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Conserved domains on  [gi|530393110|ref|XP_005269606|]
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DPY30 domain-containing protein 1 isoform X1 [Homo sapiens]

Protein Classification

DPY30 domain-containing protein( domain architecture ID 17786322)

DPY30 domain-containing protein similar to Homo sapiens DPY30 domain-containing proteins 1 and 2

CATH:  1.20.890.10
Gene Ontology:  GO:0048188|GO:0046983

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
2-43 3.86e-20

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: 78.96  E-value: 3.86e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530393110   2 ESIYLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKEN 43
Cdd:cd22966    1 DSAYLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYREN 42
 
Name Accession Description Interval E-value
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
2-43 3.86e-20

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: 78.96  E-value: 3.86e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530393110   2 ESIYLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKEN 43
Cdd:cd22966    1 DSAYLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYREN 42
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
1-42 2.64e-13

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


Pssm-ID: 428357  Cd Length: 42  Bit Score: 61.09  E-value: 2.64e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 530393110    1 MESIYLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKE 42
Cdd:pfam05186   1 PARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
 
Name Accession Description Interval E-value
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
2-43 3.86e-20

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: 78.96  E-value: 3.86e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530393110   2 ESIYLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKEN 43
Cdd:cd22966    1 DSAYLKETVGDVLTKALAEVALKRPADPIEFLANWLLKYREN 42
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
1-42 2.64e-13

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


Pssm-ID: 428357  Cd Length: 42  Bit Score: 61.09  E-value: 2.64e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 530393110    1 MESIYLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKE 42
Cdd:pfam05186   1 PARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
DD_CrRSP2-like cd22982
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
2-53 4.82e-12

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: 58.15  E-value: 4.82e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530393110   2 ESIYLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKENVTMEQLRQKE 53
Cdd:cd22982    1 DTEYLKETVGEALAKGCAAVALAQPEDPVEYLGLWLLQHVRNKEIEKKFARE 52
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
5-40 3.34e-09

dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like family includes DPY30 from animals and its homolog SDC1 from yeast, DPY30 domain-containing protein (DYDC), adenylate kinase 7 (AK7), IQ domain-containing protein K (IQCK), nucleoside diphosphate kinase homolog 5 (NDKH5), EF-hand calcium-binding domain-containing protein 5 (EFCAB5), and Chlamydomonas reinhardtii flagellar radial spoke proteins, RSP2 and RSP23. 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 allosterically 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, also called complex proteins associated with SET1 protein SDC1, Set1C component SDC1, or 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. DYDC1 plays a crucial role during acrosome biogenesis. 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 is involved in maintaining ciliary structure and function. IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. The function of IQCK remains unclear. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a DPY30/SDC1 helical bundle domain that is formed by two alpha-helices. The DPY30/SDC1 helical bundle domain is also called D/D domain and might be analogous to the D/D domain found in the regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438527  Cd Length: 40  Bit Score: 50.14  E-value: 3.34e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 530393110   5 YLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKY 40
Cdd:cd22958    4 YLSETVLPTLIPALAELLKARPEDPLEWLAEYLLRN 39
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
5-40 4.77e-08

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: 47.10  E-value: 4.77e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 530393110   5 YLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKY 40
Cdd:cd22967    5 YLMKYVMPTLTEGLVEVCKVRPEDPVDFLAEYLFKH 40
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
5-42 6.62e-07

dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 from animals and its homologs, including SDC1 from yeast. 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 allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. DPY30 is the core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. As part of the MLL1/MLL complex, DPY30 is involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In a teratocarcinoma cell, DPY30 plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. It may also play an indirect or direct role in endosomal transport. Yeast SDC1, also called complex proteins associated with SET1 (COMPASS) protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS 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. The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. This model corresponds to the C-terminal helical bundle domain of DPY30/SDC1, which is called dimerization/docking (D/D) domain. It forms a homodimer, which directly interacts with the Ash2L (Bre2 in yeast) subunit of COMPASS through its DPY30-binding motif (DBM).


Pssm-ID: 438534  Cd Length: 41  Bit Score: 43.95  E-value: 6.62e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530393110   5 YLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKE 42
Cdd:cd22965    4 YLDKTVVPVLLEGLKELAKERPEDPLEFLAEYLLKNSP 41
DD_NDKH5-like cd22970
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5) ...
5-36 8.34e-07

dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5)-like family; The NDKH5 family includes NDKH5, Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) and similar proteins. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438539  Cd Length: 45  Bit Score: 44.06  E-value: 8.34e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 530393110   5 YLQKHLGACLTQGLAEVARVRPVDPIEYLALW 36
Cdd:cd22970    8 YLSKHVNPTLLKGLTELCKEKPADPVTWLADW 39
DD_CrRSP23-like cd22983
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
5-37 1.66e-04

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) 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. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. RSP23 consists of an N-terminal catalytic NDK domain followed by a repetitive region that includes three IQ motifs and a highly acidic C-terminal segment, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438552  Cd Length: 58  Bit Score: 38.05  E-value: 1.66e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 530393110   5 YLQKHLGACLTQGLAEVARVRP----VDPIEYLALWI 37
Cdd:cd22983   10 YIKKKLQPVLVKGLTALAKAKPssdpLEAIRWLAHWL 46
 
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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