ID   A0A0Q6PGS3_9MICO        Unreviewed;      1129 AA.
AC   A0A0Q6PGS3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-FEB-2018, entry version 20.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003,
GN   ECO:0000313|EMBL:KQV03578.1};
GN   ORFNames=ASC55_00890 {ECO:0000313|EMBL:KQV03578.1};
OS   Microbacterium sp. Root322.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736514 {ECO:0000313|EMBL:KQV03578.1, ECO:0000313|Proteomes:UP000050974};
RN   [1] {ECO:0000313|EMBL:KQV03578.1, ECO:0000313|Proteomes:UP000050974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root322 {ECO:0000313|EMBL:KQV03578.1,
RC   ECO:0000313|Proteomes:UP000050974};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV03578.1, ECO:0000313|Proteomes:UP000050974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root322 {ECO:0000313|EMBL:KQV03578.1,
RC   ECO:0000313|Proteomes:UP000050974};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As
CC       IleRS can inadvertently accommodate and process structurally
CC       similar amino acids such as valine, to avoid such errors it has
CC       two additional distinct tRNA(Ile)-dependent editing activities.
CC       One activity is designated as 'pretransfer' editing and involves
CC       the hydrolysis of activated Val-AMP. The other activity is
CC       designated 'posttransfer' editing and involves deacylation of
CC       mischarged Val-tRNA(Ile). {ECO:0000256|HAMAP-Rule:MF_02003}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile). {ECO:0000256|HAMAP-
CC       Rule:MF_02003, ECO:0000256|SAAS:SAAS00654659}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated valine is
CC       translocated from the active site to the editing site, which
CC       sterically excludes the correctly activated isoleucine. The single
CC       editing site contains two valyl binding pockets, one specific for
CC       each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000256|HAMAP-
CC       Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KQV03578.1}.
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DR   EMBL; LMCS01000001; KQV03578.1; -; Genomic_DNA.
DR   RefSeq; WP_055872377.1; NZ_LMCS01000001.1.
DR   EnsemblBacteria; KQV03578; KQV03578; ASC55_00890.
DR   Proteomes; UP000050974; Unassembled WGS sequence.
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   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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   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 {ECO:0000256|RuleBase:RU363035,
KW   ECO:0000256|SAAS:SAAS00654661};
KW   ATP-binding {ECO:0000256|RuleBase:RU363035,
KW   ECO:0000256|SAAS:SAAS00654675};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050974};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003};
KW   Ligase {ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654679,
KW   ECO:0000313|EMBL:KQV03578.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363035,
KW   ECO:0000256|SAAS:SAAS00654658};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU363035,
KW   ECO:0000256|SAAS:SAAS00654687};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN       28    690       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      743    886       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        58     68       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02003}.
FT   MOTIF       655    659       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02003}.
FT   BINDING     658    658       ATP. {ECO:0000256|HAMAP-Rule:MF_02003}.
SQ   SEQUENCE   1129 AA;  125647 MW;  B29E284B3874DE7F CRC64;
     MTYPRSSFGP AADSVAPSPR FPQIEEEVLA FWKTDDTFRA SIAQREGSPE WVFYDGPPFA
     NGLPHYGHLL TGYAKDVFPR FQTMTGHKVD RVFGWDTHGL PAELEAMKQL GITEKAEIEE
     MGIDVFNAKA KSSVLTYTHE WQDYVTRQAR WVDFERGYKT LDLGYMESVL WAFKTLYDKG
     LAYEGYRVLP YCWRDETPLS AHELRMDDDV YQMRQDPSVT VTFPLTGAKA EALGLTGVRA
     LAWTTTPWTL PTNLALAVGP EIEYVVLPAG PNGAADVHQA AGTTDAAIES SAHRYLLARQ
     LVGGYAKDLG YESTEEALAA VDATVRGAEL QDVTYDRLFD YYADTETYGT ENAWRILVDD
     YVTVSDGTGI VHQAPAYGED DQRVAGAAGI PTILSLDDGG RFLPNVTDVA GELWMEANTP
     LVRLIRDNGR LIRLQSYEHS YPHCWRCRNP LIYKAVSSWF IRVTDIKDDL LANNEQITWV
     PENVKHGQFG KWLEGARDWS ISRNRYWGSP IPIWKSDDPE YPRVDAYGSL EELERDFGTL
     PRNPEGEIDL HRPYIDDLTR PNPDDPTGKS TMRRIEDVFD VWFDSGSMPY AQVHYPFENQ
     EWFDSHSPAD FIVEYIGQTR GWFYVMHVLS TALFDRPAFT GVSCHGIVLG SDGYKMSKSL
     RNYPDVSEVL DRDGSDAMRW FLMSSSVLRG GNLAVTEEGI RSGVREFLLP LWNSWYFFAT
     YANASGADGY EASWRTDSTD VLDRYILARL GDLVREVRAD LEGLDSTTAS ARLRDFAEVL
     TNWYIRRSRD RFWTGVTEDP KSREAFDTLY TVLETLTRVA APLVPLVSER VWQGLTGGRS
     VHLTDWPDAA QFPAADEIRD AMDAVRELSS VGNALRKKEK LRVRLPLARF TVVSPLAASL
     GQFEDILREE LNVKSVELVP LADDTATEYG IAHRLSVNAR AAGPRLGKDV QKAIQAARSG
     DWSEVSGVVT AGGIVLEPSE YELVLETTGR PEGEALAIVP TGGFVLLDTT TTPELEAEGL
     ARDVIRAVQE TRKNADFDVS DRIQLVLRFQ DDVDTTAVVS AFDLAGIAAE TLAEEYFVID
     AQGDSIFGHG TVLAAAAAVT PEFSAVIPAG TYANAGDFTI AVTRMGAAA
//