ID A0A0G1QG98_9BACT Unreviewed; 1146 AA.
AC A0A0G1QG98;
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};
DE Flags: Fragment;
GN ORFNames=UX24_C0002G0001 {ECO:0000313|EMBL:KKU16768.1};
OS Candidatus Giovannonibacteria bacterium GW2011_GWB1_45_9b.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1618653 {ECO:0000313|EMBL:KKU16768.1, ECO:0000313|Proteomes:UP000034020};
RN [1] {ECO:0000313|EMBL:KKU16768.1, ECO:0000313|Proteomes:UP000034020}
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:KKU16768.1}.
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DR EMBL; LCLL01000002; KKU16768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1QG98; -.
DR Proteomes; UP000034020; 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; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 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; 1.
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; 2.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKU16768.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 21..489
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 691..820
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 878..1025
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 1023..1073
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 500..507
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 555
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT NON_TER 1146
FT /evidence="ECO:0000313|EMBL:KKU16768.1"
SQ SEQUENCE 1146 AA; 130970 MW; 56F938A16084D7AC CRC64;
MADEKGFLIY DSVSPRSEEE ILRFWKDNGI FEKSLESRKK GKLFIFYEGP PYANGLPGIH
HVESRSFKDI ILRYKTMRGF FVPRRAGWDT HGLPTEMAVE KALGIKSKRE IEEKIGVEKF
VEEAKKNVFT FIDAWEKLTD RMAYWLDLKN AYVTMTNGYI ESLWAVISKI SVEKLLYEDY
KVLPWCPRCG TSLSSHELAQ GYRKVKENSI YVKFPLARDN SSKQLASFLV WTTTPWTLSG
NVALAVNPKI DYVTIECAEN SGEWLILAEP RLNVIEREYK IINREKGAAL VGTKYKALYP
NSAAAGNSYR VVAASFVSTE EGSGIVHIAP AFGGDDLAVG KKENLPTLVT VSEEGKMKTP
GALWDGKFIK DADPLIIEDL NKRSLLFKVE SYEHDYPFCW RCETPLIYYA KSSWFFKTTA
VKEKMLSENA KIAWHPKYLR DGRFGSWLKE NVDWGISRER YWGTPLPIWR CDRCKKVKTI
GALKELDELN PNPTNVVFMR HGEALHNIKN RVNPFSPEND SKDELTEKGR KDVIASAEKL
KKENIEVIVS SPSARAKETA EIVGNTLGVK NIEIIPELYD VMIGKFEGEP ISEFKKEFSS
FGERFTKKPG GAENSRELRK RVMKALGEVR VKCAGKKVLV VSHGDPIWVA IATLEGLKET
DYKESFYPSP AEFKKIKLHN WPYNPEGELD LHKPYIDKIL IKCDCGNNMK RVLEVMDVWF
DSGAMPFASQ GWLSHHLVAK PPNYPAEYIS EAIDQTRGWF YTLLAVSSLL GLESSYKRVL
SLGLVLDEKG EKMSKSKGNV VDPQMLMEKY GADAVRWYFY TINQPWDDKL FREKDIQDAS
RRFLMILWNS FVYWRTYKEV ELPLGSSTSK SRPKLVINKW ILVKWSEVLS TVTKNLEKYD
IVAAARALEN FVVEDLSRWY IRRIREHMKH EKSDAAKECS ATLGFVLLEL SKALAPFAPF
ISEGIYNGLG GERESVHLES WPSFAKATKG SNLLLENMEK IREIVSKGLE ARQKAGIKIR
QPLQKLQVTN SKLQKELLEL IKGEVNVKSV EFVKALKEEV ELDTKITDEL REEGIVREFI
RAVQDFRKGL KLTPQEKVEL AVKSSKEFEK ILKAHKNLIE KEINISDLSF GDLGESRTKE
ISIDKT
//
