SYI_CAMJE
ID SYI_CAMJE Reviewed; 917 AA.
AC P41257; Q0P9J1; Q9PNN0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; OrderedLocusNames=Cj1061c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=7582016; DOI=10.1099/13500872-141-10-2561;
RA Hong Y., Wong T., Bourke B., Chan V.L.;
RT "An isoleucyl-tRNA synthetase gene from Campylobacter jejuni.";
RL Microbiology 141:2561-2567(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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_02002}.
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_02002};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02002};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02002};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}.
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_02002}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
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DR EMBL; U15295; AAA91296.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35179.1; -; Genomic_DNA.
DR PIR; B81309; B81309.
DR RefSeq; WP_002907389.1; NC_002163.1.
DR RefSeq; YP_002344456.1; NC_002163.1.
DR AlphaFoldDB; P41257; -.
DR SMR; P41257; -.
DR IntAct; P41257; 13.
DR STRING; 192222.Cj1061c; -.
DR PaxDb; P41257; -.
DR PRIDE; P41257; -.
DR EnsemblBacteria; CAL35179; CAL35179; Cj1061c.
DR GeneID; 905353; -.
DR KEGG; cje:Cj1061c; -.
DR PATRIC; fig|192222.6.peg.1043; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_7; -.
DR OMA; PSWYIRT; -.
DR Proteomes; UP000000799; Chromosome.
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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
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 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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..917
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098372"
FT MOTIF 59..69
FT /note="'HIGH' region"
FT MOTIF 610..614
FT /note="'KMSKS' region"
FT BINDING 569
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT CONFLICT 144
FT /note="D -> N (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="E -> K (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="G -> R (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="K -> N (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="A -> T (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="S -> P (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="T -> S (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="M -> I (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="P -> S (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="A -> V (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="N -> D (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="V -> I (in Ref. 1; AAA91296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 917 AA; 105262 MW; 73E379C8F8F3D6EA CRC64;
MDYKETLLLP STTFAMRANL AELEPQRFKK WFEQNYAYEK MKENRKNAKK SFTLHDGPPY
ANGHIHIGHA LNKILKETII KTHYFKGESV RFTPGWDCHG LPIEQQVEVK LGEKKKSLSK
KEIREFCRQH ASEFVDIQRE EFKDLGIIAD WDKPYLTMKF EFEAAIYRTL CEIAKKGLLC
ERSKPVFWSW AAKSALAEAE VEYQDKEDYS IFVAFDLDVK ACEKLGVSKA SAVIWTTTPW
TLVANQAIAL NPNENYVITK EGLIFASALL KSMVEKGLTS GEIQKELNAK EFEKLEAINP
LNGRKSVLIM GEHVLMDGGS GLVHTAPGHG EDDYYACLKY GIEVLMPVDD SGCYDETLRA
KGLLPSHLLE EFIGLHIFKA NEKILELLGE KLLHSSKFIH SYPFCWRTHK PVIYRATKQW
FILMDEPKLQ GKTLRECAKE QLLKTTFYPQ SGVKRIGSMV ENRPDWCISR QRDWGTPIAF
FRDKNTKEVI FDDELFDFVA AIFEKHGADA WWEFEIKDLI PTNSKYKAEN LEKVYDILDV
WFDSGSTFNA VLNSGLYDAG EKRASMYLEG SDQHRGWFQS SLLVGTAINE SAPYESILTH
GFTTDEKGQK MSKSKGNVIA SEYVAKTYGV EILRLWILLS DYSSDLKISD NILKQVGEQY
RKIRNTIRFL LANTNDLKDL EVKEFSFIDK WILSRATKVF KASKEAFFAY EFAKGFSLLL
NFLSADLSGI YLDISKDRLY CDSENAQRRK SAQVAMALMA KELLNLLAPN LSYSVDEALE
HANVLIKGDA KDVFDLSLTQ DFDYDFGIDD TFLMSAREKF FEQIDILKKD KIIKSTLELN
LNISFNKFPN EELADWFMVS QISNENEEIL AEFEVENEKF KITKASLCKC PRCWKLQSKN
EETPCLRCEE VLKGVQC
