Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q31C61 (SYE_PROM9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:PMT9312_0473
OrganismProchlorococcus marinus (strain MIT 9312) [Complete proteome] [HAMAP]
Taxonomic identifier74546 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
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

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237385

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31C61 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 468D4900AD2942D3

FASTA47955,167
        10         20         30         40         50         60 
MEIRLRLAPS PTGLFHIGTA RTALFNWLYA QKIGGKFLIR IEDTDFLRSK SEYTKNILDG 

        70         80         90        100        110        120 
LKWLGLQWNE EPVKQSDRIS IHKKYIKKLL ECGAAYRCFT TEDEISELRE EQKKKGLPPK 

       130        140        150        160        170        180 
HDNRHRNLSK EEIETFISQG RTSVIRFKID EEIQIKWIDQ IRGEIKWQGK DLGGDLVLSR 

       190        200        210        220        230        240 
RAMGYEIGDP LYNLAVVVDD NFMNITHVVR GEDHISNTAK QILIYEALDF KLPTFSHTPL 

       250        260        270        280        290        300 
ILNNEGKKLS KRDCVTSIDE FRDMGYLPEA LSNYMAFLGW SPKSATSEIL SLDEISKIFE 

       310        320        330        340        350        360 
LSDINKAGAK FSWEKLNWIN SQYIKNMETV KLSETIGKYW DNMGWDPPSQ EWAIKLAILI 

       370        380        390        400        410        420 
KDSMTLLKDA IDQSKPFFLL PPIQKEGKDF LESNDGKTSL KLILNYLIEQ NTGKVDKDKA 

       430        440        450        460        470 
KEIINEISKM HNVKKGILMK SLRVAFFGSL SGPDLIQSWE LFSESKSDIS RIERCLKSI 

« Hide

References

[1]"Complete sequence of Prochlorococcus marinus str. MIT 9312."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9312.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000111 Genomic DNA. Translation: ABB49534.1.
RefSeqYP_396970.1. NC_007577.1.

3D structure databases

ProteinModelPortalQ31C61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74546.PMT9312_0473.

Proteomic databases

PRIDEQ31C61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB49534; ABB49534; PMT9312_0473.
GeneID3765270.
KEGGpmi:PMT9312_0473.
PATRIC23004620. VBIProMar70153_0493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPMAR74546:GHRG-490-MONOMER.

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.
IPR001412. aa-tRNA-synth_I_CS.
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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_PROM9
AccessionPrimary (citable) accession number: Q31C61
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 6, 2005
Last modified: February 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries