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Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: 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

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei57Aminoacyl-adenylate1
Metal bindingi181Zinc 11
Metal bindingi184Zinc 11
Binding sitei319Valine1 Publication1
Binding sitei328Valine1 Publication1
Metal bindingi389Zinc 11
Metal bindingi392Zinc 11
Metal bindingi461Zinc 21
Metal bindingi464Zinc 21
Metal bindingi502Zinc 21
Metal bindingi504Zinc 21
Binding sitei550Aminoacyl-adenylate1
Binding sitei553Aminoacyl-adenylate1
Binding sitei554Aminoacyl-adenylate1
Binding sitei581Aminoacyl-adenylate1
Binding sitei594ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

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

BRENDAi6.1.1.5. 2305.

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
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi228T → A: Has some defects in posttransfer editing activity. 1 Publication1
Mutagenesisi229T → A: Has some defects in posttransfer editing activity. 1 Publication1
Mutagenesisi230T → A: No change in posttransfer editing activity. 1 Publication1
Mutagenesisi233T → A: No change in posttransfer editing activity. 1 Publication1
Mutagenesisi328D → A: Has some defects in posttransfer editing activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000985671 – 1043Isoleucine--tRNA ligaseAdd BLAST1043

Interactioni

Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

STRINGi300852.TTHA1067.

Structurei

Secondary structure

11043
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 23Combined sources14
Helixi26 – 33Combined sources8
Turni34 – 36Combined sources3
Helixi57 – 73Combined sources17
Beta strandi81 – 84Combined sources4
Helixi88 – 98Combined sources11
Helixi104 – 110Combined sources7
Helixi112 – 122Combined sources11
Turni123 – 126Combined sources4
Helixi127 – 130Combined sources4
Helixi133 – 136Combined sources4
Beta strandi142 – 148Combined sources7
Helixi152 – 167Combined sources16
Beta strandi171 – 174Combined sources4
Beta strandi177 – 181Combined sources5
Turni182 – 185Combined sources4
Helixi190 – 195Combined sources6
Beta strandi204 – 212Combined sources9
Helixi214 – 217Combined sources4
Beta strandi220 – 229Combined sources10
Helixi231 – 236Combined sources6
Beta strandi239 – 242Combined sources4
Beta strandi246 – 253Combined sources8
Beta strandi256 – 261Combined sources6
Helixi262 – 269Combined sources8
Beta strandi275 – 280Combined sources6
Helixi281 – 284Combined sources4
Beta strandi302 – 305Combined sources4
Beta strandi311 – 314Combined sources4
Beta strandi318 – 320Combined sources3
Helixi322 – 324Combined sources3
Helixi326 – 335Combined sources10
Beta strandi347 – 349Combined sources3
Helixi352 – 354Combined sources3
Helixi359 – 372Combined sources14
Beta strandi376 – 380Combined sources5
Beta strandi390 – 392Combined sources3
Beta strandi397 – 400Combined sources4
Beta strandi403 – 406Combined sources4
Helixi408 – 411Combined sources4
Helixi412 – 421Combined sources10
Beta strandi422 – 426Combined sources5
Helixi427 – 429Combined sources3
Turni430 – 434Combined sources5
Helixi435 – 439Combined sources5
Beta strandi447 – 449Combined sources3
Beta strandi451 – 453Combined sources3
Beta strandi458 – 465Combined sources8
Helixi473 – 479Combined sources7
Beta strandi480 – 482Combined sources3
Helixi492 – 495Combined sources4
Beta strandi499 – 501Combined sources3
Beta strandi505 – 510Combined sources6
Helixi517 – 527Combined sources11
Turni528 – 533Combined sources6
Helixi536 – 542Combined sources7
Beta strandi543 – 551Combined sources9
Helixi552 – 556Combined sources5
Helixi558 – 570Combined sources13
Beta strandi574 – 581Combined sources8
Beta strandi587 – 589Combined sources3
Turni594 – 597Combined sources4
Helixi602 – 606Combined sources5
Turni607 – 609Combined sources3
Helixi611 – 621Combined sources11
Beta strandi624 – 626Combined sources3
Helixi632 – 641Combined sources10
Helixi643 – 660Combined sources18
Helixi670 – 672Combined sources3
Helixi675 – 696Combined sources22
Helixi700 – 714Combined sources15
Turni717 – 719Combined sources3
Helixi720 – 728Combined sources9
Beta strandi733 – 735Combined sources3
Helixi738 – 754Combined sources17
Turni755 – 757Combined sources3
Helixi761 – 769Combined sources9
Turni770 – 773Combined sources4
Turni774 – 776Combined sources3
Helixi781 – 783Combined sources3
Turni791 – 793Combined sources3
Helixi796 – 812Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56690.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi47 – 57"HIGH" regionAdd BLAST11
Motifi591 – 595"KMSKS" region5

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

eggNOGiENOG4105C07. Bacteria.
COG0060. LUCA.
HOGENOMiHOG000246403.
KOiK01870.
OMAiWGTPLNI.
PhylomeDBiP56690.

Family and domain databases

CDDicd07961. Anticodon_Ia_Ile_ABEc. 1 hit.
Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02003. Ile_tRNA_synth_type2. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR033709. Anticodon_Ile_ABEc.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_Ia_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:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70890.1.
RefSeqiWP_011228416.1. NC_006461.1.
YP_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:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70890.1.
RefSeqiWP_011228416.1. NC_006461.1.
YP_144333.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1067.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105C07. Bacteria.
COG0060. LUCA.
HOGENOMiHOG000246403.
KOiK01870.
OMAiWGTPLNI.
PhylomeDBiP56690.

Enzyme and pathway databases

BRENDAi6.1.1.5. 2305.

Miscellaneous databases

EvolutionaryTraceiP56690.

Family and domain databases

CDDicd07961. Anticodon_Ia_Ile_ABEc. 1 hit.
Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02003. Ile_tRNA_synth_type2. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR033709. Anticodon_Ile_ABEc.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_Ia_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]
ProtoNetiSearch...

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: November 2, 2016
This is version 117 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.