ID   SYI_NOCFA               Reviewed;        1042 AA.
AC   Q5YYW9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=NFA_17760;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(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; AP006618; BAD56622.1; -; Genomic_DNA.
DR   RefSeq; WP_011208307.1; NC_006361.1.
DR   AlphaFoldDB; Q5YYW9; -.
DR   SMR; Q5YYW9; -.
DR   STRING; 247156.NFA_17760; -.
DR   GeneID; 61132557; -.
DR   KEGG; nfa:NFA_17760; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000006820; 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; 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.
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..1042
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098551"
FT   MOTIF           59..69
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1042 AA;  116567 MW;  A0BEB64BBD448E4E CRC64;
     MADDSNSAYP RVDYGAGTGA AFPDLERRVL EAWAADDTFR ASIENRSGAA EFVFYDGPPF
     ANGLPHYGHL LTGYVKDVIP RFQTMRGKRV DRRFGWDCHG LPAEIEAEKQ LGITDKSQID
     AMGLAEFNAA CKSSVLRYTG EWRDYVTRQA RWVDFDNDYK TLDLDFMESV MWAFKSLYDK
     GLIYQGFRVL PYSWYEQTPL SNQETRLDDA YKMRQDPAVT VDMVLSVPGE HPLRELDGAN
     ALIWTTTPWT LPSNLAIAVH PDVRYVHLRA ADGTRYVLAA ERVSHYSREF GEDATVLAEF
     EGAALVGLSY RPPFDFFLGH PNAHRVLAAD YVTTDSGTGV VHMAPAFGEE DMEVCSANDI
     ELVQPLDPGG RFTSMVPPYE GLMVFDANPV IIKDLKAAGK LLRHETIEHS YPHSWRSGQP
     LIYMAVPSWF VAVTKFRDRM VELNKQITWV PEHIRDGQFG KWLEGARDWN ISRNRYWGSP
     IPVWVSDDPA YPRVDVYGSL EELERDFGVR PTDLHRPAID QLTRPNPDDP TGRSMMRRVP
     EVLDCWFESG SMPYAQVHYP FENKEWFDSH FPGDFIVEYN GQTRGWFYTL HVLATALFDS
     PAFKTVAAHG IVLGDDGLKM SKSKGNYPDV NEVFDRDGSD AMRWFLMSSP ILRGGNLIVT
     ERGIREGVSH ALRPLWNAWT FLQLYASKPG EWRTDSTHVL DRYILAKLAQ TRDGMTEALE
     VYDIAGACEE LRTFADALTN WYVRRSRSRF WSEDRDAVDT LHTVLEVATR LAAPLLPLIS
     EVIWRGLTGG RSVHLADWPA AADLPADPEL VSTMDEVRTV CSTVLSLRKA KNLRVRLPLA
     EVTIAAPDAE RLAPYADIVA DEVNVKKVDL TTDVAVHGRF ELAVNARAAG PRLGKDVQRV
     IKAVKAGDWT ESADGVVSAA GITLLPEEYT QRLVAAEPES TAALPGNAGL VVLDSVVTEE
     LEAEGWARDL VRELQETRKS LGLDVSDRIH VVLEVPEARR SWAQTHRDLI AGEILATSLE
     FGTAGEPAAE LAGGVRASVR KA
//