ID   SYI_BACFR               Reviewed;        1141 AA.
AC   Q64U07;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
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}; OrderedLocusNames=BF2275;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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; AP006841; BAD49022.1; -; Genomic_DNA.
DR   RefSeq; WP_011202809.1; NC_006347.1.
DR   RefSeq; YP_099556.1; NC_006347.1.
DR   AlphaFoldDB; Q64U07; -.
DR   SMR; Q64U07; -.
DR   STRING; 295405.BF2275; -.
DR   KEGG; bfr:BF2275; -.
DR   PATRIC; fig|295405.11.peg.2207; -.
DR   HOGENOM; CLU_001493_1_1_10; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002197; 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; 3.30.720.200; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; 1.
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; Zinc.
FT   CHAIN           1..1141
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098520"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           689..693
FT                   /note="'KMSKS' region"
FT   BINDING         692
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1141 AA;  130126 MW;  B5BAF18AEA5AF9C4 CRC64;
     MSKKFAEYSQ FDLSKVNKDV LKKWDENQVF AKSMTEREGC PSFVFFEGPP SANGMPGIHH
     VMARSIKDIF CRYKTMKGYQ VKRKAGWDTH GLPVELGVEK SLGITKEDIG KTISVAEYNA
     HCRQDVMKFT KEWEDLTHKM GYWVDMKHPY ITYDNRYIET LWWLLKQLYK KGLLYKGYTI
     QPYSPAAGTG LSSHELNQPG CYRDVKDTTV VAQFKMKNPK PEMAQWGTPY FLAWTTTPWT
     LPSNTALCVG PKIDYVAVQS YNAYTGQPIT VVLAKALLNA HFNPKAAELK LEDYKAGDKL
     VPFKVIAEYK GPDLVGMEYE QLIPWVNPGE GAFRVILGDY VTTEDGTGIV HIAPTFGADD
     AQVAKAAGIP PLQLVNKKGE LRPMVDLTGK FYTLDELDED FIKQRVNIDL YKEYAGRFVK
     NAYDPNLSDQ DESLDVSICM MMKVNNQAFK IEKHVHNYPH CWRTDKPVLY YPLDSWFIRS
     TACKERMIEL NKTINWKPES TGTGRFGKWL ENLNDWNLSR SRYWGTPLPI WRTEDNSDEK
     CIESVEELYN EIEKSVAAGY MQSNPYKDKG FVPGEYNEEN YNKIDLHRPY VDDIILVSKD
     GKPMKREADL IDVWFDSGAM PYAQIHYPFE NKELLDSHQV YPADFIAEGV DQTRGWFFTL
     HAIATMVFDS VSYKAVISNG LVLDKNGNKM SKRLGNAVDP FSTIEQYGSD PLRWYMITNS
     SPWDNLKFDV DGIEEVRRKF FGTLYNTYSF FALYANVDGF EYKEADLPMN ERPEIDRWIL
     SVLNTLVKEV DTCYNEYEPT KAGRLISDFV NDNLSNWYVR LNRKRFWGGG FTQDKLSAYQ
     TLYTCLETVA KLMAPIAPFY ADRLYSDLIG VTGRDNVVSV HLAKFPEYNE KMVDKELEAQ
     MQMAQDVTSM VLALRRKVNI KVRQPLQCIM IPVVDEVQKA HIEAVKALIM SEVNVKEIKF
     VDGAAGVLVK KVKCDFKKLG PKFGKQMKAV AAAVAEMSQE AIAELEKNGK YTFDLGGAEA
     VIESADVEIF SEDIPGWLVA NEGKLTVALE VTVTDELRRE GIARELVNRI QNIRKSSGFE
     ITDKIKLTLS KNPQTDDAVN EYNSYICNQV LGTSLTLADE VKDGTELNFD DFSLFVNVVK
     E
//