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Q2FPJ4 (SYI_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:ileS
Ordered Locus Names:Mhun_0606
OrganismMethanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) [Reference proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length1062 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10621062Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022154

Regions

Motif47 – 5711"HIGH" region HAMAP-Rule MF_02003
Motif591 – 5955"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5941ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FPJ4 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 55CE0BEDE48AC9EB

FASTA1,062121,693
        10         20         30         40         50         60 
MQEVTSSFTP RVIEASVQKF WTQEDIYARV QEQNRDGKTW FFVDGPPYTT GHIHLGTAWN 

        70         80         90        100        110        120 
KILKDSILRY KRMHGLHVID RAGYDMHGLP IEVRVEHELG FENKKDIEAF GIGAFIERCK 

       130        140        150        160        170        180 
QFALSHKDIM SEQFKSLGVW MNFDDPYQTI MPEYIEAAWW TLKQADEKGL LDRGHRVVNW 

       190        200        210        220        230        240 
CPRCETAIAD SEVEYWDEQD PSIFVKFPIH GLMNEYLVIW TTTPWTLPAN VAVAVDKDFI 

       250        260        270        280        290        300 
YARVEAIKEG KKEILWIAKD LVEPVLKRGK YQDYSILSEK TGEELAGTTY DSPLADLIPR 

       310        320        330        340        350        360 
QKEIVHTVVT AGFVEMDNTG MVHIAPGHGW DDYLLGVEKG LDVFCPVDGA GYYTDEGGIY 

       370        380        390        400        410        420 
AGQFVRDANE KILSDLGSHL LGRQKITHRY GHCWRCKTPI IYRATEQWFI SVPKMKEKML 

       430        440        450        460        470        480 
SEIKATSWYP DWAGSARFYD FVSDARDWCI SRQRYWGIPI PVWQCSSCSA HRVFGTVAEL 

       490        500        510        520        530        540 
NAAAGSNLTD PHRPYVDEIT VPCSCGGTMK RVEDIFDVWF DSAMASWATL GFPRNDALFH 

       550        560        570        580        590        600 
EMWPADFITE GQDQTRGWFY SQLGASTIAF NRSPYKSVLM HGFALDADGR KMSKSLGNVV 

       610        620        630        640        650        660 
TPEEVVQKFG VDVLRLYILS SNAPWEDLKF NWDGVSTVNR TMNILWNVYR FPLPYMILDG 

       670        680        690        700        710        720 
FSPAQTSDGK YDDEYIVRSY REMPEIDRWI ISRINTIARS VSADMDEYQL HRVTRLLMNF 

       730        740        750        760        770        780 
ILEDLSRWYV QIVRPRMWLE EDSPDKKFAY ETITYCLRTL CRLLAPFTPH ITEAMYENLR 

       790        800        810        820        830        840 
LPEDPVSVHM LKWPAGDIRL IDENLERRMD VVRKFDEAVA NARQAGKRKL RWPVQNVIVV 

       850        860        870        880        890        900 
TSSESVIEAF RSMEDLAKDR ANTRNIEVIQ GSWERMRFNA EPVMKKIGPS FGKKGPVVKG 

       910        920        930        940        950        960 
LIEAADGSAL RKQLEESGSV TLSDGSEEFV LTAEHMTFSQ HLPEGIFGAE MTDASVYVDT 

       970        980        990       1000       1010       1020 
TLTEDLEAEG YSREIIRRLQ EMRKQLDLNV EDNIVIDAVI EDVHLRELLS ASWLDLIKQE 

      1030       1040       1050       1060 
VRGKTLKIHD SVGGRDGSVL FQLDRDWDIE GVNVTLGISL AG 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27890 / DSM 864 / NBRC 100397 / JF-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD40364.1.
RefSeqYP_502083.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FPJ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323259.Mhun_0606.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD40364; ABD40364; Mhun_0606.
GeneID3924432.
KEGGmhu:Mhun_0606.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMATEGIDQT.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycMHUN323259:GH0L-617-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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 nameSYI_METHJ
AccessionPrimary (citable) accession number: Q2FPJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 21, 2006
Last modified: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries