ID A0A0G0CK96_9BACT Unreviewed; 748 AA.
AC A0A0G0CK96;
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=UR34_C0010G0037 {ECO:0000313|EMBL:KKP43872.1};
OS candidate division WS6 bacterium GW2011_GWC1_33_20.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1619089 {ECO:0000313|EMBL:KKP43872.1, ECO:0000313|Proteomes:UP000034302};
RN [1] {ECO:0000313|EMBL:KKP43872.1, ECO:0000313|Proteomes:UP000034302}
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:KKP43872.1}.
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DR EMBL; LBOV01000010; KKP43872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0CK96; -.
DR PATRIC; fig|1619089.3.peg.442; -.
DR Proteomes; UP000034302; 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; 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:KKP43872.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKP43872.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 133..414
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 463..610
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 748 AA; 86300 MW; 849C19FAEB591C31 CRC64;
MPLWMPHILK VYGGLWTLPG NLLVAVGKDF EYVQVEYEGV KYIVAKELVD KIFEGEYSIL
ETFNGERLIG KEYEPLFPFF SSKSSEGAFR VVHANHVTLE DGTGLVHQAP YGEEDFALMT
SMGISMFDYL DDQGNMKEEM GEFKGMFYKK ANKYIMEDLK NRSLLLKSVD YEHQMPMCWR
TNTPLIYKPI KSWYVKVTDI REKLVKENEE INWVPAYFKQ GRFGNWLADA RDWALSRNRY
WGTPLPAWIC EKCGETEVLG SFAEVKEKSG IELKDPHKPF VDEITYSCPK CGGVMKRVRD
VIDVWYDSGS MPFARFHYPF ENKEKFESKY PGQFIAEGVD QTRGWFYTLH VLGVALFNEK
SFKNVIVNGM ALAPDGTKMS KSKRNYTEVN VVLDQMGADS LRLYFLSSPI VHGEEILFSE
KFLKEITATV LLPYWNSVKY FLSYKDQFNW QYTEGWKSEN LMDIWIVAKL HQTIKSVTES
MDGYVLQKAT KDIFDLIDGL SKWYIRRSRD RFVKGDREAL NTLHYVLLEL TKLLAPFAPF
ISESVYATLT EGIVSSAKES VHLEDYPVVD EGRLNDEILI NMDRVRDICS IGLKIRDDNR
LKVRQPLSKV YVPISDLQMQ EIIKGELNVK EVVFSEKEQT GDGLISQSDG KVFVSLDINL
TNELKEEGML NEIIRGLQVA RKESGCEVGE RVSILYMTDS SEIESIITTY EEKLKSNVII
DLFEKRDTLE NGIQIKVEDK EVMVEIKK
//
