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Q8YXY3 (SYI_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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:alr1073
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length960 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

Catalytic activity

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

Cofactor

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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002.

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.

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 – 960960Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098340

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif614 – 6185"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9291Zinc By similarity
Metal binding9321Zinc By similarity
Metal binding9491Zinc By similarity
Metal binding9521Zinc By similarity
Binding site5731Aminoacyl-adenylate By similarity
Binding site6171ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YXY3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B22328C27781C30A

FASTA960108,394
        10         20         30         40         50         60 
MTETGSYKDT VNLPKTNFDM RANAIKREPE IQKFWEENKI FESLSQNNPG ELFILHDGPP 

        70         80         90        100        110        120 
YANGSLHIGH ALNKILKDII NRYQLLQGRK VRYVPGWDCH GLPIELKVLQ NLKSAERQNL 

       130        140        150        160        170        180 
TPLQLRQKAK EFALATVDNQ RQNFKRYGVW GDWDNPYLTL KPEYEAAQIG VFGQMVLKGY 

       190        200        210        220        230        240 
IYRGLKPVHW SPSSKTALAE AELEYPEGHT SRSIYAAFPV TSFAEAAKPL LGEYLPDLGV 

       250        260        270        280        290        300 
AIWTTTPWTI PGNLAVAVNG DLNYSLVEVS RIGAETQSNF KYLIVAADLV ERLAATISAQ 

       310        320        330        340        350        360 
LTVKATFKGK ELEHTTYRHP LFDRESPVVV GGDYITTESG TGLVHTAPGH GQEDYVVGLR 

       370        380        390        400        410        420 
YGLPILAPVD DNGDFTQEAG QFAGLNVLGE GNQAVIDALT AAGSLLKEEA YAHKYPYDWR 

       430        440        450        460        470        480 
TKKPTIFRAT EQWFASVEGF RDEALKAIAA VKWIPAQGEN RITPMVAERS DWCISRQRSW 

       490        500        510        520        530        540 
GVPIPVFYDE ETGEPLLNEE TINYVQAIIA EKGSDAWWEL SVAELLPESY RNNGRSYRRG 

       550        560        570        580        590        600 
TDTMDVWFDS GSSWASVVKQ RPELRYPADM YLEGSDQHRG WFQSSLLTSV SVNGIAPYKT 

       610        620        630        640        650        660 
VLTHGFVLDE QGRKMSKSEG NVVDPAIIIN GGKDQKKEPP YGADVMRLWA SSVDYTGDVR 

       670        680        690        700        710        720 
LGGNIIKQLN DVRGKIRNTA RFLLGSLYDF DPEKNAVQFE EMPQLDKYML HRIREVFEEV 

       730        740        750        760        770        780 
TEAFESFQFF RFFQTVQNFC VVDLSNFYLD VAKDRLYISA PDAFRRRSCQ TVIHIALENL 

       790        800        810        820        830        840 
ARAIAPVLCH TAEDIWQYLP YKTPYKSVFE AGWVQVEEKW HNPELAEFWQ QLRQLRTDVN 

       850        860        870        880        890        900 
KVLEQARVEK MIGSSLEAKA LIYVKDANSR KAIATLNPEV GNGVDELRYL FLTSQVELLD 

       910        920        930        940        950        960 
SADKLQDGKY TSQSDSWGIG VVNAEGQKCD RCWNYSTHVG ESAEHPLLCE RCVPALAGEF 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB73030.1.
PIRAF1940.
RefSeqNP_485116.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YXY3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING103690.alr1073.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB73030; BAB73030; BAB73030.
GeneID1104667.
KEGGana:alr1073.
PATRIC22772058. VBINosSp37423_1513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAEVMDEIT.
OrthoDBEOG644ZM1.

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 nameSYI_NOSS1
AccessionPrimary (citable) accession number: Q8YXY3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 77 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