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F2NM49 (F2NM49_MARHT) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase HAMAP-Rule MF_00022
EC=6.1.1.17 HAMAP-Rule MF_00022
Alternative name(s):
Glutamyl-tRNA synthetase HAMAP-Rule MF_00022
Gene names
Name:gltX HAMAP-Rule MF_00022
Ordered Locus Names:Marky_0769
OrganismMarinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1) [Complete proteome] [HAMAP] EMBL AEB11519.1
Taxonomic identifier869210 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Marinithermus ›

Protein attributes

Sequence length481 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

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. HAMAP-Rule MF_00022 RuleBase RU003489

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif8 – 1811"HIGH" region By similarity HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region By similarity HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
F2NM49 [UniParc].

Last modified May 31, 2011. Version 1.
Checksum: 1E509E024C5EA09C

FASTA48154,638
        10         20         30         40         50         60 
MVTTRIAPSP TGDPHVGTAY IAIFNYVWAR KNNGKFIVRI EDTDRNRYVE GAEARIQEMI 

        70         80         90        100        110        120 
RWLGLDYDEG TDIGGPNGPY RQSERTAIYQ AHAAKLIETG AAYRCFCTPE RLEALREEQK 

       130        140        150        160        170        180 
KRGLPLGYDG HCRHIPPEEA EARAKAGEPH VVRLKVPRPG QTVVKDELRG LVTYDHAEVP 

       190        200        210        220        230        240 
DVVLLKSDGF PTYHLANVVD DHLMGVTDVI RGEEWLVSTP IHVLLYQAFG WEAPLWYHMP 

       250        260        270        280        290        300 
LLRAPGGAKL SKRTGHTSVD WYRERGILAE ALMNYLSLMG FSMPDGREIF TLQELIEAFS 

       310        320        330        340        350        360 
WERVSLGGPV FDYEKLKWMN GKYIREVLTL EDLTQRVKPF LERAGLEWGS DAYLQRVVAA 

       370        380        390        400        410        420 
MRIRFETLEE FVEKARYFFT EAYPFEEKAL KKLKAGLEYV VELKERLGTL PEMDPELTEP 

       430        440        450        460        470        480 
LIRGYAAEKG AKPGAVMQPL RAALTGTLQS PGMFELLELL GKDRVLKRLE RAIQTAEAEE 


A

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References

[1]"Complete genome sequence of the aerobic, heterotroph Marinithermus hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent chimney."
Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S., Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K. expand/collapse author list , Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J., Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.
Stand. Genomic Sci. 6:21-30(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14884 / JCM 11576 / T1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002630 Genomic DNA. Translation: AEB11519.1.
RefSeqYP_004367629.1. NC_015387.1.

3D structure databases

ProteinModelPortalF2NM49.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEB11519; AEB11519; Marky_0769.
GeneID10433666.
KEGGmhd:Marky_0769.
PATRIC54433896. VBIMarHyd166763_0765.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01885.

Enzyme and pathway databases

BioCycMHYD869210:GHEE-795-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. 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_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.
PfamPF00749. 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 nameF2NM49_MARHT
AccessionPrimary (citable) accession number: F2NM49
Entry history
Integrated into UniProtKB/TrEMBL: May 31, 2011
Last sequence update: May 31, 2011
Last modified: May 1, 2013
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info