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Q46HD5 (SYI_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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:PMN2A_1605
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length967 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 – 967967Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098441

Regions

Motif68 – 7811"HIGH" region HAMAP-Rule MF_02002
Motif624 – 6285"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9371Zinc By similarity
Metal binding9401Zinc By similarity
Metal binding9571Zinc By similarity
Metal binding9601Zinc By similarity
Binding site5831Aminoacyl-adenylate By similarity
Binding site6271ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46HD5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: EDB63C23F3F932C0

FASTA967110,010
        10         20         30         40         50         60 
MNNIKKDSQK DRPTYKDTLN LLQTNFGMRA NATLREPELQ AFWREKNIDF ELGLNNSGET 

        70         80         90        100        110        120 
FTLHDGPPYA NGTLHMGHAL NKVLKDIINK FQTMKGKKVC YVPGWDCHGL PIELKVLQAM 

       130        140        150        160        170        180 
DKSQRAELTP IKLRKKAAAY AKKQVSQQMD GFKRWGVWGD WDQPYLSLDK KFEASQIKLF 

       190        200        210        220        230        240 
GEMVFKGYIY RGLKPVHWSP SSQTALAEAE LEYPTGHTSK SIYVGFKVNQ IPKRLTQEIS 

       250        260        270        280        290        300 
KQAPDLINSE GKLKELKLVI WTTTPWTIPA NEAISVNQKL EYVIAQSSDR SLIIIANDLL 

       310        320        330        340        350        360 
QEVSKSVGIN YEKRVLIKGS ILDGIIYKHP LFDKISPVVL GGDYITTESG TGLVHTAPGH 

       370        380        390        400        410        420 
GVDDFNTAKK YNLSISCPVD EKGFLTKEAG KFEGLNVLKD ANSVIISDLI NAGSLLKEIP 

       430        440        450        460        470        480 
YEHRYPYDWR TKKPTIFRAT EQWFASVEGF RDKALSAIED VIWLPESGKN RINSMVRERG 

       490        500        510        520        530        540 
DWCISRQRTW GVPIPVFYEK NGQEILLNKE TISHIADLFS VHGADIWWEY EVSELLPPSY 

       550        560        570        580        590        600 
LNQADRWQKG TDTMDVWFDS GSSWSSVISK KENLNYPADL YLEGSDQHRG WFQSSLLTSV 

       610        620        630        640        650        660 
AVNEHAPFKK VLTHGFALDE NGRKMSKSLG NIIDPLVIIN GGSNKKLDPA YGADVLRLWV 

       670        680        690        700        710        720 
SSVDYSADVP IGSNILKQIS DVYRKVRNTS RYLLGNLYDF DYKIDSIDIA NLPLLDKWML 

       730        740        750        760        770        780 
NRTAEVIDEI SDAYNNFEFS KFFQTIQNFC VVDLSNFYLD IAKDRLYVSS KSDFRRRSCQ 

       790        800        810        820        830        840 
TVLSLVIEKI SGLIAPVLCH MAEDIWQNIP YDLEEASVFQ RGWPNVPKSW KNSSFNCHVT 

       850        860        870        880        890        900 
ELRKLRAVIN RMLESCRNNQ ALGSSLEASV RVDISDEKVK AAIEWLAESE SNNVDVLRDW 

       910        920        930        940        950        960 
FLVSSLQIGG EPWAEVLVSE DNDYASVEIA KARGFKCERC WHYEIEMSKN PQHTNICKRC 


EKVVLAI 

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References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NATL2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ59093.1.
RefSeqYP_292796.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46HD5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ59093; AAZ59093; PMN2A_1605.
GeneID3607004.
KEGGpmn:PMN2A_1605.
PATRIC23022693. VBIProMar14922_0304.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.
PhylomeDBQ46HD5.

Enzyme and pathway databases

BioCycPMAR59920:GI1O-303-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_PROMT
AccessionPrimary (citable) accession number: Q46HD5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: September 13, 2005
Last modified: July 9, 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