ID   SYI_HALWD               Reviewed;        1059 AA.
AC   Q18GW3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, 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};
GN   OrderedLocusNames=HQ_2671A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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}.
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DR   EMBL; AM180088; CAJ52782.1; -; Genomic_DNA.
DR   RefSeq; WP_011571898.1; NC_008212.1.
DR   AlphaFoldDB; Q18GW3; -.
DR   SMR; Q18GW3; -.
DR   STRING; 362976.HQ_2671A; -.
DR   GeneID; 4194153; -.
DR   KEGG; hwa:HQ_2671A; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   Proteomes; UP000001975; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; 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; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 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..1059
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022149"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           606..610
FT                   /note="'KMSKS' region"
FT   BINDING         609
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1059 AA;  119617 MW;  E2353B1F064CE233 CRC64;
     MDEVDDQYTP ADVETAIETY WDDTNAYEAT KEAHADDPSF FFVDGPPYTS GQMHLGTAWN
     KTLKDAIIRY KRMTGHHVTD RPGYDMHGLP IEVKVEEELG FETKRDIEEY GMESFIEECK
     RFAVDNRKAM DEDFQSIGVW MDWDNPYETL SPEYMEAAWW AFQQVDDRGL VERGKRSVSY
     CPRCQTAIAA NEVEYDEITS PSIYVRFPLS NKEGSLVIWT TTPWTIPANT FVAVDKDLTY
     QAVRAEQGDD SEVLYIAESC VEDVLKQGRY DDYTVVEEYS GDELTGWEYD HPLADQVQTY
     ADFAGAGEVY TAEYVEADRT GLVHSAPGHG QEDFARGQEL DLETFVPVDG RGEFTEAAGQ
     YTGTFVRDAN DEIINDLDEE GVLLSSGTHE HRYGHCWRCD TDIIFLATDQ WFITVTDIKD
     ELLDNINDSE WYPQWARDNR FRDFVADAPD WNVSRQRYWG IPLPIWESVD DADTGDNSTS
     DDWIVIGTRE ELAERADQDV NPAEIDLHRP AVDPLTITEN GSRYERVPDV FDVWIDSSVA
     SWGTIDYPGE TDAYDELWPA DFIVEAHDQT RGWFWSQLGM GTAATGQVPY EEVMMHGFAN
     DENGRKMSKS RGNIVTPEEA IDRAGRDPLR AYLLSHDQQG VDLSFEWDGL GEMQSTLNIF
     WNVFRFPLPY MDLDGYDPAT ADLSEGSMNI VDEWVLSRLQ SVKATTRAAW EEYEIDTAVN
     TILEFITDDV SRFYIKAIRE RMWADEDSAS KRGAYATLST VLDETIRLLA PIAPYLTEQM
     YQHLNGSETT VHALSYPSVD PEWQNETLES EMAVLRDVEE AAANARQQGG RKLRWPVPRV
     IVEAEDDSIA DAVESLSGLL ADRVNTEAIE TVTQFDELIE RAQPEMSVIG PEFGADAQRV
     MDAIEGGSRE ILTEGVTIDG VQYEITDEMI TFDAEPPAYI SAADFDGGTV YVDTSLTESI
     EAEGYARDVI RRIQQMRKEL ALDVDTEIQT AVDVADDRVA DLVAQQRDVV ATETRTNAFV
     DNIDRASENG QALIEEWDVE GVTVTIGVAP LKAQLSDQS
//