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Conserved domains on  [gi|156616292|ref|NP_060570|]
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EF-hand domain-containing protein 1 isoform 1 [Homo sapiens]

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 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 93-198 7.03e-43

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: 149.38  E-value: 7.03e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292    93 DKKVLKFDAYFQEDVPMSteeqYRIRQVNIYYYLEDDSMSVIEPVVENSGILQGKLIKRQRLAK--NDRGDHYHWKDLNR 170
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMF----YLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKppPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 156616292   171 GINITIYGKTFRVVDCDQFTQVFLESQG 198
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 232-351 2.59e-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: 2.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292  232 LKQFLTFDKQVLRFYAIWDD-TDSMYGECRTYIIHYYLMDDTVEIREVHERNDGRdPFPLLMNRQRVPKvlveNAKNFPq 310
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPK----PGTGGP- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 156616292  311 cvleisdqevlEWYTAKDFIVGKSLTILGRTFFIYDCDPFT 351
Cdd:pfam06565  75 -----------EYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 409-512 2.19e-41

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: 145.30  E-value: 2.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292  409 VIKMLVNDNKVLRYLAVLESP--IPEDKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKYLGRTKVVKPYStvDNPVYYG 486
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDPteSPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGT--GGPEYYT 78

                          90       100
                  ....*....|....*....|....*.
gi 156616292  487 PSDFFIGAVIEVFGHRFIILDTDEYV 512
Cdd:pfam06565  79 PKDLYVGATVNIYGRRFLLYDCDEFT 104
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 579-639 1.95e-07

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: 48.31  E-value: 1.95e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156616292 579 IREAFQIYDKEASGYVDRDMFFKICESLNVPVDDSLVKELIRMC-SHGEGKINYYNFVRAFS 639
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 93-198 7.03e-43

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: 149.38  E-value: 7.03e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292    93 DKKVLKFDAYFQEDVPMSteeqYRIRQVNIYYYLEDDSMSVIEPVVENSGILQGKLIKRQRLAK--NDRGDHYHWKDLNR 170
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMF----YLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKppPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 156616292   171 GINITIYGKTFRVVDCDQFTQVFLESQG 198
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 232-351 2.59e-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: 2.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292  232 LKQFLTFDKQVLRFYAIWDD-TDSMYGECRTYIIHYYLMDDTVEIREVHERNDGRdPFPLLMNRQRVPKvlveNAKNFPq 310
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPK----PGTGGP- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 156616292  311 cvleisdqevlEWYTAKDFIVGKSLTILGRTFFIYDCDPFT 351
Cdd:pfam06565  75 -----------EYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 409-512 2.19e-41

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: 145.30  E-value: 2.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292  409 VIKMLVNDNKVLRYLAVLESP--IPEDKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKYLGRTKVVKPYStvDNPVYYG 486
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDPteSPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGT--GGPEYYT 78

                          90       100
                  ....*....|....*....|....*.
gi 156616292  487 PSDFFIGAVIEVFGHRFIILDTDEYV 512
Cdd:pfam06565  79 PKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 239-359 4.23e-41

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: 144.76  E-value: 4.23e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292   239 DKQVLRFYAIWDDTDSMYGECRTYIIHYYLMDDTVEIREVHERNDGRDPfPLLMNRQRVPKVlvenaknfpqcvleisDQ 318
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKP----------------PP 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 156616292   319 EVLEWYTAKDFIVGKSLTILGRTFFIYDCDPFTRRYYKEKF 359
Cdd:smart00676  64 DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 416-520 3.59e-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: 139.37  E-value: 3.59e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292   416 DNKVLRYLAVLESPIPE-DKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKYLGRTKVVKPysTVDNPVYYGPSDFFIGA 494
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMfYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKP--PPDDPEYYHASDLNVGT 78

                           90       100
                   ....*....|....*....|....*.
gi 156616292   495 VIEVFGHRFIILDTDEYVLKYMESNA 520
Cdd:smart00676  79 TINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 86-190 7.19e-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: 135.67  E-value: 7.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292   86 IPAHVAFDKKVLKFDAYFQEDVPmSTEEQYRirQVNIYYYLEDDSMSVIEPVVENSGILQGKLIKRQRLAKN--DRGDHY 163
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDPTE-SPEDEYR--KFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPgtGGPEYY 77

                          90       100
                  ....*....|....*....|....*..
gi 156616292  164 HWKDLNRGINITIYGKTFRVVDCDQFT 190
Cdd:pfam06565  78 TPKDLYVGATVNIYGRRFLLYDCDEFT 104
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 579-639 1.95e-07

