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Database: UniProt
Entry: A0A0G1C3G3_9BACT
LinkDB: A0A0G1C3G3_9BACT
Original site: A0A0G1C3G3_9BACT 
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
//
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