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P46207

- SYI_AQUPY

UniProt

P46207 - SYI_AQUPY

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Protein
Isoleucine--tRNA ligase
Gene
ileS
Organism
Aquifex pyrophilus
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei482 – 4821Aminoacyl-adenylate By similarity
Binding sitei526 – 5261ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. aminoacyl-tRNA editing activity Source: InterPro
  3. isoleucine-tRNA ligase activity Source: UniProtKB-EC

GO - Biological processi

  1. isoleucyl-tRNA aminoacylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiAquifex pyrophilus
Taxonomic identifieri2714 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex

Subcellular locationi

Cytoplasm By similarity

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
Chaini‹1 – ›529›529Isoleucine--tRNA ligase
PRO_0000098342Add
BLAST

Proteomic databases

PRIDEiP46207.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP46207.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi523 – 5275"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.

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
InterProiIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamiPF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSiPR00984. TRNASYNTHILE.
SUPFAMiSSF50677. SSF50677. 1 hit.

Sequencei

Sequence statusi: Fragment.

P46207-1 [UniParc]FASTAAdd to Basket

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DTHGLPIERA VEKELSKKKI RKESLPKTEF RKLCREYANR YVNIQKEEFI    50
RLGVLGDWEN PYLTMSPEYE ATEIRELGKF FEKGLAYRSK KPVYWCIYDK 100
TAEGQAEVEY YEKEDPSIYV KFPLKKEIEG KKAYAVIWTT TPWTLPANLG 150
IMVKEDADYS LVEVEGEVWI VAKELLENFF KNIGKTYTRV LKDVKGRDLV 200
GLEYEHPFVD RDELKGYLSE ETLKNMWRIY PSEFVSLDTG TGLVHMAPGH 250
GQEDYTVGKR YNLEPYAPLD DSGRFVEPAP EFIRGVRVFD ANKLIIALLK 300
EKGYLVHEAR IRHSYPHCWR CKNPVIFRAT PQWFIGMDIE YEGKTLSGES 350
LEEIEKVKWI PEYGKNRIKS MVENRPDWCI SRQRFWGVPI TVFYCENCGE 400
VIKDKEVFER IASLVEKHPG GTDVWFEKSP EEILPEGYKC PKCGGTSFRK 450
EEDILDVWFD SGCSHASVIR PLGFEKADLY LEGSDQHRGW FQASLLESVG 500
SYGEAPYRSV LTHGFIVDEQ GRKMSKSLV 529
Length:529
Mass (Da):61,379
Last modified:November 1, 1995 - v1
Checksum:iFB6C40D69E26DDD8
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei529 – 5291

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L37096 Genomic DNA. Translation: AAA87287.1.
PIRiI39658.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L37096 Genomic DNA. Translation: AAA87287.1 .
PIRi I39658.

3D structure databases

ProteinModelPortali P46207.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P46207.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
InterProi IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view ]
PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
Pfami PF00133. tRNA-synt_1. 1 hit.
[Graphical view ]
PRINTSi PR00984. TRNASYNTHILE.
SUPFAMi SSF50677. SSF50677. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications."
    Brown J.R., Doolittle W.F.
    Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiSYI_AQUPY
AccessioniPrimary (citable) accession number: P46207
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3