ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P48525


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SYEM_YEAST
Primary accession number P48525
Secondary accession number Q08203
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 66)
Name and origin of the protein
Protein name Glutamyl-tRNA synthetase, mitochondrial
Synonyms EC 6.1.1.17
Glutamate--tRNA ligase
GluRS
Gene name
Name: MSE1
OrderedLocusNames: YOL033W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 24657 / D273-10B;
Tzagoloff A.A., Shtanko A.;
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L39015; AAA61403.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74775; CAA99033.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S66716; S66716.
RefSeq NP_014609.1; -.
3D structure databases
HSSP P27000; 1J09. [HSSP ENTRY / PDB]
ModBase P48525.
Protein-protein interaction databases
DIP DIP:6368N; -.
IntAct P48525; 2.
Organism-specific databases
CYGD YOL033w; -.
SGD S000005393; MSE1.
Yeast-GFP YOL033W.
Gene expression databases
GermOnline YOL033W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004818; Molecular function: glutamate-tRNA ligase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006424; Biological process: glutamyl-tRNA aminoacylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR008925; 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 of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
G3DSA:1.10.10.350; tRNA_synt_bd; 1.
PANTHER PTHR10119; Glu_tRNA-synt_1c; 1.
Pfam PF00749; tRNA-synt_1c; 1.
Pfam graphical view of domain structure.
PRINTS PR00987; TRNASYNTHGLU.
TIGRFAMs TIGR00464; gltX_bact; 1.
PROSITE PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
Genome annotation databases
Ensembl YOL033W; Saccharomyces cerevisiae. [Contig view]
GeneID 854124; -.
GenomeReviews Y13140_GR; YOL033W.
KEGG sce:YOL033W; -.
NMPDR fig|4932.3.peg.5702; -.
Phylogenomic databases
HOGENOM P48525; -.
Other
LinkHub P48525; -.
NextBio 975831; -.
ProtoNet P48525.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   536  536     Glutamyl-tRNA synthetase, mitochondrial. PRO_0000119740
MOTIF   53    61  9     "HIGH" region. 
CONFLICT   464   464        F -> L (in Ref. 1; AAA61403). 
Sequence information
Length: 536 AA [This is the length of the unprocessed precursor] Molecular weight: 61603 Da [This is the MW of the unprocessed precursor] CRC64: 5CF36FBAD0E8C58C [This is a checksum on the sequence]
        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 

P48525 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!