SubmitCancel

Skip Header

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

Q2YXH4

- SYI_STAAB

UniProt

Q2YXH4 - SYI_STAAB

(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, SAB1057
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei554 – 5541Aminoacyl-adenylate By similarity
Binding sitei598 – 5981ATP By similarity
Metal bindingi886 – 8861Zinc By similarity
Metal bindingi889 – 8891Zinc By similarity
Metal bindingi906 – 9061Zinc By similarity
Metal bindingi909 – 9091Zinc By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. aminoacyl-tRNA editing activity Source: InterPro
  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

BioCyciSAUR273036:GJVS-1079-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:SAB1057
OrganismiStaphylococcus aureus (strain bovine RF122 / ET3-1)
Taxonomic identifieri273036 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001927: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 917917Isoleucine--tRNA ligaseUniRule annotation
PRO_1000022130Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi273036.SAB1057.

Structurei

3D structure databases

ProteinModelPortaliQ2YXH4.
SMRiQ2YXH4. Positions 1-917.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 6711"HIGH" regionUniRule annotation
Add
BLAST
Motifi595 – 5995"KMSKS" regionUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0060.
HOGENOMiHOG000246402.
KOiK01870.
OMAiLGHRVHY.
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.

Q2YXH4-1 [UniParc]FASTAAdd to Basket

« Hide

MDYKETLLMP KTDFPMRGGL PNKEPQIQEK WDAEDQYHKA LEKNKGNETF    50
ILHDGPPYAN GNLHMGHALN KILKDFIVRY KTMQGFYAPY VPGWDTHGLP 100
IEQALTKKGV DRKKMSTAEF REKCKEFALE QIELQKKDFR RLGVRGDFND 150
PYITLKPEYE AAQIRIFGEM ADKGLIYKGK KPVYWSPSSE SSLAEAEIEY 200
HDKRSASIYV AFDVKDDKGV VDADAKFIIW TTTPWTIPSN VAITVHPELK 250
YGQYNVNGEK YIIAEALSDA VAEALDWDKA SIELEKEYTG KELEYVVAQH 300
PFLDRESLVI NGDHVTTDAG TGCVHTAPGH GEDDYIVGQK YELPVISPID 350
DKGVFTEEGG QFEGMFYDKA NKAVTDLLTE KGALLKLDFI THSYPHDWRT 400
KKPVIFRATP QWFASISKVR QDILDAIENT NFKVNWGKTR IYNMVRDRGE 450
WVISRQRVWG VPLPVFYAEN GEIIMTKETV NHVADLFAEH GSNIWFEREA 500
KDLLPEGFTH PGSPNGTFTK ETDIMDVWFD SGSSHRGVLE TRPELSFPAD 550
MYLEGSDQYR GWFNSSITTS VATRGVSPYK FLLSHGFVMD GEGKKMSKSL 600
GNVIVPDQVV KQKGADIARL WVSSTDYLAD VRISDEILKQ TSDVYRKIRN 650
TLRFMLGNIN DFNPDTDSIP ESELLEVDRY LLNRLREFTA STINNYENFD 700
YLNIYQEVQN FLNVELSNFY LDYGKDILYI EQRDSHIRRS MQTVLYQILV 750
DMTKLLAPIL VHTAEEVWSH TPHVKEESVH LADMPKVVEV DQALLDKWRT 800
FMNLRDDVNR ALETARNEKV IGKSLEAKVT IASNDKFNAS EFLTSFDALH 850
QLFIVSQVKV VDKLDDQATA YEHGDIVIEH ADGEKCERCW NYSEDLGAVD 900
ELTHLCPRCQ QVVKSLV 917
Length:917
Mass (Da):104,886
Last modified:December 20, 2005 - v1
Checksum:i006C53E3FD5BAD1F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ938182 Genomic DNA. Translation: CAI80746.1.
RefSeqiYP_416540.1. NC_007622.1.

Genome annotation databases

EnsemblBacteriaiCAI80746; CAI80746; SAB1057.
GeneIDi3795257.
KEGGisab:SAB1057.
PATRICi19522949. VBIStaAur92441_1123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ938182 Genomic DNA. Translation: CAI80746.1 .
RefSeqi YP_416540.1. NC_007622.1.

3D structure databases

ProteinModelPortali Q2YXH4.
SMRi Q2YXH4. Positions 1-917.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273036.SAB1057.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAI80746 ; CAI80746 ; SAB1057 .
GeneIDi 3795257.
KEGGi sab:SAB1057.
PATRICi 19522949. VBIStaAur92441_1123.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SAUR273036:GJVS-1079-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. "Molecular correlates of host specialization in Staphylococcus aureus."
    Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
    PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: bovine RF122 / ET3-1.

Entry informationi

Entry nameiSYI_STAAB
AccessioniPrimary (citable) accession number: Q2YXH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 71 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

Similar proteinsi