Q7SIA2 (SYEP_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional glutamate/proline--tRNA ligase

Alternative name(s):
Bifunctional aminoacyl-tRNA synthetase

Including the following 2 domains:

1. Glutamate--tRNA ligase
   EC=6.1.1.17
   Alternative name(s):
   Glutamyl-tRNA synthetase
   Short name=GluRS
2. Proline--tRNA ligase
   EC=6.1.1.15
   Alternative name(s):
   Prolyl-tRNA synthetase
   Short name=ProRS

Gene names

Name:	EPRS
Synonyms:	QPRS

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	49 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation By similarity.
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
Subunit structure	Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L. Component of the GAIT complex By similarity.
Domain	The WHEP-TRS domain is involved in RNA binding.
Post-translational modification	Phosphorylated in a IFN-gamma-dependent manner; the phosphorylation is causing release from the multisynthetase complex, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition.
Sequence similarities	Contains at least 1 WHEP-TRS domain.

Ontologies

Keywords
Biological process	Protein biosynthesis Translation regulation
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Phosphoprotein
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Biological_process	regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA stem-loop binding Inferred from sequence or structural similarity. Source: UniProtKB glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC proline-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

‹1 – ›49

›49

Bifunctional glutamate/proline--tRNA ligase

PRO_0000119742

Regions

Domain

‹1 – ›49

›49

WHEP-TRS

Amino acid modifications

Modified residue

46

1

Phosphotyrosine By similarity

Experimental info

Non-terminal residue

1

1

Non-terminal residue

49

1

Secondary structure

1

.

.

.

.

.

.

.

49

Helix Strand Turn

Details...

Helix

2 – 16

15

Helix

21 – 38

18

Beta strand

40 – 45

6

Sequences

	Sequence		Length	Mass (Da)
	Q7SIA2 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: A8B609A53C7E695A	FASTA	49	5,409
	10 20 30 40 YDKIAAQGEV VRKLKAEKAP KAKVTEAVEC LLSLKAEYKE KTGKEYVPG

References

[1]	"A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases." Cahuzac B., Berthonneau E., Birlirakis N., Guittet E., Mirande M. EMBO J. 19:445-452(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-49, RNA-BINDING SITE.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D2D	NMR	-	A	1-49	[»]
1R1B	NMR	-	A	1-49	[»]

ProteinModelPortal

Q7SIA2.

SMR

Q7SIA2. Positions 1-49.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.287.10. 1 hit.

InterPro

IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR009068. S15_NS1_RNA-bd.
IPR000738. WHEP-TRS.
[Graphical view]

PANTHER

PTHR10119. PTHR10119. 1 hit.

Pfam

PF00458. WHEP-TRS. 1 hit.
[Graphical view]

SMART

SM00991. WHEP-TRS. 1 hit.
[Graphical view]

SUPFAM

SSF47060. S15/NS1_bind. 1 hit.

PROSITE

PS00762. WHEP_TRS_1. Partial match.
PS51185. WHEP_TRS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q7SIA2.

Entry information

Entry name

SYEP_CRIGR

Accession

Primary (citable) accession number: Q7SIA2
Secondary accession number(s): Q7SIG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	April 3, 2013
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program