Skip Header

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

Isoleucine--tRNA ligase

Gene

ileS

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 4 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 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei554Aminoacyl-adenylate1
Binding sitei598ATPBy similarity1
Binding sitei632tRNA1
Binding sitei640tRNA1
Metal bindingi886Zinc1
Metal bindingi889Zinc1
Metal bindingi906Zinc1
Metal bindingi909Zinc1

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. 3352.
SABIO-RKP41972.

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
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1982.
DrugBankiDB00410. Mupirocin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000984631 – 917Isoleucine--tRNA ligaseAdd BLAST917

Proteomic databases

PRIDEiP41972.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi93062.SACOL1206.

Chemistry databases

BindingDBiP41972.

Structurei

Secondary structure

1917
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Helixi20 – 33Combined sources14
Helixi36 – 43Combined sources8
Turni44 – 46Combined sources3
Beta strandi58 – 61Combined sources4
Helixi65 – 82Combined sources18
Turni83 – 85Combined sources3
Beta strandi93 – 95Combined sources3
Helixi99 – 108Combined sources10
Helixi117 – 140Combined sources24
Turni141 – 143Combined sources3
Helixi157 – 172Combined sources16
Beta strandi176 – 186Combined sources11
Turni187 – 190Combined sources4
Helixi195 – 197Combined sources3
Beta strandi198 – 209Combined sources12
Beta strandi212 – 214Combined sources3
Helixi220 – 222Combined sources3
Beta strandi230 – 232Combined sources3
Helixi234 – 236Combined sources3
Helixi237 – 239Combined sources3
Beta strandi242 – 245Combined sources4
Turni256 – 259Combined sources4
Turni265 – 268Combined sources4
Helixi269 – 272Combined sources4
Turni273 – 276Combined sources4
Turni290 – 292Combined sources3
Helixi301 – 303Combined sources3
Beta strandi306 – 312Combined sources7
Beta strandi318 – 320Combined sources3
Helixi333 – 336Combined sources4
Turni337 – 339Combined sources3
Beta strandi340 – 342Combined sources3
Beta strandi351 – 353Combined sources3
Beta strandi363 – 365Combined sources3
Helixi369 – 372Combined sources4
Helixi375 – 377Combined sources3
Helixi380 – 383Combined sources4
Beta strandi388 – 397Combined sources10
Turni398 – 400Combined sources3
Beta strandi405 – 414Combined sources10
Helixi416 – 428Combined sources13
Beta strandi430 – 434Combined sources5
Helixi435 – 447Combined sources13
Beta strandi454 – 456Combined sources3
Beta strandi458 – 460Combined sources3
Beta strandi469 – 471Combined sources3
Helixi477 – 490Combined sources14
Helixi493 – 497Combined sources5
Helixi500 – 503Combined sources4
Beta strandi504 – 507Combined sources4
Beta strandi511 – 513Combined sources3
Helixi527 – 532Combined sources6
Helixi534 – 537Combined sources4
Turni538 – 541Combined sources4
Beta strandi547 – 555Combined sources9
Helixi556 – 559Combined sources4
Helixi562 – 574Combined sources13
Beta strandi578 – 585Combined sources8
Beta strandi591 – 594Combined sources4
Beta strandi598 – 601Combined sources4
Helixi606 – 612Combined sources7
Helixi615 – 623Combined sources9
Helixi635 – 657Combined sources23
Helixi664 – 667Combined sources4
Helixi671 – 673Combined sources3
Helixi676 – 697Combined sources22
Helixi701 – 713Combined sources13
Helixi714 – 719Combined sources6
Helixi720 – 728Combined sources9
Helixi736 – 756Combined sources21
Turni757 – 759Combined sources3
Helixi761 – 768Combined sources8
Beta strandi775 – 778Combined sources4
Helixi779 – 781Combined sources3
Helixi792 – 817Combined sources26
Helixi824 – 826Combined sources3
Beta strandi827 – 832Combined sources6
Helixi839 – 842Combined sources4
Helixi843 – 845Combined sources3
Helixi849 – 852Combined sources4
Beta strandi855 – 860Combined sources6
Beta strandi868 – 871Combined sources4
Beta strandi874 – 880Combined sources7
Beta strandi882 – 885Combined sources4
Turni887 – 889Combined sources3
Beta strandi892 – 894Combined sources3
Beta strandi897 – 899Combined sources3
Beta strandi902 – 905Combined sources4
Helixi907 – 914Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFYX-ray2.20A1-917[»]
1QU2X-ray2.20A1-917[»]
1QU3X-ray2.90A1-917[»]
ProteinModelPortaliP41972.
SMRiP41972.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41972.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi57 – 67"HIGH" regionAdd BLAST11
Motifi595 – 599"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.

