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Conserved domains on  [gi|254553420|ref|NP_001116419|]
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EF-hand domain-containing protein 1 [Rattus norvegicus]

Protein Classification

DM10 domain-containing protein; EF-hand domain-containing family member C2; DUF1126 domain-containing protein( domain architecture ID 13923164)

DM10 domain-containing protein contains multiple DUF1126 domains that may has a PH-like fold; similar to EF-hand domain-containing family member C1/C2 (EFHC1/EFHC2); DM10 domain-containing protein contains one or more DUF1126 domains that may has a PH-like fold; similar to N-terminal region of Homo sapiens EF-hand domain-containing family member C2; 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; DM10 domain-containing protein contains multiple DUF1126 domains that may has a PH-like fold; similar to EF-hand domain-containing family member C1/C2 (EFHC1/EFHC2); 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; DUF1126 domain-containing protein similar to EF-hand domain-containing family member C1/C2 (EFHC1/EFHC2)

Gene Symbol:  EFHC2
PubMed:  16572395

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 ...
 232-351 3.01e-42

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: 148.00  E-value: 3.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420  232 LKQFLTFDKQVLRFYAIWDD-TDSLFGECRHYIIHYYLMDDTVEIREVHERNNGRdPFPLLMNRQRMPKvlvdNGKNFPq 310
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPK----PGTGGP- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 254553420  311 cvleisdqevlEWYTAKDFIVGKPLTILGRTFFIYDCDPFT 351
Cdd:pfam06565  75 -----------EYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 411-512 1.30e-40

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: 143.38  E-value: 1.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420  411 KMLMNDNKVLRYLAALESP--IPEDKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKFLGRTKVVKSFSPvdNPIYYGPS 488
Cdd:pfam06565   3 KFLENDRKVLRFYAYWDDPteSPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTG--GPEYYTPK 80

                          90       100
                  ....*....|....*....|....
gi 254553420  489 DFFIGAVIEVFGHRFVILDTDEYV 512
Cdd:pfam06565  81 DLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 93-198 3.35e-40

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: 142.45  E-value: 3.35e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420    93 DKKVLKFSAYFQEDVPismeEHYRIRRVNIYYYLEDDSMSVIEPVVENSGIPQGKLVKRQRLAK--NDVGDHYHWKDLNR 170
Cdd:smart00676   1 DKKVLRFDAYWEDPVA----MFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKppPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 254553420   171 GINLTIYGKTFRIVDCDRFTQDFLESQG 198
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 587-647 6.24e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 44.08  E-value: 6.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254553420 587 LRERFQVYDKEESGYVDKETFFKVCETLNVPVDDSLIKELIRLC-THGEGRINYYNFVRAFS 647
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 232-351 3.01e-42

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: 148.00  E-value: 3.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420  232 LKQFLTFDKQVLRFYAIWDD-TDSLFGECRHYIIHYYLMDDTVEIREVHERNNGRdPFPLLMNRQRMPKvlvdNGKNFPq 310
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPK----PGTGGP- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 254553420  311 cvleisdqevlEWYTAKDFIVGKPLTILGRTFFIYDCDPFT 351
Cdd:pfam06565  75 -----------EYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 411-512 1.30e-40

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: 143.38  E-value: 1.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420  411 KMLMNDNKVLRYLAALESP--IPEDKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKFLGRTKVVKSFSPvdNPIYYGPS 488
Cdd:pfam06565   3 KFLENDRKVLRFYAYWDDPteSPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTG--GPEYYTPK 80

                          90       100
                  ....*....|....*....|....
gi 254553420  489 DFFIGAVIEVFGHRFVILDTDEYV 512
Cdd:pfam06565  81 DLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 93-198 3.35e-40

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: 142.45  E-value: 3.35e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420    93 DKKVLKFSAYFQEDVPismeEHYRIRRVNIYYYLEDDSMSVIEPVVENSGIPQGKLVKRQRLAK--NDVGDHYHWKDLNR 170
Cdd:smart00676   1 DKKVLRFDAYWEDPVA----MFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKppPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 254553420   171 GINLTIYGKTFRIVDCDRFTQDFLESQG 198
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 86-190 2.14e-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: 139.91  E-value: 2.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420   86 VPAHVAFDKKVLKFSAYFQEDvPISMEEHYRirRVNIYYYLEDDSMSVIEPVVENSGIPQGKLVKRQRLAKNDVG--DHY 163
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDP-TESPEDEYR--KFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTGgpEYY 77

                          90       100
                  ....*....|....*....|....*..
gi 254553420  164 HWKDLNRGINLTIYGKTFRIVDCDRFT 190
Cdd:pfam06565  78 TPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 416-520 7.30e-39

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: 138.60  E-value: 7.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420   416 DNKVLRYLAALESPIPE-DKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKFLGRTKVVKsfSPVDNPIYYGPSDFFIGA 494
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMfYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPK--PPPDDPEYYHASDLNVGT 78

