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Protein

Isoleucine--tRNA ligase 2

Gene

ileS2

Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).UniRule annotation

Cofactori

Zn2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei593 – 5931ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Isoleucine--tRNA ligase 2UniRule annotation (EC:6.1.1.5UniRule annotation)
Alternative name(s):
Isoleucyl-tRNA synthetase 2UniRule annotation
Short name:
IleRS 2UniRule annotation
Gene namesi
Name:ileS2UniRule annotation
Ordered Locus Names:BCE_2241
OrganismiBacillus cereus (strain ATCC 10987 / NRS 248)
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002527 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10331033Isoleucine--tRNA ligase 2PRO_0000098516Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ739A1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi47 – 5711"HIGH" regionAdd
BLAST
Motifi590 – 5945"KMSKS" region

Domaini

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)).UniRule annotation

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0060.
HOGENOMiHOG000246403.
KOiK01870.
OMAiIPLPIWR.
OrthoDBiEOG644ZM1.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02003. Ile_tRNA_synth_type2.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q739A1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVDVKESA VGRETRIRKQ WNEQSIFEQS IQNREGAQSF VFYEGPPTAN
60 70 80 90 100
GLPHVGHALG RTIKDVVARY KTMAGYKVLR KAGWDTHGLP VELGVEKQLG
110 120 130 140 150
ISGKHEIEEY GIEPFIKKCK ESVFTYEKQW REFTESIGYW VDMDDPYVTL
160 170 180 190 200
ENPYIESVWH ILGTIHEKGL LYKGHRVSPY CPSCQTSLSS HEVAQGYKTV
210 220 230 240 250
KDLSATVKFK VKDSENEYFL GWTTTPWTLP ANVALAVHPN MEYVKAKQEG
260 270 280 290 300
YVYIVAKERV QDVLKEDYEV LSVHKGEELV NTSYTAPFPM KEVTNGYHVI
310 320 330 340 350
AADFVTADSG TGLVHIAPAY GEDDYRVVQS EGLSFLHVVD EKGEYTEAVP
360 370 380 390 400
FLKGKFVKDS DVDIVRYLAK EGLLYHKEKY EHSYPHCWRC DSPLLYYAGE
410 420 430 440 450
SWLIRTTAIK DTFLQNNDTV TWYPDHMKHG RFGKFLENMV DWNISRNRYW
460 470 480 490 500
GTPLNVWECE SCDHQFAPKS IADLRKHSTK ETPEDLELHK PYVDEVQVSC
510 520 530 540 550
EKCGGAMNRT PEVIDVWFDS GSMPFAQYHY PFENKELFED QFPADVIAEG
560 570 580 590 600
IDQTRGWFYS LLAVSALYTG KVPYKRVLSL GHVLDEEGQK MSKSKGNALD
610 620 630 640 650
PVDLVNQFGA DALRWALLVD SAPWNAKRFS ERTVLEAKSK FVDTLVNVYS
660 670 680 690 700
FYVLYANLDE YNPDETYDVK RTKLDEWVLS RLHSTTKKVR TALDDYQFTN
710 720 730 740 750
AAREIATLVD EVSNWYVRRS RNRFWESGMN AEKAAAYETL HEVLVTISKL
760 770 780 790 800
IAPFTPFVAE DIHLNLTGSS VHLEDYPVVN ESLLQPKLEA EMDAVLQVVE
810 820 830 840 850
LGRSNRNQHS LKVKQPLAEL VLLEHNENDM DWESYRDIVM DELNVKAFHV
860 870 880 890 900
ELDETKYTSY QLKLNFKTAG PKFGKNVNAV NDWLKQLSQD EVQNFVTTER
910 920 930 940 950
AVYEAASGEE VVVTTEDVLV EKVAKSGFSN TTNGQYTVML DTNVTEELLQ
960 970 980 990 1000
EGVAREFIRA VQEYRKQLNL PVNLRVDVIL DTEEELQQTL TNHKQLLEEN
1010 1020 1030
LLVKQFTFGH LTNEDDELSL GETKVRIKLS ATK
Length:1,033
Mass (Da):118,420
Last modified:July 5, 2004 - v1
Checksum:iC75BD19783337160
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41161.1.
RefSeqiNP_978553.1. NC_003909.8.
WP_000754918.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS41161; AAS41161; BCE_2241.
KEGGibca:BCE_2241.
PATRICi18853278. VBIBacCer118379_2141.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41161.1.
RefSeqiNP_978553.1. NC_003909.8.
WP_000754918.1. NC_003909.8.

3D structure databases

ProteinModelPortaliQ739A1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS41161; AAS41161; BCE_2241.
KEGGibca:BCE_2241.
PATRICi18853278. VBIBacCer118379_2141.

Phylogenomic databases

eggNOGiCOG0060.
HOGENOMiHOG000246403.
KOiK01870.
OMAiIPLPIWR.
OrthoDBiEOG644ZM1.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02003. Ile_tRNA_synth_type2.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
    Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
    Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10987 / NRS 248.

Entry informationi

Entry nameiSYI2_BACC1
AccessioniPrimary (citable) accession number: Q739A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.