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: 48.31  E-value: 1.95e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156616292 579 IREAFQIYDKEASGYVDRDMFFKICESLNVPVDDSLVKELIRMC-SHGEGKINYYNFVRAFS 639
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 566-636 8.00e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 48.99  E-value: 8.00e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156616292 566 IQKQLKDHSCKDNIREAFQIYDKEASGYVDRDMFFKICESLNVPVDDSLVKELIRMC-SHGEGKINYYNFVR 636
Cdd:PTZ00184  73 MARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREAdVDGDGQINYEEFVK 144
EF-hand_7 pfam13499
EF-hand domain pair;
576-639 2.52e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 2.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156616292  576 KDNIREAFQIYDKEASGYVDRD--MFFKICESLNVPVDDSLVKELIRMC-SHGEGKINYYNFVRAFS 639
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEelKKLLRKLEEGEPLSDEEVEELFKEFdLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 93-198 7.03e-43

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: 149.38  E-value: 7.03e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292    93 DKKVLKFDAYFQEDVPMSteeqYRIRQVNIYYYLEDDSMSVIEPVVENSGILQGKLIKRQRLAK--NDRGDHYHWKDLNR 170
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMF----YLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKppPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 156616292   171 GINITIYGKTFRVVDCDQFTQVFLESQG 198
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 232-351 2.59e-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: 2.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292  232 LKQFLTFDKQVLRFYAIWDD-TDSMYGECRTYIIHYYLMDDTVEIREVHERNDGRdPFPLLMNRQRVPKvlveNAKNFPq 310
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPK----PGTGGP- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 156616292  311 cvleisdqevlEWYTAKDFIVGKSLTILGRTFFIYDCDPFT 351
Cdd:pfam06565  75 -----------EYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 409-512 2.19e-41

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: 145.30  E-value: 2.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292  409 VIKMLVNDNKVLRYLAVLESP--IPEDKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKYLGRTKVVKPYStvDNPVYYG 486
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDPteSPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGT--GGPEYYT 78

                          90       100
                  ....*....|....*....|....*.
gi 156616292  487 PSDFFIGAVIEVFGHRFIILDTDEYV 512
Cdd:pfam06565  79 PKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 239-359 4.23e-41

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: 144.76  E-value: 4.23e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292   239 DKQVLRFYAIWDDTDSMYGECRTYIIHYYLMDDTVEIREVHERNDGRDPfPLLMNRQRVPKVlvenaknfpqcvleisDQ 318
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKP----------------PP 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 156616292   319 EVLEWYTAKDFIVGKSLTILGRTFFIYDCDPFTRRYYKEKF 359
Cdd:smart00676  64 DDPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 416-520 3.59e-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: 139.37  E-value: 3.59e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292   416 DNKVLRYLAVLESPIPE-DKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKYLGRTKVVKPysTVDNPVYYGPSDFFIGA 494
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMfYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKP--PPDDPEYYHASDLNVGT 78

                           90       100
                   ....*....|....*....|....*.
gi 156616292   495 VIEVFGHRFIILDTDEYVLKYMESNA 520
Cdd:smart00676  79 TINVFGRQFRIYDCDEFTRNYLESKG 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 86-190 7.19e-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: 135.67  E-value: 7.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156616292   86 IPAHVAFDKKVLKFDAYFQEDVPmSTEEQYRirQVNIYYYLEDDSMSVIEPVVENSGILQGKLIKRQRLAKN--DRGDHY 163
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDPTE-SPEDEYR--KFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPgtGGPEYY 77

                          90       100
                  ....*....|....*....|....*..
gi 156616292  164 HWKDLNRGINITIYGKTFRVVDCDQFT 190
Cdd:pfam06565  78 TPKDLYVGATVNIYGRRFLLYDCDEFT 104
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 579-639 1.95e-07

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: 48.31  E-value: 1.95e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156616292 579 IREAFQIYDKEASGYVDRDMFFKICESLNVPVDDSLVKELIRMC-SHGEGKINYYNFVRAFS 639
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 566-636 8.00e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 48.99  E-value: 8.00e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156616292 566 IQKQLKDHSCKDNIREAFQIYDKEASGYVDRDMFFKICESLNVPVDDSLVKELIRMC-SHGEGKINYYNFVR 636
Cdd:PTZ00184  73 MARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREAdVDGDGQINYEEFVK 144
EF-hand_7 pfam13499
EF-hand domain pair;
576-639 2.52e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 2.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156616292  576 KDNIREAFQIYDKEASGYVDRD--MFFKICESLNVPVDDSLVKELIRMC-SHGEGKINYYNFVRAFS 639
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEelKKLLRKLEEGEPLSDEEVEELFKEFdLDKDGRISFEEFLELYS 67
EF-hand_6 pfam13405
EF-hand domain;
578-607 7.23e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.46  E-value: 7.23e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 156616292  578 NIREAFQIYDKEASGYVDRDMFFKICESLN 607
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
 
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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