Skip Header

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

Q14HT2

- SYI_FRAT1

UniProt

Q14HT2 - SYI_FRAT1

(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

Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
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 sitei558 – 5581Aminoacyl-adenylateUniRule annotation
Binding sitei602 – 6021ATPUniRule annotation
Metal bindingi897 – 8971ZincUniRule annotation
Metal bindingi900 – 9001ZincUniRule annotation
Metal bindingi917 – 9171ZincUniRule annotation
Metal bindingi920 – 9201ZincUniRule 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

BioCyciFTUL393115:GJUT-932-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:FTF0915c
OrganismiFrancisella tularensis subsp. tularensis (strain FSC 198)
Taxonomic identifieri393115 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000001821: 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 – 935935Isoleucine--tRNA ligasePRO_1000022065Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi393115.FTF0915c.

Structurei

3D structure databases

ProteinModelPortaliQ14HT2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi58 – 6811"HIGH" regionAdd
BLAST
Motifi599 – 6035"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.

Q14HT2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDYKDTLNL PKTSFSMKGN LANKEPMILN KWEKQGIYKK IREHFAGREK
60 70 80 90 100
FVLHDGPPYA NGSIHVGHAV NKILKDIIIK SKTLSGYDAP FTPTWDCHGL
110 120 130 140 150
PIELQVEKKH GKAGQSISED DFRKECRKYA KKQVEIQKKD FKRLGVLGDW
160 170 180 190 200
EQPYLTINFD YEANMIRTLA KIIENGHLSK GFKPVHWCTD CGSALAEAEV
210 220 230 240 250
EYADKVSPAI DVKFKIKDKD KLAQAFGLDS LNHDAFAIIW TTTPWTLPAN
260 270 280 290 300
QAIAVNNQLN YSLIKIEDFY IILAENLVEQ TLKRYAIENA QIIATTTGNK
310 320 330 340 350
LTGIMAEHPF YSRHVPILHG DHVTDDSGTG LVHTAPTHGV DDFTLGKEHN
360 370 380 390 400
LSMEIFVKGN GCYSENTKLF AGEFIFKAND RIIELLGEKK RLMNSDKIKH
410 420 430 440 450
SYPHCWRHKT PLMFRATPQW FISMEKQGLR DKALQAIKET SWAPSWGQAR
460 470 480 490 500
IEGMVKDRPD WCISRQRTWG VPLPLFIHKE TEELHPNTIE ILHKVAEKIE
510 520 530 540 550
KDGIEAWFNA DDCEFITETA QYKSVKDTLD VWFDSGSSSM CILDLDKRLS
560 570 580 590 600
YPADLYLEGS DQHRGWFQTS LLVAMSAKGS QPYKEVFTHG FVVDEHGRKM
610 620 630 640 650
SKSLGNVTSP QDIYNTLGAD ILRLWTASTD YKSEMAVSDQ ILKRTADTYR
660 670 680 690 700
RLRNTARFLL SNLDGFNPVT DIIEFDKLVK LDQWAIAKTK EFQDKIIEVY
710 720 730 740 750
DKYQTHTVAQ LIHHFCSIEM GSFYLDIIKD RQYTAKTDGH PRKSAQTAIY
760 770 780 790 800
HIVHALVRWM APILSFTADE IWDATPKTTD LPIQLCEWYT GLKSFDQDAE
810 820 830 840 850
LDLEYWAKIQ EIRSEVNRVL EIKRNEDVIK ASLEAEITIY ADKYNYNLLE
860 870 880 890 900
KLGNELRFLL ISSKADLKVI EESTSSSIAA NIPGLLIEIT KIEEPKCERC
910 920 930
WHRSSTVGDN PQYKDICSRC VENITTEAGE SREFA
Length:935
Mass (Da):106,967
Last modified:August 22, 2006 - v1
Checksum:i22F62BAD3DAE8332
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM286280 Genomic DNA. Translation: CAL08931.1.
RefSeqiYP_667044.1. NC_008245.1.

Genome annotation databases

EnsemblBacteriaiCAL08931; CAL08931; FTF0915c.
GeneIDi4200661.
KEGGiftf:FTF0915c.
PATRICi17960759. VBIFraTul133500_1045.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM286280 Genomic DNA. Translation: CAL08931.1 .
RefSeqi YP_667044.1. NC_008245.1.

3D structure databases

ProteinModelPortali Q14HT2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 393115.FTF0915c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL08931 ; CAL08931 ; FTF0915c .
GeneIDi 4200661.
KEGGi ftf:FTF0915c.
PATRICi 17960759. VBIFraTul133500_1045.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci FTUL393115:GJUT-932-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. "Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
    Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
    PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FSC 198.

Entry informationi

Entry nameiSYI_FRAT1
AccessioniPrimary (citable) accession number: Q14HT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: October 29, 2014
This is version 64 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