ID A0A0G1C3G3_9BACT Unreviewed; 882 AA.
AC A0A0G1C3G3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=UV54_C0016G0007 {ECO:0000313|EMBL:KKS80092.1};
OS Candidatus Beckwithbacteria bacterium GW2011_GWA2_43_10.
OC Bacteria; Candidatus Beckwithbacteria.
OX NCBI_TaxID=1618369 {ECO:0000313|EMBL:KKS80092.1, ECO:0000313|Proteomes:UP000034213};
RN [1] {ECO:0000313|EMBL:KKS80092.1, ECO:0000313|Proteomes:UP000034213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:0000256|ARBA:ARBA00025217}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000114};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKS80092.1}.
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DR EMBL; LCEW01000016; KKS80092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1C3G3; -.
DR STRING; 1618369.UV54_C0016G0007; -.
DR PATRIC; fig|1618369.3.peg.270; -.
DR Proteomes; UP000034213; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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: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 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:KKS80092.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 22..612
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 639..774
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 818..849
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 882 AA; 102264 MW; C7A81D5F0AC55B6D CRC64;
MAKLYFKDEP GVPDFVAMEE QLLKEWEKQG IVKKYLRKNG KAKNKFSFLD GPITANNPMG
VHHARGRTYK DLWQRYFTMK GYRQRYQNGF DCQGLWVEVE VEKELKFKSK KDIEKYGVEK
FVNKCKERVL KYSAIQTEQS QRLAMWMDWN NSYFTMSDAN NYAIWNFLKV CHQHGWIYKG
RDVVPWCWRC ETAISQHEIL TEDYKQVTHD SIYLSLPIKD RDEYLLVWTT TPWTLPANIA
VAVDKDFAYS LVATKSGKKV WILTVLAKAV LKDDFGKVIK ISKGKELVDL QYTPPFKDLA
VVKATPAHRV VATDKLIMPI TVTEGTGLVH TATGTGAEDY RLGKKLKLPV IAAISDDASY
LNGFGELSGA NAKKQPELVF NYLKSHFPDV IYRIEAYTHR YPACWRCKTE LVWKVADEWY
ISMDKLRSQI ISVAKKIHWI PEFCLERELD WLNNMHDWLI SKKNRYWGLA LPIYECKKCR
HFAVIGSKAE LKKRAVQGWD KFIGHTPHKP WIDEVKIKCS HCGETVSRIE PVGNPWLDAG
IVPFSTLPKI WFPADFITEA FPGQFKNWFY AMLVMSTVLQ KTNPFQTVLG YESVVGEDGR
PMHKSWGNAI EFNQGAQNSY RFFTSNSQNW KQPKYSILDK WILSRLQQTI RTVTESLDQY
YSAPATVALE KFVSDFSTWY LRRSRNRPES LAVMHHCLVI LSQLLAPFIP YLSDYIYQQL
TKEVSVHLSD WPKINSALIN QSLEKDMLKA RELVEKIHSQ RKALNLKVRQ PLASVTIKAG
QLNSQLEDLI LAETNIKKIK FDKNIKEEII LDTKLTSVLK AEGLARDLIR AIQEARKQAK
TDLTELINLE LPDWPKEFEA EIMKKTYVKK LSQGLRLKVV RL
//