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Conserved domains on  [gi|2462631211|ref|XP_054183892|]
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EF-hand domain-containing family member C2 isoform X2 [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 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 75-182 1.37e-44

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: 154.39  E-value: 1.37e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211   75 DKQVLSFDAYLEEEVLDKsqtnYRIRYYKIYFYPEDDTIQVNEPEVKNSGLLQGTSIRRHRITLPPPDEDQFYTVYHFNV 154
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMF----YLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 2462631211  155 GTEVVFYGRTFKIYDCDAFTRNFLRKIG 182
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 419-530 1.56e-38

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: 1.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211 419 FKKFMEKDSYgsksnILRFFAKLV--TDKCVDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGqevfk 496
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWDdpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462631211 497 SELSEYIKAEELYIGVTVNVNGYLFRLLNADEYT 530
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 226-368 1.31e-35

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: 129.74  E-value: 1.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211  226 HGKILCFFCLWDDSVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRDAlKMFLRRSKLPKNCPprvyqpgqitdravln 305
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKPPP---------------- 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462631211  306 sygdfiknqadgylfdryklgkVDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFTKSYYKSKY 368
Cdd:smart00676  64 ----------------------DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
 
Name Accession Description Interval E-value
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 75-182 1.37e-44

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: 154.39  E-value: 1.37e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211   75 DKQVLSFDAYLEEEVLDKsqtnYRIRYYKIYFYPEDDTIQVNEPEVKNSGLLQGTSIRRHRITLPPPDEDQFYTVYHFNV 154
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMF----YLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 2462631211  155 GTEVVFYGRTFKIYDCDAFTRNFLRKIG 182
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 419-530 1.56e-38

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: 1.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211 419 FKKFMEKDSYgsksnILRFFAKLV--TDKCVDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGqevfk 496
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWDdpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462631211 497 SELSEYIKAEELYIGVTVNVNGYLFRLLNADEYT 530
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 432-538 5.47e-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: 5.47e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211  432 SNILRFFAKLVTDKC-VDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGQEVfkselSEYIKAEELYI 510
Cdd:smart00676   2 KKVLRFDAYWEDPVAmFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDD-----PEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 2462631211  511 GVTVNVNGYLFRLLNADEYTLNYMEQNT 538
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 226-368 1.31e-35

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: 129.74  E-value: 1.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211  226 HGKILCFFCLWDDSVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRDAlKMFLRRSKLPKNCPprvyqpgqitdravln 305
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKPPP---------------- 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462631211  306 sygdfiknqadgylfdryklgkVDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFTKSYYKSKY 368
Cdd:smart00676  64 ----------------------DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 68-174 2.83e-34

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: 126.04  E-value: 2.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211  68 VPSWVAFDKQVLSFDAYLEEEVLDKSQtnyRIRYYKIYFYPEDDTIQVNEPEVKNSGLLQGTSIRRHRITLPPPDEDQFY 147
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDPTESPED---EYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTGGPEYY 77

                          90       100
                  ....*....|....*....|....*..
gi 2462631211 148 TVYHFNVGTEVVFYGRTFKIYDCDAFT 174
Cdd:pfam06565  78 TPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 219-360 9.69e-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: 9.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211 219 LKQFLQYHGKILCFFCLWDD-SVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRdALKMFLRRSKLPKNCPPrvyqpgq 297
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPKPGTG------- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462631211 298 itdravlnsygdfiknqadgylfdryklgkvDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFT 360
Cdd:pfam06565  73 -------------------------------GPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
 
Name Accession Description Interval E-value
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 75-182 1.37e-44

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: 154.39  E-value: 1.37e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211   75 DKQVLSFDAYLEEEVLDKsqtnYRIRYYKIYFYPEDDTIQVNEPEVKNSGLLQGTSIRRHRITLPPPDEDQFYTVYHFNV 154
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMF----YLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 2462631211  155 GTEVVFYGRTFKIYDCDAFTRNFLRKIG 182
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 419-530 1.56e-38

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: 1.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211 419 FKKFMEKDSYgsksnILRFFAKLV--TDKCVDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGqevfk 496
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWDdpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462631211 497 SELSEYIKAEELYIGVTVNVNGYLFRLLNADEYT 530
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 432-538 5.47e-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: 5.47e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211  432 SNILRFFAKLVTDKC-VDLDRMFVISYYLGDDTISVFEPIERNSGIAGGMFLKRSRVKKPGQEVfkselSEYIKAEELYI 510
Cdd:smart00676   2 KKVLRFDAYWEDPVAmFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDD-----PEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 2462631211  511 GVTVNVNGYLFRLLNADEYTLNYMEQNT 538
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 226-368 1.31e-35

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: 129.74  E-value: 1.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211  226 HGKILCFFCLWDDSVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRDAlKMFLRRSKLPKNCPprvyqpgqitdravln 305
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKPPP---------------- 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462631211  306 sygdfiknqadgylfdryklgkVDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFTKSYYKSKY 368
Cdd:smart00676  64 ----------------------DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 68-174 2.83e-34

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: 126.04  E-value: 2.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211  68 VPSWVAFDKQVLSFDAYLEEEVLDKSQtnyRIRYYKIYFYPEDDTIQVNEPEVKNSGLLQGTSIRRHRITLPPPDEDQFY 147
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDPTESPED---EYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTGGPEYY 77

                          90       100
                  ....*....|....*....|....*..
gi 2462631211 148 TVYHFNVGTEVVFYGRTFKIYDCDAFT 174
Cdd:pfam06565  78 TPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 219-360 9.69e-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: 9.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631211 219 LKQFLQYHGKILCFFCLWDD-SVSMFGDRRELILHYFLCDDTIEIKELLPHSSGRdALKMFLRRSKLPKNCPPrvyqpgq 297
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPKPGTG------- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462631211 298 itdravlnsygdfiknqadgylfdryklgkvDQEFYKDSDLSLGVTINVWGRKVLLYDCDEFT 360
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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