ID   SYI_AQUPY               Reviewed;         529 AA.
AC   P46207;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Isoleucine--tRNA ligase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
DE   Flags: Fragment;
GN   Name=ileS;
OS   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7708661; DOI=10.1073/pnas.92.7.2441;
RA   Brown J.R., Doolittle W.F.;
RT   "Root of the universal tree of life based on ancient aminoacyl-tRNA
RT   synthetase gene duplications.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995).
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) (By
CC       similarity). {ECO:0000250}.
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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)) (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 1 subfamily. {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; L37096; AAA87287.1; -; Genomic_DNA.
DR   PIR; I39658; I39658.
DR   AlphaFoldDB; P46207; -.
DR   SMR; P46207; -.
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-KW.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF50677; SSF50677; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           <1..>529
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098342"
FT   MOTIF           523..527
FT                   /note="'KMSKS' region"
FT   BINDING         482
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000250"
FT   BINDING         526
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         529
SQ   SEQUENCE   529 AA;  61379 MW;  FB6C40D69E26DDD8 CRC64;
     DTHGLPIERA VEKELSKKKI RKESLPKTEF RKLCREYANR YVNIQKEEFI RLGVLGDWEN
     PYLTMSPEYE ATEIRELGKF FEKGLAYRSK KPVYWCIYDK TAEGQAEVEY YEKEDPSIYV
     KFPLKKEIEG KKAYAVIWTT TPWTLPANLG IMVKEDADYS LVEVEGEVWI VAKELLENFF
     KNIGKTYTRV LKDVKGRDLV GLEYEHPFVD RDELKGYLSE ETLKNMWRIY PSEFVSLDTG
     TGLVHMAPGH GQEDYTVGKR YNLEPYAPLD DSGRFVEPAP EFIRGVRVFD ANKLIIALLK
     EKGYLVHEAR IRHSYPHCWR CKNPVIFRAT PQWFIGMDIE YEGKTLSGES LEEIEKVKWI
     PEYGKNRIKS MVENRPDWCI SRQRFWGVPI TVFYCENCGE VIKDKEVFER IASLVEKHPG
     GTDVWFEKSP EEILPEGYKC PKCGGTSFRK EEDILDVWFD SGCSHASVIR PLGFEKADLY
     LEGSDQHRGW FQASLLESVG SYGEAPYRSV LTHGFIVDEQ GRKMSKSLV