blastp_kegg |
lcl|pper:PRUPE_ppa010923mg
|
1 |
175 |
+ |
175 |
Gaps:11 |
71.30 |
230 |
84.15 |
4e-74 |
hypothetical protein
|
blastp_kegg |
lcl|pxb:103954891
|
1 |
177 |
+ |
177 |
Gaps:9 |
71.79 |
234 |
83.93 |
1e-71 |
elongation factor 1-delta-like
|
blastp_kegg |
lcl|mdm:103413381
|
1 |
177 |
+ |
177 |
Gaps:9 |
71.79 |
234 |
83.93 |
1e-71 |
elongation factor 1-delta-like
|
blastp_kegg |
lcl|pmum:103327198
|
1 |
175 |
+ |
175 |
Gaps:10 |
71.43 |
231 |
83.03 |
1e-68 |
elongation factor 1-delta 2-like
|
blastp_kegg |
lcl|pmum:103322483
|
1 |
175 |
+ |
175 |
Gaps:10 |
71.43 |
231 |
83.03 |
1e-68 |
elongation factor 1-delta 2-like
|
blastp_kegg |
lcl|pper:PRUPE_ppa010902mg
|
1 |
175 |
+ |
175 |
Gaps:10 |
71.43 |
231 |
83.03 |
1e-68 |
hypothetical protein
|
blastp_kegg |
lcl|fve:101314310
|
1 |
175 |
+ |
175 |
Gaps:9 |
71.55 |
232 |
84.94 |
2e-68 |
elongation factor 1-delta-like
|
blastp_kegg |
lcl|cic:CICLE_v10027451mg
|
1 |
175 |
+ |
175 |
Gaps:11 |
71.30 |
230 |
73.78 |
3e-68 |
hypothetical protein
|
blastp_kegg |
lcl|cam:101496460
|
1 |
175 |
+ |
175 |
Gaps:8 |
71.67 |
233 |
79.04 |
3e-68 |
elongation factor 1-delta 2-like
|
blastp_kegg |
lcl|pxb:103945839
|
1 |
175 |
+ |
175 |
Gaps:10 |
71.43 |
231 |
82.42 |
8e-68 |
elongation factor 1-delta-like
|
blastp_pdb |
1b64_A
|
85 |
175 |
+ |
91 |
Gaps:3 |
96.70 |
91 |
62.50 |
5e-28 |
mol:protein length:91 ELONGATION FACTOR 1-BETA
|
blastp_pdb |
1g7c_B
|
82 |
175 |
+ |
94 |
Gaps:3 |
96.81 |
94 |
43.96 |
2e-18 |
mol:protein length:94 ELONGATION FACTOR 1-BETA
|
blastp_pdb |
1f60_B
|
82 |
175 |
+ |
94 |
Gaps:3 |
96.81 |
94 |
43.96 |
2e-18 |
mol:protein length:94 ELONGATION FACTOR EEF1BA
|
blastp_pdb |
1ijf_B
|
84 |
175 |
+ |
92 |
Gaps:3 |
98.89 |
90 |
43.82 |
5e-18 |
mol:protein length:90 elongation factor 1-beta
|
blastp_pdb |
1ije_B
|
84 |
175 |
+ |
92 |
Gaps:3 |
98.89 |
90 |
43.82 |
5e-18 |
mol:protein length:90 elongation factor 1-beta
|
blastp_pdb |
2b7c_B
|
82 |
175 |
+ |
94 |
Gaps:3 |
96.81 |
94 |
42.86 |
9e-18 |
mol:protein length:94 elongation factor-1 beta
|
blastp_pdb |
2b7b_B
|
82 |
175 |
+ |
94 |
Gaps:3 |
96.81 |
94 |
42.86 |
9e-18 |
mol:protein length:94 elongation factor-1 beta
|
blastp_uniprot_sprot |
sp|P93447|EF1D_PIMBR
|
1 |
175 |
+ |
175 |
Gaps:15 |
70.80 |
226 |
82.50 |
1e-76 |
Elongation factor 1-delta OS Pimpinella brachycarpa PE 2 SV 3
|
blastp_uniprot_sprot |
sp|Q9SI20|EF1D2_ARATH
|
1 |
175 |
+ |
175 |
Gaps:9 |
71.86 |
231 |
79.52 |
4e-69 |
Elongation factor 1-delta 2 OS Arabidopsis thaliana GN At2g18110 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|P48006|EF1D1_ARATH
