P46655 (SYEC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase, cytoplasmic
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
P85

Gene names

Name:	GUS1
Ordered Locus Names:	YGL245W
ORF Names:	G0583, HRB724

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	708 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity.
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
Subunit structure	Interacts with ARC1. Ref.10 Ref.11
Subcellular location	Cytoplasm Ref.7.
Miscellaneous	Present with 48700 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.
Sequence caution	The sequence AAA78905.1 differs from that shown. Reason: Frameshift at position 698. The sequence CAA64142.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA89009.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA96964.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from direct assay. Source: SGD
Cellular component	methionyl glutamyl tRNA synthetase complex Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 708

708

Glutamate--tRNA ligase, cytoplasmic

PRO_0000119739

Regions

Nucleotide binding

437 – 441

5

ATP By similarity

Region

205 – 207

3

Glutamate binding By similarity

Region

382 – 386

5

Glutamate binding By similarity

Motif

210 – 219

10

"HIGH" region

Motif

437 – 441

5

"KMSKS" region

Sites

Binding site

215

1

ATP By similarity

Binding site

241

1

Glutamate By similarity

Binding site

400

1

Glutamate By similarity

Binding site

403

1

ATP By similarity

Amino acid modifications

Modified residue

300

1

Phosphothreonine Ref.9

Modified residue

472

1

Phosphothreonine Ref.9

Experimental info

Sequence conflict

209

1

E → D in AAA78905. Ref.1

Sequence conflict

473

1

V → A in AAA78905. Ref.1

Sequence conflict

510

1

P → S in AAA78905. Ref.1

Sequence conflict

546

1

V → M in AAA78905. Ref.1

Secondary structure

1

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708

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

16 – 28

13

Beta strand

32 – 38

7

Beta strand

45 – 48

4

Helix

55 – 62

8

Turn

63 – 66

4

Helix

72 – 84

13

Turn

85 – 87

3

Helix

91 – 104

14

Helix

119 – 130

12

Helix

134 – 140

7

Helix

144 – 154

11

Helix

157 – 160

4

Helix

162 – 177

16

Sequences

	Sequence		Length	Mass (Da)
	P46655 [UniParc]. Last modified September 5, 2006. Version 3. Checksum: EADAD430A2D98974	FASTA	708	80,843
	10 20 30 40 50 60 MPSTLTINGK APIVAYAELI AARIVNALAP NSIAIKLVDD KKAPAAKLDD ATEDVFNKIT 70 80 90 100 110 120 SKFAAIFDNG DKEQVAKWVN LAQKELVIKN FAKLSQSLET LDSQLNLRTF ILGGLKYSAA 130 140 150 160 170 180 DVACWGALRS NGMCGSIIKN KVDVNVSRWY TLLEMDPIFG EAHDFLSKSL LELKKSANVG 190 200 210 220 230 240 KKKETHKANF EIDLPDAKMG EVVTRFPPEP SGYLHIGHAK AALLNQYFAQ AYKGKLIIRF 250 260 270 280 290 300 DDTNPSKEKE EFQDSILEDL DLLGIKGDRI TYSSDYFQEM YDYCVQMIKD GKAYCDDTPT 310 320 330 340 350 360 EKMREERMDG VASARRDRSV EENLRIFTEE MKNGTEEGLK NCVRAKIDYK ALNKTLRDPV 370 380 390 400 410 420 IYRCNLTPHH RTGSTWKIYP TYDFCVPIVD AIEGVTHALR TIEYRDRNAQ YDWMLQALRL 430 440 450 460 470 480 RKVHIWDFAR INFVRTLLSK RKLQWMVDKD LVGNWDDPRF PTVRGVRRRG MTVEGLRNFV 490 500 510 520 530 540 LSQGPSRNVI NLEWNLIWAF NKKVIDPIAP RHTAIVNPVK IHLEGSEAPQ EPKIEMKPKH 550 560 570 580 590 600 KKNPAVGEKK VIYYKDIVVD KDDADVINVD EEVTLMDWGN VIITKKNDDG SMVAKLNLEG 610 620 630 640 650 660 DFKKTKHKLT WLADTKDVVP VDLVDFDHLI TKDRLEEDES FEDFLTPQTE FHTDAIADLN 670 680 690 700 VKDMKIGDII QFERKGYYRL DALPKDGKPY VFFTIPDGKS VNKYGAKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence characterization of the gene encoding the yeast cytosolic glutamyl-tRNA synthetase." Frantz J.D., Gilbert W. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left arm of chromosome VII, reveals the presence of eight open reading frames." Vandenbol M., Durand P., Portetelle D., Hilger F. Yeast 11:1519-1523(1995) [PubMed: 8750240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae." Coissac E., Maillier E., Robineau S., Netter P. Yeast 12:1555-1562(1996) [PubMed: 8972578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129. Strain: ATCC 96604 / S288c / FY1679.
[6]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed: 12748633] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-300 AND THR-472, MASS SPECTROMETRY.
[10]	"Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold." Simader H., Hothorn M., Suck D. Acta Crystallogr. D 62:1510-1519(2006) [PubMed: 17139087] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-191, INTERACTION WITH ARC1.
[11]	"Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes." Simader H., Hothorn M., Koehler C., Basquin J., Simos G., Suck D. Nucleic Acids Res. 34:3968-3979(2006) [PubMed: 16914447] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-191, INTERACTION WITH ARC1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U32265 Genomic DNA. Translation: AAA78905.1. Sequence problems.
Z49149 Genomic DNA. Translation: CAA89009.1. Different initiation.
Z72767 Genomic DNA. Translation: CAA96964.1. Different initiation.
X94357 Genomic DNA. Translation: CAA64142.1. Different initiation.
BK006941 Genomic DNA. Translation: DAA07874.1.

PIR

S53934.

RefSeq

NP_011269.2. NM_001181111.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HRA	X-ray	1.90	A/B	1-191	[»]
2HRK	X-ray	2.05	A	1-191	[»]
2HSM	X-ray	3.00	A	1-191	[»]

ProteinModelPortal

P46655.

SMR

P46655. Positions 1-180, 191-701.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2212N.

IntAct

P46655. 32 interactions.

MINT

MINT-491904.

STRING

P46655.

Proteomic databases

PeptideAtlas

P46655.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL245W; YGL245W; YGL245W.

GeneID

852606.

KEGG

sce:YGL245W.

NMPDR

fig|4932.3.peg.2372.

Organism-specific databases

CYGD

YGL245w.

SGD

S000003214. GUS1.

Phylogenomic databases

eggNOG

fuNOG06587.

GeneTree

EFGT00050000004689.

HOGENOM

HBG334108.

OMA

LEGDFRK.

OrthoDB

EOG4ZSDBB.

Enzyme and pathway databases

BRENDA

6.1.1.17. 984.

Gene expression databases

ArrayExpress

P46655.

Genevestigator

P46655.

GermOnline

YGL245W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_Ib_arc/euk.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:2.40.240.10. Rbsml_L25/Gln-tRNA_synth_b-brl. 2 hits.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.

KO

K01885.

PANTHER

PTHR10119. Glu_tRNA-synt_1c. 1 hit.

Pfam

PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]

PRINTS

PR00987. TRNASYNTHGLU.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF50715. Ribosomal_L25rel. 1 hit.

TIGRFAMs

TIGR00463. GltX_arch. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

971793.

Entry information

Entry name

SYEC_YEAST

Accession

Primary (citable) accession number: P46655
Secondary accession number(s): D6VV90

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program