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D2RLA2 (D2RLA2_ACIFV) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase HAMAP-Rule MF_02002

EC=6.1.1.5 HAMAP-Rule MF_02002
Alternative name(s):
Isoleucyl-tRNA synthetase HAMAP-Rule MF_02002
Gene names
Name:ileS HAMAP-Rule MF_02002
Ordered Locus Names:Acfer_1495
OrganismAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4) [Complete proteome] [HAMAP] EMBL ADB47854.1
Taxonomic identifier591001 [NCBI]
Taxonomic lineageBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus

Protein attributes

Sequence length934 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 SAAS SAAS023585

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002 SAAS SAAS023585

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002 SAAS SAAS023585

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002 SAAS SAAS023585

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002 SAAS SAAS023585.

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. HAMAP-Rule MF_02002

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif62 – 7211"HIGH" region By similarity HAMAP-Rule MF_02002
Motif610 – 6145"KMSKS" region By similarity HAMAP-Rule MF_02002

Sites

Metal binding9061Zinc By similarity HAMAP-Rule MF_02002
Metal binding9091Zinc By similarity HAMAP-Rule MF_02002
Metal binding9261Zinc By similarity HAMAP-Rule MF_02002
Metal binding9291Zinc By similarity HAMAP-Rule MF_02002
Binding site5691Aminoacyl-adenylate By similarity HAMAP-Rule MF_02002
Binding site6131ATP By similarity HAMAP-Rule MF_02002

Sequences

Sequence LengthMass (Da)Tools
D2RLA2 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 5C86E3A662C00A6E

FASTA934106,203
        10         20         30         40         50         60 
MSKKDDKYAA TLNLPETEFP MRAGLPKREP DFLDFWYKND IYGEKQKLHA GHKKFVLHDG 

        70         80         90        100        110        120 
PPYANGKIHM GHALNKVLKD IIIKYKYAQG YDTPYVPGWD THGMPIEHAC LKATGVDRHK 

       130        140        150        160        170        180 
LSPVELRKMC REYALQWIDT QRKDFKRLGV LGDWDHPYVT LDPHFEAEQI RVFGTMANKG 

       190        200        210        220        230        240 
YIYKGKKTVY WCPHCETALA EAEIEYADQK TPTIFVKMPL VKDNGLTPEA AQGKKAYMVI 

       250        260        270        280        290        300 
WTTTPWTIPA NVAVALNPDF DYAWVEYNGE VLIMAADMVD KVAQECGVEF GPVLGTIKGR 

       310        320        330        340        350        360 
AFEYAECEHP FPEYNHRKSL VVLADYVDKE AGSGCVHTAP GHGDVDYLTG LKYNLPILCP 

       370        380        390        400        410        420 
VDQKGCFTEE AGELFQGKFV FDSNGLVIKH LAEQNAILGK KTIHHQYAHC WRCKNPIIFR 

       430        440        450        460        470        480 
ASEQWFASVD GFRDDALKAI AEDVQWIPSW GESRIHNMVA DRHDWCISRQ RVWGVPIPIF 

       490        500        510        520        530        540 
YCEDCGEPLI NEETVEKIAT IFDKEGSDAW WNHTAEELLP EGTKCPKCGG THFRKEKDIM 

       550        560        570        580        590        600 
DVWFDSGSSH MGVCKRRPEL SWPADMYLEG SDQHRGWFQS SLLTSVAVTG KAPYRSVLTH 

       610        620        630        640        650        660 
GYVLDGEGRK MSKSLGNVVV PQEVIDQYGA DIVRLWAASS DYKQDVRISP VILKQLAEAY 

       670        680        690        700        710        720 
RKVRNTIRYI LGNTHDFDYE TQKVAFAEME ELDQWALMRF EALKKDVTEA YETYDFHVLF 

       730        740        750        760        770        780 
HAIHDFCTVD MSSFYLDIIK DRLYTSRKDG KARRSAQTAM TQILRELMVM LMPVLSFTME 

       790        800        810        820        830        840 
EVYQYMNKPA DAPQSVQMLP WPQAHPEYVK EDLKAKWDAF IAIRGEITKV LEGARRAKTI 

       850        860        870        880        890        900 
GHSLDAKVEL FATGDALAEL KAVEKDLPTL LIVSQAEVHE GLTDAGEATG RDDLKVLVEA 

       910        920        930 
AEGEKCERCW CYSKTVGQDP QHPTLCAKCC EAVE 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001859 Genomic DNA. Translation: ADB47854.1.
RefSeqYP_003399169.1. NC_013740.1.

3D structure databases

ProteinModelPortalD2RLA2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB47854; ADB47854; Acfer_1495.
GeneID8737983.
KEGGafn:Acfer_1495.
PATRIC31909537. VBIAciFer109666_1477.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000246402.
KOK01870.
OMAKQVLTHG.

Enzyme and pathway databases

BioCycAFER591001:GHUL-1553-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 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. tRNAsyn_1a_bind. 1 hit.
SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD2RLA2_ACIFV
AccessionPrimary (citable) accession number: D2RLA2
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)