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Q9HDX9 (SYEM_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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
ORF Names:SPAPB1A10.11c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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. HAMAP-Rule MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022_B

Subcellular location

Mitochondrion Ref.2.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion Potential
Chain39 – 526488Glutamate--tRNA ligase, mitochondrial HAMAP-Rule MF_00022_B
PRO_0000314764

Regions

Nucleotide binding278 – 2825ATP By similarity
Region37 – 393Glutamate binding By similarity
Region222 – 2265Glutamate binding By similarity
Motif42 – 509"HIGH" region HAMAP-Rule MF_00022_B
Motif278 – 2825"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site471ATP By similarity
Binding site731Glutamate By similarity
Binding site2401Glutamate By similarity
Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HDX9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F8F34F510B43A2F4

FASTA52660,645
        10         20         30         40         50         60 
MLSYTSCAKL ICSRYIVSKI SFYSLKRCNS TAVVRTRFAP SPTGFLHLGS LRTALFNYLW 

        70         80         90        100        110        120 
AKKSNGKFIL RLEDTDQKRK VTGSDLEIYK VLKQFNLQWD EGPIVGGPYG PYEQSSRLQI 

       130        140        150        160        170        180 
YQKYAQHLIE TGRAYVSYSV PIATTKIDSS TKYHEISIDD LTDAQRKLYK SKKFPYVVRF 

       190        200        210        220        230        240 
RMKEPSPFTD LVYGKIAIKS DSREIEESNN FVILKSDGFP TYHFANVVDD HLMHITHVIR 

       250        260        270        280        290        300 
GEEWVPSTIK HIQLYEAFGW KPPKFAHLPL LVNPDGSKLS KRQNDAHVSS LLQEGFLPEA 

       310        320        330        340        350        360 
ILNFIALMGW SSRQKSDFLP MKELIDLFSI DKLTKSSSIV AFEKLYFLNK NYLRRAISDV 

       370        380        390        400        410        420 
NRLDELIELV QPRLIQKFSH SSRSHDKSYT KKLLLLLKNK VHTIKEFEKI VFYFYEASDL 

       430        440        450        460        470        480 
QQIRSLVSSL ITVEELPKIL TTILNKFETI EWNTHEIQIS LKEIAMEHQM PLKKIQSLLR 

       490        500        510        520 
YGLCGNLPGG GISDTISLLG KETVKSRLER LLLSLKHELP KRSCIV 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAC21484.1.
RefSeqNP_593525.1. NM_001018959.2.

3D structure databases

ProteinModelPortalQ9HDX9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279816. 3 interactions.
IntActQ9HDX9. 3 interactions.
MINTMINT-4702716.
STRING4896.SPAPB1A10.11c-1.

Proteomic databases

MaxQBQ9HDX9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAPB1A10.11c.1; SPAPB1A10.11c.1:pep; SPAPB1A10.11c.
GeneID2543394.
KEGGspo:SPAPB1A10.11c.

Organism-specific databases

PomBaseSPAPB1A10.11c.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAKKLWFFN.
OrthoDBEOG76MKJ7.
PhylomeDBQ9HDX9.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
ProtoNetSearch...

Other

NextBio20804409.
PROQ9HDX9.

Entry information

Entry nameSYEM_SCHPO
AccessionPrimary (citable) accession number: Q9HDX9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries