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Conserved domains on  [gi|831360224|ref|NP_001296746|]
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EF-hand domain-containing family member C2 [Danio rerio]

Protein Classification

DM10 and DUF1126 domain-containing protein( domain architecture ID 12218352)

protein containing domains DM10, DUF1126, and EFh

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 ...
 219-358 2.00e-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: 2.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224  219 LKQFLEHDRQVLRFYCYWDD-SESMFGDPRELILHYFLADDTMEMYEVVPPNSGRdTVPKFLHRGKLPKHapipkrqpge 297
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPKP---------- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 831360224  298 itdrtvlnvfgpvgqggryildslktGALEEEFYKDSDLTIGAVINVWGRRVLICDCDYFT 358
Cdd:pfam06565  70 --------------------------GTGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 416-527 1.67e-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: 141.07  E-value: 1.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224  416 FKKLMEKDRQglvsnVLRFVGKM--LTDSPVDKERVFIICFYLTDDTIAVFEPPQRNSGVIGGKFLERGRVKKPGqelfk 493
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWddPTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 831360224  494 SEMSEYFTAQDLYVGAHLLLNSQPFQLVDADDFT 527
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 75-178 5.28e-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: 139.75  E-value: 5.28e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224    75 DKQVLCFDAYFNEDVPqrreEKYRVRKCKIYFYLEDDTIQVVEPEFKNSGIPQGTLIRRHRIPLPAPKDDCFYNVHHFNI 154
Cdd:smart00676   1 DKKVLRFDAYWEDPVA----MFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....
gi 831360224   155 NQEVVFYSRNFMITDCDPFTRNFL 178
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYL 100
EFh_PEF super family cl25352
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 617-694 1.10e-03

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


The actual alignment was detected with superfamily member cd15897:

Pssm-ID: 355382 [Multi-domain]  Cd Length: 165  Bit Score: 40.49  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224 617 MLAVA-QDHLKKKNFEKFSE-------MIQAFTHEDRDRCGQLSSKEARIICKAFRLPLSDDLLRALLEKFAGESEKIDY 688
Cdd:cd15897   45 MIAMMdRDHSGKLNFSEFKGlwnyikaWQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYDRGRGNIDF 124


                 ....*.
gi 831360224 689 HAFLSG 694
Cdd:cd15897  125 DDFIQC 130
 
Name Accession Description Interval E-value
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 219-358 2.00e-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: 2.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224  219 LKQFLEHDRQVLRFYCYWDD-SESMFGDPRELILHYFLADDTMEMYEVVPPNSGRdTVPKFLHRGKLPKHapipkrqpge 297
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPKP---------- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 831360224  298 itdrtvlnvfgpvgqggryildslktGALEEEFYKDSDLTIGAVINVWGRRVLICDCDYFT 358
Cdd:pfam06565  70 --------------------------GTGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 416-527 1.67e-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: 141.07  E-value: 1.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224  416 FKKLMEKDRQglvsnVLRFVGKM--LTDSPVDKERVFIICFYLTDDTIAVFEPPQRNSGVIGGKFLERGRVKKPGqelfk 493
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWddPTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 831360224  494 SEMSEYFTAQDLYVGAHLLLNSQPFQLVDADDFT 527
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 75-178 5.28e-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: 139.75  E-value: 5.28e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224    75 DKQVLCFDAYFNEDVPqrreEKYRVRKCKIYFYLEDDTIQVVEPEFKNSGIPQGTLIRRHRIPLPAPKDDCFYNVHHFNI 154
Cdd:smart00676   1 DKKVLRFDAYWEDPVA----MFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....
gi 831360224   155 NQEVVFYSRNFMITDCDPFTRNFL 178
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYL 100
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 69-174 5.80e-37

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: 133.75  E-value: 5.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224   69 PAWLAFDKQVLCFDAYFNEDvPQRREEKYRvrKCKIYFYLEDDTIQVVEPEFKNSGIPQGTLIRRHRIPLPAPKDDCFYN 148
Cdd:pfam06565   2 PKFLENDRKVLRFYAYWDDP-TESPEDEYR--KFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTGGPEYYT 78

