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P13188

- SYQ_YEAST

UniProt

P13188 - SYQ_YEAST

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Protein

Glutamine--tRNA ligase

Gene

GLN4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei498 – 4981ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamine-tRNA ligase activity Source: SGD

GO - Biological processi

  1. glutaminyl-tRNA aminoacylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33684-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine--tRNA ligase (EC:6.1.1.18)
Alternative name(s):
Glutaminyl-tRNA synthetase
Short name:
GlnRS
Gene namesi
Name:GLN4
Ordered Locus Names:YOR168W
ORF Names:O3601
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR168w.
SGDiS000005694. GLN4.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. mitochondrion Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 809809Glutamine--tRNA ligasePRO_0000195866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei378 – 3781Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP13188.
PaxDbiP13188.
PeptideAtlasiP13188.

Expressioni

Gene expression databases

GenevestigatoriP13188.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-18789,EBI-18789

Protein-protein interaction databases

BioGridi34564. 19 interactions.
IntActiP13188. 1 interaction.
MINTiMINT-663565.
STRINGi4932.YOR168W.

Structurei

Secondary structure

1
809
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1310Combined sources
Helixi18 – 247Combined sources
Helixi28 – 3912Combined sources
Helixi49 – 6214Combined sources
Helixi70 – 789Combined sources
Helixi85 – 9814Combined sources
Helixi99 – 1013Combined sources
Helixi104 – 1096Combined sources
Turni110 – 1145Combined sources
Helixi119 – 13214Combined sources
Helixi134 – 1407Combined sources
Helixi141 – 1444Combined sources
Helixi145 – 1539Combined sources
Helixi156 – 1583Combined sources
Helixi166 – 17813Combined sources
Helixi183 – 1853Combined sources
Helixi222 – 2254Combined sources
Helixi238 – 2403Combined sources
Helixi241 – 2488Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi260 – 2623Combined sources
Helixi267 – 28115Combined sources
Beta strandi285 – 2906Combined sources
Helixi300 – 31213Combined sources
Beta strandi318 – 3225Combined sources
Helixi323 – 3264Combined sources
Helixi327 – 33913Combined sources
Beta strandi343 – 3464Combined sources
Helixi350 – 3567Combined sources
Helixi373 – 3764Combined sources
Helixi379 – 39012Combined sources
Beta strandi400 – 4034Combined sources
Helixi412 – 4143Combined sources
Beta strandi418 – 4225Combined sources
Turni428 – 4303Combined sources
Beta strandi435 – 4384Combined sources
Helixi440 – 45011Combined sources
Beta strandi456 – 4594Combined sources
Helixi460 – 4656Combined sources
Helixi466 – 47510Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi489 – 4946Combined sources
Helixi498 – 5069Combined sources
Beta strandi509 – 5124Combined sources
Helixi521 – 5277Combined sources
Helixi531 – 54111Combined sources
Beta strandi548 – 5514Combined sources
Helixi552 – 56615Combined sources
Beta strandi572 – 58110Combined sources
Beta strandi590 – 5978Combined sources
Helixi601 – 6033Combined sources
Beta strandi605 – 6106Combined sources
Beta strandi612 – 6176Combined sources
Helixi618 – 6203Combined sources
Beta strandi632 – 6343Combined sources
Beta strandi639 – 6413Combined sources
Beta strandi648 – 6558Combined sources
Beta strandi661 – 6688Combined sources
Helixi692 – 6943Combined sources
Beta strandi698 – 7069Combined sources
Beta strandi709 – 7135Combined sources
Helixi715 – 7173Combined sources
Helixi722 – 7254Combined sources
Beta strandi730 – 73910Combined sources
Helixi743 – 7486Combined sources
Helixi755 – 7584Combined sources
Helixi771 – 7733Combined sources
Beta strandi776 – 7783Combined sources
Turni779 – 7813Combined sources
Beta strandi782 – 7865Combined sources
Beta strandi792 – 7943Combined sources
Beta strandi796 – 8016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TL4X-ray2.30X1-187[»]
4H3SX-ray2.15A1-809[»]
ProteinModelPortaliP13188.
SMRiP13188. Positions 2-187, 215-809.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi258 – 26811"HIGH" regionAdd
BLAST
Motifi495 – 4995"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
GeneTreeiENSGT00550000074972.
HOGENOMiHOG000259233.
InParanoidiP13188.
KOiK01886.
OMAiRMQKRAK.
OrthoDBiEOG7MD4ZK.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth.
IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. 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]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF50715. SSF50715. 1 hit.
TIGRFAMsiTIGR00440. glnS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13188-1 [UniParc]FASTAAdd to Basket

« Hide

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

VSLKDATSK
Length:809
Mass (Da):93,133
Last modified:November 1, 1997 - v2
Checksum:iC7AB13D02BC483F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791G → Q(PubMed:3301841)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS67056. SYBYQT.
RefSeqiNP_014811.3. NM_001183587.3.

Genome annotation databases

EnsemblFungiiYOR168W; YOR168W; YOR168W.
GeneIDi854339.
KEGGisce:YOR168W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S67056. SYBYQT.
RefSeqi NP_014811.3. NM_001183587.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TL4 X-ray 2.30 X 1-187 [» ]
4H3S X-ray 2.15 A 1-809 [» ]
ProteinModelPortali P13188.
SMRi P13188. Positions 2-187, 215-809.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34564. 19 interactions.
IntActi P13188. 1 interaction.
MINTi MINT-663565.
STRINGi 4932.YOR168W.

Proteomic databases

MaxQBi P13188.
PaxDbi P13188.
PeptideAtlasi P13188.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOR168W ; YOR168W ; YOR168W .
GeneIDi 854339.
KEGGi sce:YOR168W.

Organism-specific databases

CYGDi YOR168w.
SGDi S000005694. GLN4.

Phylogenomic databases

eggNOGi COG0008.
GeneTreei ENSGT00550000074972.
HOGENOMi HOG000259233.
InParanoidi P13188.
KOi K01886.
OMAi RMQKRAK.
OrthoDBi EOG7MD4ZK.

Enzyme and pathway databases

BioCyci YEAST:G3O-33684-MONOMER.

Miscellaneous databases

NextBioi 976411.
PROi P13188.

Gene expression databases

Genevestigatori P13188.

Family and domain databases

Gene3Di 1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth.
IPR007638. Gln-tRNA-synth_Ib_RNA-bd_2.
IPR007639. Gln-tRNA-synth_Ib_RNA-bd_N.
IPR000924. Glu/Gln-tRNA-synth.
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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami 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 ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF50715. SSF50715. 1 hit.
TIGRFAMsi TIGR00440. glnS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYQ_YEAST
AccessioniPrimary (citable) accession number: P13188
Secondary accession number(s): D6W2M6, Q12005
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 37500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3