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Conserved domains on  [gi|1370470880|ref|XP_024306510|]
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EF-hand calcium-binding domain-containing protein 5 isoform X10 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DD_EFCAB5 cd22968
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ...
114-169 6.29e-22

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


:

Pssm-ID: 438537  Cd Length: 60  Bit Score: 90.33  E-value: 6.29e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370470880  114 NTAYLLDKLLPTLVPGVENMLTQVEKKKVLTEADTP---SKFDPINYLGEYLIRNNPNY 169
Cdd:cd22968      2 TRAYLVEKVLPTLVPGLEKLLKEVERRGLLEEEGRPepaPRFNPINWLAQYLMRNNPRY 60
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1005-1097 1.27e-05

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


:

Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.61  E-value: 1.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370470880  1005 YRDMKGISFTVVDEGKPIHVPQVQYHGniFFWNQSRNKHDYNGSFLALPL--QDaymRIFGVLAVDTLRDPHEiniFLPH 1082
Cdd:smart00065   52 FPLDEGLAGRVAETGRPLNIPDVEADP--LFAEDLLGRYQGVRSFLAVPLvaDG---ELVGVLALHNKKSPRP---FTEE 123
                            90
                    ....*....|....*
gi 1370470880  1083 EIRFYQGVANVFSTA 1097
Cdd:smart00065  124 DEELLQALANQLAIA 138
 
Name Accession Description Interval E-value
DD_EFCAB5 cd22968
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ...
114-169 6.29e-22

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438537  Cd Length: 60  Bit Score: 90.33  E-value: 6.29e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370470880  114 NTAYLLDKLLPTLVPGVENMLTQVEKKKVLTEADTP---SKFDPINYLGEYLIRNNPNY 169
Cdd:cd22968      2 TRAYLVEKVLPTLVPGLEKLLKEVERRGLLEEEGRPepaPRFNPINWLAQYLMRNNPRY 60
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1005-1097 1.27e-05

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.61  E-value: 1.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370470880  1005 YRDMKGISFTVVDEGKPIHVPQVQYHGniFFWNQSRNKHDYNGSFLALPL--QDaymRIFGVLAVDTLRDPHEiniFLPH 1082
Cdd:smart00065   52 FPLDEGLAGRVAETGRPLNIPDVEADP--LFAEDLLGRYQGVRSFLAVPLvaDG---ELVGVLALHNKKSPRP---FTEE 123
                            90
                    ....*....|....*
gi 1370470880  1083 EIRFYQGVANVFSTA 1097
Cdd:smart00065  124 DEELLQALANQLAIA 138
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
115-167 3.32e-03

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: 36.82  E-value: 3.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370470880  115 TAYLLDKLLPTLVPGvenmLTQVEKKKvlteadtPSkfDPINYLGEYLIRNNP 167
Cdd:pfam05186    3 RQYLNKTVAPILLQG----LTELAKER-------PE--DPIEYLADYLLKNNP 42
 
Name Accession Description Interval E-value
DD_EFCAB5 cd22968
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ...
114-169 6.29e-22

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438537  Cd Length: 60  Bit Score: 90.33  E-value: 6.29e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370470880  114 NTAYLLDKLLPTLVPGVENMLTQVEKKKVLTEADTP---SKFDPINYLGEYLIRNNPNY 169
Cdd:cd22968      2 TRAYLVEKVLPTLVPGLEKLLKEVERRGLLEEEGRPepaPRFNPINWLAQYLMRNNPRY 60
DD_IQCK cd22969
dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar ...
108-167 8.69e-09

dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar proteins; IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. Although its function remains unclear, IQCK contains a conserved region 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.


Pssm-ID: 438538  Cd Length: 58  Bit Score: 52.89  E-value: 8.69e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370470880  108 DSMTLNNTAYLLDKLLPTLVPGVENMLTQVEKKKVLTEADTpsKFDPINYLGEYLIRNNP 167
Cdd:cd22969      1 DLKTCSPVEYLEEYIFPVLLPALEEMLEEAKKEDCFERKRT--KFNGLDFLTEYLYNNNP 58
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
115-166 1.28e-07

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: 48.98  E-value: 1.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370470880  115 TAYLLDKLLPTLVPGVENMLTQVEKkkvlteadtpskfDPINYLGEYLIRNN 166
Cdd:cd22958      2 REYLSETVLPTLIPALAELLKARPE-------------DPLEWLAEYLLRNN 40
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1005-1097 1.27e-05

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.61  E-value: 1.27e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370470880  1005 YRDMKGISFTVVDEGKPIHVPQVQYHGniFFWNQSRNKHDYNGSFLALPL--QDaymRIFGVLAVDTLRDPHEiniFLPH 1082
Cdd:smart00065   52 FPLDEGLAGRVAETGRPLNIPDVEADP--LFAEDLLGRYQGVRSFLAVPLvaDG---ELVGVLALHNKKSPRP---FTEE 123
                            90
                    ....*....|....*
gi 1370470880  1083 EIRFYQGVANVFSTA 1097
Cdd:smart00065  124 DEELLQALANQLAIA 138
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
116-166 4.60e-05

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: 41.70  E-value: 4.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370470880  116 AYLLDKLLPTLVPGvenmLTQVEKKKvlteadtPSkfDPINYLGEYLIRNN 166
Cdd:cd22967      4 NYLMKYVMPTLTEG----LVEVCKVR-------PE--DPVDFLAEYLFKHN 41
DD_NDKH5-like cd22970
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5) ...
115-167 1.01e-04

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: 40.98  E-value: 1.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370470880  115 TAYLLDKLLPTLVPGvenmLTQVEKKKvlteadtPSkfDPINYLGEYLIRNNP 167
Cdd:cd22970      6 KDYLSKHVNPTLLKG----LTELCKEK-------PA--DPVTWLADWLLENNP 45
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
116-167 9.75e-04

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: 38.17  E-value: 9.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370470880  116 AYLLDKLLPTLVPGvenmLTQVEKKKvlteadtPSkfDPINYLGEYLIRNNP 167
Cdd:cd22965      3 QYLDKTVVPVLLEG----LKELAKER-------PE--DPLEFLAEYLLKNSP 41
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
115-167 3.32e-03

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: 36.82  E-value: 3.32e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1370470880  115 TAYLLDKLLPTLVPGvenmLTQVEKKKvlteadtPSkfDPINYLGEYLIRNNP 167
Cdd:pfam05186    3 RQYLNKTVAPILLQG----LTELAKER-------PE--DPIEYLADYLLKNNP 42
 
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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