                          90       100
                  ....*....|....*....|....*.
gi 831360224  149 VHHFNINQEVVFYSRNFMITDCDPFT 174
Cdd:pfam06565  79 PKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 226-366 3.42e-34

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: 125.89  E-value: 3.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224   226 DRQVLRFYCYWDDSESMFGDPRELILHYFLADDTMEMYEVVPPNSGRDTvPKFLHRGKLPKHAPIpkrqpgeitdrtvln 305
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKPPPD--------------- 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 831360224   306 vfgpvgqggryildslktgalEEEFYKDSDLTIGAVINVWGRRVLICDCDYFTKEYYRSKY 366
Cdd:smart00676  65 ---------------------DPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 429-535 9.60e-27

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: 104.70  E-value: 9.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224   429 SNVLRFVGKMLTDSP-VDKERVFIICFYLTDDTIAVFEPPQRNSGVIGGKFLERGRVKKPGQELfksemSEYFTAQDLYV 507
Cdd:smart00676   2 KKVLRFDAYWEDPVAmFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDD-----PEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 831360224   508 GAHLLLNSQPFQLVDADDFTFSYMEQHA 535
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 617-694 1.10e-03

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 40.49  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224 617 MLAVA-QDHLKKKNFEKFSE-------MIQAFTHEDRDRCGQLSSKEARIICKAFRLPLSDDLLRALLEKFAGESEKIDY 688
Cdd:cd15897   45 MIAMMdRDHSGKLNFSEFKGlwnyikaWQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYDRGRGNIDF 124


                 ....*.
gi 831360224 689 HAFLSG 694
Cdd:cd15897  125 DDFIQC 130
 
Name Accession Description Interval E-value
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 219-358 2.00e-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: 2.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224  219 LKQFLEHDRQVLRFYCYWDD-SESMFGDPRELILHYFLADDTMEMYEVVPPNSGRdTVPKFLHRGKLPKHapipkrqpge 297
Cdd:pfam06565   1 LPKFLENDRKVLRFYAYWDDpTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGR-PGGKFLKRQRIPKP---------- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 831360224  298 itdrtvlnvfgpvgqggryildslktGALEEEFYKDSDLTIGAVINVWGRRVLICDCDYFT 358
Cdd:pfam06565  70 --------------------------GTGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 416-527 1.67e-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: 141.07  E-value: 1.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224  416 FKKLMEKDRQglvsnVLRFVGKM--LTDSPVDKERVFIICFYLTDDTIAVFEPPQRNSGVIGGKFLERGRVKKPGqelfk 493
Cdd:pfam06565   1 LPKFLENDRK-----VLRFYAYWddPTESPEDEYRKFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPG----- 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 831360224  494 SEMSEYFTAQDLYVGAHLLLNSQPFQLVDADDFT 527
Cdd:pfam06565  71 TGGPEYYTPKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 75-178 5.28e-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: 139.75  E-value: 5.28e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224    75 DKQVLCFDAYFNEDVPqrreEKYRVRKCKIYFYLEDDTIQVVEPEFKNSGIPQGTLIRRHRIPLPAPKDDCFYNVHHFNI 154
Cdd:smart00676   1 DKKVLRFDAYWEDPVA----MFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDDPEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....
gi 831360224   155 NQEVVFYSRNFMITDCDPFTRNFL 178
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYL 100
DM10_dom pfam06565
DM10 domain; This entry represents the DM10 domain, which consists of approximately 105 ...
 69-174 5.80e-37

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: 133.75  E-value: 5.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224   69 PAWLAFDKQVLCFDAYFNEDvPQRREEKYRvrKCKIYFYLEDDTIQVVEPEFKNSGIPQGTLIRRHRIPLPAPKDDCFYN 148
Cdd:pfam06565   2 PKFLENDRKVLRFYAYWDDP-TESPEDEYR--KFVISYYLADDTIEIFEPPVRNSGRPGGKFLKRQRIPKPGTGGPEYYT 78

                          90       100
                  ....*....|....*....|....*.
gi 831360224  149 VHHFNINQEVVFYSRNFMITDCDPFT 174
Cdd:pfam06565  79 PKDLYVGATVNIYGRRFLLYDCDEFT 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 226-366 3.42e-34

