ID A0A0U5BK64_9BACL Unreviewed; 1033 AA.
AC A0A0U5BK64;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
GN Name=ileS_2 {ECO:0000313|EMBL:BAU28606.1};
GN Synonyms=ileS {ECO:0000256|HAMAP-Rule:MF_02003};
GN ORFNames=CB4_02781 {ECO:0000313|EMBL:BAU28606.1}, DFP93_105161
GN {ECO:0000313|EMBL:PYE62206.1};
OS Aneurinibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1500254 {ECO:0000313|EMBL:BAU28606.1, ECO:0000313|Proteomes:UP000217696};
RN [1] {ECO:0000313|EMBL:BAU28606.1, ECO:0000313|Proteomes:UP000217696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:BAU28606.1,
RC ECO:0000313|Proteomes:UP000217696};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Aneurinibacillus soli.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PYE62206.1, ECO:0000313|Proteomes:UP000247363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8566 {ECO:0000313|EMBL:PYE62206.1,
RC ECO:0000313|Proteomes:UP000247363};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-Rule:MF_02003}.
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, ECO:0000256|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated valine is translocated from the
CC active site to the editing site, which sterically excludes the
CC correctly activated isoleucine. The single editing site contains two
CC valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC tRNA(Ile)). {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000256|ARBA:ARBA00007078,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
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DR EMBL; AP017312; BAU28606.1; -; Genomic_DNA.
DR EMBL; QJSZ01000005; PYE62206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5BK64; -.
DR KEGG; asoc:CB4_02781; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000217696; Chromosome.
DR Proteomes; UP000247363; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 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; 2.
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|HAMAP-Rule:MF_02003};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02003};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02003}; Reference proteome {ECO:0000313|Proteomes:UP000217696};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 17..619
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 675..817
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 590..594
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1033 AA; 118553 MW; F4967F2278F14405 CRC64;
MEEVNVKELA VRREQRIHER WKEQNTFQQS IQNREGNPSF VFYEGPPTAN GLPHVGHALG
RTIKDVVARY KTMTGHQVIR KAGWDTHGLP VELGVEKQLG ISGKHEIEKY GVEAFIAKCK
ESVFTYEKQW RDFTEQIGYW VDMDSPYITL DNSYIESVWN ILGTLHERGL LYKGHRVSPY
CPSCQTSLSS HEVAQGYKNV KDLTATAKFK VKDRENEYFL GWTTTPWTLP ANVALAVHPD
MEYVRVKEGD CIYIVAKART EHVLQQEYTV LSEHKGKELA GLSYVSPFDF VNVEKGHQVV
TADYVTEQSG TGIVHIAPAY GEDDYKVIRE NGFSFVNVVD GKGQYTSEVP VFQGRFVKDC
DVDIIRYLAD KGLLYHKEKH EHSYPHCWRC DAPLLYYANE SWFIQTTAVK EQFIQNNEGV
TWYPDHIKHG RFGNFLENMV DWNISRNRYW GTPLNVWQCQ ACDHQYAPKS IQELKEHATH
LVPESIELHK PYVDEVKLCC TKCGAAMTRT PEVIDVWFDS GSMPFAQYHY PFANKTQFEK
QFPADVVIEG IDQTRGWFYS LLAVSTLFTG KAPYKRVLSL GHILDENGQK MSKSKGNALD
PVDLIQKFGA DALRWALLAD SAPWNPKRFS ERVVQEAKSK VIDTFVNVYG FYVLYANLDG
YQPNQEYKGK QTKLDEWILS RLHSTIKRVR QSLDDYQFTN AAREIATFVE ELSNWYVRRS
RDRFWSQGMS EEKAAAYATL HEVIVKTSQL LAPLTPFVAE DIYSNLEGGS VHLTDYPDYN
ETKINKKLEE EMNAVLQVVE VGRSIRNTAS LKVKQPLASL SLLVPNHQDI QWNAYRTIIK
EELNVKAFHV TQNDENFVSY KLKLDFKKAG PKFGNKTNQV HQWLQSVTNT EAKELVEKGN
VQWRMSDDTS LLITAEDVQI EKVPNEGFAI ASNGPYTVIL DTTLTEELIQ EGVARELLRA
IQEYRKKLNL PVNLRIDLEM SMDEEMKQIV VRYESLLQEN LLMNSLQVCD ELATGEQLKV
GSKLVTVRIV NHP
//
