2IZX,2HWN,2KYG,1L6E,2IZY,5XBY,3J4Q,3TMH,5H77,5H78,4ZP3


Conserved Protein Domain Family
DD_RIIalpha_PKA

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cd12103: DD_RIIalpha_PKA 
Click on image for an interactive view with Cn3D
dimerization/docking (D/D) domain of the Type II alpha 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. RIIalpha plays a role in the association and dissociation of PKA with the centrosome during interphase and mitosis, respectively. It is also involved in endosome-to-Golgi and Golgi-to-ER transport. 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.
Statistics
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PSSM-Id: 438524
Aligned: 16 rows
Threshold Bit Score: 71.018
Created: 25-May-2012
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interfaceAKAP
Conserved site includes 23 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Comment:the Dimerization/Docking (D/D) domain of RIIalpha dimerizes to form an X-type four-helix bundle
  • Structure:2IZX; Human RIIalpha D/D domain forms a homodimer; contacts at 4A.
  • Structure:1L6E; Mus musculus RIIalpha D/D domain forms a homodimer; contacts at 4A.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        ##### #  ##  ##  ##  #  #### ##  ## ##   
2IZX_A         1 IQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREAR 41  human
1L6E_A         5 IQIPPGLTELLQGYTVEVLRQQPPDLVDFAVEYFTRLREAR 45  house mouse
NP_001070838   3 IEIPVGLTELLQGYTVEVLRQRPPDLVEFAVQYFTRLRDTR 43  zebrafish
2IZY_A         4 IQIPPGLTELLQGYTVEVLRQQPPDLVDFAVEYFTRLREAR 44  house mouse
XP_018116896   3 IEIPPGLTDLLQGYTVEVLRQKPPDLVEFAIQYFTRLKEKQ 43  African clawed frog
5XBY_A         4 WQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREAR 44  human
3J4Q_B         4 IQIPAGLTELLQGYTVEVLRQQPPDLVDFAVEYFTRLREAR 44  house mouse
3TMH_B         7 IQIPPGLTELLQGYTVEVLRQQPPDLVDFAVEYFTRLREAR 47  Norway rat
5H77_A         4 WQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLRQQR 44  human
5H78_A         4 MQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLRSER 44  human

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