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Reviewed, UniProtKB/Swiss-Prot Q62HL4 (SYI1_BURMA)

Last modified November 3, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Isoleucyl-tRNA synthetase 1
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase 1
      Short name=IleRS 1
Gene names
Name: ileS1
Synonyms: ileS-1
Ordered Locus Names: BMA2242
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

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Protein attributes

Sequence length945 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

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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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 945945Isoleucyl-tRNA synthetase 1 HAMAP MF_02002
PRO_0000098368

Regions

Motif66 – 7611"HIGH" region HAMAP MF_02002
Motif622 – 6265"KMSKS" region HAMAP MF_02002

Sites

Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Metal binding9281Zinc By similarity
Metal binding9311Zinc By similarity
Binding site5811Aminoacyl-adenylate By similarity
Binding site6251ATP By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q62HL4-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 5E7C07BF9C19C03C

FASTA945105,680
        10         20         30         40         50         60 
MSNKKADSKP QAKYPVNLLD TPFPMRGDLP KREPQWVEDW EARGVYEKIR AASQGRPKFI 

        70         80         90        100        110        120 
LHDGPPYANG DIHLGHAVNK ILKDMVVKSR NMAGFDAPYV PGWDCHGMPI EIQIEKRFGK 

       130        140        150        160        170        180 
SLPAAEVMAK ARAYATEQIE KQKVGFKRLG VLGEWGNPYK TMNFQNEAEE IRALGKIIEK 

       190        200        210        220        230        240 
GYVYRGLKPV NWCFDCGSAL AEAEVEYKDR TDPTIDVLFA FAEPEKTAHA FGLAELPRAE 

       250        260        270        280        290        300 
GGIVIWTTTP WTIPANQALN LHPEIVYALV DTERGLLVMA EERVEACMKD FGLTGRVIAR 

       310        320        330        340        350        360 
TPGEKLANLR FHHPLAAAHP GYKRTSPVYL GDYVTTDTGT GVVHSSPAYG VEDFTSCKAH 

       370        380        390        400        410        420 
GMTDSDIINP VMGDGRYIES LPLFGGLTIW DANPKIVDAL KAAGSLLRNE RYAHSYMHCW 

       430        440        450        460        470        480 
RHKTPIIYRA TSQWFAGMDT QPAGGGKTLR ETALDAVDAT AFYPSWGKQR LHAMIANRPD 

       490        500        510        520        530        540 
WTLSRQRQWG VPMAFFVHKE TGELHPRTLE LLEEVAKRVE RQGIEAWQTL DARELIGDDA 

       550        560        570        580        590        600 
NLYEKNRDTL DVWFDSGTTH WHVLRGSHKD QLQFPADLYL EGSDQHRGWF HSSLLTASML 

       610        620        630        640        650        660 
DGRAPYKGLL THGFTVDGEG RKMSKSLGNG IDPHEVANRL GAEIIRLWIA STDYSGELAI 

       670        680        690        700        710        720 
SEEILKRVTE GYRRIRNTLR FLLANLSDFD YAKDALPAGQ WLEIDRYAVA FAAQLQAELL 

       730        740        750        760        770        780 
AHYEKYEFHP VVAKLQTFCS EDLGGFYLDV LKDRLYTSAP ASPARRSAQT ALYHVTQGLL 

       790        800        810        820        830        840 
RVLAPFLSFT AEEAWRVFQP QSDTIFTETY YAYPEIAGAE ALIAKWTLLR DVRGDVTKAL 

       850        860        870        880        890        900 
EEARTANRIG SSLQAQVEVR ASGARYDALA SLGDDLKFVL ITSAATVVKV DAQGDESVDV 

       910        920        930        940 
AASTYPKCER CWHYREDVGA HADHPTLCGR CFSNLFENGE TRSAA

« Hide

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Cross-references

Sequence databases

CP000010 Genomic DNA. Translation: AAU50245.1.
RefSeqYP_103806.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3090843.
GenomeReviewsGene locus BMA2242 in contig CP000010_GR.
KEGGbma:BMA2242.
TIGRBMA2242.

Phylogenomic databases

HOGENOMQ62HL4.
OMAFPMRGNL.

Enzyme and pathway databases

BioCycBMAL243160:BMA_2242-MON.
BRENDA6.1.1.5. 260531.

Family and domain databases

HAMAPMF_02002.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR010663. DNA_glyclase/IsotRNA_synth_Znf.
IPR002301. Ile-tRNA-synt_Ia.
IPR015905. Ile-tRNA-synt_Ia_N.
IPR018353. Isoleucyl-tRNA_synthetase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYI1_BURMA
AccessionPrimary (citable) accession number: Q62HL4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 25, 2004
Last modified: November 3, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents