SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q67TJ2

- SYE_SYMTH

UniProt

Q67TJ2 - SYE_SYMTH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutamate--tRNA ligase
Gene
gltX, STH16
Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061Zinc By similarity
Metal bindingi108 – 1081Zinc By similarity
Metal bindingi133 – 1331Zinc By similarity
Metal bindingi135 – 1351Zinc By similarity
Binding sitei253 – 2531ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW
  4. tRNA binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciSTHE292459:GJMM-17-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:gltX
Ordered Locus Names:STH16
OrganismiSymbiobacterium thermophilum (strain T / IAM 14863)
Taxonomic identifieri292459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium
ProteomesiUP000000417: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Glutamate--tRNA ligaseUniRule annotation
PRO_0000119673Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi292459.STH16.

Structurei

3D structure databases

ProteinModelPortaliQ67TJ2.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionUniRule annotation
Add
BLAST
Motifi250 – 2545"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiVTGQTHG.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q67TJ2-1 [UniParc]FASTAAdd to Basket

« Hide

MTVRVRIAPS PTGPIHVGNV HTALFNWLFA RHHGGKFILR FEDTDLERSR    50
PEWEQVIFED LKWLGIDWDE GPDIGGPYGP YRQTERLDLY RKYAQQLLES 100
GHVYKCYCTK EEEDADRREA QAAGRPYQYK GRCRDLTPEQ QAAFEAEGRK 150
PVLRFRVPRG EVIRFNDLVR GPIEVPTDSI GDFIIMRANG MPLYNFAVVV 200
DDVTMNITHV LRGEGHIPNT PVQILIYQAL GFPVPEFGHL GHMTNPERGK 250
LSKRKGEAAI RDYREQGYLP EAMLNFMSLL GWTPPGAESG REFLTKEELI 300
REFDLSRVTK ASSVFDRNKL NWMNGVYIRK KSLEEFAELA LPFVVSAGLC 350
TEEQARARWD WFKEVMAQVH ERVETLAEIP QHVDIFLKDE IEMDEKAARK 400
FLTEAVKPFF QRVSEGLRSV EWSVPAIEQL VRSIQEEMGL TPKESFQPIR 450
VAITGRTASP GLFETIYLIG RERVLERMAP YC 482
Length:482
Mass (Da):55,490
Last modified:October 11, 2004 - v1
Checksum:iEEC40EB190A7FBFD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006840 Genomic DNA. Translation: BAD39001.1.
RefSeqiWP_011194151.1. NC_006177.1.
YP_073845.1. NC_006177.1.

Genome annotation databases

EnsemblBacteriaiBAD39001; BAD39001; STH16.
GeneIDi2980022.
KEGGisth:STH16.
PATRICi23778064. VBISymThe116959_0018.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006840 Genomic DNA. Translation: BAD39001.1 .
RefSeqi WP_011194151.1. NC_006177.1.
YP_073845.1. NC_006177.1.

3D structure databases

ProteinModelPortali Q67TJ2.
ModBasei Search...

Protein-protein interaction databases

STRINGi 292459.STH16.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD39001 ; BAD39001 ; STH16 .
GeneIDi 2980022.
KEGGi sth:STH16.
PATRICi 23778064. VBISymThe116959_0018.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252720.
KOi K09698.
OMAi VTGQTHG.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci STHE292459:GJMM-17-MONOMER.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF48163. SSF48163. 1 hit.
TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
    Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
    Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: T / IAM 14863.

Entry informationi

Entry nameiSYE_SYMTH
AccessioniPrimary (citable) accession number: Q67TJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 11, 2004
Last modified: September 3, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi