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Q5PAL9 (SYI_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:AM684
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length1101 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 – 11011101Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098514

Regions

Motif50 – 6011"HIGH" region HAMAP-Rule MF_02003
Motif629 – 6335"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6321ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PAL9 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 981A2927BF1933CD

FASTA1,101125,904
        10         20         30         40         50         60 
MNYYPEVKGN PEFSAIEKEI LQYWNSEKIF EESVNTRSRD RSFVFYDGPP FANGLPHYGH 

        70         80         90        100        110        120 
LLTGFIKDAV ARYKTMRGFR VERKFGWDCH GLPAEMLAEK ELGVSGKVSI ESFGIDKFND 

       130        140        150        160        170        180 
YCRSSIMRFT QQWREYVERQ GRWVDFENGY RTMDKSFMES VMWAFHELWH KGLVYESVKV 

       190        200        210        220        230        240 
VPYSWACQTP LSNFETKMDN AYREKVSKSV TVRFKLSEQV GFVPQGVESC SILAWTTTPW 

       250        260        270        280        290        300 
TLVSNFALAI NTNMDYVGAV VGAEMLIFSA GYLDHFMRYC ERHSLECAKV VQIPAKELLA 

       310        320        330        340        350        360 
VKYMPPFPYF ADSKNAFMVL DAEFVAEGAG TGIVHLAPGF GEDDFLLCKQ HGIPNLGEES 

       370        380        390        400        410        420 
RGMLSVICPI DDAGRFTAAV GDFAGQHVFD VVDAVIRQLK EKGLWFATEQ CTHSYPHCWR 

       430        440        450        460        470        480 
TDTPLIYRAT SSWYVEVTKL KARMVELNKE VNWVPEHVQS GQFGKWLDGA KDWSVSRHRF 

       490        500        510        520        530        540 
WGAPVPVWRS DDPKYPRTDV YGSIKKVLPD VKALEEDFGP VEDLHRPYID NLVRPNPDDP 

       550        560        570        580        590        600 
TGKSMMRRVP DVLDCWFESG SMPYAQMHYP FENKEFFDSH FPADFITEYI AQTRGWFYTL 

       610        620        630        640        650        660 
FVLSTGLFDR HPFKNCICHG VVLDIKGQKL SKRLNNYPDP MEMFEKYGAD SVRFTMLSHA 

       670        680        690        700        710        720 
VSIGGDLLLD QDGDVVRDTL KSVVKPIWNS YSFFTVYANS DQMQGRILES LEGITNIMDQ 

       730        740        750        760        770        780 
YILYECACMV VKVLEAMESS SAGVRDPYNI RLACAAIVQF SDKLNNWYIR GCRGRFWMRD 

       790        800        810        820        830        840 
KTADKSDAYN TLYTVLYHLA RTIAPFLPFI AESIWLGLSF QREKSVHLAD FPDASSFSAV 

       850        860        870        880        890        900 
HQYKKNAEYM QLAMDVCSHV LSLRNAHNIR VRQPLRRMVV YPYNCESLLD MPQQYRDIIL 

       910        920        930        940        950        960 
NEVNVKSLQI ASTIGDMASF ELKLNFALLG QRVPEKVKQI ITLARAGVWE VQSDGSLLLG 

       970        980        990       1000       1010       1020 
APGCEQCVIQ KDEFSLNLKV HSEYACQIIS GGVPVGVLHI DHELTRELLL EGIARDVMRL 

      1030       1040       1050       1060       1070       1080 
IQQARKDCGL EMLDHAEVII NTDAAEIIEA ISIWYDFIKQ QTFSHTLEHR PAQAVVEDCS 

      1090       1100 
KYTKISGKDF DIFLCKSALC S 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86661.1.
RefSeqYP_153916.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5PAL9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234826.AM684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV86661; AAV86661; AM684.
GeneID3171286.
KEGGama:AM684.
PATRIC20947361. VBIAnaMar46146_0597.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAENRDWFE.
OrthoDBEOG644ZM1.

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.
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]
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_ANAMM
AccessionPrimary (citable) accession number: Q5PAL9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 67 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