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Conserved domains on  [gi|578838115|ref|XP_006724625|]
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EF-hand domain-containing family member C2 isoform X3 [Homo sapiens]

Protein Classification

EF-hand domain-containing family member C2( domain architecture ID 12218346)

EF-hand domain-containing family member C2 (EFHC2) is a protein with one predicted calcium-binding EF-hand motif and three DM10 domains, whose function is unknown

Gene Symbol:  EFHC2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 223-334 5.34e-39

DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 residues whose function is unknown. It has been identified in nucleoside diphosphate kinases, namely Nucleoside diphosphate kinase 7 (NDK7), which contain a single copy of the DM10 domain, and in uncharacterized proteins including Rib72 from Chlamydomonas and EF-hand domain-containing protein 1/EF-hand domain-containing family member C2 (EFHC1/2) from mammals, which contain multiple copies of DM10 domains. In Chlamydomonas, and possibly mammals, DM10 domain-containing proteins are tightly bound to the flagellar doublet microtubules. This suggests that DM10 domains might act as flagellar NDK regulatory modules or as units specifically involved in axonemal targeting or assembly. This domain have a PH-like fold which includes seven beta strands, with a short 3-4 residue helix after the first strand, and a more extended alpha helical region at the C terminus.


:

Pssm-ID: 461948  Cd Length: 104  Bit Score: 137.99  E-value: 5.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115  223 FKKFMEKDSYgsksnILRFFAKLV--TDKCVDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGqevfk 300
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWDdpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 578838115  301 SELSEYIKAEELYIGVTVNVNGYLFRLLNADEYT 334
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 30-172 7.40e-36

Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some nucleoside diphosphate kinases;


:

Pssm-ID: 128921  Cd Length: 104  Bit Score: 129.35  E-value: 7.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115    30 HGKILCFFCLWDDSVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRDAlKMFLRRSKLPKNCPprvyqpgqitdravln 109
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKPPP---------------- 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578838115   110 sygdfiknqadgylfdryklgkVDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFTKSYYKSKY 172
Cdd:smart00676  64 ----------------------DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
 
Name Accession Description Interval E-value
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 223-334 5.34e-39

DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 residues whose function is unknown. It has been identified in nucleoside diphosphate kinases, namely Nucleoside diphosphate kinase 7 (NDK7), which contain a single copy of the DM10 domain, and in uncharacterized proteins including Rib72 from Chlamydomonas and EF-hand domain-containing protein 1/EF-hand domain-containing family member C2 (EFHC1/2) from mammals, which contain multiple copies of DM10 domains. In Chlamydomonas, and possibly mammals, DM10 domain-containing proteins are tightly bound to the flagellar doublet microtubules. This suggests that DM10 domains might act as flagellar NDK regulatory modules or as units specifically involved in axonemal targeting or assembly. This domain have a PH-like fold which includes seven beta strands, with a short 3-4 residue helix after the first strand, and a more extended alpha helical region at the C terminus.


Pssm-ID: 461948  Cd Length: 104  Bit Score: 137.99  E-value: 5.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115  223 FKKFMEKDSYgsksnILRFFAKLV--TDKCVDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGqevfk 300
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWDdpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 578838115  301 SELSEYIKAEELYIGVTVNVNGYLFRLLNADEYT 334
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 236-342 2.52e-38

Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some nucleoside diphosphate kinases;


Pssm-ID: 128921  Cd Length: 104  Bit Score: 136.29  E-value: 2.52e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115   236 SNILRFFAKLVTDKC-VDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGQEVfkselSEYIKAEELYI 314
Cdd:smart00676   2 KKVLRFDAYWEDPVAmFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDD-----PEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 578838115   315 GVTVNVNGYLFRLLNADEYTLNYMEQNT 342
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 30-172 7.40e-36

Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some nucleoside diphosphate kinases;


Pssm-ID: 128921  Cd Length: 104  Bit Score: 129.35  E-value: 7.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115    30 HGKILCFFCLWDDSVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRDAlKMFLRRSKLPKNCPprvyqpgqitdravln 109
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKPPP---------------- 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578838115   110 sygdfiknqadgylfdryklgkVDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFTKSYYKSKY 172
Cdd:smart00676  64 ----------------------DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 23-164 5.35e-31

DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 residues whose function is unknown. It has been identified in nucleoside diphosphate kinases, namely Nucleoside diphosphate kinase 7 (NDK7), which contain a single copy of the DM10 domain, and in uncharacterized proteins including Rib72 from Chlamydomonas and EF-hand domain-containing protein 1/EF-hand domain-containing family member C2 (EFHC1/2) from mammals, which contain multiple copies of DM10 domains. In Chlamydomonas, and possibly mammals, DM10 domain-containing proteins are tightly bound to the flagellar doublet microtubules. This suggests that DM10 domains might act as flagellar NDK regulatory modules or as units specifically involved in axonemal targeting or assembly. This domain have a PH-like fold which includes seven beta strands, with a short 3-4 residue helix after the first strand, and a more extended alpha helical region at the C terminus.


