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O13775 (SYEC_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable glutamate--tRNA ligase, cytoplasmic
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
ORF Names:SPAC17A5.15c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length716 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

Cytoplasm By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 716716Probable glutamate--tRNA ligase, cytoplasmic
PRO_0000119738

Regions

Nucleotide binding441 – 4455ATP By similarity
Region210 – 2123Glutamate binding By similarity
Region386 – 3905Glutamate binding By similarity
Motif215 – 22410"HIGH" region
Motif441 – 4455"KMSKS" region

Sites

Binding site2201ATP By similarity
Binding site2461Glutamate By similarity
Binding site4041Glutamate By similarity
Binding site4071ATP By similarity

Amino acid modifications

Modified residue1901Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
O13775 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2ACE0A35ED393227

FASTA71680,750
        10         20         30         40         50         60 
MSVSVALKAK PIAYGAVACA NYVNLSGAGS ISVKYEDVAL LDKQNKESNV SIQLNGSDSP 

        70         80         90        100        110        120 
VFGSKLALQT FSQVYPKLFI GENDRSLVES WVETASALAG NHNFLELSSL LAQLDDHLIM 

       130        140        150        160        170        180 
RSLFVGYSLT SADFSIWGAL KSNNMAAGAV RTGQYFNLAR WYKFMDSQNA VSVTMEEFTK 

       190        200        210        220        230        240 
AVNISKKQKS SGPNYEIGLP DAIDGKVVTR FPPEPSGYLH IGHAKAALLN QYFANKYHGK 

       250        260        270        280        290        300 
LIVRFDDTNP SKENSEFQDA ILEDVALLGI KPDVVTYTSD YLDTIHQYCV DMIKSGQAYA 

       310        320        330        340        350        360 
DDTDVETMRH ERTEGIPSKH RDRPIEESLE ILSEMDKGSD VGLKNCIRAK ISYENPNKAM 

       370        380        390        400        410        420 
RDPVIYRCNL LPHHRTGTKY RAYPTYDFAC PIVDSLEGVT HALRTTEYRD RNPLYQWMIK 

       430        440        450        460        470        480 
AMNLRKIHVW EFSRMNFVRT LLSKRKLTEI VDHGLVWGWD DPRFPTVRGV RRRGMTIEAL 

       490        500        510        520        530        540 
QQYIVSQGPS KNILTLDWTS FWATNKKIID PVAPRHTAVE SGDVVKATIV NGPAAPYAED 

       550        560        570        580        590        600 
RPRHKKNPEL GNKKSIFANE ILIEQADAQS FKQDEEVTLM DWGNAYVREI NRDASGKVTS 

       610        620        630        640        650        660 
LKLELHLDGD FKKTEKKVTW LADTEDKTPV DLVDFDYLIT KDKLEEGENY KDFLTPQTEF 

       670        680        690        700        710 
HSPVFADVGI KNLKKGDIIQ VERKGYYIVD VPFDGTQAVL FNIPDGKTVN RYGVKN

« 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]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB11515.1.
PIRT37830.
RefSeqNP_593483.1. NM_001018916.2.

3D structure databases

ProteinModelPortalO13775.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC17A5.15c-1.

Proteomic databases

PaxDbO13775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC17A5.15c.1; SPAC17A5.15c.1:pep; SPAC17A5.15c.
GeneID2542408.
KEGGspo:SPAC17A5.15c.

Organism-specific databases

PomBaseSPAC17A5.15c.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000259234.
KOK01885.
OMADFDHLIT.
OrthoDBEOG4ZSDBB.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_Ib_arc/euk.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF50715. Ribosomal_L25rel. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803467.

Entry information

Entry nameSYEC_SCHPO
AccessionPrimary (citable) accession number: O13775
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: January 1, 1998
Last modified: April 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents