SYI_CAMFF
ID SYI_CAMFF Reviewed; 916 AA.
AC A0RNK3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
GN OrderedLocusNames=CFF8240_0610;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) 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: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; CP000487; ABK82625.1; -; Genomic_DNA.
DR RefSeq; WP_011731879.1; NC_008599.1.
DR AlphaFoldDB; A0RNK3; -.
DR SMR; A0RNK3; -.
DR STRING; 360106.CFF8240_0610; -.
DR EnsemblBacteria; ABK82625; ABK82625; CFF8240_0610.
DR GeneID; 61064455; -.
DR KEGG; cff:CFF8240_0610; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_0_7; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000760; 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; Zinc.
FT CHAIN 1..916
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000022054"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT MOTIF 609..613
FT /note="'KMSKS' region"
FT BINDING 568
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 916 AA; 104180 MW; 9A053BBF79057565 CRC64;
MDYKDTLLLP TTDFAMRGNL PECEPARYAK WDEQKVYEKM KAKREKSAIS FNIHDGPPYA
NGHLHIGHAL NKILKDIILK THYFFGQGIR YTPGWDCHGL PIEQQVEVKL GDKKKSMSKS
DIRQECRNWA KEFITVQKDE FKSLGVIGDW NDPYLTMKFK FEANIYRTLC EVAKKGLLVE
RSKPVFWSWA ARSALAEAEV EYEDKEDYSL YVAFCLSDAA CKKLGVSDAK AVIWTTTPWT
LVANQAISLN PNEKYALTSE GYIIALPLKE TLINQGIING KILKEFASSE LEGLSAINPL
NGRDSRFILG EHVLMDGGTG LVHTAPGHGE DDYFASLKYG IEVIMPVDEA GLYDETLRVK
KLLPEHLLNE FIGLHIFKAN EKLIELLGDA AVKVSKFVHS YPFCWRTHKP VIYRATKQWF
IAMDEPKLSG KTLRQTALEA LKSVKFYPEV GVKRISSMIE NRPDWCISRQ RDWGVPIAFF
RDSATKEPIF DSRVLEHVAK VFDEKGSDAW WNLEISELLP KGTNLDPSKL EKVTDILDVW
FDSGSTWNAV LNSGDYDAGG YQADMYLEGS DQHRGWFQSS LLLSCAINQK APYKSVLTHG
FTVDGNGNKM SKSKGNVIAP SDVAKRYGVE ILRLWVGLSD YSSDLKISDD ILKQVAEQYR
KIRNTIRFLL ANINDLDDIS SHFGTLDKWI LARATKSFKE VSECFKNYEY SKGFNILLNF
LSTDLSGIYL DICKDRLYCD EKDGLRRRSS QSAMAIIAKS LLSLIAPTLT YTVDEAIEFA
PDIIKNGAKD AFDLVYEPLV FEFKIDDELL TSSREKFNEI IDVLKKDKII KSTLEVILET
SSNEILANDL DEIIDWYMVS FVRNIESDEF LAEFAVGNDK FKIVKADRYK CPRCWKYAAK
IDNDLCPRCA KVLKRV