Pssm-ID: 461948  Cd Length: 104  Bit Score: 116.03  E-value: 5.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115   23 LKQFLQYHGKILCFFCLWDD-SVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRdALKMFLRRSKLPKNCPPrvyqpgq 101
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPKPGTG------- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578838115  102 itdravlnsygdfiknqadgylfdryklgkvDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFT 164
Cdd:pfam06565  73 -------------------------------GPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
 
Name Accession Description Interval E-value
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 223-334 5.34e-39

DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 residues whose function is unknown. It has been identified in nucleoside diphosphate kinases, namely Nucleoside diphosphate kinase 7 (NDK7), which contain a single copy of the DM10 domain, and in uncharacterized proteins including Rib72 from Chlamydomonas and EF-hand domain-containing protein 1/EF-hand domain-containing family member C2 (EFHC1/2) from mammals, which contain multiple copies of DM10 domains. In Chlamydomonas, and possibly mammals, DM10 domain-containing proteins are tightly bound to the flagellar doublet microtubules. This suggests that DM10 domains might act as flagellar NDK regulatory modules or as units specifically involved in axonemal targeting or assembly. This domain have a PH-like fold which includes seven beta strands, with a short 3-4 residue helix after the first strand, and a more extended alpha helical region at the C terminus.


Pssm-ID: 461948  Cd Length: 104  Bit Score: 137.99  E-value: 5.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115  223 FKKFMEKDSYgsksnILRFFAKLV--TDKCVDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGqevfk 300
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWDdpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 578838115  301 SELSEYIKAEELYIGVTVNVNGYLFRLLNADEYT 334
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 236-342 2.52e-38

Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some nucleoside diphosphate kinases;


Pssm-ID: 128921  Cd Length: 104  Bit Score: 136.29  E-value: 2.52e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115   236 SNILRFFAKLVTDKC-VDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGQEVfkselSEYIKAEELYI 314
Cdd:smart00676   2 KKVLRFDAYWEDPVAmFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDD-----PEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 578838115   315 GVTVNVNGYLFRLLNADEYTLNYMEQNT 342
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 30-172 7.40e-36

Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some nucleoside diphosphate kinases;


Pssm-ID: 128921  Cd Length: 104  Bit Score: 129.35  E-value: 7.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115    30 HGKILCFFCLWDDSVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRDAlKMFLRRSKLPKNCPprvyqpgqitdravln 109
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKPPP---------------- 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578838115   110 sygdfiknqadgylfdryklgkVDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFTKSYYKSKY 172
Cdd:smart00676  64 ----------------------DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 23-164 5.35e-31

DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 residues whose function is unknown. It has been identified in nucleoside diphosphate kinases, namely Nucleoside diphosphate kinase 7 (NDK7), which contain a single copy of the DM10 domain, and in uncharacterized proteins including Rib72 from Chlamydomonas and EF-hand domain-containing protein 1/EF-hand domain-containing family member C2 (EFHC1/2) from mammals, which contain multiple copies of DM10 domains. In Chlamydomonas, and possibly mammals, DM10 domain-containing proteins are tightly bound to the flagellar doublet microtubules. This suggests that DM10 domains might act as flagellar NDK regulatory modules or as units specifically involved in axonemal targeting or assembly. This domain have a PH-like fold which includes seven beta strands, with a short 3-4 residue helix after the first strand, and a more extended alpha helical region at the C terminus.


Pssm-ID: 461948  Cd Length: 104  Bit Score: 116.03  E-value: 5.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838115   23 LKQFLQYHGKILCFFCLWDD-SVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRdALKMFLRRSKLPKNCPPrvyqpgq 101
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPKPGTG------- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578838115  102 itdravlnsygdfiknqadgylfdryklgkvDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFT 164
Cdd:pfam06565  73 -------------------------------GPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
 
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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