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Reviewed, UniProtKB/Swiss-Prot P48525 (SYEM_YEAST)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase, mitochondrial
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase
      Short name=GluRS
Gene names
Name: MSE1
Ordered Locus Names: YOL033W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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).

Subcellular location

Mitochondrion matrix.

Miscellaneous

Present with 2940 molecules/cell in log phase SD medium. Ref.3

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmitochondrial glutamyl-tRNA aminoacylation

Inferred by curator. Source: SGD

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399401EBI-18669,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 536536Glutamyl-tRNA synthetase, mitochondrial
PRO_0000119740

Regions

Nucleotide binding291 – 2955ATP By similarity
Region48 – 503Glutamate binding By similarity
Region235 – 2395Glutamate binding By similarity
Motif53 – 619"HIGH" region
Motif291 – 2955"KMSKS" region

Sites

Binding site581ATP By similarity
Binding site841Glutamate By similarity
Binding site2531Glutamate By similarity
Binding site2561ATP By similarity

Experimental info

Sequence conflict4641F → L in AAA61403. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48525-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 5CF36FBAD0E8C58C

FASTA53661,603
        10         20         30         40         50         60 
MIMLRIPTRS YCSPSKLIKG VGLSPLKKSL LSKKIKEDIH PSLPVRTRFA PSPTGFLHLG 

        70         80         90        100        110        120 
SLRTALYNYL LARNTNGQFL LRLEDTDQKR LIEGAEENIY EILKWCNINY DETPIKQSER 

       130        140        150        160        170        180 
KLIYDKYVKI LLSSGKAYRC FCSKERLNDL RHSAMELKPP SMASYDRCCA HLGEEEIKSK 

       190        200        210        220        230        240 
LAQGIPFTVR FKSPERYPTF TDLLHGQINL QPQVNFNDKR YDDLILVKSD KLPTYHLANV 

       250        260        270        280        290        300 
VDDHLMGITH VIRGEEWLPS TPKHIALYNA FGWACPKFIH IPLLTTVGDK KLSKRKGDMS 

       310        320        330        340        350        360 
ISDLKRQGVL PEALINFCAL FGWSPPRDLA SKKHECFSME ELETIFNLNG LTKGNAKVDD 

       370        380        390        400        410        420 
KKLWFFNKHF LQKRILNPST LRELVDDIMP SLESIYNTST ISREKVAKIL LNCGGSLSRI 

       430        440        450        460        470        480 
NDFHDEFYYF FEKPKYNDND AVTKFLSKNE SRHIAHLLKK LGQFQEGTDA QEVESMVETM 

       490        500        510        520        530 
YYENGFSRKV TYQAMRFALA GCHPGAKIAA MIDILGIKES NKRLSEGLQF LQREKK 

« Hide

References

« Hide 'large scale' references
[1]Tzagoloff A.A., Shtanko A.
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 24657 / D273-10B.
[2]"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. expand/collapse author list , 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: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

L39015 Genomic DNA. Translation: AAA61403.1.
Z74775 Genomic DNA. Translation: CAA99033.1.
PIRS66716.
RefSeqNP_014609.1.

3D structure databases

HSSPHSSP built from PDB template 1J09 based on UniProtKB P27000.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6368N.
IntActP48525. 3 interactions.

Genome annotation databases

EnsemblYOL033W. Saccharomyces cerevisiae. [Contig view]
GeneID854124.
GenomeReviewsGene locus YOL033W in contig Y13140_GR.
KEGGsce:YOL033W.
NMPDRfig|4932.3.peg.5702.

Organism-specific databases

CYGDYOL033w.
SGDS000005393. MSE1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP48525.
OMAP48525. PKHIALY.

Enzyme and pathway databases

BRENDA6.1.1.17. 250.

Gene expression databases

GermOnlineYOL033W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio975831.

Entry information

Entry nameSYEM_YEAST
AccessionPrimary (citable) accession number: P48525
Secondary accession number(s): Q08203
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents