ID   SYI_MYCPA               Reviewed;        1053 AA.
AC   Q740U6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 116.
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=MAP_1246;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(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_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; AE016958; AAS03563.1; -; Genomic_DNA.
DR   RefSeq; WP_003877692.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q740U6; -.
DR   SMR; Q740U6; -.
DR   STRING; 262316.MAP_1246; -.
DR   KEGG; mpa:MAP_1246; -.
DR   PATRIC; fig|262316.17.peg.1310; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   Proteomes; UP000000580; 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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; 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..1053
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098549"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           69..79
FT                   /note="'HIGH' region"
FT   MOTIF           631..635
FT                   /note="'KMSKS' region"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1053 AA;  118305 MW;  0F210268429438E0 CRC64;
     MTDNLGFQAD REAQPADSVQ TYPKPAGGAP DFPALELEVL DYWARDDTFR ASIARRDGAE
     EYVFYDGPPF ANGLPHYGHL LTGYVKDIVP RYRTMRGNKV ERRFGWDTHG LPAELEVERQ
     LGITDKSQID DMGIAAFNDA CRESVLRYTD EWRAYVTRQA RWVDFDHDYK TLDLPYMESV
     IWAFKQLWDK GLAYEGYRVL PYCWRDETPL SNHELRMDDD VYPSRQDPAL TVGFKVVGGE
     LDGAHLLIWT TTPWTLPSNL AVAVHPEVTY VQVRSGDRRF VLAQPRLAAY ARELGPEPEI
     LGSYRGAELL GTRYLPPFPY FMDNPNAFRV LAGEFVTTED GTGIVHLAPA YGEDDMAVAD
     AAGIAPVTPV DSNGRFDAAV PDYQGLNVFD ANPQIIWDLK NGSGAAAANA PVLLRHETYE
     HPYPHCWRCR NPLIYRAVSS WFVAVTRFRD RMVELNQQIT WYPEHVKDGQ FGKWLAGARD
     WSISRNRYWG TPIPVWKSDD PAYPRIDVYG SLDELERDFG VRPDNLHRPY IDELTRPNPD
     DPSGRSTMRR IPDVLDVWFD SGSMPYAQVH YPFENRDWFE THYPGDFIVE YIGQTRGWFY
     TLHVLATALF DRPAFKTCVA HGIVLGSDGQ KMSKSLRNYP DVSEVFDRDG SDAMRWFLMA
     SPILRGGNLI VTEQGIRDGV RQVLLPFWNA YSFLALYAPK IGTWRTDSPQ VLDRYILAKL
     AELRDDLTRE MDACDISRAC EQLRQFTEAL TNWYVRRSRS RFWSEDADAI DTLHTVLEVT
     ARLAAPLLPS VTELVWRGLT GGRSVHLTDW PRSGELPADP GLVAAMDQVR EVCSAASSLR
     KAKKLRVRLP LPKLTVAVEN PQHLAPFVDL IADELNVKSV ELTDAIDTYG TFELTVNARV
     AGPRLGKDVQ AAIKAVKAGE GVVNADGTLT AGPAVLRPEE YSSRLVAADP EFTAALPNGA
     GLVVLDGTVT PELEAEGWAK DRIRELQELR KSTGLDVSDR ISVVMSVPAG RAEWARTHRD
     LIAGEILATR FEFGEPADPV AIGDGVRVSI SKV
//