dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55)-like family; The TEX55-like family includes TEX55, F-box/LRR-repeat protein 13 (FBXL13), adenylate kinase isoenzymes AK5 and AK8, as well as uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), and protein VEST-1. TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. AK5 and AK8 act as nucleoside monophosphate (NMP) kinases that catalyze the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Members of this family contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

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gi 1243457485   7 ELQAAEYLEKHQIKEVVSYLTSALLFFRPEKPKEYLISLLERL 49
Cdd:cd22961     1 LEDAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQI 43

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

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gi 1243457485   9 QAAEYLEKHQIKEVVSYLTSALLFFRPEKPKEYLISLLERLR 50
Cdd:cd22978     3 DAKDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKIR 44

dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and similar proteins; AK (EC 2.7.4.3), also called ATP-AMP transphosphorylase, ATP:AMP phosphotransferase, or adenylate monophosphate kinase, catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. It plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Members of this subfamily contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.

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gi 1243457485   5 SRELQaaEYLEKHQIKEVVSYLTSALLFFRPEKPKEYLISLLER 48
Cdd:cd22981     2 SEDAQ--KYLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLER 43