ID   SYI_PELUB               Reviewed;         905 AA.
AC   Q4FPA9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; OrderedLocusNames=SAR11_0158;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(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_02002}.
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_02002};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}.
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_02002}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
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DR   EMBL; CP000084; AAZ20980.1; -; Genomic_DNA.
DR   RefSeq; WP_006997752.1; NC_007205.1.
DR   AlphaFoldDB; Q4FPA9; -.
DR   SMR; Q4FPA9; -.
DR   STRING; 335992.SAR11_0158; -.
DR   EnsemblBacteria; AAZ20980; AAZ20980; SAR11_0158.
DR   GeneID; 66294658; -.
DR   KEGG; pub:SAR11_0158; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_7_0_5; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002528; 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:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023585; Ile-tRNA-ligase_type1.
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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..905
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098435"
FT   MOTIF           56..66
FT                   /note="'HIGH' region"
FT   MOTIF           604..608
FT                   /note="'KMSKS' region"
FT   BINDING         563
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   905 AA;  105047 MW;  B8CD6E7541EDEF57 CRC64;
     MSKENINLPK TAFSMKANLQ NKEPEILEYW KKIDLYKELR KSNKGKEKFI LHDGPPYANG
     NIHMGTALNK ILKDIIVKFH QMDGKDSVYV PGWDCHGLPI EWKIEEQYKK NKKNKNEVPI
     TEFRKECREF AEKWIEVHKT QFKRLGVVGD WENHYATMSF EAEAQIVREL GKFLKEGSLY
     RGFKPVLWST VEKTALADAE VEYQDHKSDT IYTAFPVKKT NIKELENTDV IIWTTTPWTI
     PANKALAYNE ALDYLIIELG DEGDFKNKKI VVAEALLESV IKDCEIKSYK EIKKFKGKDF
     KDTICSHPFL ELGYDYDIPM LEARFVTTEQ GTGIVHCAPS HGPDDFNLCL KYGIKAIETV
     DGDGKYTKNL PLFEGTHIFK ANPIVIEKLK EQKKLLSNGE LVHSYPHSWR SKAPLVHRAT
     PQWFISMESH GLRKKALKAL DDTKFYPDKG RERIKAMIET RPDWCVSRQR VWGVPLPIFV
     HKTTKEILVD DNVNENIASI YEKEGSDCWF SDSPQRFLGD KYKAEDYEKI SDIVEVWFDS
     GCTHAFVLEK REDLQWPASM YLEGSDQHRG WFHSSLLESC GTRGRAPYES ILSHGFVVDG
     KGLKMSKSVG NVIAPEDILK KYGADILRIW VASSNYAEDL RIDYSILEQH ADSYRKIRNT
     FRYLLGNLND DFQKIDLESL DIKQLPELER YMLHRVYELN NNFKNYFKSY DFHNLYKELL
     NFCTVDLSSF YFDIRKDALY CDSKNSDRRK SSIVVLNIIL ESLVKWFAPI LSFTTEEIFT
     LINKEQKSIH LEQFMKYPES FQDEELHKKW IELKKIRDIC NISIEAKRAS KEIGSSLEAS
     LIINLNKSLF EISKNVDFSE ICITSSALVH QSNTDEIIIK TIKAEGNKCP VCWKINKVKC
     ERHSD