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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).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-adenylateBy similarity
Binding sitei526 – 5261ATPBy similarity

GO - Molecular functioni

  1. aminoacyl-tRNA editing activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  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-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›529›529Isoleucine--tRNA ligasePRO_0000098342Add
BLAST

Proteomic databases

PRIDEiP46207.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP46207.
ModBaseiSearch...
MobiDBiSearch...

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).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

« Hide

        10         20         30         40         50
DTHGLPIERA VEKELSKKKI RKESLPKTEF RKLCREYANR YVNIQKEEFI
60 70 80 90 100
RLGVLGDWEN PYLTMSPEYE ATEIRELGKF FEKGLAYRSK KPVYWCIYDK
110 120 130 140 150
TAEGQAEVEY YEKEDPSIYV KFPLKKEIEG KKAYAVIWTT TPWTLPANLG
160 170 180 190 200
IMVKEDADYS LVEVEGEVWI VAKELLENFF KNIGKTYTRV LKDVKGRDLV
210 220 230 240 250
GLEYEHPFVD RDELKGYLSE ETLKNMWRIY PSEFVSLDTG TGLVHMAPGH
260 270 280 290 300
GQEDYTVGKR YNLEPYAPLD DSGRFVEPAP EFIRGVRVFD ANKLIIALLK
310 320 330 340 350
EKGYLVHEAR IRHSYPHCWR CKNPVIFRAT PQWFIGMDIE YEGKTLSGES
360 370 380 390 400
LEEIEKVKWI PEYGKNRIKS MVENRPDWCI SRQRFWGVPI TVFYCENCGE
410 420 430 440 450
VIKDKEVFER IASLVEKHPG GTDVWFEKSP EEILPEGYKC PKCGGTSFRK
460 470 480 490 500
EEDILDVWFD SGCSHASVIR PLGFEKADLY LEGSDQHRGW FQASLLESVG
510 520
SYGEAPYRSV LTHGFIVDEQ GRKMSKSLV
Length:529
Mass (Da):61,379
Last modified:November 1, 1995 - v1
Checksum:iFB6C40D69E26DDD8
GO

Experimental Info

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: October 29, 2014
This is version 81 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