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Q3J8W1 (SYI_NITOC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Noc_2277
OrganismNitrosococcus oceani (strain ATCC 19707 / NCIMB 11848) [Complete proteome] [HAMAP]
Taxonomic identifier323261 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Nitrosococcus ›

Protein attributes

Sequence length940 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.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 940940Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022094

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9031Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9231Zinc By similarity
Metal binding9261Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3J8W1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 487268DA2324ED16

FASTA940106,115
        10         20         30         40         50         60 
MAKYKETLNL PKTAFPMKAN LAQREPQALK RWQAMDLYGK LRNAARGRPR FILHDGPPYA 

        70         80         90        100        110        120 
NGAIHIGHAV NKILKDIIVK SKSLSGFDAP YVPGWDCHGL PIELNVEKKV GKPGRKIDVA 

       130        140        150        160        170        180 
SFRRACRDYA RKQVNAQRED FERLGVLGDW CHPYLTMDYQ FEADVIRTLG KIIEKGHLHK 

       190        200        210        220        230        240 
GVKPVHWCVD CGSALAEAEV EYQEKTSPAI DVRFPVVEEV ELLARCKAEI PGAGPMSVVI 

       250        260        270        280        290        300 
WTTTPWTLPA NQAVALHPAL KYVLVECSAG QGRERLLLAE GLYREVLARY SAESAVILAT 

       310        320        330        340        350        360 
CQGDELEGLK LQHPFYERTV PIILGEHVNL EAGTGAVHTA PGHGQDDYVV GNRYQLSIDN 

       370        380        390        400        410        420 
PVGGNGCFLP ETPLFAGEPV FKANDHIIQV LKERGNLLRE QSLQHSYPHC WRHKTPIIFR 

       430        440        450        460        470        480 
ATPQWFINME REGLRTAALA EIKKTRWLPG WGQQRIEGMV ENRPDWCISR QRAWGTPIPL 

       490        500        510        520        530        540 
FVHCQTGELH PDTPRLMEEV ARRVEEKGIE AWFELEPKEL LGNQAPAYEK VGDTLDVWFD 

       550        560        570        580        590        600 
SGVTHTCVLE TREELGVPAD LYLEGSDQHR GWFQSSLLTS VAIRGTAPYR MVLTHGFTVD 

       610        620        630        640        650        660 
AKGKKMSKSQ GNVVAPQQVM GSLGADILRL WVAATDYRGE MNVSDEILKR IADSYRRMRN 

       670        680        690        700        710        720 
TARYLLANLN GFDPTIHGVP AKDMLALDRW ALDRASLLQG EIVQAYEDYN FHLIYQRVHN 

       730        740        750        760        770        780 
FCAVDMGAIY LDIIKDRQYT TQADSRARRS AQTAMYHIAE ALVRWLAPVL SFTADEIWQY 

       790        800        810        820        830        840 
LPGERGESVF LTTWYEDLPS LGEEAPWGRA FWDVILAARE AIAKVLEGVR VEGRIGSSLD 

       850        860        870        880        890        900 
AEVDLYVEES LYQALRKLGD ELRFVLITSY ARVYPAQKRP VEALETEMPG LWTVVIPSHY 

       910        920        930        940 
PKCVRCWHHR EEVGSHEDHP ELCSRCVENT EGGGEQRAFA

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References

[1]"Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."
Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., Vergez L.M., Ward B.B.
Appl. Environ. Microbiol. 72:6299-6315(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19707 / NCIMB 11848.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000127 Genomic DNA. Translation: ABA58735.1.
RefSeqYP_344265.1. NC_007484.1.

3D structure databases

HSSPHSSP built from PDB template 2AJG based on UniProtKB P07813.
ProteinModelPortalQ3J8W1.
ModBaseSearch...

Protein-protein interaction databases

STRING323261.Noc_2277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA58735; ABA58735; Noc_2277.
GeneID3705069.
KEGGnoc:Noc_2277.
PATRIC22708946. VBINitOce57959_2682.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKQVLTHG.
ProtClustDBPRK05743.

Family and domain databases

Gene3D3.40.50.620. 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. tRNAsyn_1a_bind. 1 hit.
SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_NITOC
AccessionPrimary (citable) accession number: Q3J8W1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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