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Q7V352 (SYI_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:PMM0238
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length965 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 – 965965Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098442

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
Q7V352 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 06D4C8BF586957A7

FASTA965111,413
        10         20         30         40         50         60 
MKSKHNKEKK SGFSYKETLN LLKTDFSMRA NSVIREPEIH EFWSRNKIDL ELGSTNSGKN 

        70         80         90        100        110        120 
FTLHDGPPYA NGSLHMGHAL NKVLKDIINK YKTLQGFKVH FIPGWDCHGL PIELKVLQSL 

       130        140        150        160        170        180 
KSNERRNLDS LGLRKKATDY AKIQINNQLE GFKRWGIWGD WDNPYLTLKK NYESAQIGVF 

       190        200        210        220        230        240 
GKMFLNGYIY RGLKPVHWSP SSRTALAEAE LEYPEEHFSK SIYVSLNITK LSDAVLLKLE 

       250        260        270        280        290        300 
EKDLRNKLLS SLNKLFIAIW TTTPWTIPGN EAVAINPRIN YVFASDQNGN IYLFARDLIS 

       310        320        330        340        350        360 
EICEKLDREF NVLLDVKGSL LEGLEYKHPT KNKFCNIVIG GDYITTESGT GIVHTAPGHG 

       370        380        390        400        410        420 
MDDFNVGQKY QLPITCIVDE KGNLNKHAEK FCGLNVLKDA NDLIIEDLEK NNLLLLKENY 

       430        440        450        460        470        480 
KHRYPYDWRT KKPTIFRATE QWFASVEGFR SSALKAIEDV EWMPKTGKKR IYSMVVGRGD 

       490        500        510        520        530        540 
WCISRQRSWG VPIPVFYEKE GKGVLINTET INHIKSLFEE YGADVWWEWD EKKLLPEKYR 

       550        560        570        580        590        600 
NESDRWEKGL DTMDVWFDSG SSWAAVCEQR EELQYPADLY LEGSDQHRGW FQSSLLTSVA 

       610        620        630        640        650        660 
VNNKPPYKTV LTHGFALDEN GRKMSKSLGN VVDPNIIING GPNQKIQPAY GADVLRLWVS 

       670        680        690        700        710        720 
SVDYSVDVPI GSNILKQLSD VYRKVRNTAR YLLGNIHDYD PALEEIDIDQ LPLLDQWMLN 

       730        740        750        760        770        780 
RLVEVSDEVT IAYENYEFSK FFQILQSFCV VDLSNFYLDI AKDRLYVSAK TQFRRRSCQF 

       790        800        810        820        830        840 
VMSRIVENLA VIISPVLCHM AEDIWQNIPY STIEKSVFER RWPKFPESWL NPELNEHISN 

       850        860        870        880        890        900 
LRTLRVEINK AIEGCRTQQM IGAALETEVN YLPENEFFKN SLSWLDKFGN KEVDLYRDWL 

       910        920        930        940        950        960 
IVSDFNIVNN LSKDCLSIDN NELGKIQILK AKGLKCDRCW HYQNITVKGI ENTKLCERCA 


NIINL 

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References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE18697.1.
RefSeqNP_892357.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM0238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE18697; CAE18697; PMM0238.
GeneID1726535.
KEGGpmm:PMM0238.
PATRIC23031124. VBIProMar68066_0245.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-245-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_PROMP
AccessionPrimary (citable) accession number: Q7V352
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 72 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