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Q9Z972 (SYI_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. 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:CPn_0109, CP_0665, CpB0110
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length1043 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 10431043Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098528

Regions

Motif48 – 5811"HIGH" region HAMAP-Rule MF_02003
Motif591 – 5955"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5941ATP By similarity

Experimental info

Sequence conflict3841H → Y in AAF38477. Ref.2
Sequence conflict7981R → H in AAP98043. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9Z972 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 08ABB8B9364E640C

FASTA1,043120,287
        10         20         30         40         50         60 
MTADEVGKNS FAKKEEQVLK FWKDNQIFEK SLQNRQGKTL YSFYDGPPFA TGLPHYGHLL 

        70         80         90        100        110        120 
ASTIKDVVGR YATMDGYYVP RRFGWDCHGV PVEYEVEKSL SLTAPGAIED FGIASFNEEC 

       130        140        150        160        170        180 
RKIVFRYVHE WEYYINRIGR WVDFSSTWKT MDASFMESVW WVFQSLYNQG LVYEGTKVVP 

       190        200        210        220        230        240 
FSTALGTPLS NFEASQNYKE VDDPSLVVRM PLQNDSASLL VWTTTPWTLP SNMAIAVGET 

       250        260        270        280        290        300 
LVYVRIQDKK SGEQWILSQG CVSRWFSNPE EFVILESFSG KDLVGRTYEP PFTFFQSKRE 

       310        320        330        340        350        360 
EGAFRVIAAS FVEESEGTGV VHMAPAFGEG DFLVCKENHV PLVCPVDAHG SFTEEIPQYQ 

       370        380        390        400        410        420 
GQYIKHADKE IIKFLKKEGR IFYHGTVKHR YPFCWRTDTP LIYKAVNSWF VAVEKIKDKM 

       430        440        450        460        470        480 
LRANSSIHWV PEHIQEGRFG KWLEGARDWA ISRNRYWGTP IPIWKSADGE ILVVGSIREL 

       490        500        510        520        530        540 
EELTGTQITD IHRHFIDDLN IVKDGKPFHR IPYVFDCWFD SGAMPYAQNH YPFENQKETE 

       550        560        570        580        590        600 
EAFPADFIAE GLDQTRGWFY TLTVISAILF DRPAFRNAIV NGIILAEDGN KMSKRLNNYP 

       610        620        630        640        650        660 
SPKYVLDTYG ADALRLYLLH SVVVKAEDLR FSDKGIEGVL KQILLPLTNV LSFFNTYAEL 

       670        680        690        700        710        720 
YGFDPKSQDI EPAYTEIDQW ILSNLYSVVG KVRESMSQYH LNFAVEPFVT FIDDLTNWYI 

       730        740        750        760        770        780 
RRCRRRFWEA EDTPDRRAAF STLYEVLTVF CKVIAPFVPF LAEDIYQKLK LEKEPESVHL 

       790        800        810        820        830        840 
CDFPQVEMDK ILPDLEKRMH DIREIVGLGH SLRKEHKLKV RQPLANFYVV GSKDRLSLLK 

       850        860        870        880        890        900 
TFEGLIAEEL NVKNVIFYEE APSFIYTTVK PNFRMLGKKV GSKMKEVQKA LSELPNNAID 

       910        920        930        940        950        960 
KLIQEETWVL TIDDREIALD GDDVVICRHT DPGYIARSSA LFSVILDCQL REPLIVEGIA 

       970        980        990       1000       1010       1020 
RELVNKINTM RRNQQLHVSD RIALRIKTTE AVHRAFLDYE NYICEETLII AYDFTQDSDF 

      1030       1040 
QGENWDINGH ATQIEITVSS IDS 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD18262.1.
AE002161 Genomic DNA. Translation: AAF38477.1.
BA000008 Genomic DNA. Translation: BAA98320.1.
AE009440 Genomic DNA. Translation: AAP98043.1.
PIRC81552.
E72118.
F86504.
RefSeqNP_224317.1. NC_000922.1.
NP_300169.1. NC_002491.1.
NP_445207.1. NC_002179.2.
NP_876386.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z972.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn0109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD18262; AAD18262; CPn_0109.
AAF38477; AAF38477; CP_0665.
AAP98043; AAP98043; CpB0110.
BAA98320; BAA98320; BAA98320.
GeneID1466793.
894633.
918769.
963852.
KEGGcpa:CP0665.
cpj:CPj0109.
cpn:CPn0109.
cpt:CpB0110.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAENRDWFE.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-687-MONOMER.
CPNE115713:GHEY-113-MONOMER.
CPNE138677:GH8N-112-MONOMER.
CPNE182082:GH4N-113-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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_CHLPN
AccessionPrimary (citable) accession number: Q9Z972
Secondary accession number(s): Q9JQK2, Q9K221
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 101 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