Family and domain databases

CDDicd07960. Anticodon_Ia_Ile_BEm. 1 hit.
Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02002. Ile_tRNA_synth_type1. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR033708. Anticodon_Ile_BEm.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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.
IPR010663. Znf_FPG/IleRS.
[Graphical view]
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.

P41972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYKETLLMP KTDFPMRGGL PNKEPQIQEK WDAEDQYHKA LEKNKGNETF
60 70 80 90 100
ILHDGPPYAN GNLHMGHALN KILKDFIVRY KTMQGFYAPY VPGWDTHGLP
110 120 130 140 150
IEQALTKKGV DRKKMSTAEF REKCKEFALE QIELQKKDFR RLGVRGDFND
160 170 180 190 200
PYITLKPEYE AAQIRIFGEM ADKGLIYKGK KPVYWSPSSE SSLAEAEIEY
210 220 230 240 250
HDKRSASIYV AFNVKDDKGV VDADAKFIIW TTTPWTIPSN VAITVHPELK
260 270 280 290 300
YGQYNVNGEK YIIAEALSDA VAEALDWDKA SIKLEKEYTG KELEYVVAQH
310 320 330 340 350
PFLDRESLVI NGDHVTTDAG TGCVHTAPGH GEDDYIVGQK YELPVISPID
360 370 380 390 400
DKGVFTEEGG QFEGMFYDKA NKAVTDLLTE KGALLKLDFI THSYPHDWRT
410 420 430 440 450
KKPVIFRATP QWFASISKVR QDILDAIENT NFKVNWGKTR IYNMVRDRGE
460 470 480 490 500
WVISRQRVWG VPLPVFYAEN GEIIMTKETV NHVADLFAEH GSNIWFEREA
510 520 530 540 550
KDLLPEGFTH PGSPNGTFTK ETDIMDVWFD SGSSHRGVLE TRPELSFPAD
560 570 580 590 600
MYLEGSDQYR GWFNSSITTS VATRGVSPYK FLLSHGFVMD GEGKKMSKSL
610 620 630 640 650
GNVIVPDQVV KQKGADIARL WVSSTDYLAD VRISDEILKQ TSDVYRKIRN
660 670 680 690 700
TLRFMLGNIN DFNPDTDSIP ESELLEVDRY LLNRLREFTA STINNYENFD
710 720 730 740 750
YLNIYQEVQN FINVELSNFY LDYGKDILYI EQRDSHIRRS MQTVLYQILV
760 770 780 790 800
DMTKLLAPIL VHTAEEVWSH TPHVKEESVH LADMPKVVEV DQALLDKWRT
810 820 830 840 850
FMNLRDDVNR ALETARNEKV IGKSLEAKVT IASNDKFNAS EFLTSFDALH
860 870 880 890 900
QLFIVSQVKV VDKLDDQATA YEHGDIVIEH ADGEKCERCW NYSEDLGAVD
910
ELTHLCPRCQ QVVKSLV
Length:917
Mass (Da):104,885
Last modified:November 1, 1995 - v1
Checksum:i8A2B644A03A85636
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74219 Genomic DNA. Translation: CAA52296.1.
PIRiS40178.
RefSeqiWP_000384706.1. NZ_LWRD01000027.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74219 Genomic DNA. Translation: CAA52296.1.
PIRiS40178.
RefSeqiWP_000384706.1. NZ_LWRD01000027.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFYX-ray2.20A1-917[»]
1QU2X-ray2.20A1-917[»]
1QU3X-ray2.90A1-917[»]
ProteinModelPortaliP41972.
SMRiP41972.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1206.

Chemistry databases

BindingDBiP41972.
ChEMBLiCHEMBL1982.
DrugBankiDB00410. Mupirocin.

Proteomic databases

PRIDEiP41972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C07. Bacteria.
COG0060. LUCA.

Enzyme and pathway databases

BRENDAi6.1.1.5. 3352.
SABIO-RKP41972.

Miscellaneous databases

EvolutionaryTraceiP41972.

Family and domain databases

CDDicd07960. Anticodon_Ia_Ile_BEm. 1 hit.
Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_02002. Ile_tRNA_synth_type1. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR033708. Anticodon_Ile_BEm.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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.
IPR010663. Znf_FPG/IleRS.
[Graphical view]
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]
ProtoNetiSearch...

Entry informationi

Entry nameiSYI1_STAAU
AccessioniPrimary (citable) accession number: P41972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 114 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

3D-structure, Direct protein sequencing

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.