ID A0A0G0T8B5_9BACT Unreviewed; 1077 AA.
AC A0A0G0T8B5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=UT78_C0005G0044 {ECO:0000313|EMBL:KKR43320.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWF2_40_12.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618776 {ECO:0000313|EMBL:KKR43320.1, ECO:0000313|Proteomes:UP000034301};
RN [1] {ECO:0000313|EMBL:KKR43320.1, ECO:0000313|Proteomes:UP000034301}
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:KKR43320.1}.
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DR EMBL; LBYC01000005; KKR43320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0T8B5; -.
DR PATRIC; fig|1618776.3.peg.307; -.
DR Proteomes; UP000034301; 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 CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
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; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
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; PF00300; His_Phos_1; 2.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKR43320.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 1..437
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 628..748
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 798..950
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1077 AA; 123793 MW; 738782B1FEB2CB2B CRC64;
MQGYHVPRKW GWDCHGLPIE NIVEKELKIA GHQEIEEYGI DKFVEYARSK VLQYDKDWEK
GIERIGRWVD FRGSYKTMDN TFIESVWWAL SELNKKNLIY EGVRVLAYCS RCETPIANSE
IAMDNSYKDI SDISVYVKFE LEDLPAQAGE PKTYLLAWTT TPWTLPGNTA IAINKNFTYV
KAKVGDEIFI LAKETLQNVL KDKEYSVLGE ISGGDLVGKK YKPIFPYYKD SEAAKNKNIW
KVWHADFVTL DKGTGMAHEA PAFGEDDMNL AKQNDIPWII HVDETGRFKP EVTDFAGMQV
KPKSEDKDGH QKADVEVIKY LAKSNVLFAK EKIIHSYPHC YRCDTPIIYY ALPSWFINIK
KVKENVIKRA ENMNWIPAHL KEGRFKNIME NAPDWNISRN RYWASPLPIW KCEKCKEQTF
VSSLEDLKNK TKKSGNKYFV MRHGVSIANA KNAESLKAGE ANDALTEEGI KQVKTKAESL
EKKPDIIISS SFTRTKQTAE IVAEFFDIQK DQIIINEELR EAGAEKSPDE NSEDIRKRMI
GILSDLEKKY SGKNILIISH EYPIRVLLSS YESLSEKEEF DNLNIKYPAI QNAEVFQCDF
LSLPRNANGQ LDLHRPYIDE VNLVCGCGND LVRIPEVLDC WFESGSMPFA QDHYPFENKD
WQKNNFPAGF VAEYIGQVRT WFYYTHVVST ILFNQAPFEN VVTTGTIRAG DGEKMSKSKN
NYPDPWSFID KYGADALRIY LMSSTLMKGE DANFSEKAVQ DISSKIIGRL FNVLAFYELY
RDKKCEFNNV EESKAVLDQW ILSRLLQTID EITKGMENYD MAEATRPIDL FIDDLSTWYL
RRSRDRIKEG DINAKQSLYY ILKTLAKILA PFAPFAAEDI WLRLRNTDEV ESVHLTEWLA
LNGSAVSLFK IFSYDDKSKI IEKMEKTRNI VTLGLEARQK AGLKVRQPLS KLEIKNFALG
EEYTELIKDE INVKEVVENK NIENEVELDI QITPELKEEG DYRELARALQ DMRKKMGLTP
NDIVTLSVET NEAGKKLVLV SKIEFKNTDG EPARPHDEGA GGEVKIDELV FKIKIEK
//
