SYI_BORHD
ID SYI_BORHD Reviewed; 1044 AA.
AC B2S1H8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=BH0833;
OS Borrelia hermsii (strain HS1 / DAH).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 / DAH;
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) 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;
CC Evidence={ECO:0000255|HAMAP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000048; AAX17330.1; -; Genomic_DNA.
DR RefSeq; WP_012422580.1; NC_010673.1.
DR AlphaFoldDB; B2S1H8; -.
DR SMR; B2S1H8; -.
DR KEGG; bhr:BH0833; -.
DR HOGENOM; CLU_001493_1_1_12; -.
DR OMA; HLGTAWN; -.
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 Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR42780; PTHR42780; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 2.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 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..1044
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000216250"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 594..598
FT /note="'KMSKS' region"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1044 AA; 122955 MW; EEF5E826DF30426D CRC64;
MFKKVESKVN FPKIEEKVLK FWNDNKIFEK SMQQREGCEE FTFYDGPPFA TGLPHFGHFV
PNTIKDIIPR YKTMKGKHVK RYFGWDTHGL PVEYEVEKSL QISGRYEIEK YGVDKFNEEC
KNIVLRYTKE WQKTISRLGR WVDFEHNYKT MDTTFMESVW WVFQTLYNKG LIYESYYVLP
YSPKLATPLS NFEVNLGEYK EVHDPSLTIK FKIKDKNEYL LAWTTTPWTL PTNLGIAVGR
DIDYSKIFDK EKNETFIIGT KRLNHYYKDD KTYTVIEQFK GEHIKGIEYE PVFDYFLSQR
NKGAFRIHTA EYVTTDDGTG IVHIAPFGEE DYNILKKNTK TDMITPIDAE CRFTNEVKDF
EGLFVKDADN KIIEKLKSMN LLFKRENFLH RYPFCYRTNS PLIYRPISSW FVNIEAIKEK
LIKSNEQINW IPSHLKKGRF GKWLENARDW AISRNRFWGN PIPVWICSKT GNKICIGSKE
ELERLSGQKV NDLHKDKIDK ITWPSQYGGT YVRTSEVLDC WFESGSMPYA SKHYPFKDKD
KFHDIFPADF IAEGLDQTRG WFYTLTILGT ALFEQTAFKN VIVNGLVLSS DGRKMSKSLR
NYTDPMEVIN TFGADALRLY LVMSPVVRAD DLKYSDDGVK DVLKNIIIPI WNAYSFFITY
AIIDKFEPNS NIVLYKTNIL DKWIISEIES LKKTLNEEID KYNLTKSIEE LLAFIDKLNN
WYIRRSRRRF WKSENDNDKI DAYETLYYAL KNLMLMLAPF IPFLTEEIYQ NLKTKDEKES
IHLNEYPQEI KELINIDLEE KMNFIRKVVS IARALRASHN IKIRKPISTI YIVTKDQKEQ
QILSEMKEII LEEINSEEIK IKSNEEELVT YKAKANFREL GSKLGTNMKA VALEIMKLNN
EDILKIINGN KHTIKIKDNT YDITLKDIIL ERHEKENLKV INEDSVTIGL DALITEELYL
KGLSRELIRK VQNLRKENNF NVSDRIILYI DNNEILKKII SQFESYIKNE TLTLKIEINN
EKALTKVELD DEILIKIGIE KWSN
