Skip Header

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

P56690

- SYI_THET8

UniProt

P56690 - SYI_THET8

(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
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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).By similarity

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571Aminoacyl-adenylate
Metal bindingi181 – 1811Zinc 1
Metal bindingi184 – 1841Zinc 1
Binding sitei319 – 3191Valine1 Publication
Binding sitei328 – 3281Valine1 Publication
Metal bindingi389 – 3891Zinc 1
Metal bindingi392 – 3921Zinc 1
Metal bindingi461 – 4611Zinc 2
Metal bindingi464 – 4641Zinc 2
Metal bindingi502 – 5021Zinc 2
Metal bindingi504 – 5041Zinc 2
Binding sitei550 – 5501Aminoacyl-adenylate
Binding sitei553 – 5531Aminoacyl-adenylate
Binding sitei554 – 5541Aminoacyl-adenylate
Binding sitei581 – 5811Aminoacyl-adenylate
Binding sitei594 – 5941ATPBy 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

BioCyciTTHE300852:GH8R-1099-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:TTHA1067
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2281T → A: Has some defects in posttransfer editing activity. 1 Publication
Mutagenesisi229 – 2291T → A: Has some defects in posttransfer editing activity. 1 Publication
Mutagenesisi230 – 2301T → A: No change in posttransfer editing activity. 1 Publication
Mutagenesisi233 – 2331T → A: No change in posttransfer editing activity. 1 Publication
Mutagenesisi328 – 3281D → A: Has some defects in posttransfer editing activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10431043Isoleucine--tRNA ligasePRO_0000098567Add
BLAST

Interactioni

Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

STRINGi300852.TTHA1067.

Structurei

Secondary structure

1
1043
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314Combined sources
Helixi26 – 338Combined sources
Turni34 – 363Combined sources
Helixi57 – 7317Combined sources
Beta strandi81 – 844Combined sources
Helixi88 – 9811Combined sources
Helixi104 – 1107Combined sources
Helixi112 – 12211Combined sources
Turni123 – 1264Combined sources
Helixi127 – 1304Combined sources
Helixi133 – 1364Combined sources
Beta strandi142 – 1487Combined sources
Helixi152 – 16716Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi177 – 1815Combined sources
Turni182 – 1854Combined sources
Helixi190 – 1956Combined sources
Beta strandi204 – 2129Combined sources
Helixi214 – 2174Combined sources
Beta strandi220 – 22910Combined sources
Helixi231 – 2366Combined sources
Beta strandi239 – 2424Combined sources
Beta strandi246 – 2538Combined sources
Beta strandi256 – 2616Combined sources
Helixi262 – 2698Combined sources
Beta strandi275 – 2806Combined sources
Helixi281 – 2844Combined sources
Beta strandi302 – 3054Combined sources
Beta strandi311 – 3144Combined sources
Beta strandi318 – 3203Combined sources
Helixi322 – 3243Combined sources
Helixi326 – 33510Combined sources
Beta strandi347 – 3493Combined sources
Helixi352 – 3543Combined sources
Helixi359 – 37214Combined sources
Beta strandi376 – 3805Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi397 – 4004Combined sources
Beta strandi403 – 4064Combined sources
Helixi408 – 4114Combined sources
Helixi412 – 42110Combined sources
Beta strandi422 – 4265Combined sources
Helixi427 – 4293Combined sources
Turni430 – 4345Combined sources
Helixi435 – 4395Combined sources
Beta strandi447 – 4493Combined sources
Beta strandi451 – 4533Combined sources
Beta strandi458 – 4658Combined sources
Helixi473 – 4797Combined sources
Beta strandi480 – 4823Combined sources
Helixi492 – 4954Combined sources
Beta strandi499 – 5013Combined sources
Beta strandi505 – 5106Combined sources
Helixi517 – 52711Combined sources
Turni528 – 5336Combined sources
Helixi536 – 5427Combined sources
Beta strandi543 – 5519Combined sources
Helixi552 – 5565Combined sources
Helixi558 – 57013Combined sources
Beta strandi574 – 5818Combined sources
Beta strandi587 – 5893Combined sources
Turni594 – 5974Combined sources
Helixi602 – 6065Combined sources
Turni607 – 6093Combined sources
Helixi611 – 62111Combined sources
Beta strandi624 – 6263Combined sources
Helixi632 – 64110Combined sources
Helixi643 – 66018Combined sources
Helixi670 – 6723Combined sources
Helixi675 – 69622Combined sources
Helixi700 – 71415Combined sources
Turni717 – 7193Combined sources
Helixi720 – 7289Combined sources
Beta strandi733 – 7353Combined sources
Helixi738 – 75417Combined sources
Turni755 – 7573Combined sources
Helixi761 – 7699Combined sources
Turni770 – 7734Combined sources
Turni774 – 7763Combined sources
Helixi781 – 7833Combined sources
Turni791 – 7933Combined sources
Helixi796 – 81217Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILEX-ray2.50A1-821[»]
1JZQX-ray3.00A1-821[»]
1JZSX-ray2.50A1-821[»]
1UDZX-ray1.80A/B201-381[»]
1UE0X-ray2.00A/B201-381[»]
1WK8X-ray1.70A/B196-388[»]
1WNYX-ray1.60A/B201-385[»]
1WNZX-ray1.70A201-385[»]
ProteinModelPortaliP56690.
SMRiP56690. Positions 1-821.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56690.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi47 – 5711"HIGH" regionAdd
BLAST
Motifi591 – 5955"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)) (By similarity).By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0060.
HOGENOMiHOG000246403.
KOiK01870.
OMAiRVEHMVE.
OrthoDBiEOG644ZM1.
PhylomeDBiP56690.

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.
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.
[Graphical view]
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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.

