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Q7MUD3 (SYI_PORGI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:PG_1596
OrganismPorphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]
Taxonomic identifier242619 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length1137 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 – 11371137Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098554

Regions

Motif50 – 6011"HIGH" region HAMAP-Rule MF_02003
Motif688 – 6925"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6911ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7MUD3 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 2952F7799895B543

FASTA1,137129,945
        10         20         30         40         50         60 
MSRRFAEYES LDLSRVNEEV LADWMQHRLF EESLKSREGA PSFVFYEGPP SANGMPGIHH 

        70         80         90        100        110        120 
VMARAIKDTI CRYKTMKGFR VDRKAGWDTH GLPVELGVEK SLGITKEDIG KSISVEEYNA 

       130        140        150        160        170        180 
ACRRDVMKFT KEWEDLTHKM GYWVDMEHPY ITYDNRYIET LWWLLAELYK KGLLYKGYTI 

       190        200        210        220        230        240 
QPYSPAAGTG LSTHELNQPG CYRDVKDTTC VAQFKIMDPK PEMQLHGDAF FLAWTTTPWT 

       250        260        270        280        290        300 
LPSNTALCVG PEIEYLAVQT FNPYNGIPIT VVLGKPLLHT LFNPKGECEE IPASYDPAQK 

       310        320        330        340        350        360 
LLPYKVIASW KGKELEGMRY EQLIPWVNPG EGAFRVITGD FVTTEDGTGI VHIAPTFGAD 

       370        380        390        400        410        420 
DDRVAKKSGV PPLMLRDKEG NMRPMVDLAG RYFPTTDLDP VFVEKHMDLP LYDVYAGRYV 

       430        440        450        460        470        480 
KNAYDAGKTE KDETLDVELC VMLKMQNRVF RIEKMTHNYP HCWRTDKPVL YYPLDSWFIR 

       490        500        510        520        530        540 
TTACKEEMIA NNGKIYWKPE STGTGRFGKW LENLQDWNLS RSRYWGTPLP IWRTEDGSEE 

       550        560        570        580        590        600 
ICIGSVEELY NEIEKAVKAG MMERNPWAGF KPGVYTEENY AKIDLHRPFV DGITLCSPSG 

       610        620        630        640        650        660 
QPMRRELDLI DVWFDSGAMP YAQMHYPFEN RERVEDGSVF PADFIAEGVD QTRGWFFTLH 

       670        680        690        700        710        720 
AIATMISGTS SFKVVVSNGL VLDKKGNKMS KRLGNAVDPF ETIKKYGSDP LRWYMITNSS 

       730        740        750        760        770        780 
PWDNLKFDTD GVEEVRRKFF GTLYNTYQFF ALYANLDGFT GEEESIPFAK RPEIDRWILS 

       790        800        810        820        830        840 
ELNTLIREVD DQLSDYEPTR AGRAISDFVS ENLSNWYVRL SRRRFWAGDM TEDKLSAYQT 

       850        860        870        880        890        900 
LYTSLLTVSK LMAPISPFYA DRLYRDLTGK DESVHLALFP RPDQSQVDRA LEQSMQMAQQ 

       910        920        930        940        950        960 
ISSMVLALRR RVNLKVRQPL ATLMIPAIDD EQRRCIESVQ PLILSEVNVK ELRFVDDSMG 

       970        980        990       1000       1010       1020 
ILVKRIKPDF KRLGPRYGKV MKALAEAVTA MTQEEIRSLE KAGTFRMEVA GTPVELELAD 

      1030       1040       1050       1060       1070       1080 
VEIVSEDIPG WLVANEGNLT VALDITVTDE LRSEGLAREL VNRVQNIRKQ SGFEVSDKVD 

      1090       1100       1110       1120       1130 
VLLLSNDIMD KVVAEHHDYI AQQIQAESLE ISDAVSDGVE LDFDDFVLSI QVVKHQG 

« Hide

References

[1]"Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83."
Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., Fraser C.M.
J. Bacteriol. 185:5591-5601(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-308 / W83.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015924 Genomic DNA. Translation: AAQ66625.1.
RefSeqNP_905726.1. NC_002950.2.

3D structure databases

ProteinModelPortalQ7MUD3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242619.PG1596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ66625; AAQ66625; PG_1596.
GeneID2552895.
KEGGpgi:PG1596.
PATRIC22980196. VBIPorGin134034_1479.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKWIISEI.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycPGIN242619:GHX8-1439-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.
InterProIPR002300. 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. 2 hits.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_PORGI
AccessionPrimary (citable) accession number: Q7MUD3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 15, 2003
Last modified: May 14, 2014
This is version 76 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