ID   SYI_RICAH               Reviewed;        1103 AA.
AC   A8GPA1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
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=A1C_04840;
OS   Rickettsia akari (strain Hartford).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=293614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hartford;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia akari.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000847; ABV75226.1; -; Genomic_DNA.
DR   RefSeq; WP_012149856.1; NC_009881.1.
DR   AlphaFoldDB; A8GPA1; -.
DR   SMR; A8GPA1; -.
DR   STRING; 293614.A1C_04840; -.
DR   KEGG; rak:A1C_04840; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_5; -.
DR   Proteomes; UP000006830; 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; IPR022439; RPE4.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   NCBIfam; TIGR00392; ileS; 1.
DR   NCBIfam; TIGR03777; RPE4; 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; Zinc.
FT   CHAIN           1..1103
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000022158"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           628..632
FT                   /note="'KMSKS' region"
FT   BINDING         631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1103 AA;  126771 MW;  2D5D718E96221D88 CRC64;
     MANTKYYPEV SSNANFAAIE REILKFWQDN NIFQKSIDGR NGESEFIFYD GPPFANGLPH
     YGHLLTGFIK DVYARYQTVK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAITNFGIEK
     FNAHCRASVM EYASDWEEYV TRQARWVDFK NSYKTMDKNF MESVLWAFKE LYNKGLLCES
     MRVVPYSWAC ETPLSNFETR LDNSYRERSD KAVTVSFVLR DKLHEIPAFA GMISRESEMT
     VGGDYQEYRI LTWTTTPWTL PSNLAIAVGS DIDYALVPQE NICYIIAASS VSKYAKELGL
     SGEENFEIIK GSQLQGLRYK PLFDYFEHHP NSFKIFDVDF VVEGDGTGVV HMAPGFGEDD
     QILCESKGIS LVCPVDNSGK FTKEIPDLEG VQVFDANDKI IIKLKEQGNW LKTEQYIHNY
     PHCWRTDTPL IYKAVPSWYV KVTQFKDRMV ELNQQINWIP HHVKDNLFGK WLENARDWSI
     SRNRFWGTPL PVWKSDDPKY PRIDVYGSIE ELEKDFGVKV TDLHRPFIDK LTRPNPNDPT
     GKSTMRRIED VFDCWFESGS MPYGQAHYPF ENKEWFEDHF PADFIVEYSA QTRGWFYTLM
     VLSTALFDRP PFLNCICHGV ILDATGQKLS KRLNNYADPL ELFDQYGSDA LRVTMLSSNI
     VKGQELLIDK DGKMVFDTLR LFIKPIWSSY HFFTMYANAD SLKGEISFAS ENVLDVYILS
     KLKIAVSKIE ESLDNFDTQT AYHAVLEFFE VLNNWYIRRS RARFWKSEKD TDKQNAYNTL
     YSCLKTMAIA MSALVPMISE AIYKGLCHCE ETSTLSSRDL IAGSSKSINN LNPVVKPRDY
     TPSVHHNDQI SVHLCNYPTL SDFEINHELV ATMDNVLDIC SNSLFIRSTK NIRVRQPLAS
     ITIISKHNND LKAFENLIKD EINVKSVIYC DDLENYASKK LSINFPMLGK RLPAKMKEII
     AASKKGDWKA IAGGLTICGE TLNNEEYKLI LEPYSHIKGA ASFENNSSLL ILDLELTAEL
     IEEGYARDIV RFIQQARKDA GFSITDRILI EIISEFDLSE IIYNYGDFIT EQTLGEFSKN
     FTPDYVSKVE LEDHPIQLKI KKS
//