(data stored in SCRATCH zone)

SWISSPROT: C6B2K4_RHILS

ID   C6B2K4_RHILS            Unreviewed;       963 AA.
AC   C6B2K4;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 67.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02002};
DE            EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02002};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002};
DE            Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02002};
GN   Name=ileS {ECO:0000256|HAMAP-Rule:MF_02002};
GN   OrderedLocusNames=Rleg_0519 {ECO:0000313|EMBL:ACS54824.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54824.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54824.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54824.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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_02002}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile). {ECO:0000256|HAMAP-
CC       Rule:MF_02002, ECO:0000256|SAAS:SAAS00654659}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002}.
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_02002}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02002}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02002}.
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DR   EMBL; CP001622; ACS54824.1; -; Genomic_DNA.
DR   RefSeq; WP_012756209.1; NC_012850.1.
DR   ProteinModelPortal; C6B2K4; -.
DR   EnsemblBacteria; ACS54824; ACS54824; Rleg_0519.
DR   KEGG; rlg:Rleg_0519; -.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; ATEQWFI; -.
DR   OrthoDB; POG091H028I; -.
DR   Proteomes; UP000002256; 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:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
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;
DR   PRODOM; C6B2K4.
DR   SWISS-2DPAGE; C6B2K4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654661,
KW   ECO:0000313|EMBL:ACS54824.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654675};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654679};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654658};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654687}.
FT   DOMAIN       34    675       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      719    867       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        64     74       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   MOTIF       637    641       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   BINDING     596    596       Aminoacyl-adenylate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02002}.
FT   BINDING     640    640       ATP. {ECO:0000256|HAMAP-Rule:MF_02002}.
SQ   SEQUENCE   963 AA;  108416 MW;  1857919737AFF0D2 CRC64;
     MTDTAEKIDY SKTLYLPETD FPMRAGLPQK EPELVKRWQE MGLYKKLRAS AAGREKFVLH
     DGPPYANGNI HIGHALNKIL KDVINRSFQM RGYDANYVPG WDCHGLPIEW KIEEKYREKG
     KNKDEVPVNE FRRECREFAA GWIKVQAEEF KRLGIEGDFD NPYTTMNFHA ESRIAGELLK
     IAASGQLYRG SKPIMWSVVE RTALAEAEVE YQDYESDTIW VKFPVVEGPV ALKDAFVVIW
     TTTPWTIPGN RAVSFSPRIS YGLYEVTAAE NDFGPRPGEK LIFADKLAEE SFAKAKLQYK
     RLSDVSAADF AAMTCAHPFK GLGGGYEFRV PLLDGDHVTD DAGTGFVHTA PSHGREDFDA
     WMSAVRALEA RGIDTKIPFP VDDGGFYTSD APGFEGARVI DDNGKKGDAN DRVIRELIAR
     GALFARGRLK HQYPHSWRSK KPVIFRNTPQ WFVYMDKTLA DGTTLRSRAL GAIDDTRFVP
     AAGQNRLRAM IEGRPDWVLS RQRAWGVPIA VFADDDGDVL VDEAVNARIL EAFEHEGADA
     WFAEGAKERF LGNDHDHSRW TQVMDILDVW FDSGSTHTFT LEDRPDLKWP ADLYLEGSDQ
     HRGWFHSSLL ESAATRGRAP YNAVLTHGFT MDEKGEKMSK SKGNVTAPQE VMKDAGADIL
     RLWVMTSDYA DDLRVGKTII QTNVDAYRKL RNTIRWMLGT LAHDKGEEIA LADLPELEQL
     MLHRLAELDE LVRENYDAFD FKKIARALID FANVELSAFY FDVRKDALYC DAPSSLRRRA
     SLHVIRQIFD CMVTWLAPML PFTTEEAWLS RNPSAVSVHL EQFAPVAKEW RNDALAEKWK
     KIRTVRSVVT GALEIERKDK RIGSSLEAAP VVHIADPELL KALEGQDFTE VCITSAIEIK
     VGEGPGDAFR LAEVPQVSVV PKLAEGEKCA RSWRITRDVG SDPEYPDVSA RDAAALRELA
     ALT
//

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