|
pycom07g10870.1
|
pyrus_communis |
-
|
Phosphatidate |
Detail
|
|
pycom07g10880.1
|
pyrus_communis |
-
|
EF-hand domain pair |
Detail
|
|
pycom07g10890.1
|
pyrus_communis |
VAP27-1
|
Vesicle-associated membrane protein-associated protein |
Detail
|
|
pycom07g10900.1
|
pyrus_communis |
-
|
None |
Detail
|
|
pycom07g10910.1
|
pyrus_communis |
-
|
Helicase-like protein |
Detail
|
|
pycom07g10920.1
|
pyrus_communis |
-
|
spliceosomal complex assembly |
Detail
|
|
pycom07g10970.1
|
pyrus_communis |
-
|
transposition, RNA-mediated |
Detail
|
|
pycom07g10980.1
|
pyrus_communis |
-
|
transposition, RNA-mediated |
Detail
|
|
pycom07g11020.1
|
pyrus_communis |
KU80
|
ATP-dependent DNA helicase 2 subunit |
Detail
|
|
pycom07g11030.1
|
pyrus_communis |
PBF1
|
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH |
Detail
|
|
pycom07g11050.1
|
pyrus_communis |
-
|
Protein cornichon homolog 4-like |
Detail
|
|
pycom07g11070.1
|
pyrus_communis |
-
|
MORC family CW-type zinc finger protein |
Detail
|
|
pycom07g11080.1
|
pyrus_communis |
-
|
None |
Detail
|
|
pycom07g11090.1
|
pyrus_communis |
-
|
AT-hook motif nuclear-localized protein |
Detail
|
|
pycom07g11100.1
|
pyrus_communis |
-
|
AT-hook motif nuclear-localized protein |
Detail
|
|
pycom07g11140.1
|
pyrus_communis |
-
|
None |
Detail
|
|
pycom07g11180.1
|
pyrus_communis |
-
|
Brefeldin A-inhibited guanine nucleotide-exchange protein |
Detail
|
|
pycom07g11190.1
|
pyrus_communis |
-
|
Brefeldin A-inhibited guanine nucleotide-exchange protein |
Detail
|
|
pycom07g11200.1
|
pyrus_communis |
-
|
calcium-binding protein |
Detail
|
|
pycom07g11240.1
|
pyrus_communis |
-
|
Chloroplast-localized elongation factor EF-G involved in protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome |
Detail
|