ID A0A1F7JTR2_9BACT Unreviewed; 995 AA.
AC A0A1F7JTR2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, 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=A3I56_01425 {ECO:0000313|EMBL:OGK58991.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_02_FULL_43_10.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802078 {ECO:0000313|EMBL:OGK58991.1, ECO:0000313|Proteomes:UP000176269};
RN [1] {ECO:0000313|EMBL:OGK58991.1, ECO:0000313|Proteomes:UP000176269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGK58991.1}.
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DR EMBL; MGBC01000053; OGK58991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7JTR2; -.
DR Proteomes; UP000176269; 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 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:OGK58991.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 18..686
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 735..881
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 995 AA; 115435 MW; 9D02CFE29BE72209 CRC64;
MFKPVEARPN FPEKEQELLK RWYETGIVSK YLHKNDTANQ YFSFLDGPIT ANNPMGVHHA
WGRTYKDVWQ RFYNLLGYRQ RFQNGFDCQG LWVEVEVEKE IGIRNKKDIE NLVPGDRIAS
IAQFVKLCKE RVIKFAGIQT EQTKRLGNFM DWEHSYFTMA DENNYMIWHF LKVCHEHGWI
YKGRDAVPWC PRCETAISQH EMLTEDYKEL THESIYLKLP ITSKGWENTA LLIWTTTPWT
VPANVAVGVH TDYVYGVWEN ESGERIIFLD QDDEEKIPER TIKERVLPIN EYILHDAKED
WNKINVIKGS DLLGLRYNGP FDNIPRVQDA QEERPETFHT VVDASELINA HEGTGLLHIA
PGAGTEDFRI GKKLGLAVIS VIADDASYLD GLGEFSGKNA KTHPELIIDA LKDQGALLTT
EMYTHRYPAC WRCRKELVWK VADEWYIAMD IPSNIDTLTL RTKMIRNAQN IKWLPSFGLD
RELDWLEHME DWLISKKNRY WGLALPIYEC AQCGYINVLG GKEELKDRSI EWWKEFEGKS
PHKPYIDLVK ISCEKCSKPV SRIDDVGNPW LDAGIVPYST ITEKNHGEPL YSKNREEWQN
WFPADFITES FPGQFKNWFY ALIAMSSALE DQKPFKTVLG FGTLFAEDGR AMHKSWGNAI
EFGEGAEKIG VDVMRWMFCR ANPAENMVFG YTAANEVRRS FILVLWNIYK FFVEYAQADN
YTRTDASPGT KHPLDRWILT HLRQTILTVE EAMNAYDARS ATNALESFIA DLSTWYIRRS
RNRIWTNSKD DGDKNDFYAT LHYVLVHISI VLSPFMPFMS DEIFVNLTGQ ESVHLTSWPY
VVKEETDESI LSTMAYVRKL IEIGHRERKL LKIKVRQPLQ SVTFTLPVKP EFSPDIQSLI
KDELNIHDVY FRVEEVSGPT AQYDTHITDT LQKEGEIREL IRNVQQMRQE QGLVSTDYIV
LTIPEIPSGY EDYIKQRVMA KSINIGEEYA IAKTS
//