                           90       100
                   ....*....|....*....|....*.
gi 254553420   495 VIEVFGHRFVILDTDEYVLKYMESNA 520
Cdd:smart00676  79 TINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 239-359 2.00e-37

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: 134.75  E-value: 2.00e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420   239 DKQVLRFYAIWDDTDSLFGECRHYIIHYYLMDDTVEIREVHERNNGRDPfPLLMNRQRMPKVlvdngknfpqcvleisDQ 318
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKP----------------PP 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 254553420   319 EVLEWYTAKDFIVGKPLTILGRTFFIYDCDPFTRQFYKDKF 359
Cdd:smart00676  64 DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 587-647 6.24e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 44.08  E-value: 6.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254553420 587 LRERFQVYDKEESGYVDKETFFKVCETLNVPVDDSLIKELIRLC-THGEGRINYYNFVRAFS 647
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
584-647 3.00e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.24  E-value: 3.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254553420  584 KDNLRERFQVYDKEESGYVDKETFFKVCETL--NVPVDDSLIKELIRLC-THGEGRINYYNFVRAFS 647
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFdLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 578-644 2.17e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.06  E-value: 2.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254553420 578 LKDISCKDNLRERFQVYDKEESGYVDKETFFKVCETLNVPVDDSLIKELIRLC-THGEGRINYYNFVR 644
Cdd:PTZ00184  77 MKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREAdVDGDGQINYEEFVK 144
 
Name Accession Description Interval E-value
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 232-351 3.01e-42

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: 148.00  E-value: 3.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420  232 LKQFLTFDKQVLRFYAIWDD-TDSLFGECRHYIIHYYLMDDTVEIREVHERNNGRdPFPLLMNRQRMPKvlvdNGKNFPq 310
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPK----PGTGGP- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 254553420  311 cvleisdqevlEWYTAKDFIVGKPLTILGRTFFIYDCDPFT 351
Cdd:pfam06565  75 -----------EYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 411-512 1.30e-40

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: 143.38  E-value: 1.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420  411 KMLMNDNKVLRYLAALESP--IPEDKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKFLGRTKVVKSFSPvdNPIYYGPS 488
Cdd:pfam06565   3 KFLENDRKVLRFYAYWDDPteSPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTG--GPEYYTPK 80

                          90       100
                  ....*....|....*....|....
gi 254553420  489 DFFIGAVIEVFGHRFVILDTDEYV 512
Cdd:pfam06565  81 DLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 93-198 3.35e-40

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: 142.45  E-value: 3.35e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420    93 DKKVLKFSAYFQEDVPismeEHYRIRRVNIYYYLEDDSMSVIEPVVENSGIPQGKLVKRQRLAK--NDVGDHYHWKDLNR 170
Cdd:smart00676   1 DKKVLRFDAYWEDPVA----MFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKppPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 254553420   171 GINLTIYGKTFRIVDCDRFTQDFLESQG 198
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 86-190 2.14e-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: 139.91  E-value: 2.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420   86 VPAHVAFDKKVLKFSAYFQEDvPISMEEHYRirRVNIYYYLEDDSMSVIEPVVENSGIPQGKLVKRQRLAKNDVG--DHY 163
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDP-TESPEDEYR--KFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTGgpEYY 77

                          90       100
                  ....*....|....*....|....*..
gi 254553420  164 HWKDLNRGINLTIYGKTFRIVDCDRFT 190
Cdd:pfam06565  78 TPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 416-520 7.30e-39

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: 138.60  E-value: 7.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420   416 DNKVLRYLAALESPIPE-DKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKFLGRTKVVKsfSPVDNPIYYGPSDFFIGA 494
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMfYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPK--PPPDDPEYYHASDLNVGT 78

                           90       100
                   ....*....|....*....|....*.
gi 254553420   495 VIEVFGHRFVILDTDEYVLKYMESNA 520
Cdd:smart00676  79 TINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 239-359 2.00e-37

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: 134.75  E-value: 2.00e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553420   239 DKQVLRFYAIWDDTDSLFGECRHYIIHYYLMDDTVEIREVHERNNGRDPfPLLMNRQRMPKVlvdngknfpqcvleisDQ 318
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKP----------------PP 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 254553420   319 EVLEWYTAKDFIVGKPLTILGRTFFIYDCDPFTRQFYKDKF 359
Cdd:smart00676  64 DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 587-647 6.24e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 44.08  E-value: 6.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254553420 587 LRERFQVYDKEESGYVDKETFFKVCETLNVPVDDSLIKELIRLC-THGEGRINYYNFVRAFS 647
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
584-647 3.00e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.24  E-value: 3.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254553420  584 KDNLRERFQVYDKEESGYVDKETFFKVCETL--NVPVDDSLIKELIRLC-THGEGRINYYNFVRAFS 647
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFdLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 578-644 2.17e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.06  E-value: 2.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254553420 578 LKDISCKDNLRERFQVYDKEESGYVDKETFFKVCETLNVPVDDSLIKELIRLC-THGEGRINYYNFVR 644
Cdd:PTZ00184  77 MKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREAdVDGDGQINYEEFVK 144
 
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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