ID A0A0G1NNS9_9BACT Unreviewed; 969 AA.
AC A0A0G1NNS9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, 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=UX31_C0004G0023 {ECO:0000313|EMBL:KKU22294.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWA1_46_11.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618732 {ECO:0000313|EMBL:KKU22294.1, ECO:0000313|Proteomes:UP000034107};
RN [1] {ECO:0000313|EMBL:KKU22294.1, ECO:0000313|Proteomes:UP000034107}
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:KKU22294.1}.
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DR EMBL; LCLS01000004; KKU22294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1NNS9; -.
DR PATRIC; fig|1618732.3.peg.197; -.
DR Proteomes; UP000034107; 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; cd00818; IleRS_core; 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 NCBIfam; TIGR00392; ileS; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKU22294.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 24..633
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 686..833
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 969 AA; 110657 MW; 8CDACF28196A44E5 CRC64;
MAGSTHKKFK ELSSKSLFQK EEEVLAFWKK NKIFKKSLER NPKSRIFSFY DGPPFITGLP
HYATLLPSIA KDIIPRYQTM KGRYVPRVWG WDVHGLPAEQ KVEEQLGLKV KKDIETFGVG
NFIKAAREYV AKGSAQWRWY IDHIGRWADM DNPYRTDDLK YMETVIWIFK QLYDRGLIYK
GRRVSLYCPR CATPLSKFEV TMDAAENYKN VDDPGVTISF KLKGQKDTYA LAWTTTPWTL
PANNGLAVNP KIKYVTVTNG KKKYILAKEA LSRYPELQGW RILKTQSGKE IAGQSFEPLF
EPTFSPDYRK DFKIWMASFP TIDEGTGIVH IAPAFGEDDF NLGQAKKLSA PMILDEDGKF
KKSLPFPWAG EYFKKADGAI IDALKEKGLL VRLEKITHAY PHCYRCSTPL IYMAQDAWFM
KIDPLRKQML KTNEQINWVP DHFGKKRFKY NIENAPDWSL SRARYWGTPM PIWETKDGER
VVVGSLAELE KLSRRKIKDL HRPGIDEVVL TTPSGKKAYR IKEILDVWFE SGAMPYAQDH
YPFENKKVFE GGFPTDFITE YTGQLRGWFY TLHVLATALK NKPAFKNVVV SGVIMGTDGK
KMSKSKGNYP DPRGTIEKYG AEAIRLYLMS NKIMLGEDLN INERDIQEAR NSINILHNSF
KYFTTYANLH KWQPSPKSTS SSHILDKWVK ARLQQCIGEY VLGLDHFDFP ASTRPIAPFI
EDLSTWYIRR SRDRFVAGDT KALSTLYEVL VTLSKAIAPT LPFTAEQIYT SLQSVKDPES
VHLCDYPKHN QSLVAKNKLL LEKMQIVRGL ASLVHNLRSE AKQPLRQKMA SVVIKGSKGI
KSDKELVRLL KEEANVLAVN FDTPMRKGFV KSKIGSVTVG LDTNLTPELE KEGLLRELLR
ELQDARKEQG LAVGQKAKLT YDTQDAMLSK LMEENQKEIA SIGHFLKVER GTVKGKSVMG
GKLQVKITA
//
