ID A0A0G1MTU9_9BACT Unreviewed; 977 AA.
AC A0A0G1MTU9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=UX16_C0006G0011 {ECO:0000313|EMBL:KKU11731.1};
OS Parcubacteria group bacterium GW2011_GWB1_45_7.
OC Bacteria.
OX NCBI_TaxID=1618878 {ECO:0000313|EMBL:KKU11731.1, ECO:0000313|Proteomes:UP000034347};
RN [1] {ECO:0000313|EMBL:KKU11731.1, ECO:0000313|Proteomes:UP000034347}
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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000256|ARBA:ARBA00007078}.
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:KKU11731.1}.
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DR EMBL; LCLD01000006; KKU11731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1MTU9; -.
DR PATRIC; fig|1618878.3.peg.160; -.
DR Proteomes; UP000034347; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035}.
FT DOMAIN 25..632
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 684..829
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 977 AA; 111338 MW; 5B8F1E7FA8B2279E CRC64;
MQNDNDKKVF DDPVKQTLFE REEEVLKFWK ESKIFEKSLD KNPKSKLFSF YDGPPFITGK
PHYGNLLSSI AKDVVPRYQT MKGRYVPRVW GWDVHGLPIE NKVEQALGLK NKKDVEALGI
GKFIEEARKY VNVSTEEWRW YIDHIGRWAD MDHPYRTDQI GYIESVIWVF KQLFDKGLVY
KGRKVFLYCT RCATVVSKFE TTMEAGNYRD VEDPAVTIAF KLKDEENTYV LAWTTTPWTL
PANNGLAAGP DVKYVKISDG GRSYILAEGA LARYPEFDSW ERKENFSGKD LAGKSYEPLL
TPNITPDPNK DYKIYLGAFA TTEEGTGIVH IAPAFGEDDF TLGQENNLTV PMILDDDGKF
LENSPWSWAG KFYKSANADI VSALKEKNLL VREDKIRHSY PHCYRCGTPL IYMAQDSWLI
NIDSIRKHLQ KTNKKINWVP AHFGDKRFAY NIETAPDWSI SRTRYWGIPI PIWETDDGEL
IVPESIEEIE KLSGQKVTDL HRPDIDEIVL KTPSGKEARR VKEVLDVWFE SGSMPYAQDH
YPFENKEKFE NGFPTDFIVE HVGQLRGWFY SLHVISTILK NKPTFKNAVV TGTLAGTDGR
KMSKSFGNFP DPRETIEKYG AEALRLYLMS NKIMMGEDAS FSEDELKEAY ATLNILHNSH
KYFVTYANLH GWTPSGSTSE NPLDMWITAR TEQFVRNYSE ALDKFDLVNS SREIRPFIED
LSTWYIRRSR DRFAAGDKDA LETLHMVLVK FAKAAAPLLP FSADSIYKDL CPPSGGGLES
VHLEDYPEVD KKLIRKNENL IERMSLVRDI ASIAHSLRSE AGHALRQKLA TLVVKNTKNL
DDELVEILRD EVNVSEVRFD LPAPSAARQA GGSADSFACG KLGDIEICLD TNLTDELRKE
GIYREIMRAL QDARKKAGLE VGEKVQLSYK VEDVMVATVL KEKLEEIKEA ANFSSIDLSS
DDLPIEILNG KIKIKIG
//
