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Q31CU4 (SYI_PROM9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:PMT9312_0240
OrganismProchlorococcus marinus (strain MIT 9312) [Complete proteome] [HAMAP]
Taxonomic identifier74546 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length968 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 – 968968Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022100

Regions

Motif68 – 7811"HIGH" region HAMAP-Rule MF_02002
Motif623 – 6275"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9361Zinc By similarity
Metal binding9391Zinc By similarity
Metal binding9561Zinc By similarity
Metal binding9591Zinc By similarity
Binding site5821Aminoacyl-adenylate By similarity
Binding site6261ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31CU4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 7C924A4490B4BEDA

FASTA968111,880
        10         20         30         40         50         60 
MKSQNNKEYK SEFSYKETLN LLKTDFSMRA NSVLREPEIQ NFWAKNNIDF ELGSNNSGKI 

        70         80         90        100        110        120 
FTLHDGPPYA NGALHMGHAL NKVLKDIINK YKTLRGFRVH YVPGWDCHGL PIELKVLQNL 

       130        140        150        160        170        180 
KSSERKNLDT LNLRKKATDY AYVQINNQME GFKRWGIWGN WDNPYLTLKK SYESAQIGVF 

       190        200        210        220        230        240 
GKMFLNGYIY RGLKPVHWSP SSRTALAEAE LEYPDEHYSK SIYVSLKITK LSDEILLKFY 

       250        260        270        280        290        300 
QENPNFKKDF FLSNSFITIW TTTPWTIPAN EAVAVNPKIN YVFAIDEEKR IYLLAKELSS 

       310        320        330        340        350        360 
EISNKFNKDL TTLLEVKGVT LEDIEYQHPT KNKNCRIVIG GDYITIESGT GIVHTAPGHG 

       370        380        390        400        410        420 
IDDFNVGRKY DLPTTCVVDE KGNLNEYSGQ FQGSNVLKDA NDLIIDYLEE KDLLLLQENY 

       430        440        450        460        470        480 
KHRYPYDWRT KKPTIFRATE QWFASVNGFR SSALKAIEDV EWIPATGKKR IYSMVVGRGD 

       490        500        510        520        530        540 
WCISRQRSWG LPIPVFYKKN GNEILLNSEI INHIQKLFSE HGADIWWDWD VKHLLPDNYV 

       550        560        570        580        590        600 
KESDLWKKGT DTMDVWFDSG SSWAAVCEQR SELKYPADLY LEGSDQHRGW FQSSLLTSVA 

       610        620        630        640        650        660 
VNNKPPYKKV LTHGFALDEN GRKMSKSLGN VVDPNIIING GNNKKIEPAY GADVLRLWVS 

       670        680        690        700        710        720 
SVDYSVDVPI GSNILKQLSD VYRKVRNTAR YLLGNIHDYD PNIDSFEIDQ LPLLDQWMLG 

       730        740        750        760        770        780 
RLVEVTDQIS NAYENYEFSK FFQILQSFCV VDLSNFYLDI AKDRLYVSSK SQFRRRSCQF 

       790        800        810        820        830        840 
VMSKVVENLA VLISPVLCHM AEDIWQNVPY STKEKSVFQR GWPNFSQSWK NEILNEHIAN 

       850        860        870        880        890        900 
LRNLRVEINK AIEGCRNKQI IGAALETEVN YLPKDKVVKD SLTWLKKFGN EEVDLFRDWL 

       910        920        930        940        950        960 
IVSNFQVVSE LAKNSLIIDN NEIGKIQILK AHGQKCDRCW HYQEEIFSGI QNTKLCKRCS 


HIINLEFT 

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References

[1]"Complete sequence of Prochlorococcus marinus str. MIT 9312."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9312.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000111 Genomic DNA. Translation: ABB49301.1.
RefSeqYP_396737.1. NC_007577.1.

3D structure databases

ProteinModelPortalQ31CU4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74546.PMT9312_0240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB49301; ABB49301; PMT9312_0240.
GeneID3765026.
KEGGpmi:PMT9312_0240.
PATRIC23004102. VBIProMar70153_0245.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycPMAR74546:GHRG-246-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_PROM9
AccessionPrimary (citable) accession number: Q31CU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 63 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