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 21357001  17 VPEGLPELLSDVTREVLRCQPkkECLCQFIIDYLHS 52
Cdd:cd12084   1 VPEGLRELLEDFTREVLREQP--EDVYEFAADYFEK 34

translocon at the inner envelope of chloroplast subunit 62; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357001  221 AEKEDDGEEKRREQAASVLQRFFRKVMLRVVTKPI-VDPCAEPTEPTEVDASSSPDTAKDGYDDVNLSTVPTTAAI---- 295
Cdd:PLN03209 353 SPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTSPIpTPPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAqvea 432

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21357001  296 -TAGP-TPLPTAPGTVPPSAPG-TAPATARTSAT 326
Cdd:PLN03209 433 kKTRPlSPYARYEDLKPPTSPSpTAPTGVSPSVS 466

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 21357001  17 VPEGLPELLSDVTREVLRCQPkkECLCQFIIDYLHS 52
Cdd:cd12084   1 VPEGLRELLEDFTREVLREQP--EDVYEFAADYFEK 34

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.

                           10        20
                   ....*....|....*....|.
gi 21357001    190 RNQAAITIQAAWRGYWVRLQF 210
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22

translocon at the inner envelope of chloroplast subunit 62; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357001  221 AEKEDDGEEKRREQAASVLQRFFRKVMLRVVTKPI-VDPCAEPTEPTEVDASSSPDTAKDGYDDVNLSTVPTTAAI---- 295
Cdd:PLN03209 353 SPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTSPIpTPPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAqvea 432

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21357001  296 -TAGP-TPLPTAPGTVPPSAPG-TAPATARTSAT 326
Cdd:PLN03209 433 kKTRPlSPYARYEDLKPPTSPSpTAPTGVSPSVS 466

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 21357001  17 VPEGLPELLSDVTREVLRCQPkkECLCQFIIDYLHS 52
Cdd:cd12084   1 VPEGLRELLEDFTREVLREQP--EDVYEFAADYFEK 34

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 7 (RSP7) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP7 is a cAMP-dependent protein kinase (PKA) RII-like protein. RSP7 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of PKA. The D/D domain of RSP7 heterodimerizes with the D/D domain of RSP11 to form an X-type four-helix bundle within the radial spoke RS1 complex.

                        10        20
                ....*....|....*....|....*..
gi 21357001  12 QQAINVPEGLPELLSDVTREVLRCQPK 38
Cdd:cd22984   5 AKKYTIPEEFPAILKDFAREVLREQPK 31

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.

                        10        20
                ....*....|....*....|....*...
gi 21357001 180 RELKRINEAMRNQAAITIQAAWRGYWVR 207
Cdd:cd22307 136 DCRTREPTIEEHEAATKIQAFFRGTLVR 163

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.

                           10        20
                   ....*....|....*....|.
gi 21357001    190 RNQAAITIQAAWRGYWVRLQF 210
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22

dimerization/docking (D/D) domain of the Type II beta Regulatory subunit of cAMP-dependent protein kinase; 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. RII subunits contain a phosphorylation site in their inhibitory site and are both substrates and inhibitors. RIIbeta plays an important role in adipocytes and neuronal tissues. Mice deficient with RIIbeta have small fat cells, and are resistant to obesity, diet-induced diabetes, and alcohol-induced motor defects. The R subunit contains an N-terminal dimerization/docking (D/D) domain, a linker with an inhibitory sequence, and two c-AMP binding domains. 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 21357001  15 INVPEGLPELLSDVTREVLRCQPKKecLCQFIIDYL 50
Cdd:cd12104   1 IEIPEGLTELLQGFTVEVLRNQPGD--LLEFALQYF 34

translocon at the inner envelope of chloroplast subunit 62; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357001  221 AEKEDDGEEKRREQAASVLQRFFRKVMLRVVTKPI-VDPCAEPTEPTEVDASSSPDTAKDGYDDVNLSTVPTTAAI---- 295
Cdd:PLN03209 353 SPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTSPIpTPPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAqvea 432

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21357001  296 -TAGP-TPLPTAPGTVPPSAPG-TAPATARTSAT 326
Cdd:PLN03209 433 kKTRPlSPYARYEDLKPPTSPSpTAPTGVSPSVS 466