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P48525 (SYEM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase, mitochondrial

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:MSE1
Ordered Locus Names:YOL033W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
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.4

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
Reference 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 536536Glutamate--tRNA ligase, 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 [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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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

EMBL
GenBank
DDBJ
L39015 Genomic DNA. Translation: AAA61403.1.
Z74775 Genomic DNA. Translation: CAA99033.1.
BK006948 Genomic DNA. Translation: DAA10748.1.
PIRS66716.
RefSeqNP_014609.1. NM_001183287.1.

3D structure databases

ProteinModelPortalP48525.
SMRP48525. Positions 45-529.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6368N.
IntActP48525. 2 interactions.
MINTMINT-607917.
STRINGP48525.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL033W; YOL033W; YOL033W.
GeneID854124.
KEGGsce:YOL033W.
NMPDRfig|4932.3.peg.5702.

Organism-specific databases

CYGDYOL033w.
SGDS000005393. MSE1.

Phylogenomic databases

eggNOGfuNOG06505.
GeneTreeEFGT00050000004690.
HOGENOMHBG628189.
OMAFEDLLHG.
OrthoDBEOG4GMZ5K.

Gene expression databases

ArrayExpressP48525.
GenevestigatorP48525.
GermOnlineYOL033W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio975831.

Entry information

Entry nameSYEM_YEAST
AccessionPrimary (citable) accession number: P48525
Secondary accession number(s): D6W232, Q08203
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families