|
Rmu_sc0004016.1_g000017.1
|
rosa_multiflora |
-
|
nuclease HARBI1 |
Detail
|
|
Rmu_sc0004016.1_g000020.1
|
rosa_multiflora |
-
|
BTB POZ domain-containing protein |
Detail
|
|
Rmu_sc0004018.1_g000005.1
|
rosa_multiflora |
-
|
2,3-bisphosphoglycerate-independent phosphoglycerate |
Detail
|
|
Rmu_sc0004018.1_g000009.1
|
rosa_multiflora |
-
|
Aldo/keto reductase family |
Detail
|
|
Rmu_sc0004019.1_g000002.1
|
rosa_multiflora |
-
|
None |
Detail
|
|
Rmu_sc0004019.1_g000005.1
|
rosa_multiflora |
-
|
NAC domain-containing protein |
Detail
|
|
Rmu_sc0004019.1_g000006.1
|
rosa_multiflora |
-
|
Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells |
Detail
|
|
Rmu_sc0004019.1_g000007.1
|
rosa_multiflora |
-
|
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family |
Detail
|
|
Rmu_sc0004020.1_g000002.1
|
rosa_multiflora |
-
|
Protein of unknown function (DUF789) |
Detail
|
|
Rmu_sc0004020.1_g000006.1
|
rosa_multiflora |
-
|
ubiquitin-60S ribosomal protein |
Detail
|
|
Rmu_sc0004020.1_g000007.1
|
rosa_multiflora |
-
|
Photosystem II repair protein PSB27-H1, chloroplastic |
Detail
|
|
Rmu_sc0004020.1_g000009.1
|
rosa_multiflora |
-
|
phosphatase 2c |
Detail
|
|
Rmu_sc0004020.1_g000010.1
|
rosa_multiflora |
-
|
F-box FBD LRR-repeat protein |
Detail
|
|
Rmu_sc0004020.1_g000011.1
|
rosa_multiflora |
-
|
None |
Detail
|
|
Rmu_sc0004020.1_g000013.1
|
rosa_multiflora |
-
|
Belongs to the terpene synthase family |
Detail
|
|
Rmu_sc0004020.1_g000022.1
|
rosa_multiflora |
-
|
Indole-3-acetic acid-amido synthetase |
Detail
|
|
Rmu_sc0004020.1_g000025.1
|
rosa_multiflora |
-
|
Ribonuclease H protein |
Detail
|
|
Rmu_sc0004020.1_g000026.1
|
rosa_multiflora |
-
|
None |
Detail
|
|
Rmu_sc0004020.1_g000028.1
|
rosa_multiflora |
-
|
None |
Detail
|
|
Rmu_sc0004020.1_g000029.1
|
rosa_multiflora |
LIP1
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives |
Detail
|