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Q0P499 (SYEM_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. 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:
Probable glutamate--tRNA ligase, mitochondrial

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:ears2
ORF Names:zgc:153247
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. 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 matrix By similarity HAMAP-Rule MF_00022_B.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Potential
Chain23 – 503481Probable glutamate--tRNA ligase, mitochondrial HAMAP-Rule MF_00022_B
PRO_0000254564

Regions

Nucleotide binding265 – 2695ATP By similarity
Region21 – 233Glutamate binding By similarity
Region209 – 2135Glutamate binding By similarity
Motif26 – 349"HIGH" region HAMAP-Rule MF_00022_B
Motif265 – 2695"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site311ATP By similarity
Binding site571Glutamate By similarity
Binding site2271Glutamate By similarity
Binding site2301ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0P499 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: B5E856B44B303AD7

FASTA50357,023
        10         20         30         40         50         60 
MKILRGVSRQ MCTSRPEVRV RFAPSPTGFL HLGGLRTALY NFLFSRQRRG VFILRLEDTD 

        70         80         90        100        110        120 
QKRLVPGAAE HIEDMLEWAG IPPDESSRRG GDYGPYVQSE RLHLYTEAAS SLLNTGHAYY 

       130        140        150        160        170        180 
CFCSNQRLEL LKKEAQRSGH APRYDNRCRR LQPQQVEQKL AAGVPAVVRF KLHTGTEEFQ 

       190        200        210        220        230        240 
DLVFGWTGHA VGAVEGDPVI LKADGYPTYH LASVVDDHHM RISHVLRGCE WLISSAKHLQ 

       250        260        270        280        290        300 
LYRALRWTPP TYAHLPLLLN RDGSKLSKRQ GDIFLQSFRD RGVLPETLLD LVTHAGSGFS 

       310        320        330        340        350        360 
DNRMGRRLDE LIRDFNISKI TTHSALLDLD KLEEFSRLHL QRRIEDPQQC VWLCEELKQM 

       370        380        390        400        410        420 
VKHTHSSEIS AAAVLEPEYI ERVLQLRKGH ISSLQDLLSS THSYLWVRPR VSQTQLQSES 

       430        440        450        460        470        480 
AHAKDIATAV MQMVLAGGSL VSMERLSSEL KQISSRTNST HSSVMKVLRL LLSAQQRGPS 

       490        500 
VAEMMLSLGE QEVCVRLQKA LEL 

« Hide

References

[1]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC122204 mRNA. Translation: AAI22205.1.
RefSeqNP_001038907.1. NM_001045442.1.
UniGeneDr.83804.

3D structure databases

ProteinModelPortalQ0P499.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ0P499.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID751732.
KEGGdre:751732.

Organism-specific databases

ZFINZDB-GENE-060825-214. zgc:153247.

Phylogenomic databases

HOVERGENHBG056174.
InParanoidQ0P499.
KOK01885.
PhylomeDBQ0P499.

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...

Other

NextBio20917872.

Entry information

Entry nameSYEM_DANRE
AccessionPrimary (citable) accession number: Q0P499
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 19, 2006
Last modified: April 16, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries