(data stored in ACNUC7421 zone)

SWISSPROT: B8IB40_METNO

ID   B8IB40_METNO            Unreviewed;       989 AA.
AC   B8IB40;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 70.
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=Mnod_0391 {ECO:0000313|EMBL:ACL55433.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55433.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55433.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) 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_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; CP001349; ACL55433.1; -; Genomic_DNA.
DR   RefSeq; WP_015927144.1; NC_011894.1.
DR   ProteinModelPortal; B8IB40; -.
DR   STRING; 460265.Mnod_0391; -.
DR   EnsemblBacteria; ACL55433; ACL55433; Mnod_0391.
DR   KEGG; mno:Mnod_0391; -.
DR   eggNOG; ENOG4105C07; Bacteria.
DR   eggNOG; COG0060; LUCA.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; ATEQWFI; -.
DR   OrthoDB; POG091H028I; -.
DR   Proteomes; UP000008207; 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; -; 1.
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; B8IB40.
DR   SWISS-2DPAGE; B8IB40.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654661,
KW   ECO:0000313|EMBL:ACL55433.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654675};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT   DOMAIN       36    694       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      739    888       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        66     76       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   MOTIF       656    660       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   BINDING     615    615       Aminoacyl-adenylate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02002}.
FT   BINDING     659    659       ATP. {ECO:0000256|HAMAP-Rule:MF_02002}.
SQ   SEQUENCE   989 AA;  109921 MW;  B9B8DD724BAD1277 CRC64;
     MTETKPASGR DYSETLFLPR TDFPMRAGLP EREPEILKRW QAIDLYGRIR AAAAGRPKFV
     LHDGPPYANG HIHIGTALNK ILKDVVVRAA GLLGTDANYV PGWDCHGLPI EWKIEEQYRA
     KGRNKDEVPV IEFRRECRAF AEHWLSVQRE EFKRLGVTGD WDHPYSTMAY PAEAQIAREL
     MTFAMTGQLY RGSKPVMWSV VEKTALAEAE VEYEDIVSDA IWAAFPVVTS ADPALAGAHV
     VIWTTTPWTI PANRAVAYSR KISYGLYRVS AAPEENWVQP DFRCIVADEL AGDVFKAARV
     DAVERLADVA PEALAGLTLA HPLGGWNEGY RFPVPMLEGE HVTDEAGTGF VHTAPSHGRE
     DFEVWMANSR ALRERGIDVR IPYTVDADGV LTVEAPGFTG RRVLTEKGEK GDANKAVIAA
     LAEAGTLVAR GTLKHSYPHS WRSKKRVIFR NTPQWFIALD APVASLGSKT LREVALREIA
     ATEWVPPQGQ NRITGMIANR PDWVVSRQRA WGVPITVFVK KGTSEILRDE RVNARIVAAF
     AEEGADAWFA DPDGARFLAP DHDPAAYEKV TDVLDVWFDS GSTHAFTLED PVAFPGLAGI
     RRRRDGGDDT VMYLEGSDQH RGWFHSSLLE SCGTRGRAPY DVVLTHGFVL DPKGEKMSKS
     RGNVVAPQDV IAASGADILR LWVAASDYTD DLRIGPPIIK TFSETYRKLR NSLRWMLGTL
     AHHRPEDRVA PQAMPELERF ILHRLAELDG EIREAYRTYD FKRVVALLNG FMTGDLSSFY
     FDVRKDALYC DPLSSTVRRA ALTVVDETFR RVVVWLAPVL AFTAEEAWLS RYPSEDGSVH
     LQTLPDTPSD WRDEALAARW ARIRRVRRVV TGALEIERAK KRIGASLEAA PIVYLADPDL
     QAALDGIDFA EICITSDIRI EAGEGPQDAF RLDDVGGVAV VPALAEGRKC ARSWKVLPSV
     GSDPDYPDVT PRDAQALREW DALHAKAAE
//

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