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.

P67508

- SYI_STAAM

UniProt

P67508 - SYI_STAAM

(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, SAV1193
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 3 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.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

BioCyciSAUR158878:GJJ5-1211-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:SAV1193
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002481: 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_0000098467Add
BLAST

Proteomic databases

PRIDEiP67508.

2D gel databases

World-2DPAGE0002:P67508.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi158878.SAV1193.

Structurei

3D structure databases

ProteinModelPortaliP67508.
SMRiP67508. 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.
KOiK01870.
OMAiKPVHWCL.
OrthoDBiEOG644ZM1.
PhylomeDBiP67508.

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.

P67508-1 [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 SIKLEKEYTG 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 FINVELSNFY 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:October 11, 2004 - v1
Checksum:i800E8384630FB0FC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB57355.1.
RefSeqiNP_371717.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57355; BAB57355; SAV1193.
GeneIDi1121170.
KEGGisav:SAV1193.
PATRICi19563097. VBIStaAur52173_1226.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB57355.1 .
RefSeqi NP_371717.1. NC_002758.2.

3D structure databases

ProteinModelPortali P67508.
SMRi P67508. Positions 1-917.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158878.SAV1193.

2D gel databases

World-2DPAGE 0002:P67508.

Proteomic databases

PRIDEi P67508.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB57355 ; BAB57355 ; SAV1193 .
GeneIDi 1121170.
KEGGi sav:SAV1193.
PATRICi 19563097. VBIStaAur52173_1226.

Phylogenomic databases

eggNOGi COG0060.
KOi K01870.
OMAi KPVHWCL.
OrthoDBi EOG644ZM1.
PhylomeDBi P67508.

Enzyme and pathway databases

BioCyci SAUR158878:GJJ5-1211-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.

Entry informationi

Entry nameiSYI_STAAM
AccessioniPrimary (citable) accession number: P67508
Secondary accession number(s): Q99US4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 74 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