ID U1R8U7_9BIFI Unreviewed; 1107 AA.
AC U1R8U7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
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 {ECO:0000256|HAMAP-Rule:MF_02003};
GN ORFNames=HMPREF9244_01428 {ECO:0000313|EMBL:ERH29974.1};
OS Alloscardovia omnicolens F0580.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Alloscardovia.
OX NCBI_TaxID=1321816 {ECO:0000313|EMBL:ERH29974.1, ECO:0000313|Proteomes:UP000016519};
RN [1] {ECO:0000313|EMBL:ERH29974.1, ECO:0000313|Proteomes:UP000016519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0580 {ECO:0000313|EMBL:ERH29974.1,
RC ECO:0000313|Proteomes:UP000016519};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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}.
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:ERH29974.1}.
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DR EMBL; AWSI01000039; ERH29974.1; -; Genomic_DNA.
DR RefSeq; WP_021618544.1; NZ_KE952646.1.
DR AlphaFoldDB; U1R8U7; -.
DR STRING; 419015.HMPREF3214_00954; -.
DR PATRIC; fig|1321816.3.peg.1258; -.
DR HOGENOM; CLU_001493_1_1_11; -.
DR Proteomes; UP000016519; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; 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|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:UP000016519};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 31..683
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 742..892
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 64..74
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 649..653
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 652
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1107 AA; 125734 MW; A048332E2BB9C9FC CRC64;
MSNRVYPKAV TDRGFETITP SPHFPAMEES VLKYWDVDDT FRRSIAQRDS GNANDEFVFF
DGPPFANGLP HYGHLLTGYA KDVIPRFHTM LGKKVNRVFG WDTHGLPAEL EAEKELGITD
KSQIDEMGIK AFNEACRRSV LKYTQEWKDY IHRQARWVDF DHGYKTLNVS YMESVIWAFK
QLYDRDLAYQ GFRVLPYCWK DETPLSAHEL RMDADVYQDR QDNTLSVAMK LRDEDAYVVI
WTTTAWTIPN NLAIVVGKDI DYVLVEPVEG AFAGKKMYFA KDLVANFAKE LGEDYKVVKE
LKGSELVGRR YYPAFDYFLD GSLTDPEGKA NEDENAFTIY AADYVATTEG TGLVHQAVYG
EDDINTLNAH RVRTYDYLDE HAQFLDVIPD YAGMHVFDAN KPITRDLRAG SGPLERVPEE
RRAFIVQEKS HVHSYPHCWR CGNPLIYKPV SSWFVSVTKI KERLLELNQD VNWIPDNVKD
GQFGKWLENA RDWSISRNRY WGSPIPVWVS DDPKYPHVDV YGSLEELKRD FGKYPTDDEG
NINLHRPWID ELTRPNPADP TGKSHMRRIE DVLDCWFESG SMPFAQFHYP FENKDYFEEH
MPSDFVVEYI GQTRGWFYVM LIMNGALFDK APFKNVMCHG IVLGDDGQKM SKHLRNYPDV
NGVFNEYGSD AMRWFLMSSP ILRGGNLIVT ADGIRDTVRQ IMLPLWSTYY FFSLYANAAN
SGEGFDARQV RADEVHDLPH MDRYLLARTR TLVESTQKHL QDYGVADACA DVADYIDILT
NWYVRNTRDR FWNEDENAFN TLYTALEVLA RVMAPLAPME AETVWRGLTG GESVHLADWP
FLTDEESEKS TELGDVLKAD DDLVRTMDKV REVVSSTLSL RKAQKIRVRQ PLAQLTVVAD
NVDAVREYEE LLESELNVKQ IQYTTLENAG DHGLRVVNEL RVNARAAGPR LGKNVQFAIR
ASKSGAWHVN GEGMPVVDAQ GVDGGIALVE GEYELISRVE AAEGGADEAS SVSASLPTGG
FVLLDTTLTD DLLAEGYARD AIRSVQDARK AADLDISDRI SLVLTAPAAD ADKLKQFEEL
ISTETLATSF SVNVADVQEL EVKVEKA
//
