ID   SYI_CYTH3               Reviewed;        1110 AA.
AC   Q11NV4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=CHU_3676;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS   15051 / NCIMB 9469 / D465).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX   PubMed=17400776; DOI=10.1128/aem.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA   Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA   Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA   McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG60909.1; -; Genomic_DNA.
DR   RefSeq; WP_011587014.1; NZ_FPJX01000004.1.
DR   AlphaFoldDB; Q11NV4; -.
DR   SMR; Q11NV4; -.
DR   STRING; 269798.CHU_3676; -.
DR   PRIDE; Q11NV4; -.
DR   EnsemblBacteria; ABG60909; ABG60909; CHU_3676.
DR   KEGG; chu:CHU_3676; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_10; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001822; 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; 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; 2.
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..1110
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000070895"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           658..662
FT                   /note="'KMSKS' region"
FT   BINDING         661
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1110 AA;  126860 MW;  BF665BCB606DE8B9 CRC64;
     MKYNEKKTEL SEVGKEVQQF WNDKKIFEKS VETREGNPTF TFYEGPPSAN GTPGIHHVMG
     RTVKDIFCRF KTMQGFQVKR KGGWDTHGLP VELQVEKELG ITKEDIGKKI TVEQYNQKCR
     EAVMKYKSQW DELTVKMGYW VDLEKPYITF ENNYIESVWY LLKEFHQKKL LYKGYTIQPY
     SPAAGTGLSS HELNQPGTYK DVRDTSAVAQ FKLKANPKFA DNTYFLAWTT TPWTLPSNSA
     LAVGENIEYV LVSTFNPYTF KPVQVILAKA LLGKYFSEKA KDLSLEAYKD GDKLIPFKIL
     QSYKGKDLVG IEYEQLMPYL QPETPAFRVI AGDFVSTEDG TGIVHIAPTF GADDARVAKL
     AGIPSIVTKD DRGNEYPLVD KRGRFTKEVT DFAGEYVKEA YLTDEEKEAE RVKQGRDKYL
     SVDERISIKL KEANRAFKVE KYEHSYPHCW RTDKPVLYYP LDSWFIKTTA KKERLVELNK
     TINWKPESTG VGRFGNWLEN LVDWNLSRSR YWGTPLPIWR SEDGSEEKCI GSIEELKTEI
     AKAQKAGIET ATDIKDLHRP YVDNIVLVSD SGKPMKRELD LIDVWFDSGA MPYAQWHYPF
     ENKELFNNNY PADFIAEGVD QTRGWFFTLH AISGMLYDKV AFKNVIANGL VLDKNGNKMS
     KRVGNVVNPF ETIDKYGPDA TRWYMITNAP PWDNLKFNLD GITEVQRRFF GTLQNTYSFF
     ALYANLDNFT FAEAEIPLAQ RTESDRWILS KLQSLVKDVA DAYSDYEPTK AGRAIQDFVV
     DDLSNWYVRL NRKRFWKGEY NADKTAAYQT LYTCLETVAK LGAPIAPFYM DKLFSDLNQV
     SKKNAVESVH LADFPKVNEA FLDVELEERM SLAQRISSLV HSIRKAQTIK VRQPLSRILI
     PILQPHLKAQ IQAVEDLIKN EVNIKAVEYI EDTSGVVIKT IKPNFKKLGK EYGAKLKEIG
     NAIAELRAED ITAIERNVFE LKLADGTVIP ITSEDVEIRS QDIPGWSVAS EGGITVALDI
     TLSDDLRKEG IARDVVNRVQ NLRKDMGLEV QDKIRITIQK VDELINSALS ANQEYICTET
     QAFSLELVEK LADGKEVEMD EQTLIMKIEK