SYI_DEIRA
ID SYI_DEIRA Reviewed; 1078 AA.
AC Q9RUP8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=DR_1335;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02003}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR EMBL; AE000513; AAF10907.1; -; Genomic_DNA.
DR PIR; E75407; E75407.
DR RefSeq; NP_295058.1; NC_001263.1.
DR RefSeq; WP_010887976.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RUP8; -.
DR SMR; Q9RUP8; -.
DR STRING; 243230.DR_1335; -.
DR EnsemblBacteria; AAF10907; AAF10907; DR_1335.
DR KEGG; dra:DR_1335; -.
DR PATRIC; fig|243230.17.peg.1531; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_0; -.
DR InParanoid; Q9RUP8; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002524; Chromosome I.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 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; PTHR42780; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..1078
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098542"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT MOTIF 637..641
FT /note="'KMSKS' region"
FT BINDING 640
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1078 AA; 120273 MW; DF007ED70528F70F CRC64;
MTKRTFAPVP TQPNFRQLEA DILQKWKDEQ VFEQTQTRPA PAGEFVFYEG PPTANGKPAL
HHVLARSFKD LFPRFKVMQG HHVTRKGGWD THGLPVEISV EKKLGWLGRN HGASREELEE
FNRLCRTSVW ETIQDWNELT ERMGYWLDLG DPYITYQNSY VESVWNLLRR LHEKGLVAQD
YKVVPLSPRI SSTLSRAELG EVDSYRMVDD PSVYVRLPIV WDTLPERAHA ALSSLSGEQR
QGLSLLVWTT TPWTLPSNTL AAVNPDLDYV VADSPSGRVI VAEGAVERLS ALHKDAAPLE
VLARFKGRDL EWVEYEPPFP EVASQLGVVS ELHERRDGKP VLHFVVMADF VSDVDGSGVA
HEAPAYGAED LEVARAYGVP LMFGVDDHGI LQVTHEQGKF FKDADKGLIA DMKARGLMFW
AGTLKHRYPF HDRTGDPILY FAKKGWYIRT SQVAGEMLAQ NEKINWVPGN IKHGRFGNWL
EGNVDWAISR ERYWGTPLPF WQSESGQLRV IGSVAELSEL AGRDLSDLDL HRPYIDDITF
TLDGEEYRRV PEVLDVWFDS GSMPYAQWGL LLNEQGEAVR GAEQFAKHYP ADYICEAIDQ
TRGWFYSLHA ISTMLYDQPA YKNVICLGHI VDEKGLKMSK SKGNVVAPLP LFDQYGADSV
RWYMFMASDP GDQKRFSERL VAEAQRSYVN TLWNVYSFFV LYANLDQPDL AAAPAVAERP
EMDRWLLARL EETVRDVTAA LESYDARSGG RALEGFVDDL SNWYVRRSRS RFWGEGGTVD
TAAYATLHEA LLVVSQLTAP FTPFLADALY RNLSGEESSV HLTPWPTVRA ERLDRKLTAD
MAAVMKVVEL GRAVRGAHNL KTRQPLAGVQ VRAASPEALD ALKRSQTQIM EELNVKAVTF
LEGDTDLVQY SLRPNLPVVG KQYGKQLPVL KKALTEADAR AVATAVQAGQ GFSVQADGVT
FDLTPGSVLV DAKAPEGVAA AEDAGYLVAF DTALTPELVR EGLARDLVRA IQEARKAAGF
EVQDRIALAL ELDGEALEAA QAWQDFIAGE VLAEQVAYGS GEGFRAEVEG GAVTLKKL
