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Q4FUS5 (SYI_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:Psyc_0364
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length941 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 – 941941Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098451

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif600 – 6045"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9041Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9241Zinc By similarity
Metal binding9271Zinc By similarity
Binding site5591Aminoacyl-adenylate By similarity
Binding site6031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4FUS5 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 25BC970ED2D84732

FASTA941105,220
        10         20         30         40         50         60 
MPSQDYKDTL NLADTPFAMR ANLAKREPDW LAAWEADDVY GKIRQARAGA TKYILHDGPP 

        70         80         90        100        110        120 
YANGQIHLGH AVNKVLKDII VKSKTLSGFD APYVPGWDCH GLPIEQKVEA KHGKVGQKVS 

       130        140        150        160        170        180 
ATEFRGLCRE YARTQIELQK ADFKRLGVFG DWDNPYLTMN FHQEANIVRA LAKIYDNGHV 

       190        200        210        220        230        240 
TRGMKPVNWC LDCSSALAEA EVEYQDKVSD AIYVSFDIVD SGKVAALAEI DGNIAAVIWT 

       250        260        270        280        290        300 
TTPWTLPANQ AIALHSEHNY SVVATENGNL LLATDLVESA LSEFKLENKG VLATVLGREL 

       310        320        330        340        350        360 
EGLHAQHPLI EARQVPLILG DHVTTDSGTG LVHTAPGHGL DDYIVGLKYN LPVENPVSGT 

       370        380        390        400        410        420 
GVYLESAAVF AGEHIYKANP QIIAALHENG HLIRHTKIEH SYPHCWRHKS PIIFRATPQW 

       430        440        450        460        470        480 
FISMETKGLR ERALADIPTV QWTPAWGQNR IESMMTGRPD WCISRQRTWG VPITFFTHKE 

       490        500        510        520        530        540 
TGELHPNTLE LMETAAQRIH EGGVEAWFDA SCEDFLGAEA ADYDKATDTL DVWFDSGTTH 

       550        560        570        580        590        600 
FAVLDQRDEL TNPADMYLEG SDQHRGWFQT SLLTSEAMYE RPPFKQVLTH GFVVDENGRK 

       610        620        630        640        650        660 
MSKSLGNIIT PQEEINKTGA DMLRLWIASS DYRYEMSAGK TVFKGSIDMY RRIRNTLRFL 

       670        680        690        700        710        720 
LANTDDFDPA TNSVDINELV SLDKFIIERA QTVQAQIISA YDAMDFHQVT QHITAFCSQD 

       730        740        750        760        770        780 
LGSFYLDIIK DRQYTTQTDG QPRRSAQTAI YHIVQALIRW ITPILSFTAQ EAWEVLHGAD 

       790        800        810        820        830        840 
SYVFTEEWYT FPEFELSAIS NDDWQRIMLA KDMVNKHIET ARGEKIINAN LSADVNLYAD 

       850        860        870        880        890        900 
GAMHESLAKL GEELRFVLIT SNATLKPLST VPAHSASTDE QTDSNSTGVV DLVVEVHAAT 

       910        920        930        940 
GTKCVRCWHI RDDIGTDSTH PELCARCATN VSGDGEVRHY A 

« Hide

References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ18233.1.
RefSeqYP_263667.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FUS5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259536.Psyc_0364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ18233; AAZ18233; Psyc_0364.
GeneID3514055.
KEGGpar:Psyc_0364.
PATRIC23055027. VBIPsyArc98534_0450.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycPARC259536:GI3A-375-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.
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_PSYA2
AccessionPrimary (citable) accession number: Q4FUS5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 68 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