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Q4A5K5 (SYI_MYCS5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:MS53_0558
OrganismMycoplasma synoviae (strain 53) [Complete proteome] [HAMAP]
Taxonomic identifier262723 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length897 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 – 897897Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098426

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif594 – 5985"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8661Zinc By similarity
Metal binding8691Zinc By similarity
Metal binding8831Zinc By similarity
Metal binding8861Zinc By similarity
Binding site5531Aminoacyl-adenylate By similarity
Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4A5K5 [UniParc].

Last modified June 12, 2007. Version 2.
Checksum: A74A22BE93E9AF17

FASTA897104,509
        10         20         30         40         50         60 
MSLDFKKTLN MPSTKFDMKA NLVEKEPLFR KKWLEDDIYQ KVLKNNANNE RFVVHDGPPY 

        70         80         90        100        110        120 
ANGDIHVGHA LNKILKDIIV RYKSLQGYYS PFVPGWDTHG LPIEHKMLTE SKLDRDQITV 

       130        140        150        160        170        180 
ELLRKKSRNY ALKQIEHQKK QFQKLQLFSD FSKIYITLDK SYEAKQLKVF KKLALDGLVY 

       190        200        210        220        230        240 
KGLKPIYWSP SSQSALAEAE VEYETVTTNS IYVSFDVTKS TFNKVPVGSK LVVWTTTPWT 

       250        260        270        280        290        300 
LIANAAVAIS FDITYLTVKY QDSLYVVAKN LFYNDLLEKF QWENYEVVDE FLGKEMPRNS 

       310        320        330        340        350        360 
IWYKAPLLDF DAPVIATNYV LEDSGTGLVH SAPLFGEDDF SLTFDNDLKL IMHISDTGHI 

       370        380        390        400        410        420 
ENSQTKYDSL FYEEANKEII KDLAEKVVHV YTYSHSYPHD WRTKKPIIYR ATPQWFVSID 

       430        440        450        460        470        480 
KVRSKIVSEL QNKVKTFPEW SKNRMISMIE NRGDWTISRQ RTWGVPIIIF YDENEKPVIN 

       490        500        510        520        530        540 
EEIFDHVIDL VANHGTDIWF SSTVDELLPE KYRNRNWTKE NDIMDVWFDS GVSSIAVDID 

       550        560        570        580        590        600 
GGKTTLPFDV YLEGNDQFRG WFNSSVINAV AYAGVSPYIN LVSHGFALDG QGKKMSKSRN 

       610        620        630        640        650        660 
NVVDPLDVIK KYGADILRLW VANSEYSSDV HISESILVQN SEIYRKIRNT VKFLLGNLNN 

       670        680        690        700        710        720 
FKYDKDLKLT SIHHYINEEL KSVKKEVLEN YDKFRFINVI KVLNRYVIDL SSFYFSVTKD 

       730        740        750        760        770        780 
ILYIRKENDE ERQMVLKNFY EILDFLMLAL APIIPTTADE MYSYFNKENK KESLFLERLE 

       790        800        810        820        830        840 
KAGDVSFDEK VLEQFKEFFE LRDQVNILIE NQIQNKVIKR SNELELVLPE TASEFLKSLD 

       850        860        870        880        890 
LKTLLMVSKI SYGKTLQVVK FESEKCKRCW NHFASLNKEY EICDLCFSVL KDTLANA 

« Hide

References

[1]"Swine and poultry pathogens: the complete genome sequences of two strains of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae."
Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R., Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M., Brocchi M., Burity H.A., Camargo A.A., Camargo S.S. expand/collapse author list , Carepo M.S., Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P., Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S., Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B., Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A., Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B., Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L., Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R., Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N., Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C., Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P., Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.
J. Bacteriol. 187:5568-5577(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 53.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017245 Genomic DNA. Translation: AAZ43966.2.
RefSeqYP_278677.1. NC_007294.1.

3D structure databases

ProteinModelPortalQ4A5K5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262723.MS53_0558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ43966; AAZ43966; MS53_0558.
GeneID3564027.
KEGGmsy:MS53_0558.
PATRIC20025766. VBIMycSyn118523_0598.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycMSYN262723:GH37-572-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
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_MYCS5
AccessionPrimary (citable) accession number: Q4A5K5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 68 of the entry and version 2 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