P56690-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFKEVGEPNF PKLEEEVLAF WKREKIFQKS VENRKGGPRY TVYEGPPTAN
60 70 80 90 100
GLPHVGHAQA RSYKDLFPRY KTMRGYYAPR RAGWDTHGLP VELEVEKKLG
110 120 130 140 150
LKSKREIEAY GIERFNQACR ESVFTYEKEW EAFTERIAYW VDLENAYATL
160 170 180 190 200
EPTYIESIWW SLKNLFDRGL LYRDHKVVPY CPRCGTPLSS HEVALGYKEI
210 220 230 240 250
QDPSVYVRFP LKEPKKLGLE KASLLIWTTT PWTLPGNVAA AVHPEYTYAA
260 270 280 290 300
FQVGDEALIL EEGLGRKLLG EGTPVLKTFP GKALEGLPYT PPYPQALEKG
310 320 330 340 350
YFVVLADYVS QEDGTGIVHQ APAFGAEDLE TARVYGLPLL KTVDEEGKLL
360 370 380 390 400
VEPFKGLYFR EANRAILRDL RGRGLLFKEE SYLHSYPHCW RCSTPLMYYA
410 420 430 440 450
TESWFIKNTL FKDELIRKNQ EIHWVPPHIK EGRYGEWLKN LVDWALSRNR
460 470 480 490 500
YWGTPLPIWV CQACGKEEAI GSFQELKARA TKPLPEPFDP HRPYVDQVEL
510 520 530 540 550
ACACGGTMRR VPYVIDVWYD SGAMPFASLH YPFEHEEVFR ESFPADFIAE
560 570 580 590 600
GIDQTRGWFN SLHQLGVMLF GSIAFKNVIC HGLILDEKGQ KMSKSKGNVV
610 620 630 640 650
DPWDIIREFG ADALRWYIYV SAPPEADRRF GPNLVRETVR DYFLTLWNVY
660 670 680 690 700
SFFVTYANLD RPDLKNPPPP EKRPEMDRWL LARMQDLIQR VTEALEAYDP
710 720 730 740 750
TTSARALRDF VVEDLSQWYV RRNRRRFWKN EDALDREAAY ATLYEALVLV
760 770 780 790 800
ATLAAPFTPF LAEVLWQNLV RSVRPEAKES VHLADWPEAD PALADEALVA
810 820 830 840 850
QMRAVLKVVD LARAARAKSG VKTRTPLPLL LVTAPTALER EGLKRFAHEI
860 870 880 890 900
AEELNVKEVR VLEPGEEILS YRVLPNLKLL GRKYGKLVPK IREALQRERE
910 920 930 940 950
RAAALALKGE AIPLEVEGEA LTLLPEEVLL EAEAPKGYQA LEKDGYVAAL
960 970 980 990 1000
KVEVTEALRM EGLARDLIRL LQQARKDMGL KVSDRIRVGY EAEGPYLEAL
1010 1020 1030 1040
KRHGPWIAEE VLATAFGEGL FGGFEARVED EEGKAVFHLA RAE
Length:1,043
Mass (Da):119,247
Last modified:March 29, 2005 - v2
Checksum:i0F8010BBE8F83A30
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70890.1.
RefSeqiYP_144333.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70890; BAD70890; BAD70890.
GeneIDi3168241.
KEGGittj:TTHA1067.
PATRICi23957094. VBITheThe93045_1047.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70890.1 .
RefSeqi YP_144333.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ILE X-ray 2.50 A 1-821 [» ]
1JZQ X-ray 3.00 A 1-821 [» ]
1JZS X-ray 2.50 A 1-821 [» ]
1UDZ X-ray 1.80 A/B 201-381 [» ]
1UE0 X-ray 2.00 A/B 201-381 [» ]
1WK8 X-ray 1.70 A/B 196-388 [» ]
1WNY X-ray 1.60 A/B 201-385 [» ]
1WNZ X-ray 1.70 A 201-385 [» ]
ProteinModelPortali P56690.
SMRi P56690. Positions 1-821.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1067.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70890 ; BAD70890 ; BAD70890 .
GeneIDi 3168241.
KEGGi ttj:TTHA1067.
PATRICi 23957094. VBITheThe93045_1047.

Phylogenomic databases

eggNOGi COG0060.
HOGENOMi HOG000246403.
KOi K01870.
OMAi RVEHMVE.
OrthoDBi EOG644ZM1.
PhylomeDBi P56690.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1099-MONOMER.

Miscellaneous databases

EvolutionaryTracei P56690.

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_02003. Ile_tRNA_synth_type2.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view ]
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Enzyme structure with two catalytic sites for double-sieve selection of substrate."
    Nureki O., Vassylyev D.G., Tateno M., Shimada A., Nakama T., Fukai S., Konno M., Hendrickson T.L., Schimmel P., Yokoyama S.
    Science 280:578-582(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-821 IN COMPLEX WITH ZINC IONS.
  3. "Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase."
    Nakama T., Nureki O., Yokoyama S.
    J. Biol. Chem. 276:47387-47393(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-821 IN COMPLEX WITH ZINC IONS; ILE-ADENYLATE AND MUPIROCIN.
  4. "Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine."
    Fukunaga R., Fukai S., Ishitani R., Nureki O., Yokoyama S.
    J. Biol. Chem. 279:8396-8402(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH VAL, MUTAGENESIS OF THR-228; THR-229; THR-230; THR-233 AND ASP-328.

Entry informationi

Entry nameiSYI_THET8
AccessioniPrimary (citable) accession number: P56690
Secondary accession number(s): Q5SJE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: March 29, 2005
Last modified: October 29, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The ATP consumption with regard to L-valine is nonproductive and is solely for substrate selection, which demonstrates the high cost of accuracy.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3