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B2FTJ0

- SYI_STRMK

UniProt

B2FTJ0 - SYI_STRMK

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Protein

Isoleucine--tRNA ligase

Gene

ileS

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).UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei577 – 5771Aminoacyl-adenylateUniRule annotation
Binding sitei621 – 6211ATPUniRule annotation
Metal bindingi906 – 9061ZincUniRule annotation
Metal bindingi909 – 9091ZincUniRule annotation
Metal bindingi926 – 9261ZincUniRule annotation
Metal bindingi929 – 9291ZincUniRule annotation

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 ligaseUniRule annotation (EC:6.1.1.5UniRule annotation)
Alternative name(s):
Isoleucyl-tRNA synthetaseUniRule annotation
Short name:
IleRSUniRule annotation
Gene namesi
Name:ileSUniRule annotation
Ordered Locus Names:Smlt1340
OrganismiStenotrophomonas maltophilia (strain K279a)
Taxonomic identifieri522373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
ProteomesiUP000008840: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 943943Isoleucine--tRNA ligasePRO_1000189200Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi522373.Smlt1340.

Structurei

3D structure databases

ProteinModelPortaliB2FTJ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 6911"HIGH" regionAdd
BLAST
Motifi618 – 6225"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 1 subfamily.UniRule annotation

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

        10         20         30         40         50
MSQDYKTTLN LPATEFPMRG DLPKREPGIL ARWEAQGLYQ QLRDNAAGRP
60 70 80 90 100
LFVLHDGPPY ANGRIHLGHA VNKILKDIIV KSRYLAGFDA PYVPGWDCHG
110 120 130 140 150
LPIEIAVEKK WGKVGTKLDA VEFRQKCREF AEEQINIQRV DFKRLGVTGD
160 170 180 190 200
WDNPYKTLSF DFEANEIRAL SKVVANGHLV RGAKPVYWCF DCGSALAEAE
210 220 230 240 250
IEYQEKESPA IDVAYAARDA QAIGQAFGVS VPADVEVAVP IWTTTPWTLP
260 270 280 290 300
ASLAVSLGAE ITYVLAEGPA HNGKRRWLVL AAALAERALQ RYGVENLVLH
310 320 330 340 350
GETTGAALEN QLLAHPFYPE REILVLNGDH VSDEDGTGAV HTAPGHGQED
360 370 380 390 400
FVVSQKYGLL DKYNAGQVTP IDGRGVYLES TPPAGDVVLA GQHLWKAQEA
410 420 430 440 450
IVGVLRDNGS LLAFHPIRHS YPHCWRHKTP VVFRATPQWF ISMDKANLRN
460 470 480 490 500
DALAAIDTVG WFPTWGKARI QSMVDGRPDW TISRQRTWGV PIALFTHRQT
510 520 530 540 550
GEIHPRSVEL MQQVADRVEA EGIDVWYSLD ATELLGAEAA DYEKVTDILD
560 570 580 590 600
VWFDSGVTHE GVLAARGFGK PADLYLEGSD QHRGWFQSSL LTGVAIDKRA
610 620 630 640 650
PYKQCLTHGF TVDEHGRKMS KSLGNGIEPQ DIMNKLGADI LRLWIASADY
660 670 680 690 700
SNEMSLSQEI LKRNADAYRR LRNTARFLLG NLDGFDPAQH LRPLDQMVAL
710 720 730 740 750
DRWIVHRAWE LQEKIKAAYD GYNMAEIVQL LLNFCSVDLG SLYLDVTKDR
760 770 780 790 800
LYTMPTDSHG RRSAQSAMYH IAEAFTRWVA PILTFTADEL WGYLPGEHAG
810 820 830 840 850
HVLFTTWYDG LAPLPADAQL NATDFDQLLA VREQVAKVLE PMRANGAIGA
860 870 880 890 900
ALEAEITIAA NEEQAAKWQP LADELRFLFI SGDVQVRPAT TDEVFVSAQP
910 920 930 940
TTKAKCVRCW HHRADVGRNA DHPELCGRCV SNVTGAGEVR SWF
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: October 29, 2014
This is version 52 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, Reference 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