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}; 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;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO44574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; 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
//
