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B8HMX3 (SYI_CYAP4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 38. 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:Cyan7425_3114
OrganismCyanothece sp. (strain PCC 7425 / ATCC 29141) [Complete proteome] [HAMAP]
Taxonomic identifier395961 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length955 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 – 955955Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189146

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif604 – 6085"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9261Zinc By similarity
Metal binding9291Zinc By similarity
Metal binding9461Zinc By similarity
Metal binding9491Zinc By similarity
Binding site5631Aminoacyl-adenylate By similarity
Binding site6071ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B8HMX3 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: D41AC42C142D7C1A

FASTA955108,361
        10         20         30         40         50         60 
MTEPGSYKET VNLPQTAFDM RANAVKREPE LQKFWAENQI YENLSQENPG DPFILHDGPP 

        70         80         90        100        110        120 
YANGDLHIGH ALNKILKDII NKYWMLQGRK VRYVPGWDCH GLPIELKVLQ GMKSEQRAAL 

       130        140        150        160        170        180 
TPLSLRQAAK EFALQTVERQ KQSFKRYGVW GEWDNPYLTL KPEYEAAQIG VFGQMVLKGY 

       190        200        210        220        230        240 
IYRGLKPVYW SPSSQTALAE AELEYPEGHT SRSIYVSFAL TSLSATAEAV LKDYLPNLKV 

       250        260        270        280        290        300 
AIWTTTPWTI PGNLAVALNP DLTYAVVEKD GSYLLVANEL VERLETTLGV SLPIKTTIAG 

       310        320        330        340        350        360 
QALEHSTYQH PLFDRQGPLV MGDYVTTDSG TGLVHTAPGH GQEDYVVGQH YGLPILSPVD 

       370        380        390        400        410        420 
GNGRFTEEAG QFAGLKVLDE GNEAVIQALQ QVGALLKEEA YSHKYPYDWR TKKPVILRAT 

       430        440        450        460        470        480 
EQWFASVEGF REAALQAIAQ VQWIPAQGEN RITAMVSERS DWCISRQRNW GVPIPVFYDE 

       490        500        510        520        530        540 
ETGEPLLNAE TIAHVQAIVA EKGSDAWWEL SIEELLPQAY RNNGRRYRKG TDTMDVWFDS 

       550        560        570        580        590        600 
GSSWAAVLEQ REQLRYPAEM YLEGSDQHRG WFQSSLLTSV ATHGIAPYKT VLTHGFVLDE 

       610        620        630        640        650        660 
QGRKMSKSLG NVVDPAIVIE GGKNQKEDPP YGADILRLWV SSVDYSSDVP LGKNILKQMA 

       670        680        690        700        710        720 
DIYRKIRNTA RFLLGNLHDF DPANNKVEYD RLPQLDRYML HRIVEVFTEV NEAFTSYQFF 

       730        740        750        760        770        780 
RFFQTVQNFC VVDLSNFYLD IAKDRLYISA PDDFRRRSCQ TVLWIALENL AKAIAPVVPH 

       790        800        810        820        830        840 
LAEDIWQFLP YPTPYKSVFE AGWVSLDATW TNPDPQLLET FEQVRLLRFK VNECLEKLRV 

       850        860        870        880        890        900 
NKVIGASLEA KVLLYIADPE KRQQWQNLNP PALAAISGVD ELRYFFLTSQ VELLNSPDQL 

       910        920        930        940        950 
SELKSEYRFE FGDSSGGVLP ADGQKCDRCW NYSTYVGKDD KHLLLCERCV AVMER 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7425 / ATCC 29141.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001344 Genomic DNA. Translation: ACL45442.1.
RefSeqYP_002483803.1. NC_011884.1.

3D structure databases

ProteinModelPortalB8HMX3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395961.Cyan7425_3114.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL45442; ACL45442; Cyan7425_3114.
GeneID7289048.
KEGGcyn:Cyan7425_3114.
PATRIC21567193. VBICyaSp30657_3102.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycCSP395961:GJDE-2942-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 nameSYI_CYAP4
AccessionPrimary (citable) accession number: B8HMX3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 38 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