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Q5PBW1

- SYE1_ANAMM

UniProt

Q5PBW1 - SYE1_ANAMM

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Protein

Glutamate--tRNA ligase 1

Gene

gltX1

Organism
Anaplasma marginale (strain St. Maries)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. 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, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase 1UniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetase 1UniRule annotation
Short name:
GluRS 1UniRule annotation
Gene namesi
Name:gltX1UniRule annotation
Ordered Locus Names:AM039
OrganismiAnaplasma marginale (strain St. Maries)
Taxonomic identifieri234826 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma
ProteomesiUP000006557: 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 – 441441Glutamate--tRNA ligase 1PRO_0000119492Add
BLAST

Proteomic databases

PRIDEiQ5PBW1.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi234826.AM039.

Structurei

3D structure databases

ProteinModelPortaliQ5PBW1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi7 – 1711"HIGH" regionAdd
BLAST
Motifi236 – 2405"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252721.
KOiK01885.
OMAiRIALFNW.
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.

Q5PBW1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MITRFAPSPT GYMHIGNART ALICWLYARS RSGKLLLRID DTDLERSENR
60 70 80 90 100
YVEGIKNDLT WLAMDWDICF NQRSRISRYD EVFNSLMDAG AVYPCYETPE
110 120 130 140 150
ELELKRKMML KMGLPPIYDR SALNMTEQDQ KAYSGRKPYF RLKIGRDQAI
160 170 180 190 200
SWEDEIRGKV VFQAKNISDP ILRRTDGSYT YMFPSTVDDI DFEVTHIVRG
210 220 230 240 250
EDHVSNTAVQ IYIMGLLGAK IPSFAHLPLL RMGGSKMSKR VGGTEIFKMR
260 270 280 290 300
DMNLEPMAIN SYMARIGTSL PVEPHTNMRS LVDSFDIKLF NQAPIKFELE
310 320 330 340 350
DISKLNVRLL QKLPFAEVQD RLEACGIKCS EGFWYAVRDN INVISEVKGW
360 370 380 390 400
AEICGPGVTP VVDDVNRQLL QLASDLLPEG EPNDGTWKTW LQKIKECSGC
410 420 430 440
ETRDILLPLR LALTGVPKGP EFAKLLPLIG RVEILRRLRG A
Length:441
Mass (Da):50,239
Last modified:January 4, 2005 - v1
Checksum:i3CC9F08ABE6409A6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000030 Genomic DNA. Translation: AAV86218.1.
RefSeqiWP_011114091.1. NC_004842.2.
YP_153473.1. NC_004842.2.

Genome annotation databases

EnsemblBacteriaiAAV86218; AAV86218; AM039.
GeneIDi3171397.
KEGGiama:AM039.
PATRICi20946191. VBIAnaMar46146_0036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000030 Genomic DNA. Translation: AAV86218.1 .
RefSeqi WP_011114091.1. NC_004842.2.
YP_153473.1. NC_004842.2.

3D structure databases

ProteinModelPortali Q5PBW1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 234826.AM039.

Proteomic databases

PRIDEi Q5PBW1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV86218 ; AAV86218 ; AM039 .
GeneIDi 3171397.
KEGGi ama:AM039.
PATRICi 20946191. VBIAnaMar46146_0036.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252721.
KOi K01885.
OMAi RIALFNW.
OrthoDBi EOG6DRPF7.

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. "Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
    Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: St. Maries.

Entry informationi

Entry nameiSYE1_ANAMM
AccessioniPrimary (citable) accession number: Q5PBW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 4, 2005
Last modified: October 29, 2014
This is version 66 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