ID   C6D538_PAESJ            Unreviewed;      1029 AA.
AC   C6D538;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   18-JAN-2017, entry version 64.
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   OrderedLocusNames=Pjdr2_3873 {ECO:0000313|EMBL:ACT02503.1};
OS   Paenibacillus sp. (strain JDR-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=324057 {ECO:0000313|EMBL:ACT02503.1, ECO:0000313|Proteomes:UP000002510};
RN   [1] {ECO:0000313|Proteomes:UP000002510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDR-2 {ECO:0000313|Proteomes:UP000002510};
RX   PubMed=22675593; DOI=10.4056/sigs.2374349;
RA   Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA   Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S.,
RA   Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L.,
RA   Jones J.B., Ingram L.O., Shanmugam K.T., Preston J.F.;
RT   "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL   Stand. Genomic Sci. 6:1-10(2012).
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}.
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DR   EMBL; CP001656; ACT02503.1; -; Genomic_DNA.
DR   RefSeq; WP_015845443.1; NC_012914.1.
DR   ProteinModelPortal; C6D538; -.
DR   STRING; 324057.Pjdr2_3873; -.
DR   EnsemblBacteria; ACT02503; ACT02503; Pjdr2_3873.
DR   KEGG; pjd:Pjdr2_3873; -.
DR   PATRIC; 22838281; VBIPaeSp118865_3854.
DR   eggNOG; ENOG4105C07; Bacteria.
DR   eggNOG; COG0060; LUCA.
DR   HOGENOM; HOG000246403; -.
DR   KO; K01870; -.
DR   OMA; WGTPLNI; -.
DR   OrthoDB; POG091H028I; -.
DR   Proteomes; UP000002510; 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-HAMAP.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 1.10.730.10; -; 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   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654661,
KW   ECO:0000313|EMBL:ACT02503.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654675};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002510};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654679};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654658};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02003,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654687};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002510};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT   DOMAIN       17    620       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      675    820       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        47     57       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02003}.
FT   MOTIF       589    593       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02003}.
FT   BINDING     592    592       ATP. {ECO:0000256|HAMAP-Rule:MF_02003}.
SQ   SEQUENCE   1029 AA;  115521 MW;  2C4AE9A58145387D CRC64;
     MQRVDVKEKA RARELRVLKQ WAENDTFKQS IENRAGKPNY VFYEGPPTAN GAPHIGHVLG
     RVIKDFIGRY KTMSGYRVVR KAGWDTHGLP VELGVEKQLG ISGKQEIEKY GVEEFIKKCK
     DSVFVYEKQW RELTEAIAYW TDLDNPYITL KNEYIESVWH ILSTIHGKGL LYRGHRVSPY
     CPCCQTTLSS HEVAQGYEDV KDLSATVKFK LASGESILAW TTTPWTLPAN VALAVNPELD
     YVRASKDGEV YIVAQNLAES VLKEGYETLS TLKGSELVGL SYEPPFRYVP VEHGHVVIPG
     DFVSDTSGTG IVHIAPAHGE DDYKVSRQNG ISMLSVVNNA GRYIDEVTDL AGRFVKDCDV
     DIVKMLSERG LLFSKERYEH SYPFCWRCKS PLLYYATESW FIETTKVKDQ LIANNSTVDW
     YPGHIREGRF GKFLEDLVDW NISRNRYWGT PLNVWVCEAT GKEYAPSSIA DLRERAVDFV
     PEDIELHKPY VDEIKLKSPF QEGAVMTRTS EVIDVWFDSG SMPFAQQHHP FENAEEFAEQ
     YPADMICEGI DQTRGWFFSL LAVSTLYNGK APYKAVISTG HILDENGQKM SKSKGNVIDP
     WEIINEYGTD AFRWALLADS APWNSKRFSR GIVGEAKSKV IDTIVNTHAF YALYASIDGF
     NPADHEERSS ASKLDRWIVS RLNSLIKTVV KGLEVNDFLN PAKTIEVFVD ELSNWYIRRS
     RDRFWGSGLT EDKVAAYQTL RHVLLTLSRV IAPYAPLLAE DVYGNLGGES SVHLADYPVA
     DESAIDETLE RDMDSAKQIV ELARNVRNET GIKTRQPLSE LIVSLDRDFA VTEYEDIIKD
     EINVKSIVVQ TSDSGFVDFT LKLNLKVAGK KYGKHVGPIQ GYLKGLAPEA TREAVTSGSL
     VFTSAEGEAI TVTTEELLVE KQAKSGFASA SANGLTVALN TDITPELEQE GWVREVIRAV
     QDTRKKLDLP IEKRIDLVLD VDGGLQAALE TFSNVLNENV LLNSVSYEKA EGMECVQLGE
     KEIGILVRV
//