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Q63BZ8 (SYI2_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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 2

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase 2
Short name=IleRS 2
Gene names
Name:ileS2
Ordered Locus Names:BCE33L1977
OrganismBacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]
Taxonomic identifier288681 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length1033 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 – 10331033Isoleucine--tRNA ligase 2 HAMAP-Rule MF_02003
PRO_0000098518

Regions

Motif47 – 5711"HIGH" region HAMAP-Rule MF_02003
Motif590 – 5945"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5931ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q63BZ8 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 2AE9F189D2EBC158

FASTA1,033118,486
        10         20         30         40         50         60 
MKKVDVKESA VGRETRIRKQ WNEQSIFEQS IQNREGAQSF VFYEGPPTAN GLPHVGHALG 

        70         80         90        100        110        120 
RTIKDVVARY KTMAGYKVLR KAGWDTHGLP VELGVEKQLG ISGKHEIEEY GIEPFIKKCK 

       130        140        150        160        170        180 
ESVFTYEKQW REFTESIGYW VDMDDPYVTL ENPYIESVWH ILGTIHEKGL LYKGHRVSPY 

       190        200        210        220        230        240 
CPSCQTSLSS HEVAQGYKTV KDLSATVKFK VKDSENEYFL GWTTTPWTLP ANVALAVHPN 

       250        260        270        280        290        300 
MEYVKAKQEG HVYIVAKERV QDVLKENYEV LSVHKGEELL NISYTAPFPM KEVTNGYRVI 

       310        320        330        340        350        360 
GADFVTADSG TGLVHIAPAY GEDDYRVVQS EGLSFLHVVD EKGEYTEAVP FLKGKFVKDC 

       370        380        390        400        410        420 
DVDIVRYLAK EGLLYHKEKY EHSYPHCWRC DSPLLYYAGE SWLIRTTAIK DTFLQNNDSV 

       430        440        450        460        470        480 
TWYPDHMKHG RFGKFLENMV DWNISRNRYW GTPLNVWECE SCDHQFAPKS IDDLRKHSTK 

       490        500        510        520        530        540 
ETQEDLELHK PYVDEVQVCC EKCGGTMTRT PEVIDVWFDS GSMPFAQYHY PFENKELFEE 

       550        560        570        580        590        600 
QFPADVIAEG IDQTRGWFYS LLAVSALYTG KVPYKRVLSL GHVLDEEGQK MSKSKGNALD 

       610        620        630        640        650        660 
PVDLVNQFGA DALRWALLVD SAPWNAKRFS ERTVLEAKSK FVDTLVNVYS FYVLYANLDE 

       670        680        690        700        710        720 
YNPNETYDVK RTKLDEWVLS RLHSTTKKVR IALDDYQFTN AAREIAALVD EVSNWYVRRS 

       730        740        750        760        770        780 
RNRFWESGMN AEKAAAYETL HDVLVTISKL IAPFTPFVAE DIHLNLTGSS VHLEDYPVVN 

       790        800        810        820        830        840 
ESLLQPKLEA EMNAVLQVVE LGRSNRNQHS LKVKQPLAEL VLLEHNENDM DWESYRDIVM 

       850        860        870        880        890        900 
DELNVKAFHV ELDETKYTSY QLKLNFKTAG PKFGKNVNAV NGWLKQLSQD EVQNFVSTER 

       910        920        930        940        950        960 
AVYEVASGEE IVVTTEDVLV EKVAKSGFSN TTNGQYTVML DTNVTEELLQ EGVAREFIRA 

       970        980        990       1000       1010       1020 
VQEYRKQLNL PVNLRVDVIL DTEEELQQTL TNHKELLEEN LLVKQFTFGH LTNEDDELSL 

      1030 
GETKVRIKLS ATK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000001 Genomic DNA. Translation: AAU18279.1.
RefSeqYP_083569.1. NC_006274.1.

3D structure databases

ProteinModelPortalQ63BZ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288681.BCZK1977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU18279; AAU18279; BCE33L1977.
GeneID3024309.
KEGGbcz:BCZK1977.
PATRIC18887486. VBIBacCer95304_2082.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBCER288681:GHG7-2050-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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI2_BACCZ
AccessionPrimary (citable) accession number: Q63BZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 77 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