dimerization/docking (D/D) domain found in ciliogenesis-associated TTC17-interacting protein (CATIP) and similar proteins; CATIP, also called C2orf62, plays a role in primary ciliogenesis by modulating actin polymerization. It interacts with TTC17. Mutations in CATIP may contribute to asthenozoospermia through its involvement in actin polymerization and the actin cytoskeleton. CATIP contains a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 74738883 316 SYLRQHPEAHALISDFLLFLLLRQPEDVVTFAAEFFGPF 354
Cdd:cd22973   1 KYLRDHPELKAILSDFLQALLLRKPEDVYQFAAEYFSSF 39

dimerization/docking (D/D) domain found in ciliogenesis-associated TTC17-interacting protein (CATIP) and similar proteins; CATIP, also called C2orf62, plays a role in primary ciliogenesis by modulating actin polymerization. It interacts with TTC17. Mutations in CATIP may contribute to asthenozoospermia through its involvement in actin polymerization and the actin cytoskeleton. CATIP contains a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 74738883 316 SYLRQHPEAHALISDFLLFLLLRQPEDVVTFAAEFFGPF 354
Cdd:cd22973   1 KYLRDHPELKAILSDFLQALLLRKPEDVYQFAAEYFSSF 39

dimerization/docking (D/D) domain found in ciliogenesis-associated TTC17-interacting protein (CATIP) and similar proteins; CATIP, also called C2orf62, plays a role in primary ciliogenesis by modulating actin polymerization. It interacts with TTC17. Mutations in CATIP may contribute to asthenozoospermia through its involvement in actin polymerization and the actin cytoskeleton. CATIP contains a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 74738883 316 SYLRQHPEAHALISDFLLFLLLRQPEDVVTFAAEFFGPF 354
Cdd:cd22973   1 KYLRDHPELKAILSDFLQALLLRKPEDVYQFAAEYFSSF 39

dimerization/docking (D/D) domain of the type II Regulatory subunit of cAMP-dependent protein kinase and similar domains; cAMP-dependent protein kinase (PKA) is a serine/threonine kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. There are two classes of R subunits, RI and RII; each exists as two isoforms (alpha and beta) from distinct genes. These functionally non-redundant R isoforms allow for specificity in PKA signaling. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence (IS), and two c-AMP binding domains. RI and RII subunits are distinguished by their IS; RII subunits contain a phosphorylation site and are both substrates and inhibitors while RI subunits are pseudo-substrates. RI subunits require ATP and Mg ions to form a stable holoenzyme while RII subunits do not. The D/D domain dimerizes to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs), which facilitates the localization of PKA to specific sites in the cell. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis.

                        10        20        30
                ....*....|....*....|....*....|..
gi 74738883 320 QHPEAHALISDFLLFLLLRQPEDVVTFAAEFF 351
Cdd:cd12084   1 VPEGLRELLEDFTREVLREQPEDVYEFAADYF 32