Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5UZ84 (SYI_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:rrnAC2634
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length1074 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
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 – 10741074Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098576

Regions

Motif50 – 6011"HIGH" region HAMAP-Rule MF_02003
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5UZ84 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: D476C7E610567942

FASTA1,074122,156
        10         20         30         40         50         60 
MERFAAVDDQ YDPDAVEDGV FEYWDDVDAY EQTKAHRADG EDYFFVDGPP YTSGAAHMGT 

        70         80         90        100        110        120 
TWNKTLKDCY IRYLRMQGYN VTDRPGYDMH GLPIETKVEE RLDFENKKDI EQFGEENFIE 

       130        140        150        160        170        180 
ECKDFAEEQL EGLQTDFQDF GVWMDWDDPY KTVNPEYMEA AWWGFQQAHE RDLVEQGQRS 

       190        200        210        220        230        240 
INQCPRCETG IANNEVEYHD VGKPSIYVKF PLAEQDGSLV IWTTTPWTIV ANTFVAADGD 

       250        260        270        280        290        300 
LEYVGVDAEK DGDTERLYLA EACVEDVLKA GRYDDYEVVE ELSGEEMVGW AYEHPLAEEV 

       310        320        330        340        350        360 
PDHAQGEGSG QVYTADYVEA DRTGLVHSAP GHGEEDFERG QELDLEIFCP VGSDGVYTDD 

       370        380        390        400        410        420 
AGKYAGTFVR DANDEVIDDL DENGVLLSSE PGHTVREGQC WRCDTDIVRI VTDQWFITVT 

       430        440        450        460        470        480 
DIKDELLANI EDSEWYPQWA RDNRFRDFVE DAPDWNVSRQ RYWGIPIPIW LPEDWSGDMD 

       490        500        510        520        530        540 
DAIVVGDREE LAERVDQDID PENVDLHKGT VDDLTITEDS TTYTRVGDVF DVWLDSSVAT 

       550        560        570        580        590        600 
WGTVNYPEQT EDFEELWPAD LIMEAHDQTR GWFWSQLGMS TAATGEIPYK QVLMHGYANM 

       610        620        630        640        650        660 
PDGRGMSKSK GVLIDPHEVI EKHGRDPMRL FLLSVTAQGE DMNFSWEETA EMQRRLNILW 

       670        680        690        700        710        720 
NVARFPLPYM RADDFDPEET TVEDLRDDLE LVDEWVLSRL QSVTEAMTDS MDDFENDKAV 

       730        740        750        760        770        780 
DELLEFVVED VSRFYIQVVR ERMWEEEDSA SKQAAYATLY RVLESVAALF APFTPFVAEQ 

       790        800        810        820        830        840 
VYGALTGDAG HPTVHMCDWP EVDADLHDPA LEREIEVVRE VEEAGSNARQ QAERKLRWPV 

       850        860        870        880        890        900 
TRVVVDVDSD DVADAVRAQE AIIADRLNAR AVEVVGADDE WGELQYSAEA DMSELGPAFG 

       910        920        930        940        950        960 
DDAGRVMNAL NEARVTEQSL DTLEGTVREA LGEDVDLTEE MVEFRRETPE GVTGTEFTAL 

       970        980        990       1000       1010       1020 
DGGGVVYVDT ALTEDIESEG YAREVIRRIQ EMRKDLELDI EERIAVDLTI DDERVDSLVR 

      1030       1040       1050       1060       1070 
EHEALIKEEV RADELDGVED GHRKTWEVEG TDMEIAIAPC EADQREASEQ ASGD 

« Hide

References

[1]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY596297 Genomic DNA. Translation: AAV47419.1.
RefSeqYP_137125.1. NC_006396.1.

3D structure databases

ProteinModelPortalQ5UZ84.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC2634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV47419; AAV47419; rrnAC2634.
GeneID3129589.
KEGGhma:rrnAC2634.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARYVEGKW.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-2375-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.
InterProIPR002300. 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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_HALMA
AccessionPrimary (citable) accession number: Q5UZ84
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 7, 2004
Last modified: May 14, 2014
This is version 70 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