P13188 (SYQ_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamine--tRNA ligase
EC=6.1.1.18

Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS

Gene names

Name:	GLN4
Ordered Locus Names:	YOR168W
ORF Names:	O3601

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	809 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).
Miscellaneous	Present with 37500 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutaminyl-tRNA aminoacylation Inferred from mutant phenotype PubMed 2991203. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 15706032. Source: SGD mitochondrion Inferred from direct assay PubMed 15706032. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamine-tRNA ligase activity Inferred from direct assay PubMed 2991203. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-18789,EBI-18789

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 809

809

Glutamine--tRNA ligase

PRO_0000195866

Regions

Motif

258 – 268

11

"HIGH" region

Motif

495 – 499

5

"KMSKS" region

Sites

Binding site

498

1

ATP By similarity

Amino acid modifications

Modified residue

802

1

Phosphoserine Ref.6

Experimental info

Sequence conflict

179

1

G → Q Ref.1

Secondary structure

1

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809

Helix Strand Turn

Details...

Helix

4 – 13

10

Helix

18 – 24

7

Helix

28 – 39

12

Helix

49 – 62

14

Helix

70 – 78

9

Helix

85 – 98

14

Helix

99 – 101

3

Helix

104 – 109

6

Turn

110 – 114

5

Helix

119 – 132

14

Helix

134 – 140

7

Helix

141 – 144

4

Helix

145 – 153

9

Helix

156 – 158

3

Helix

166 – 178

13

Helix

183 – 185

3

Sequences

	Sequence		Length	Mass (Da)
	P13188 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: C7AB13D02BC483F6	FASTA	809	93,133
	10 20 30 40 50 60 MSSVEELTQL FSQVGFEDKK VKEIVKNKKV SDSLYKLIKE TPSDYQWNKS TRALVHNLAS 70 80 90 100 110 120 FVKGTDLPKS ELIVNGIING DLKTSLQVDA AFKYVKANGE ASTKMGMNEN SGVGIEITED 130 140 150 160 170 180 QVRNYVMQYI QENKERILTE RYKLVPGIFA DVKNLKELKW ADPRSFKPII DQEVLKLLGP 190 200 210 220 230 240 KDERDLIKKK TKNNEKKKTN SAKKSSDNSA SSGPKRTMFN EGFLGDLHKV GENPQAYPEL 250 260 270 280 290 300 MKEHLEVTGG KVRTRFPPEP NGYLHIGHSK AIMVNFGYAK YHNGTCYLRF DDTNPEKEAP 310 320 330 340 350 360 EYFESIKRMV SWLGFKPWKI TYSSDYFDEL YRLAEVLIKN GKAYVCHCTA EEIKRGRGIK 370 380 390 400 410 420 EDGTPGGERY ACKHRDQSIE QNLQEFRDMR DGKYKPGEAI LRMKQDLNSP SPQMWDLIAY 430 440 450 460 470 480 RVLNAPHPRT GTKWRIYPTY DFTHCLVDSM ENITHSLCTT EFYLSRESYE WLCDQVHVFR 490 500 510 520 530 540 PAQREYGRLN ITGTVLSKRK IAQLVDEKFV RGWDDPRLFT LEAIRRRGVP PGAILSFINT 550 560 570 580 590 600 LGVTTSTTNI QVVRFESAVR KYLEDTTPRL MFVLDPVEVV VDNLSDDYEE LATIPYRPGT 610 620 630 640 650 660 PEFGERTVPF TNKFYIERSD FSENVDDKEF FRLTPNQPVG LIKVSHTVSF KSLEKDEAGK 670 680 690 700 710 720 IIRIHVNYDN KVEEGSKPKK PKTYIQWVPI SSKYNSPLRV TETRVYNQLF KSENPSSHPE 730 740 750 760 770 780 GFLKDINPES EVVYKESVME HNFGDVVKNS PWVVDSVKNS EFYVEEDKDS KEVCRFQAMR 790 800 VGYFTLDKES TTSKVILNRI VSLKDATSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal extension and provides a strong confirmation of the signature sequence for a group of the aminoacyl-tRNA synthetases." Ludmerer S.W., Schimmel P. J. Biol. Chem. 262:10801-10806(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of a 22,956 bp region on the right arm of Saccharomyces cerevisiae chromosome XV." Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P. Yeast 12:1563-1573(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / FY1678.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-802, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29184 Genomic DNA. Translation: AAA34646.1.
M29185 Genomic DNA. No translation available.
U55021 Genomic DNA. Translation: AAB47415.1.
Z75076 Genomic DNA. Translation: CAA99374.1.
BK006948 Genomic DNA. Translation: DAA10942.1.

PIR

SYBYQT. S67056.

RefSeq

NP_014811.3. NM_001183587.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TL4	X-ray	2.30	X	1-187	[»]

ProteinModelPortal

P13188.

SMR

P13188. Positions 2-187, 250-623.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13188. 1 interaction.

MINT

MINT-663565.

STRING

4932.YOR168W.

Proteomic databases

PaxDb

P13188.

PeptideAtlas

P13188.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR168W; YOR168W; YOR168W.

GeneID

854339.

KEGG

sce:YOR168W.
sce:YOR172W.

Organism-specific databases

CYGD

YOR168w.

SGD

S000005694. GLN4.

Phylogenomic databases

eggNOG

COG0008.

GeneTree

ENSGT00550000074972.

HOGENOM

HOG000259233.

KO

K01886.

OMA

KEVCRFQ.

OrthoDB

EOG4FBN23.

Gene expression databases

Genevestigator

P13188.

GermOnline

YOR168W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth_Ib.
IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
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.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

PANTHER

PTHR10119. PTHR10119. 1 hit.

Pfam

PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PF04558. tRNA_synt_1c_R1. 1 hit.
PF04557. tRNA_synt_1c_R2. 1 hit.
[Graphical view]

PRINTS

PR00987. TRNASYNTHGLU.

SUPFAM

SSF50715. Ribosomal_L25rel. 1 hit.

TIGRFAMs

TIGR00440. glnS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

976411.

Entry information

Entry name

SYQ_YEAST

Accession

Primary (citable) accession number: P13188
Secondary accession number(s): D6W2M6, Q12005

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program