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Q39YT0 (Q39YT0_GEOMG) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase HAMAP-Rule MF_02002

EC=6.1.1.5 HAMAP-Rule MF_02002
Alternative name(s):
Isoleucyl-tRNA synthetase HAMAP-Rule MF_02002
Gene names
Name:ileS HAMAP-Rule MF_02002 EMBL ABB30594.1
Ordered Locus Names:Gmet_0351 EMBL ABB30594.1
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP] EMBL ABB30594.1
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length923 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity. HAMAP-Rule MF_02002 SAAS SAAS023585

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002 SAAS SAAS023585

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002 SAAS SAAS023585

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002 SAAS SAAS023585

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002 SAAS SAAS023585.

Domain

IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity. HAMAP-Rule MF_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. HAMAP-Rule MF_02002

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif57 – 6711"HIGH" region By similarity HAMAP-Rule MF_02002
Motif601 – 6055"KMSKS" region By similarity HAMAP-Rule MF_02002

Sites

Metal binding8951Zinc By similarity HAMAP-Rule MF_02002
Metal binding8981Zinc By similarity HAMAP-Rule MF_02002
Metal binding9151Zinc By similarity HAMAP-Rule MF_02002
Metal binding9181Zinc By similarity HAMAP-Rule MF_02002
Binding site5601Aminoacyl-adenylate By similarity HAMAP-Rule MF_02002
Binding site6041ATP By similarity HAMAP-Rule MF_02002

Sequences

Sequence LengthMass (Da)Tools
Q39YT0 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 7BCF7E69BF1B2E7F

FASTA923103,598
        10         20         30         40         50         60 
MEYKNTLNLP VTDFPMKANL PQREPEILAG WQKNDLYGKL TAAGEGKPRY VLHDGPPYAN 

        70         80         90        100        110        120 
GHIHIGHALN KILKDIILKS KRMQGFDAPY VPGWDCHGLP IELQVEKNLG SKKHETTKLQ 

       130        140        150        160        170        180 
MRKQCREYAE KFVKIQRDEF ERLGVIGDWD RPYLTMTHDY EGITARELAR FAANGGLYKG 

       190        200        210        220        230        240 
KKPVHWCSSC VTALAEAEVE YADKTSPSIY VKFLLQDDIS ASVPALAGKK VSLVIWTTTP 

       250        260        270        280        290        300 
WTIPANLAVA LHPELEYVAL EAGGEVLVVA EGLKDAFMAA TGVQGSVIAT FRADILYRKR 

       310        320        330        340        350        360 
CKHPFYDRDS IVLLGEHVTL DAGTGCVHTA PGHGQEDYEL ALVEGLDIYN PVDNRGRYIQ 

       370        380        390        400        410        420 
SLEFFGGQFV FDANATVIEK LQEVGALVGQ GSVEHSYPHC WRCKKPIIFR ATEQWFISME 

       430        440        450        460        470        480 
KNDLRKKALE EIDRVSWVPK WGRERIHGMI ENRPDWCISR QRSWGVPITA FYCTECGEIL 

       490        500        510        520        530        540 
ADGTIMHHVA DLFMEGGADL WYEKEAAELL PPGTVCPQCG KSAFEKEMDI LDVWFDSGVS 

       550        560        570        580        590        600 
HAAVLENRPE LGSPANMYLE GSDQHRGWFH SSLLASVGTR GTAPYKEVLT HGFVVDGSGR 

       610        620        630        640        650        660 
KMSKSVGNVV APEEVIKKYG AEILRLWVAA QDYRDDVRIS QEILTRLAEA YRRIRNTCRY 

       670        680        690        700        710        720 
LLGNLYDFDP ATDMVPFGEM TELDRWALHQ LEVLKEKVFT AYNEYEFHIL YHAVNGFCTV 

       730        740        750        760        770        780 
EMSAFYLDII KERYTSRKDS PERRSAQTVM YLVLESLVRL MAPVLSFTAD EVWGYMPKRA 

       790        800        810        820        830        840 
EASVHLASFP ELCPERKDEA LVERWARTMA VRGDVSKALE QARVQKTIGH SLDAAVTLSA 

       850        860        870        880        890        900 
EPELLGFLKE YAGELATVFI VSKVELVGEI AGEFVEAEGV KGLKIGVTAA PGDKCERCWH 

       910        920 
YDEEIGGDAE HPTLCPKCVA AVK 

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000148 Genomic DNA. Translation: ABB30594.1.
RefSeqYP_006719314.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39YT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269799.Gmet_0351.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB30594; ABB30594; Gmet_0351.
GeneID3739717.
KEGGgme:Gmet_0351.
PATRIC21999848. VBIGeoMet55070_0371.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycGMET269799:GHNY-351-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ39YT0_GEOMG
AccessionPrimary (citable) accession number: Q39YT0
Entry history
Integrated into UniProtKB/TrEMBL: November 22, 2005
Last sequence update: November 22, 2005
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)