SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B0RY28

- SYI_XANCB

UniProt

B0RY28 - SYI_XANCB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Isoleucine--tRNA ligase
Gene
ileS, xcc-b100_3183
Organism
Xanthomonas campestris pv. campestris (strain B100)
Status
Reviewed - 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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei577 – 5771Aminoacyl-adenylate By similarity
Binding sitei621 – 6211ATP By similarity
Metal bindingi906 – 9061Zinc By similarity
Metal bindingi909 – 9091Zinc By similarity
Metal bindingi926 – 9261Zinc By similarity
Metal bindingi929 – 9291Zinc By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. aminoacyl-tRNA editing activity Source: InterPro
  3. isoleucine-tRNA ligase activity Source: UniProtKB-HAMAP
  4. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. isoleucyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciXCAM509169:GHW4-3250-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoleucine--tRNA ligase (EC:6.1.1.5)
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name:
IleRS
Gene namesi
Name:ileS
Ordered Locus Names:xcc-b100_3183
OrganismiXanthomonas campestris pv. campestris (strain B100)
Taxonomic identifieri509169 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000001188: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 943943Isoleucine--tRNA ligaseUniRule annotation
PRO_1000189216Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi509169.xccb100_3183.

Structurei

3D structure databases

ProteinModelPortaliB0RY28.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 6911"HIGH" regionUniRule annotation
Add
BLAST
Motifi618 – 6225"KMSKS" regionUniRule annotation

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)) By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0060.
KOiK01870.
OMAiKPVHWCL.
OrthoDBiEOG644ZM1.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02002. Ile_tRNA_synth_type1.
InterProiIPR001412. 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]
PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00392. ileS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B0RY28-1 [UniParc]FASTAAdd to Basket

« Hide

MTQDYKATLH LPATDFPMRG DLPKREPAML ERWEREGLYA QVRANAAGRP    50
LFVLHDGPPY ANGQIHLGHA VNKILKDIIV KSKYLAGFDA PYIPGWDCHG 100
LPIEIAIEKK FGKVGVKLDA AQFRQKCREY ATEQIDLQRR DFKRLGVIGD 150
WDNPYKTLDF RFEANEIRAL AKVIDNGHLT RGVKPVHWCF DCGSALAEAE 200
IEYADKVSPT VDIAYPARDP AAVAAAFGVT LSAGTQVAVP IWTTTPWTLP 250
ASLAVSLGAE LDYVLVEGAA DHGQPRWLVI AEALAGKALA RYGVDAVVVH 300
GHAKGAALDQ LLLAHPFYAE RDIPLILGDH VSDDDGTGAV HTAPGHGQED 350
YQVSKQYGLL ERYSAAQINP IDGRGVYLPS TPPLGDTVLA GLHIWKANDV 400
IIDALRDTGA LLAASKMEHS YPHCWRHKTP IAFRATPQWF ISMEQANLRA 450
DALKAIETVH WYPSWGQARI AGMIDGRPDW TISRQRTWGV PIALFVHRET 500
GEPHPRSTEL MRQVAERVEQ GGVDVWYTLD AAELLGDEAG DYDKITDILD 550
VWFDSGVTHE TVLVDRGLPK PADLYLEGSD QHRGWFQSSL LTGVAMDKVA 600
PYKQCLTHGF TVDEHGRKMS KSLGNGIEPQ EIMRTLGADI LRLWIASADY 650
SNEMSLSQEI LKRNADAYRR LRNTARFLLG NLHGFDPLQH LVALDDMVLL 700
DRWIVHRAHE LQEKITAAYA RYDFAEIVQG LLNFCSVDLG SLYLDVTKDR 750
LYTMAEDARG RRSAQSAMYH VAEAFVRWIA PVLSFTAEEL WAYLPGEHSG 800
NVLFATWYDG LAPMPADAAL TSADVDKLLA LREQVAKVLE PMRANGAIGA 850
ALEAEITVAA DAQTAARWQP LSDELRFLFI SGDVTVTAAS TDDIFVSAQP 900
TTKAKCVRCW HHQASVGSDP RHPELCSRCV SNIEGPGEER RWF 943
Length:943
Mass (Da):104,524
Last modified:April 8, 2008 - v1
Checksum:i5C5D14E3FFEA0CB4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM920689 Genomic DNA. Translation: CAP52548.1.
RefSeqiYP_001904588.1. NC_010688.1.

Genome annotation databases

EnsemblBacteriaiCAP52548; CAP52548; xcc-b100_3183.
GeneIDi6323119.
KEGGixca:xccb100_3183.
PATRICi24086268. VBIXanCam108527_3211.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM920689 Genomic DNA. Translation: CAP52548.1 .
RefSeqi YP_001904588.1. NC_010688.1.

3D structure databases

ProteinModelPortali B0RY28.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 509169.xccb100_3183.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAP52548 ; CAP52548 ; xcc-b100_3183 .
GeneIDi 6323119.
KEGGi xca:xccb100_3183.
PATRICi 24086268. VBIXanCam108527_3211.

Phylogenomic databases

eggNOGi COG0060.
KOi K01870.
OMAi KPVHWCL.
OrthoDBi EOG644ZM1.

Enzyme and pathway databases

BioCyci XCAM509169:GHW4-3250-MONOMER.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPi MF_02002. Ile_tRNA_synth_type1.
InterProi IPR001412. 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 ]
PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view ]
PRINTSi PR00984. TRNASYNTHILE.
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsi TIGR00392. ileS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
    Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
    J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B100.

Entry informationi

Entry nameiSYI_XANCB
AccessioniPrimary (citable) accession number: B0RY28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 51 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