ID   SYI_HALMA               Reviewed;        1074 AA.
AC   Q5UZ84;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=rrnAC2634;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV47419.1; -; Genomic_DNA.
DR   RefSeq; WP_011224343.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UZ84; -.
DR   SMR; Q5UZ84; -.
DR   STRING; 272569.rrnAC2634; -.
DR   PaxDb; 272569-rrnAC2634; -.
DR   EnsemblBacteria; AAV47419; AAV47419; rrnAC2634.
DR   GeneID; 40153513; -.
DR   KEGG; hma:rrnAC2634; -.
DR   PATRIC; fig|272569.17.peg.3231; -.
DR   eggNOG; arCOG00807; Archaea.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   Proteomes; UP000001169; Chromosome I.
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   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..1074
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098576"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           605..609
FT                   /note="'KMSKS' region"
FT   BINDING         608
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1074 AA;  122156 MW;  D476C7E610567942 CRC64;
     MERFAAVDDQ YDPDAVEDGV FEYWDDVDAY EQTKAHRADG EDYFFVDGPP YTSGAAHMGT
     TWNKTLKDCY IRYLRMQGYN VTDRPGYDMH GLPIETKVEE RLDFENKKDI EQFGEENFIE
     ECKDFAEEQL EGLQTDFQDF GVWMDWDDPY KTVNPEYMEA AWWGFQQAHE RDLVEQGQRS
     INQCPRCETG IANNEVEYHD VGKPSIYVKF PLAEQDGSLV IWTTTPWTIV ANTFVAADGD
     LEYVGVDAEK DGDTERLYLA EACVEDVLKA GRYDDYEVVE ELSGEEMVGW AYEHPLAEEV
     PDHAQGEGSG QVYTADYVEA DRTGLVHSAP GHGEEDFERG QELDLEIFCP VGSDGVYTDD
     AGKYAGTFVR DANDEVIDDL DENGVLLSSE PGHTVREGQC WRCDTDIVRI VTDQWFITVT
     DIKDELLANI EDSEWYPQWA RDNRFRDFVE DAPDWNVSRQ RYWGIPIPIW LPEDWSGDMD
     DAIVVGDREE LAERVDQDID PENVDLHKGT VDDLTITEDS TTYTRVGDVF DVWLDSSVAT
     WGTVNYPEQT EDFEELWPAD LIMEAHDQTR GWFWSQLGMS TAATGEIPYK QVLMHGYANM
     PDGRGMSKSK GVLIDPHEVI EKHGRDPMRL FLLSVTAQGE DMNFSWEETA EMQRRLNILW
     NVARFPLPYM RADDFDPEET TVEDLRDDLE LVDEWVLSRL QSVTEAMTDS MDDFENDKAV
     DELLEFVVED VSRFYIQVVR ERMWEEEDSA SKQAAYATLY RVLESVAALF APFTPFVAEQ
     VYGALTGDAG HPTVHMCDWP EVDADLHDPA LEREIEVVRE VEEAGSNARQ QAERKLRWPV
     TRVVVDVDSD DVADAVRAQE AIIADRLNAR AVEVVGADDE WGELQYSAEA DMSELGPAFG
     DDAGRVMNAL NEARVTEQSL DTLEGTVREA LGEDVDLTEE MVEFRRETPE GVTGTEFTAL
     DGGGVVYVDT ALTEDIESEG YAREVIRRIQ EMRKDLELDI EERIAVDLTI DDERVDSLVR
     EHEALIKEEV RADELDGVED GHRKTWEVEG TDMEIAIAPC EADQREASEQ ASGD
//