(data stored in SCRATCH zone)

SWISSPROT: C3MGU5_SINFN

ID   C3MGU5_SINFN            Unreviewed;       973 AA.
AC   C3MGU5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
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   ECO:0000313|EMBL:ACP24210.1};
GN   OrderedLocusNames=NGR_c04140 {ECO:0000313|EMBL:ACP24210.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24210.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24210.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24210.1; -; Genomic_DNA.
DR   RefSeq; WP_012706995.1; NC_012587.1.
DR   RefSeq; YP_002824963.1; NC_012587.1.
DR   ProteinModelPortal; C3MGU5; -.
DR   STRING; 394.NGR_c04140; -.
DR   EnsemblBacteria; ACP24210; ACP24210; NGR_c04140.
DR   GeneID; 7791640; -.
DR   KEGG; rhi:NGR_c04140; -.
DR   PATRIC; fig|394.7.peg.3220; -.
DR   eggNOG; ENOG4105C07; Bacteria.
DR   eggNOG; COG0060; LUCA.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; ATEQWFI; -.
DR   OrthoDB; POG091H028I; -.
DR   Proteomes; UP000001054; 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; C3MGU5.
DR   SWISS-2DPAGE; C3MGU5.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654661,
KW   ECO:0000313|EMBL:ACP24210.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00654675};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:UP000001054}.
FT   DOMAIN       39    685       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      729    877       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        68     78       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   MOTIF       647    651       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   BINDING     606    606       Aminoacyl-adenylate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02002}.
FT   BINDING     650    650       ATP. {ECO:0000256|HAMAP-Rule:MF_02002}.
SQ   SEQUENCE   973 AA;  109615 MW;  D645697EE71E3CCD CRC64;
     MQKTMTETAE KIDYSSTLYL PQTEFPMRAG LPQKEPETVA RWQKMELYKK LRASAAGREK
     FVLHDGPPYA NGNIHIGHAL NKILKDVINR SFQMRGFDAN YVPGWDCHGL PIEWKIEEKY
     REKGRNKDDV PVNEFRQECR DFASGWIEVQ TEEFKRLGIE GDFDKPYTTM NFHAEARIAG
     ELMKIAKAGQ LYRGSKPVMW SVVERTALAE AEIEYADVES DMIWVKFPVA EGPDALAGAF
     VVIWTTTPWT IPGNRAVAYS SRYAYGLYEV ATAENDYGPQ PGEKLIFAKR LADESAAKAK
     VTFNFVRDLE PEELGTVTCA HPLHGLGGGY AFQVPLLDGE HVTDDAGTGF VHTAPSHGRE
     DFEAWMENVR LLEDRGISSA IPFPVDDAGY YTADAPGFGP EAEGGAGRVI DDKGKKGDAN
     DRVIKALIAR HALFARGRMK HSYPHSWRSK KPVIFRNTPQ WFVYMDKDFG DGTTLRSRAL
     NAIDDTRFVP GAGQNRLRAM IEQRPDWVLS RQRAWGVPIA IFADDDGQIL VDEKVNARIL
     EAFEEEGADA WFAEGAKERF LGNDHDHARW HQVMDILDVW FDSGSTHTFT LEDRPDLKWP
     ADVYLEGSDQ HRGWFHSSLL ESCATRGRAP YDAVVTHGFT MDEKGEKMSK SKGNTVTPQE
     VMKDAGADIL RLWVMTTDYW EDQRLGKTII QTNIDAYRKL RNTIRWMLGT LAHDKGETIA
     LADMPELEQL MLHRLAELDR LVREGYDAFD FKRIARALID FSNVELSAFY FDIRKDALYC
     DAPSSLRRRA ALQVIRTLFD CLVTWLAPML PFTAEEAWLS RNPEAVSVHL EQFPAVPAEW
     RNEVLAEKWR KIREVRKVVT GALEIERKDK RIGSSLEAAP IVHVADPDLR AALDGQDFAE
     ICITSAIEID GAEGPAGAFT LPDVAKVGVV PKLAEGRKCA RSWRITTDIG SDPFYPDVSA
     RDAAALRELG FKP
//

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