02003};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02003}; Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN          32..700
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          755..894
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          562..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           66..76
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   MOTIF           666..670
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT   BINDING         669
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1115 AA;  124517 MW;  910F5AA17F892F2F CRC64;
     MSENIYPKVS TFEAAGNGVS ASPQFPKLEE AVLDYWKKDG TFQASIDNRE AGPHGDNEFV
     FYDGPPFANG LPHYGHLLTG YAKDLVARYQ TQRGHKVERR FGWDTHGLPA ELEAMKQLGM
     TDKQEILEMG IDNFNDAARA SVLKYTNEWE QYVTRQARWV DFENDYKTLN VEYMESVIWA
     FKRLYDKGLT YQGFRVLPYC WKDETPLSNH ELRMDDDVYQ DRQDQTVTVA FTLTADDSLA
     ANKNVVAELA GVEALAWTTT PWTLPTNQAL AVGPDIEYVV VPGAGEHGGR RFLIAADLLG
     TYAKDLGYAG ENPAEDAAAA VTARYTGSQL EGVRYTPLWD YFADAEKWGT GTSWQILVAD
     YVSTTDGTGI VHQAPAYGED DQKVCESYDI PVVLSVDEGA RFLPLFGQPS PSGSTALAGI
     AGVQVFEANR TIINALKADG ALIVEKSYVH SYPHCWRCRN PLIYRAITSW YVKVTEFKDR
     MSELNEQINW IPENVKYGQF GKWVENARDW SISRNRFWGS PIPVWVSDDP NYPRVDVYGS
     LEELKADFGR LPLNKEGQPD LHRPYIDELT RPNPDDPTGK STMRRVEDVL DVWFDSGSMP
     YAQVHYPFEN KDWFENHYPA DFIVEYIGQT RGWFYTLHIL ATALFDRPAF KNVVSHGIVL
     GSDGQKMSKS LRNYPDVSEV LDRDGSDAMR WFLMSSPILR GGNLIVTEQG IREGVRQVML
     PLWNVYHFFA LYANAANKGA GYTAQVKYDS QHVMDRFILG KTRELVQQVT ADMDSYDIWS
     ACEHLRLYAD ALTNWYVRRS RERFFDEDPD AFDTLYTALV TVSKVAASLL PLTTEEIYRG
     LTGERSVHLA DWPAAEDFAD ESELLSLMET VRAVCSTGSS LRKEKKIRVR QPLQSLTAAI
     ANEQFAQLET AFGAKGADYF AKIVKDELNL REVILVNAQD ANPADYGISQ QLKVNARAAG
     PRLGKQVQAA IKASKSGDWT IAEDGTVTVA FNTIDGGLAL VDGEYELATV VASSDDGTER
     EAAAVLPGGF LVLNIELTDE LVAEGIARDT IRAIQQARKD AGLNVSDRIN LTVSAPQETL
     EALRTHEELV TGETLAVSLD LTEGETLTIT VAKAA
//