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Q119Z5 (SYE_TRIEI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Tery_0188
OrganismTrichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP]
Taxonomic identifier203124 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Oscillatoriales › Trichodesmium ›

Protein attributes

Sequence length881 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_B

Catalytic activity

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

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity. Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

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: EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Glutamate--tRNA ligase HAMAP-Rule MF_00022_B
PRO_0000367797

Regions

Transmembrane809 – 82921Helical; Potential
Transmembrane832 – 85221Helical; Potential
Region1 – 480480Glutamyl-tRNA synthetase HAMAP-Rule MF_00022_B
Region481 – 881401Unknown HAMAP-Rule MF_00022_B
Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022_B
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022_B
Compositional bias510 – 772263Thr-rich HAMAP-Rule MF_00022_B

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q119Z5 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 1C675432E0CA07E9

FASTA88198,269
        10         20         30         40         50         60 
MSVRVRLAPS PTGNLHIGTA RTAVFNWLFA RNQKGKFILR IEDTDQERSR PEYTDNILEG 

        70         80         90        100        110        120 
LSWLGLEWDE GPFYQCQRYE LYQKATQSLL DKGLAYRCYC TAAELEEMRE AQKARKEAPR 

       130        140        150        160        170        180 
YDNRHRNLTD LEKKAFEAEG RQAVIRFRID DDQIITWNDM VRGKVTWKGS DLGGDMVISR 

       190        200        210        220        230        240 
AAGGDEVGQP LYNMAVVVDD MDMEITHVIR GEDHIANTAK QILLYEALGG KIPEFGHTPL 

       250        260        270        280        290        300 
ILNKEGRKLS KRDGVTSISD FQELGFTPEA LANYMCLLGW TPPDATEEIF TLAQAGQNFS 

       310        320        330        340        350        360 
FERVNKAGAK FDWDKLDWIS SQYLHNLPVK QLTDKLIPIW QKAGYELDPE GDRSWLEQLV 

       370        380        390        400        410        420 
TLIRPSLTRL TDAVEMSELF FFPTVELNED AKTQMQNEDS VKSINSILEI INADAPLLVA 

       430        440        450        460        470        480 
DVKQTIKKVT QKVHVKKGVV MRSLRASLTG AMQGPDLIES WLLLHQKGFD ILRFKKSIGQ 

       490        500        510        520        530        540 
EIEDTKIEDT KKAETTPHKS KGEGNVLLKT TTPKSPALSK EQTQTTKPPK KGQTATPVAT 

       550        560        570        580        590        600 
TPTATDVTEN TSVGTQETQS QITTPVATTP TATDVTENTS VGTQETQSQI TTPVATTPTA 

       610        620        630        640        650        660 
TDVTENTSVE TQETQSQITT PVATTPTATD VTENTSVETQ ETQSQITTPV ATTPTATDVT 

       670        680        690        700        710        720 
ENTSVGTQET QSQITTPVAT TPTATDVTEN TSVETQETQS QITTPVATTS TATDVTENTS 

       730        740        750        760        770        780 
VETQETQSQI TTPVATTPTA TDAETREQKV ATQVETSILD DQKPVDTVTN QTVEVEQPNK 

       790        800        810        820        830        840 
IKEQFINIFF NFPDYINQLY QQYQGQLKLF GWLALVILTF TFMAVVIEAL DGIPILSIIF 

       850        860        870        880 
ELIGVIYLVW FVYRYLLKRS NRQELLDKIE NIKREIFGKP S

« Hide

References

[1]"Complete sequence of Trichodesmium erythraeum IMS101."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IMS101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000393 Genomic DNA. Translation: ABG49679.1.
RefSeqYP_720152.1. NC_008312.1.

3D structure databases

ProteinModelPortalQ119Z5.
SMRQ119Z5. Positions 2-480.
ModBaseSearch...

Protein-protein interaction databases

STRING203124.Tery_0188.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG49679; ABG49679; Tery_0188.
GeneID4242194.
KEGGter:Tery_0188.
PATRIC23983588. VBITriEry99848_0240.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.

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. Fused.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR025564. DUF4308.
IPR004527. Glu-tRNA-ligase_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF14159. DUF4308. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_TRIEI
AccessionPrimary (citable) accession number: Q119Z5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: August 22, 2006
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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