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A3CSI6 (SYI_METMJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:Memar_0403
OrganismMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [Complete proteome] [HAMAP]
Taxonomic identifier368407 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus

Protein attributes

Sequence length1059 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 – 10591059Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022156

Regions

Motif47 – 5711"HIGH" region HAMAP-Rule MF_02003
Motif591 – 5955"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5941ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CSI6 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 9C554469148FCFD1

FASTA1,059120,495
        10         20         30         40         50         60 
MKEVTGSYNP RELEAGVQDT WKRENTYARV QEVRKDGKAF FFVDGPPYTT GHIHLGTAWN 

        70         80         90        100        110        120 
KIIKDTILRY HRMGGRNIIE RAGYDMHGLP IEVKVEHQLG FTSKKDIEDY GIAAFIEQCR 

       130        140        150        160        170        180 
TFAVTHMEIM SEQFRQLGIW LDFDDPYQTI KAEYIESAWW AVQRAEERGL LERGHRVVNW 

       190        200        210        220        230        240 
CPRCETAIAD SEVEYWDETD PSIFVKFPVT GRENEYLVIW TTTPWTLPAN VAVAVSPAFT 

       250        260        270        280        290        300 
YARVAAKKDG SEEILWIADE LVESVLKMGR YQDYTVLERV NGSDLVGTEY ESPLAGQVPH 

       310        320        330        340        350        360 
QAEIRHRVVA ADYVALENTG LVHIAPGHGW DDYLIGIQEG LEAFCPVDAG GCFTREAGAF 

       370        380        390        400        410        420 
ADMYVRDAND LVIDALGDYL LARRTITHRY GHCWRCKTSI IYRATAQWFL KATEIREPML 

       430        440        450        460        470        480 
QEIAKVKWYP EWAGSARFHD FVRDSRDWCI SRQRYWGIPI PIWQCEQCGE RTVIGTIAEL 

       490        500        510        520        530        540 
EERSGARVPD PHRPYVDEVV IPCSCGGEMH RVADIFDVWF DSAVASWATL GFPREREAFD 

       550        560        570        580        590        600 
RLWPADFITE GQDQTRGWFY SQLGASTVAF GRAPYKSVLM HGFALDADGR KMSKSFGNVV 

       610        620        630        640        650        660 
TPEEVMNQFG VDVLRFYVLW ANAPWDDLKF NWDSVKTIHR TLNILWNVYR FPLPYMVLDS 

       670        680        690        700        710        720 
FEPAAGDGGL WDGSFVRGNI NDMPEEDRWI ISRVNSLART TAGDMQEYHL HRVTRALAAF 

       730        740        750        760        770        780 
ILEDLSRWYV QLVRPRMWLE EDSPEKRYAY ETVYYVMRRL VALLAPFTPH IAEEIYGNLR 

       790        800        810        820        830        840 
LAGDPESVHM LDWPEADDLL IAPDLESAME VVRSFDDAVA TARQNGRRKL RWPVAETVVV 

       850        860        870        880        890        900 
TGSDGVKTAL EDLNDLALNR ANSRTVRVVT GRWDRILWQA EPVMRAIGPE FGKEGPKVKA 

       910        920        930        940        950        960 
LIEGADGTAL KAAIERDGKA ELGGYEIAER HVTFAEALPE GVFAAPMKDA TVYVDVTLTP 

       970        980        990       1000       1010       1020 
ALEAEGYARE VIRRIQEMRR QLDLNVDDFI VAAVDVADDR VASLIAEEEW QKEIAGEVRA 

      1030       1040       1050 
AALTVRRTDG ERPTETFALE KDWDVEGVQM QIGISRAGE 

« Hide

References

[1]"Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1."
Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., Land M. expand/collapse author list , Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:189-196(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35101 / DSM 1498 / JR1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000562 Genomic DNA. Translation: ABN56336.1.
RefSeqYP_001046318.1. NC_009051.1.

3D structure databases

ProteinModelPortalA3CSI6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368407.Memar_0403.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN56336; ABN56336; Memar_0403.
GeneID4847697.
KEGGmem:Memar_0403.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAGARDWCI.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycMMAR368407:GH7L-409-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.
IPR023585. Ile-tRNA-ligase_type1.
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]
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_METMJ
AccessionPrimary (citable) accession number: A3CSI6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 50 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