ID   SYI_RHOBA               Reviewed;        1213 AA.
AC   Q7UNZ2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=RB7259;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294145; CAD75273.1; -; Genomic_DNA.
DR   RefSeq; NP_867726.1; NC_005027.1.
DR   AlphaFoldDB; Q7UNZ2; -.
DR   SMR; Q7UNZ2; -.
DR   STRING; 243090.RB7259; -.
DR   PRIDE; Q7UNZ2; -.
DR   EnsemblBacteria; CAD75273; CAD75273; RB7259.
DR   KEGG; rba:RB7259; -.
DR   PATRIC; fig|243090.15.peg.3516; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_0; -.
DR   InParanoid; Q7UNZ2; -.
DR   OMA; KMMAPFT; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001025; 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; 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   Gene3D; 3.90.740.10; -; 1.
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; 2.
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..1213
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098557"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           100..110
FT                   /note="'HIGH' region"
FT   MOTIF           742..746
FT                   /note="'KMSKS' region"
FT   BINDING         745
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1213 AA;  137200 MW;  353E3470B13258B3 CRC64;
     MPRQAPTRPR SPKKPRESDG GGGNVLQRIK LCVVLTFPSH SSGYHVSANS TAAFRAPAAS
     PHFPTLEEQV LAFWDQHSIY EQSLARRANA PTFVFYEGPP TANGMPHPGH CLTRAIKDVF
     PRYKTMRGYR CERKAGWDTH GLPVEVEVGK ELGIHSKEEI EAYGVEPFIQ KCQSSVWRYM
     QEWQTLTRRL GFWVNLEEAY VTYHQSYVES VWWSLKNLFD RGLLYQGHKI VWWWAQGGTA
     LSAGEVGQGY REVADPSVYV LFPLVDQPER SLVVWTTTPW TLPSNMYAAV KPELEYAVVK
     DSETGQELVL AAALVDSLAG KLKRELTVVD TISGESLVGQ RYQPPFEDYQ TRLNDPTGEL
     VTGGKESLYW RVVAADFVTT DSGSGLVHLA PAFGEIDHEV LVTERTRFVD GQRPELLCAV
     GPDGKFTDEF ASMKGVWVKE ADKTLTRTLR ESGRLLHLEQ YLHDYPFCWR ADDDPLIQYP
     RESWFIRTTK FRDLMLKNNS KIGWQPEHIR DGRFGNFLES NVDWALSRER YWGTPLPIWV
     CQSTGRMEAI ESYEELLAKP GVDGTQVWDN AKAANPELPD DLRVHKPYID SVTYDSPFES
     GARMQRVSEV IDCWYDSGAM PFAQWGWPHQ NDAQFQEQFP ADFISEAIDQ TRGWFYSQLA
     ISTMLFGEGA SIREAGTKAN ELAPSRDSES DYPHPFRNCI VLGLMLSQWY ESAGKEGQPK
     TVLLSESEAE QADGKFTKKT GKMSKSLRNY RSPSEIFDKY GADAMRWYFF ANQAPWNSII
     YADQAIRDSI PEFLLRLWNT YSFFSIYAEI DGFDPTSATD VDEQLSPESL ASAPTYRPIS
     ERSEIDRWIH SELHRTLATV IDRMDAFDNY NACQAITNLL DGLSNWYVRR SRDRFWAPDS
     DSPDKHDAYW TLYEVMLELT KVIAPFVPFL ADTLWQELTA PFGDKALKSV HLCDFPKPDA
     SRVDQKLSDS MRLLREIASM GRSARADAKL KVRLPLAKVE VILTDDSAID WLQSHDALVR
     EELNVKAVDY TTDGGDYVQY TIVPNFKRLG PKVGKNIPVV KKMLGEADGN QLLTQLQTAG
     FVELELASGP LKLDGEDIEV RLQAREGWAA AQGSGCVVVL NTEVTPELRR EGLAKDLIRG
     IQSQRKELDC QYTDRIRVAV ETSDAELQSA IEEHRTMICG ETLADDLVIG TLPNAQQVAI
     EGGELYVAKV SDK