ID SYI_NATPD Reviewed; 1061 AA.
AC Q3ITY7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=NP_0610A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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}.
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DR EMBL; CR936257; CAI48396.1; -; Genomic_DNA.
DR RefSeq; WP_011322032.1; NC_007426.1.
DR AlphaFoldDB; Q3ITY7; -.
DR SMR; Q3ITY7; -.
DR STRING; 348780.NP_0610A; -.
DR EnsemblBacteria; CAI48396; CAI48396; NP_0610A.
DR GeneID; 3702863; -.
DR KEGG; nph:NP_0610A; -.
DR eggNOG; arCOG00807; Archaea.
DR HOGENOM; CLU_001493_1_1_2; -.
DR OrthoDB; 30823at2157; -.
DR Proteomes; UP000002698; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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..1061
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098585"
FT MOTIF 50..60
FT /note="'HIGH' region"
FT MOTIF 604..608
FT /note="'KMSKS' region"
FT BINDING 607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1061 AA; 120589 MW; 2B24147A2FCB2EA2 CRC64;
MSRFAEVDDQ YDPDAVEDRV FDYWDEVDAY ERTVEHRADG EDFFFVDGPP YTSGSAHMGT
TWNKTLKDAY IRYHRMRGYN VTDRPGYDMH GLPIETKVEE RLGFDNKKDI EEFGEQNFID
ECKSFAEEQL EGLQEDFKSF GVWMDWDDPY KTVDPEYMEA AWWGFSKAHD RDLVEQGQRS
ISQCPRCETA IANNEVEYDH VEDPSIYVKF PLAEREGHLV IWTTTPWTVP ANTFVAVDEE
MTYQAIEVDT GDGTETLYVG EPCVEDVVDH GGYEDYEVVG EHEGSDLVGW RYEHPLREEV
PEAPAFEGAL EVYGADYVEA DRTGLVHSAP GHGEVDFERG QELGLSVFCP VGPDGVYEDA
AGDYAGQFVK DADAAIMDDL EAKGLLLSRG TVNHDYGHCW RCDTPIIQMV TDQWFITVTD
IKDELLANME ESEWFPQEAR DNRFRSFIEE SPDWNVSRQR YWGIPIPIWT PDDWSGDVEE
AIVVSTREEL AERVDQDIDP ESVDLHKDTV DDLTITADGT TYTRVPDVFD VWLDSSVASW
GTLGYPGNED DFEELWPADL IMEAHDQTRG WFWSQLGMGS AALGEAPYET VLMHGWALAE
DGRKMSKSIG NIVAPQEAID RHGADPMRLF LLTQNPQGDD MRFSWDEMEN RQRDLNILWN
VFRFPLPYMR LDDFDPDAVA LDEAALETVD EWVLSRLSTV TAEMTDHWEN FRQDKALDEL
LAFIVEDVSR FYIQVVRERM WEEETSESKL AAYATLHHVL VETTKLLAPY APFVAEEIYG
TLTGDGGHET VHMADWPDPD ERFRDPQLET DVDIVAAVEE AGSNARQQAE RKLRWPVTRV
VVAADDDRAA EAVDRHRDLL RDRLNAREIE LVEPGSDWEE LSYTARADMS VLGPTFGDEA
GEVMNAINAV SVTDTAVEAL EAAVETELGR DIELTDEMVS FNTETPEGVE GTAFTVDGDD
RGVVYVDTAL TEDIESEGYA REVIRRVQEM RKDLDLDIEA EIRVDLDIAD ERVATLVDEH
EGLIADEVRA AEFADLNAGH ERVWDVESTD ITITIDPVSE R
//
