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Q7TUN3 (SYI_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:PMT_1817
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [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_0000098440

Regions

Motif68 – 7811"HIGH" region HAMAP-Rule MF_02002
Motif625 – 6295"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9381Zinc By similarity
Metal binding9411Zinc By similarity
Metal binding9581Zinc By similarity
Metal binding9611Zinc By similarity
Binding site5841Aminoacyl-adenylate By similarity
Binding site6281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7TUN3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: B20E527F5FADDA19

FASTA968108,894
        10         20         30         40         50         60 
MTQGKQPDGV ARTSYKDTLN LLQTSFGMRA NASQREPELQ EFWKQQGIDL ELGLNNQGQN 

        70         80         90        100        110        120 
FTLHDGPPYA NGALHMGHAL NKVLKDIINK HQILRGRQVR FVPGWDCHGL PIELKVLQNL 

       130        140        150        160        170        180 
NQEQREALTP LKLRKKAAAF ARKQVDSQMA GFRRWGIWAD WEHPYLTLQK EYEAAQIQVF 

       190        200        210        220        230        240 
GKMFQKGYIY RGLKPVHWSP SSRTALAEAE LEYPDGHTSP SVYVAFPAAK LPEKLRTSLG 

       250        260        270        280        290        300 
NQGLELPNNG LELGQALQIA IWTTTPWTLP ANLAVSVNEK LDYSFAVDNQ GRLLLVAAEL 

       310        320        330        340        350        360 
LPSLRDTLAL ELTARATVKG ALLAGLIYKH PLLDRDSPIV IGGEYITTES GTGLVHTAPG 

       370        380        390        400        410        420 
HGVDDFNTGQ KHDLGMLCPV DESGTMTSEA GPFAGLNVLK DANPTIIAAL EERGALLKHE 

       430        440        450        460        470        480 
PYAHRYPYDW RTKKPTIFRA TEQWFASVEG FRNEALTAIN SVEWLPASGR NRMEAMVRER 

       490        500        510        520        530        540 
GDWCISRQRT WGVPIPVFYE REGNEVLLND ETLAHVKALI TEHGADVWWE RNEVELLPPA 

       550        560        570        580        590        600 
YAAEAERWRK GTDTMDVWFD SGSSWAAVAS QQEGLAYPTE LYLEGSDQHR GWFQSSLLTS 

       610        620        630        640        650        660 
VAINSQAPYR QVLTHGFALD EKGRKMSKSL GNVVDPAVII DGGKNQKQEP PYGADVLRLW 

       670        680        690        700        710        720 
VSSVDYSADV PIGASILRQI ADVYRKVRNT SRYLLGNLHD FDPERDAIPV PELPLLDRWM 

       730        740        750        760        770        780 
LQRTAEVMDE ISTAFDRYEF YRFFQLLQSY CVVDLSNFYL DIAKDRLYVS SPSERRRRSC 

       790        800        810        820        830        840 
QTAMALIIER LAGAISPVLC HMAEDIWQNL PYSVAEDSVF RRGWPTVPET WRDPSMMAPM 

       850        860        870        880        890        900 
HQLRELRSAV NRVLEDCRSQ GELGAALEAA VRLEAHSEAL QEALDWLRQQ GDPDVDGLRD 

       910        920        930        940        950        960 
WLLVSHLQVG GEPWAELLAS QDNALATIEV ARARGSKCER CWHYETDVGQ HTTHPTLCGR 


CVGVLEHQ 

« Hide

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: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE21992.1.
RefSeqNP_895644.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7TUN3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT1817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE21992; CAE21992; PMT_1817.
GeneID1728103.
KEGGpmt:PMT1817.
PATRIC23012413. VBIProMar135351_2334.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKPVHWCL.
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_PROMM
AccessionPrimary (citable) accession number: Q7TUN3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 73 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