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Conserved domains on  [gi|24648147|ref|NP_650788|]
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uncharacterized protein Dmel_CG14282 [Drosophila melanogaster]

Protein Classification

dimerization/docking domain-containing protein( domain architecture ID 1990)

dimerization/docking (D/D) domain-containing protein similar to Mus musculus ciliogenesis-associated TTC17-interacting protein that plays a role in primary ciliogenesis by modulating actin polymerization

CATH:  1.20.890.10
SCOP:  4000882

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DD_R_PKA_DPY30-like super family cl02594
dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory ...
219-258 1.89e-05

dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory subunit (PRKAR) and the DPY30/SDC1-like family; This hierarchy includes the dimerization/docking (D/D) domains of type I and type II cAMP-dependent protein kinase (PKA) regulatory (R) subunits, DPY30 from animals and its homologs, SDC1 from yeasts, and similar domains. 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 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 D/D domain, a linker with an inhibitory sequence (IS), 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. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. Yeast SDC1 (suppressor of CDC25 protein 1) is the smallest subunit of COMPASS (COMplex of Proteins ASsociated with Set1) and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. DPY30/SDC1 contains a C-terminal helical bundle domain that directly interacts with Ash2L (in human)/Bre2 (in yeast) COMPASS through the DPY30-binding motif (DBM). The DPY30/SDC1 helical bundle domain, also called D/D domain, is formed of two alpha-helices that may be analogous to the D/D domain found in regulatory subunit of PKA.


The actual alignment was detected with superfamily member cd22966:

Pssm-ID: 445844  Cd Length: 44  Bit Score: 41.21  E-value: 1.89e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24648147 219 IKEQMGDVLVRAFAQLHIHSPQDPRAFIAAYLMNLDRNEQ 258
Cdd:cd22966   5 LKETVGDVLTKALAEVALKRPADPIEFLANWLLKYRENEE 44
 
Name Accession Description Interval E-value
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
219-258 1.89e-05

dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like family; The DYDC-like family includes DYDC1 and DYDC2, as well as Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins. DYDC1 plays a crucial role during acrosome biogenesis. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. Members of this family contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438535  Cd Length: 44  Bit Score: 41.21  E-value: 1.89e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24648147 219 IKEQMGDVLVRAFAQLHIHSPQDPRAFIAAYLMNLDRNEQ 258
Cdd:cd22966   5 LKETVGDVLTKALAEVALKRPADPIEFLANWLLKYRENEE 44
 
Name Accession Description Interval E-value
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
219-258 1.89e-05

dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like family; The DYDC-like family includes DYDC1 and DYDC2, as well as Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins. DYDC1 plays a crucial role during acrosome biogenesis. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. Members of this family contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438535  Cd Length: 44  Bit Score: 41.21  E-value: 1.89e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24648147 219 IKEQMGDVLVRAFAQLHIHSPQDPRAFIAAYLMNLDRNEQ 258
Cdd:cd22966   5 LKETVGDVLTKALAEVALKRPADPIEFLANWLLKYRENEE 44
DD_CrRSP2-like cd22982
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
219-264 1.88e-03

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) 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 the 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. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. This model corresponds to the C-terminal domain of RSP2, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438551  Cd Length: 53  Bit Score: 35.81  E-value: 1.88e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24648147 219 IKEQMGDVLVRAFAQLHIHSPQDPRAFIAAYLMNLDRNeQEMKEKL 264
Cdd:cd22982   5 LKETVGEALAKGCAAVALAQPEDPVEYLGLWLLQHVRN-KEIEKKF 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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