|
1 |
175 |
+ |
175 |
Gaps:9 |
71.86 |
231 |
73.49 |
1e-64 |
Elongation factor 1-delta 1 OS Arabidopsis thaliana GN At1g30230 PE 2 SV 2
|
blastp_uniprot_sprot |
sp|Q84WM9|EF1B1_ARATH
|
56 |
175 |
+ |
120 |
none |
52.63 |
228 |
80.00 |
3e-55 |
Elongation factor 1-beta 1 OS Arabidopsis thaliana GN At5g12110 PE 2 SV 2
|
blastp_uniprot_sprot |
sp|Q40682|EF1D2_ORYSJ
|
3 |
175 |
+ |
173 |
Gaps:15 |
69.91 |
226 |
77.22 |
4e-53 |
Elongation factor 1-delta 2 OS Oryza sativa subsp. japonica GN Os03g0406200 PE 1 SV 3
|
blastp_uniprot_sprot |
sp|P29545|EF1B_ORYSJ
|
56 |
175 |
+ |
120 |
Gaps:1 |
53.12 |
224 |
80.67 |
4e-53 |
Elongation factor 1-beta OS Oryza sativa subsp. japonica GN Os07g0662500 PE 1 SV 3
|
blastp_uniprot_sprot |
sp|Q40680|EF1D1_ORYSJ
|
54 |
175 |
+ |
122 |
none |
53.28 |
229 |
86.07 |
2e-51 |
Elongation factor 1-delta 1 OS Oryza sativa subsp. japonica GN Os07g0614500 PE 2 SV 3
|
blastp_uniprot_sprot |
sp|O81918|EF1D_BETVU
|
1 |
175 |
+ |
175 |
Gaps:12 |
71.43 |
231 |
72.12 |
3e-50 |
Elongation factor 1-delta OS Beta vulgaris PE 2 SV 3
|
blastp_uniprot_sprot |
sp|Q9SCX3|EF1B2_ARATH
|
54 |
175 |
+ |
122 |
none |
54.46 |
224 |
79.51 |
2e-48 |
Elongation factor 1-beta 2 OS Arabidopsis thaliana GN At5g19510 PE 1 SV 1
|
blastp_uniprot_sprot |
sp|P29546|EF1B_WHEAT
|
80 |
175 |
+ |
96 |
Gaps:2 |
43.52 |
216 |
80.85 |
9e-44 |
Elongation factor 1-beta OS Triticum aestivum PE 1 SV 2
|
rpsblast_cdd |
gnl|CDD|29372
|
85 |
175 |
+ |
91 |
Gaps:4 |
98.86 |
88 |
45.98 |
2e-18 |
cd00292 EF1B Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein EF1A for GTP an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B which is the alpha subunit in yeast is responsible for the catalysis of this exchange reaction..
|
rpsblast_cdd |
gnl|CDD|201421
|
87 |
175 |
+ |
89 |
Gaps:6 |
100.00 |
87 |
52.87 |
2e-18 |
pfam00736 EF1_GNE EF-1 guanine nucleotide exchange domain. This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.
|
rpsblast_cdd |
gnl|CDD|197956
|
87 |
175 |
+ |
89 |
Gaps:6 |
98.86 |
88 |
40.23 |
6e-17 |
smart00888 EF1_GNE EF-1 guanine nucleotide exchange domain. Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria and can consist of three subunits: EF1B-alpha (or EF-1beta) EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta also known as EF1B-alpha) and delta (EF-1delta also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity which mainly resides in their homologous guanine nucleotide exchange domains found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).
|