SYI_BORT9
ID SYI_BORT9 Reviewed; 1044 AA.
AC A1R0Q9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, 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=BT0833;
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135;
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}.
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DR EMBL; CP000049; AAX18150.1; -; Genomic_DNA.
DR RefSeq; WP_011772768.1; NC_008710.1.
DR AlphaFoldDB; A1R0Q9; -.
DR SMR; A1R0Q9; -.
DR STRING; 314724.BT0833; -.
DR KEGG; btu:BT0833; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_12; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001205; 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 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_1000216252"
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; 122959 MW; 90243AEF3409511A CRC64;
MFKKVESKVN FPKIEERILK FWNDNKIFEK SIQQREGCEE FTFYDGPPFA TGLPHFGHFV
PNTIKDIIPR YKTMKGKQVK RYFGWDTHGL PVEYEVEKSL KISGRYEIEK YGIDKFNEEC
RKIVLRYTKE WQKTISRLGR WIDFENNYKT MDTTFMESVW WVFQTLYNKG LIYESYYVLP
YSPKLATPLS NFEVNLGEYK EIHDPSLTIK FKIKDKNEYL LAWTTTPWTL PTNLGIAVGK
DIDYSKIFDK EKDETFIIGT KRLNHYYKDE KAYTVIEQFK GEYIKGIEYE PIFNYFLNQR
DKGAFKIHTA EYVTTDDGTG IVHIAPFGEE DYNILKNNTK TDMITPIDAE CRFTNEVKDF
EGLFVKDADN KIIEKLKSMN LLFKRENFLH RYPFCYRTNS PLIYRPISSW FVNIEAIKEK
LIKSNEQINW MPSHLKKGRF GKWLENARDW AISRNRFWGN PIPVWICSKT GNKICIGSKE
ELERLSGQKV NDLHKDKVDK ITWPSEYGGV YVRTSEVLDC WFESGSMPYA SKHYPFKDKD
NFHNIFPADF IAEGLDQTRG WFYTLTILGT ALFENTAFKN VIVNGLVLSS DGRKMSKSLR
NYTDPMEVIN TFGADALRLY LVMSPVIRAD DLKYSDDGVK DVLKNIIIPI WNAYSFFITY
AIIDKFEPNN NINLHKTNIL DKWIVSEIES LKKILNEEID KYNLTKSIEE LLAFIDKLNN
WYIRRSRRRF WKSENDNDKI DAHETLYYVI KNLMLMLAPF IPFLTEEIYQ NLKTKDEKES
IHLNKYPQAI EKLINIDLEE KMNFIRKVVS IARALRASHN IKIRKPISTI YVVTKDQKEQ
QILNEMKEII LEEINAKEIK IKSNEEELVT YKAKANFREL GSKLGVNMKV GSLEIMKLTN
EDILKIINGN KHIIKINENT YNITLKDIIL ERHERENLKI INEDSVTIGL DALITEELYL
EGLSRELIRK VQNLRKENNF NVSDRIILYI DNSDILKKIT NQFESYIKTE TLTLKIEINK
EKALTNVELD DAIFIKIGIK RWSN
