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|
Annotation rule MF_00118 |
General rule information
[?]
Accession |
MF_00118 |
Dates |
1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 41) |
Scope |
Bacteria
Archaea
Plastid |
case <OC:Bacteria> or <OG:Chloroplast>
end case
case <OC:Archaea>
end case
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Bacteria>
Protein name |
RecName:
|
Full=Elongation factor Tu;
|
|
Short=EF-Tu;
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|
else case <OC:Archaea>
Protein name |
RecName:
|
Full=Elongation factor 1-alpha;
|
|
Short=EF-1-alpha;
|
AltName:
|
Full=Elongation factor Tu;
|
|
Short=EF-Tu;
|
|
else case <OG:Chloroplast>
Protein name |
RecName:
|
Full=Elongation factor Tu, chloroplastic;
|
|
Short=EF-Tu;
|
|
end case
Function |
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. |
case <OC:Bacteria>
Subunit |
Monomer. |
Subcellular location |
Cytoplasm. |
end case
case <OC:Archaea>
Subcellular location |
Cytoplasm. |
end case
case <OG:Chloroplast>
Subcellular location |
Plastid, chloroplast. |
end case
Similarity |
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. |
case not <OG:Chloroplast>
end case
GO:0005525; Molecular function: GTP binding.
GO:0003746; Molecular function: translation elongation factor activity.
case <OC:Bacteria> or <OC:Archaea>
end case
case <OG:Chloroplast>
end case
case <OC:Bacteria> or <OG:Chloroplast>
From: EFTU1_ECOLI (P0CE47) |
Key
|
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From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
NP_BIND
|
|
19
|
|
26
|
|
GTP
|
|
|
|
G-[HQ]-[IV]-[DY]-H-G-K-[ST]
|
|
|
NP_BIND
|
|
81
|
|
85
|
|
GTP
|
|
|
|
D-x-P-G-H
|
|
|
NP_BIND
|
|
136
|
|
139
|
|
GTP
|
|
|
|
N-K-x-D
|
|
|
end case
case <OC:Archaea>
From: EF1A_METJA (Q57770) |
NP_BIND
|
|
14
|
|
21
|
|
GTP
|
|
|
|
G-H-[IV]-D-[NHA]-G-K-S
|
|
|
NP_BIND
|
|
91
|
|
95
|
|
GTP
|
|
|
|
D-x-P-G-H
|
|
|
NP_BIND
|
|
149
|
|
152
|
|
GTP
|
|
|
|
N-K-M-D
|
|
|
end case
Additional information
[?]
Size range |
350-550 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
Duplicated in some but not necessarily all Acidobacteria, Proteobacteria, Alkaliohilus, Clostrium, Chloroflexi, Deinococcus, Magnetococcus, Sphingobacter, Streptomyces, Syntrophobacter. Short versions in EHRRW, VIBVU, and a divergent copy in CHAGL are atypical. |