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.

B2FTJ0

- SYI_STRMK

UniProt

B2FTJ0 - SYI_STRMK

(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, Smlt1340
Organism
Stenotrophomonas maltophilia (strain K279a)
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. aminoacyl-tRNA editing activity Source: InterPro
  2. ATP binding Source: UniProtKB-HAMAP
  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

BioCyciSMAL522373:GJE8-1306-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:Smlt1340
OrganismiStenotrophomonas maltophilia (strain K279a)
Taxonomic identifieri522373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
ProteomesiUP000008840: 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 annotationPRO_1000189200Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi522373.Smlt1340.

Structurei

3D structure databases

ProteinModelPortaliB2FTJ0.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 6911"HIGH" regionUniRule annotationAdd
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.
HOGENOMiHOG000246402.
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.

B2FTJ0-1 [UniParc]FASTAAdd to Basket

« Hide

MSQDYKTTLN LPATEFPMRG DLPKREPGIL ARWEAQGLYQ QLRDNAAGRP    50
LFVLHDGPPY ANGRIHLGHA VNKILKDIIV KSRYLAGFDA PYVPGWDCHG 100
LPIEIAVEKK WGKVGTKLDA VEFRQKCREF AEEQINIQRV DFKRLGVTGD 150
WDNPYKTLSF DFEANEIRAL SKVVANGHLV RGAKPVYWCF DCGSALAEAE 200
IEYQEKESPA IDVAYAARDA QAIGQAFGVS VPADVEVAVP IWTTTPWTLP 250
ASLAVSLGAE ITYVLAEGPA HNGKRRWLVL AAALAERALQ RYGVENLVLH 300
GETTGAALEN QLLAHPFYPE REILVLNGDH VSDEDGTGAV HTAPGHGQED 350
FVVSQKYGLL DKYNAGQVTP IDGRGVYLES TPPAGDVVLA GQHLWKAQEA 400
IVGVLRDNGS LLAFHPIRHS YPHCWRHKTP VVFRATPQWF ISMDKANLRN 450
DALAAIDTVG WFPTWGKARI QSMVDGRPDW TISRQRTWGV PIALFTHRQT 500
GEIHPRSVEL MQQVADRVEA EGIDVWYSLD ATELLGAEAA DYEKVTDILD 550
VWFDSGVTHE GVLAARGFGK PADLYLEGSD QHRGWFQSSL LTGVAIDKRA 600
PYKQCLTHGF TVDEHGRKMS KSLGNGIEPQ DIMNKLGADI LRLWIASADY 650
SNEMSLSQEI LKRNADAYRR LRNTARFLLG NLDGFDPAQH LRPLDQMVAL 700
DRWIVHRAWE LQEKIKAAYD GYNMAEIVQL LLNFCSVDLG SLYLDVTKDR 750
LYTMPTDSHG RRSAQSAMYH IAEAFTRWVA PILTFTADEL WGYLPGEHAG 800
HVLFTTWYDG LAPLPADAQL NATDFDQLLA VREQVAKVLE PMRANGAIGA 850
ALEAEITIAA NEEQAAKWQP LADELRFLFI SGDVQVRPAT TDEVFVSAQP 900
TTKAKCVRCW HHRADVGRNA DHPELCGRCV SNVTGAGEVR SWF 943
Length:943
Mass (Da):104,911
Last modified:June 10, 2008 - v1
Checksum:iB1B1C87F4A4328A1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM743169 Genomic DNA. Translation: CAQ44887.1.
RefSeqiWP_012479507.1. NC_010943.1.
YP_001971197.1. NC_010943.1.

Genome annotation databases

EnsemblBacteriaiCAQ44887; CAQ44887; Smlt1340.
GeneIDi6395039.
KEGGisml:Smlt1340.
PATRICi23698397. VBISteMal45202_1288.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM743169 Genomic DNA. Translation: CAQ44887.1 .
RefSeqi WP_012479507.1. NC_010943.1.
YP_001971197.1. NC_010943.1.

3D structure databases

ProteinModelPortali B2FTJ0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 522373.Smlt1340.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAQ44887 ; CAQ44887 ; Smlt1340 .
GeneIDi 6395039.
KEGGi sml:Smlt1340.
PATRICi 23698397. VBISteMal45202_1288.

Phylogenomic databases

eggNOGi COG0060.
HOGENOMi HOG000246402.
KOi K01870.
OMAi KPVHWCL.
OrthoDBi EOG644ZM1.

Enzyme and pathway databases

BioCyci SMAL522373:GJE8-1306-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 complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
    Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
    , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
    Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K279a.

Entry informationi

Entry nameiSYI_STRMK
AccessioniPrimary (citable) accession number: B2FTJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 10, 2008
Last modified: September 3, 2014
This is version 50 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