ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us HAMAP Swiss-Prot
Search for

HAMAP annotation rule: MF_00118

Send feedback new

General rule information

Accession MF_00118
Dates 1-JUN-2001 (Created)
25-SEP-2008 (Last updated, Version 34)
Data class Protein

case <OC:Bacteria> or <OG:Chloroplast>
Predictors HAMAP; MF_00118_B; [distribution of match scores in UniProtKB];[seed alignment for MF_00118_B]
end case


case <OC:Archaea>
Predictors HAMAP; MF_00118_A; [distribution of match scores in UniProtKB];[seed alignment for MF_00118_A]
end case



Propagated annotation

Identifier, protein and gene names

case <OC:Bacteria>
Identifier EFTU
Protein name
RecName: Full=Elongation factor Tu;
Short=EF-Tu;
Gene name tuf

else case <OC:Archaea>
Identifier EF1A
Protein name
RecName: Full=Elongation factor 1-alpha;
Short=EF-1-alpha;
AltName: Full=Elongation factor Tu;
Short=EF-Tu;
Gene name tuf

else case <OG:Chloroplast>
Identifier EFTU
Protein name
RecName: Full=Elongation factor Tu, chloroplastic;
Short=EF-Tu;
Gene name tufA
end case

Comments
FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity).

case <OC:Bacteria>
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
end case


case <OC:Archaea>
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
end case


case <OG:Chloroplast>
SUBCELLULAR LOCATION: Plastid, chloroplast.
end case

SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Cross-references
Pfam PF00009; GTP_EFTU; 1;
PRINTS PR00315; ELONGATNFCT; 1;
TIGRFAMs TIGR00483; EF-1_alpha; 1;
TIGR00485; EF-Tu; 1;
PROSITE PS00301; EFACTOR_GTP; 1;
Keywords

case <FT:4>
Acetylation.
end case


case not <OG:Chloroplast>
Cytoplasm.
end case

Elongation factor, Protein biosynthesis, GTP-binding, Nucleotide-binding.
Gene Ontology
GO:0005525; Molecular function: GTP binding.
GO:0003746; Molecular function: translation elongation factor activity.

case <OC:Bacteria> or <OC:Archaea>
GO:0005737; Cellular component: cytoplasm.
end case


case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case

Features

case <OC:Bacteria> or <OG:Chloroplast>
From: EFTU_ECOLI (P0A6N1)
Key     From     To       Description   Condition   FTGroup
NP_BIND     19     26       GTP (By similarity)   G-[HQ]-[IV]-[DY]-H-G-K-[ST]  
NP_BIND     81     85       GTP (By similarity)   D-x-P-G-H  
NP_BIND     136     139       GTP (By similarity)   N-K-x-D  
end case

case <OC:Escherichia> or <OC:Shigella>
Key     From     To       Description   Condition   FTGroup
MOD_RES     314     314       N6-acetyllysine (By similarity)   K  
end case

case <OC:Archaea>
From: EF1A_METJA (Q57770)
Key     From     To       Description   Condition   FTGroup
NP_BIND     14     21       GTP (By similarity)   G-H-[IV]-D-[NHA]-G-K-S  
NP_BIND     91     95       GTP (By similarity)   D-x-P-G-H  
NP_BIND     149     152       GTP (By similarity)   N-K-M-D  
end case



Additional information


case <OC:Bacteria>
Size range: 389-430 amino acids
end case


case <OC:Archaea>
Size range: 413-444 amino acids
end case

Related UniRules: None
Template: P35021 (EF1A_SULSO); P0A6N1 (EFTU_ECOLI); Q01698 (EFTU_THEAQ); P60338 (EFTU1_THETH); Q57770 (EF1A_METJA): [Recover all]
Scope: Bacteria
Archaea
Plastid
Fusion: Nter: None; Cter: None
Duplicate: in AQUAE, ECOLI, HAEIN, STRCO, STRRA, THET8
Plasmid encoded: in SHEB5
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.

View rule in raw text format (no links)




UniProtKB rule member sequences



ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us HAMAP Swiss-Prot