ID   SYI_TROWT               Reviewed;        1056 AA.
AC   Q83G52;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   27-MAR-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=TWT_477;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC   Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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=AAO44574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014184; AAO44574.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011096241.1; NC_004572.3.
DR   AlphaFoldDB; Q83G52; -.
DR   SMR; Q83G52; -.
DR   STRING; 203267.TWT_477; -.
DR   GeneID; 67388063; -.
DR   KEGG; twh:TWT_477; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002200; 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; HUPs; 2.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
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; 2.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1056
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098571"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           63..73
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1056 AA;  119751 MW;  D1D531A27E790967 CRC64;
     MCDQGEVSSQ NSSDYKEQRP TPRPNLPKIE ESVLAFWSSD KTFEASLEQR QHGKRWVFYD
     GPPFANGLPH FGHLLTGYIK DAIPRYQTMR GQYVPRVFGW DTHGLPAELE AMKRLGITEK
     SQIESMGIAS FNEAARKSVL TYVDQWEEYV NRQARWVDFK NGYKTLDLDY MESVLWAFKT
     LYKKGVIYEG YKVLPYCWND QTPLSNHELR MDDEVYKQRL DDSLTVTFPL IGQKAKTCGL
     DGVAALAWTT TPWTLPSNMA LIVSPNVEYV VVSSARQNSN SDFLLCKSSL DSYAECLGYE
     SGQDARASIR RTLLGKEIEG IHYKPLFDYY ADLHNAFTIL SDNYVDVTEG TGIVHASPAH
     GEDDKRVCDA FGVPTVVSIN DAACFTDVIS NYAGMHIFDA NAVIRSDLSR DGRILRHESY
     KHSYPHCWRC RSPLIYKAVT SWFFRITDSV NRMLELNQQI NWVPKSVKNG QFAKWLSSAK
     DWSISRTRYW GTPIPVWKSD NPEYPRIDCY GSLKELEDDF GIKLTDLHRP EIDRLTRPNP
     DDPTGASTMR RVPDVLDVWF DAASMPFAQL HYPFENIERF EANKSADFIV EYAGQIRGWF
     YLLHAMSTAL FDGVAFKNAI CHGIVLGDDG QKASKSLRNY PDVYDVFENE GSDAVRWYLI
     SSSILRGGSL IVSRKKIQDA IRQYITPLWS SWYFFHIYSE AARPGGYKAR FSVDSQDILD
     RYILSKTGLL VEDVTRFMDS FDMASAALQL RDFVAVLTNW YIRRSRDRFW DGSDTGAFDT
     LYTVLETLCR LGAVFVPMVS EHVYKCLTNS RSVHLSDWPD VATFPNETGL VETMDRVRKI
     CSTGLSLRKR LGIKARQPLS SAHIRVAQVG SLAQYKDIIS GELNVKTVSI EEGSCTQRML
     KILPRVAGPR LAGDVQTVIA AARRGDWTDH DGHVTAGGIP LLENEYQLVA GAQDSKNSQP
     LPFGGSVTLD TRIDETLRSE GVARDTVRQI QIARKEKDLN ITDRISLEVC VPDEQVKNNL
     LAFSELICKE TLCDRLDILV KKGIDGITVS LEKFRQ
//