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Protein

Glutamate--tRNA ligase, mitochondrial

Gene

mse1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471ATPBy similarity
Binding sitei73 – 731GlutamateBy similarity
Binding sitei240 – 2401GlutamateBy similarity
Binding sitei243 – 2431ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi278 – 2825ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase, mitochondrial (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:mse1
ORF Names:SPAPB1A10.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAPB1A10.11c.
PomBaseiSPAPB1A10.11c. mse1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionSequence AnalysisAdd
BLAST
Chaini39 – 526488Glutamate--tRNA ligase, mitochondrialPRO_0000314764Add
BLAST

Proteomic databases

MaxQBiQ9HDX9.

Interactioni

Protein-protein interaction databases

BioGridi279816. 3 interactions.
IntActiQ9HDX9. 3 interactions.
MINTiMINT-4702716.
STRINGi4896.SPAPB1A10.11c.1.

Structurei

3D structure databases

ProteinModelPortaliQ9HDX9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 393Glutamate bindingBy similarity
Regioni222 – 2265Glutamate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 509"HIGH" region
Motifi278 – 2825"KMSKS" region

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
InParanoidiQ9HDX9.
KOiK01885.
OMAiHSGPEFD.
OrthoDBiEOG76MKJ7.
PhylomeDBiQ9HDX9.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9HDX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSYTSCAKL ICSRYIVSKI SFYSLKRCNS TAVVRTRFAP SPTGFLHLGS
60 70 80 90 100
LRTALFNYLW AKKSNGKFIL RLEDTDQKRK VTGSDLEIYK VLKQFNLQWD
110 120 130 140 150
EGPIVGGPYG PYEQSSRLQI YQKYAQHLIE TGRAYVSYSV PIATTKIDSS
160 170 180 190 200
TKYHEISIDD LTDAQRKLYK SKKFPYVVRF RMKEPSPFTD LVYGKIAIKS
210 220 230 240 250
DSREIEESNN FVILKSDGFP TYHFANVVDD HLMHITHVIR GEEWVPSTIK
260 270 280 290 300
HIQLYEAFGW KPPKFAHLPL LVNPDGSKLS KRQNDAHVSS LLQEGFLPEA
310 320 330 340 350
ILNFIALMGW SSRQKSDFLP MKELIDLFSI DKLTKSSSIV AFEKLYFLNK
360 370 380 390 400
NYLRRAISDV NRLDELIELV QPRLIQKFSH SSRSHDKSYT KKLLLLLKNK
410 420 430 440 450
VHTIKEFEKI VFYFYEASDL QQIRSLVSSL ITVEELPKIL TTILNKFETI
460 470 480 490 500
EWNTHEIQIS LKEIAMEHQM PLKKIQSLLR YGLCGNLPGG GISDTISLLG
510 520
KETVKSRLER LLLSLKHELP KRSCIV
Length:526
Mass (Da):60,645
Last modified:March 1, 2001 - v1
Checksum:iF8F34F510B43A2F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC21484.1.
RefSeqiNP_593525.1. NM_001018959.2.

Genome annotation databases

EnsemblFungiiSPAPB1A10.11c.1; SPAPB1A10.11c.1:pep; SPAPB1A10.11c.
GeneIDi2543394.
KEGGispo:SPAPB1A10.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAC21484.1.
RefSeqiNP_593525.1. NM_001018959.2.

3D structure databases

ProteinModelPortaliQ9HDX9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279816. 3 interactions.
IntActiQ9HDX9. 3 interactions.
MINTiMINT-4702716.
STRINGi4896.SPAPB1A10.11c.1.

Proteomic databases

MaxQBiQ9HDX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAPB1A10.11c.1; SPAPB1A10.11c.1:pep; SPAPB1A10.11c.
GeneIDi2543394.
KEGGispo:SPAPB1A10.11c.

Organism-specific databases

EuPathDBiFungiDB:SPAPB1A10.11c.
PomBaseiSPAPB1A10.11c. mse1.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
InParanoidiQ9HDX9.
KOiK01885.
OMAiHSGPEFD.
OrthoDBiEOG76MKJ7.
PhylomeDBiQ9HDX9.

Miscellaneous databases

NextBioi20804409.
PROiQ9HDX9.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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].

Entry informationi

Entry nameiSYEM_SCHPO
AccessioniPrimary (citable) accession number: Q9HDX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: June 24, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.