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Conserved domains on  [gi|2065645380|ref|XP_007897087|]
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tubulin polyglutamylase complex subunit 1 [Callorhinchus milii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DD_TPGS1 cd22960
dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) ...
14-49 1.14e-13

dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) and similar proteins; TPGS1 is part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. It is required for the development of the spermatid flagellum. TPGS1 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).


:

Pssm-ID: 438529  Cd Length: 39  Bit Score: 63.38  E-value: 1.14e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2065645380  14 RLPPGVGDVVRDALLRVLENRPEDPLSFLSEYFGNL 49
Cdd:cd22960     3 LERTGVTSLLRDALLKVLENRPEDPIAFLAEYFESL 38
 
Name Accession Description Interval E-value
DD_TPGS1 cd22960
dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) ...
14-49 1.14e-13

dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) and similar proteins; TPGS1 is part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. It is required for the development of the spermatid flagellum. TPGS1 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438529  Cd Length: 39  Bit Score: 63.38  E-value: 1.14e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2065645380  14 RLPPGVGDVVRDALLRVLENRPEDPLSFLSEYFGNL 49
Cdd:cd22960     3 LERTGVTSLLRDALLKVLENRPEDPIAFLAEYFESL 38
 
Name Accession Description Interval E-value
DD_TPGS1 cd22960
dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) ...
14-49 1.14e-13

dimerization/docking (D/D) domain found in tubulin polyglutamylase complex subunit 1 (TPGS1) and similar proteins; TPGS1 is part of the neuronal tubulin polyglutamylase complex which contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. It is required for the development of the spermatid flagellum. TPGS1 contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438529  Cd Length: 39  Bit Score: 63.38  E-value: 1.14e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2065645380  14 RLPPGVGDVVRDALLRVLENRPEDPLSFLSEYFGNL 49
Cdd:cd22960     3 LERTGVTSLLRDALLKVLENRPEDPIAFLAEYFESL 38
DD_C11orf49 cd22959
dimerization/docking (D/D) domain found in UPF0705 protein C11orf49 and similar proteins; ...
25-46 1.18e-05

dimerization/docking (D/D) domain found in UPF0705 protein C11orf49 and similar proteins; UPF0705 protein C11orf49 is an uncharacterized protein which contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438528  Cd Length: 53  Bit Score: 41.76  E-value: 1.18e-05
                          10        20
                  ....*....|....*....|..
gi 2065645380  25 DALLRVLENRPEDPLSFLSEYF 46
Cdd:cd22959    15 DAVTQLLENRPENPAKFLAEYF 36
DD_R_PKA_DPY30-like cd22957
dimerization/docking (D/D) domains found in the cAMP-dependent protein kinase regulatory ...
24-49 8.52e-04

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.


Pssm-ID: 438526  Cd Length: 29  Bit Score: 35.94  E-value: 8.52e-04
                          10        20
                  ....*....|....*....|....*.
gi 2065645380  24 RDALLRVLENRPEDPLSFLSEYFGNL 49
Cdd:cd22957     4 QDAVAKLLEERPEDPVEFLAEYFEKA 29
DD_AtENO3-like cd22962
dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and ...
21-52 1.07e-03

dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and similar proteins; Enolase (EC 4.2.1.11), also known as phosphopyruvate hydratase, is a metalloenzyme responsible for catalyzing the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. The subfamily includes Arabidopsis thaliana ENO3, also called ENOC, 2-phospho-D-glycerate hydro-lyase 3, or 2-phosphoglycerate dehydratase 3. It contains an N-terminal domain which 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.


Pssm-ID: 438531  Cd Length: 45  Bit Score: 36.02  E-value: 1.07e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2065645380  21 DVVRDALLRVLENRPEDPLSFLSEYFGNLTAA 52
Cdd:cd22962    14 EKLEEAVNAVVKEKPEDPFGFLAQLLRKRAPP 45
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
19-45 2.82e-03

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: 34.66  E-value: 2.82e-03
                          10        20
                  ....*....|....*....|....*..
gi 2065645380  19 VGDVVRDALLRVLENRPEDPLSFLSEY 45
Cdd:cd22966     9 VGDVLTKALAEVALKRPADPIEFLANW 35
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
22-45 4.43e-03

dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate kinase (AK7, EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK7 is involved in maintaining ciliary structure and function. This model corresponds to the C-terminal domain of AK7, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438536 [Multi-domain]  Cd Length: 41  Bit Score: 34.00  E-value: 4.43e-03
                          10        20
                  ....*....|....*....|....
gi 2065645380  22 VVRDALLRVLENRPEDPLSFLSEY 45
Cdd:cd22967    13 TLTEGLVEVCKVRPEDPVDFLAEY 36
DD_RI_PKA cd12097
dimerization/docking (D/D) domain of the Type I Regulatory subunit of cAMP-dependent protein ...
21-49 4.99e-03

dimerization/docking (D/D) domain of the Type I 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. RI subunits are pseudo-substrates as they do not contain a phosphorylation site in their inhibitory site unlike RII subunits. RIalpha function is required for normal development as its deletion is embryonically lethal. RIbeta is expressed highly in the brain and is associated with hippocampal function. 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.


Pssm-ID: 438518  Cd Length: 49  Bit Score: 34.44  E-value: 4.99e-03
                          10        20
                  ....*....|....*....|....*....
gi 2065645380  21 DVVRDALLRVLENRPEDPLSFLSEYFGNL 49
Cdd:cd12097    15 QLLKDCIVQLCVDRPDNPVAFLREYFEKL 43
 
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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