Skip Header

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

Q6MEN1

- SYE_PARUW

UniProt

Q6MEN1 - SYE_PARUW

(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

Organism
Protochlamydia amoebophila (strain UWE25)
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).UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061ZincUniRule annotation
Metal bindingi108 – 1081ZincUniRule annotation
Metal bindingi133 – 1331ZincUniRule annotation
Metal bindingi135 – 1351ZincUniRule annotation
Binding sitei253 – 2531ATPUniRule annotation

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

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

BioCyciPAMO264201:GH0M-248-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:pc0244
OrganismiProtochlamydia amoebophila (strain UWE25)
Taxonomic identifieri264201 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia
ProteomesiUP000000529: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Glutamate--tRNA ligasePRO_0000119618Add
BLAST

Proteomic databases

PRIDEiQ6MEN1.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi264201.pc0244.

Structurei

3D structure databases

ProteinModelPortaliQ6MEN1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionAdd
BLAST
Motifi250 – 2545"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OMAiVTGQTHG.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
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.

Q6MEN1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVRVRIAPS PTGDPHVGTA YMALFNMIFA RHYNGTFILR IEDTDRARSR
60 70 80 90 100
PEYEENIYSA LKWANIQWDE GPDIGGAYGP YRQSERFDIY KQYAEELLSK
110 120 130 140 150
GKAYKCFCTA AELDEMRELS AKQGGRQGYD RRCRHLTPDE IIEREQAELS
160 170 180 190 200
YVIRLKVPLN GECVYEDAIK KRMTFPWADI DDQVLLKSDG FPTYHLANVV
210 220 230 240 250
DDYLMKISHV IRGDEWMSST PKHILLYESF GWTPPTFLHM PLLLGKDGKK
260 270 280 290 300
LSKRKNPTSI FFYRDSGYLS EAFINFLTLM GYSMTGDQEI YSLDDIIREF
310 320 330 340 350
DYKRIGVSGA IFDVQKLDWV NQQYLIKNIP VEQLWDRIKE WSFNDEFMQR
360 370 380 390 400
LMPLCHSRIK TFGDFMDLFN FLFINHLHYN DAIFVVKDLS KEQICYLIQS
410 420 430 440 450
LIWRLDELEN WNGTGVNQAS REIAEIFGVN HKKIVMPILF ASLMSKTQGP
460 470 480 490 500
PLFDSVNLLG KDRTRARLLK AMEYLGGISN KKMASLKKAW QEKSGQPLMI

KD
Length:502
Mass (Da):58,420
Last modified:July 5, 2004 - v1
Checksum:i1903CD607A03A1A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX908798 Genomic DNA. Translation: CAF22968.1.
RefSeqiYP_007243.1. NC_005861.1.

Genome annotation databases

EnsemblBacteriaiCAF22968; CAF22968; pc0244.
GeneIDi2781428.
KEGGipcu:pc0244.
PATRICi31995772. VBICanPro72727_0246.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX908798 Genomic DNA. Translation: CAF22968.1 .
RefSeqi YP_007243.1. NC_005861.1.

3D structure databases

ProteinModelPortali Q6MEN1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264201.pc0244.

Proteomic databases

PRIDEi Q6MEN1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAF22968 ; CAF22968 ; pc0244 .
GeneIDi 2781428.
KEGGi pcu:pc0244.
PATRICi 31995772. VBICanPro72727_0246.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252720.
KOi K01885.
OMAi VTGQTHG.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci PAMO264201:GH0M-248-MONOMER.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. 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 ]
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UWE25.

Entry informationi

Entry nameiSYE_PARUW
AccessioniPrimary (citable) accession number: Q6MEN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 71 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, Reference 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