Protein Domain

A protein domain is a conserved part of a given protein sequence and structure that can exist, function, and evolve independently from the rest of the protein chain. Each domain usually forms a compact three-dimensional structure and is independently stable and folded. Many proteins consist of several structural domains. One domain may appear in a variety of distinct proteins. Moreover, domains could form functional units to work together. Here, we collect and annotate 85 common domains in the kiwifruit genome.

AAA ACT ACBP Ankyrin repeat AP2 ARM repeat B3 BEL1-like α/β hydrolase AT-rich interactive
BRCA1 BRCT BSD Bromodomain BTB/POZ BURP C2 CAMK CAP-Gly Calponin homology
CBS MIF4G Chitinase Chromodomain COBW Coiled-coil Cold shock CRAL-TRIO C-terminus CDGSH iron-sulfur
DENN DUF EF hand Cytochrome b561 ELMO FHA G patch GRAM GRAB HAD-like hydrolase
IQ KH KOW Homeodomain LRR LisH LOB LysM MACPF L-type lectin
MAP7 MATH MBD Chaperone DnaJ MYB NAC NB-ARC OTU PAN MADS box
R3H RWP-RK SAM RNA-binding SET SH3 Smr SNF2 SPX Rhodanese-like
SAM SUN TBC1 Ubiquitin TCP TLD Tudor U-box UBX Thioredoxin
VHS WPP YTH WD40 repeat Zinc finger

In molecular biology, the ACT domain is a protein domain that is found in a variety of proteins involved in metabolism. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH), which folds with a ferredoxin-like topology. A pair of ACT domains form an eight-stranded antiparallel sheet with two molecules of allosteric inhibitor serine bound in the interface. Biochemical exploration of a few other proteins containing ACT domains supports the suggestions that these domains contain the archetypical ACT structure.
Protein name Gene name Description Pathway Interaction
Protein name Gene name Description Pathway Interaction
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0
Ach00g016841.1Ach00g016841Posttranslational modification, protein turnover, chaperones0