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: 125.89  E-value: 3.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224   226 DRQVLRFYCYWDDSESMFGDPRELILHYFLADDTMEMYEVVPPNSGRDTvPKFLHRGKLPKHAPIpkrqpgeitdrtvln 305
Cdd:smart00676   1 DKKVLRFDAYWEDPVAMFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQ-GTFLRRQRVPKPPPD--------------- 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 831360224   306 vfgpvgqggryildslktgalEEEFYKDSDLTIGAVINVWGRRVLICDCDYFTKEYYRSKY 366
Cdd:smart00676  65 ---------------------DPEYYHASDLNVGTTINVFGRQFRIYDCDEFTRNYLESKG 104
DM10 smart00676
Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some ...
 429-535 9.60e-27

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: 104.70  E-value: 9.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224   429 SNVLRFVGKMLTDSP-VDKERVFIICFYLTDDTIAVFEPPQRNSGVIGGKFLERGRVKKPGQELfksemSEYFTAQDLYV 507
Cdd:smart00676   2 KKVLRFDAYWEDPVAmFYLIRRFKIYYYLEDDTIEVFEPDVRNSGILQGTFLRRQRVPKPPPDD-----PEYYHASDLNV 76

                           90       100
                   ....*....|....*....|....*...
gi 831360224   508 GAHLLLNSQPFQLVDADDFTFSYMEQHA 535
Cdd:smart00676  77 GTTINVFGRQFRIYDCDEFTRNYLESKG 104
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 617-694 1.10e-03

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 40.49  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 831360224 617 MLAVA-QDHLKKKNFEKFSE-------MIQAFTHEDRDRCGQLSSKEARIICKAFRLPLSDDLLRALLEKFAGESEKIDY 688
Cdd:cd15897   45 MIAMMdRDHSGKLNFSEFKGlwnyikaWQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYDRGRGNIDF 124


                 ....*.
gi 831360224 689 HAFLSG 694
Cdd:cd15897  125 DDFIQC 130
EFh_PEF_CAPN12 cd16194
Penta-EF hand, calcium binding motifs, found in calpain-12 (CAPN12); CAPN12, also termed ...
 627-693 4.39e-03

Penta-EF hand, calcium binding motifs, found in calpain-12 (CAPN12); CAPN12, also termed calcium-activated neutral proteinase 12 (CANP 12), is a calpain large subunit mainly expressed in the cortex of the hair follicle. It may affect apoptosis regulation. CAPN12 contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320069 [Multi-domain]  Cd Length: 169  Bit Score: 38.70  E-value: 4.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 831360224 627 KKNFEKFSEMIQAFTHEDRDRCGQLSSKEARIICKAFRLPLSDDLLRALLEKFAGESEKIDYHAFLS 693
Cdd:cd16194   66 QQLWGYLLEWQAIFTKFDEDTSGTMDSYELRLALNAAGFHLNNQLTETLTSRYRDSRLRVDFESFLS 132
EFh_PEF_CAPN9 cd16192
Penta-EF hand, calcium binding motifs, found in calpain-9 (CAPN9); CAPN9, also termed ...
 630-700 4.86e-03

Penta-EF hand, calcium binding motifs, found in calpain-9 (CAPN9); CAPN9, also termed digestive tract-specific calpain, or new calpain 4 (nCL-4), or protein CG36, is a calpain large subunit predominantly expressed in gastrointestinal tract. It plays a physiological role in the suppression of tumorigenesis. It acts as an important biomolecule link for the regression of colorectal cancer via intracellular calcium homeostasis. CAPN9 may also play a critical role in lumen formation. Moreover, CAPN9, together with CAPN8, forms an active protease complex, G-calpain, in which both proteins are essential for stability and activity. The G-Calpain has been implicated in gastric mucosal defense. Furthermore, down-regulation of calpain 9 has been linked to hypertensive heart and kidney disease in salt-sensitive Dahl rats. CAPN9 contains a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320067 [Multi-domain]  Cd Length: 169  Bit Score: 38.63  E-value: 4.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 831360224 630 FEKFSEMIQAFTHEDRDRCGQLSSKEARIICKAFRLPLSDDLLRALLEKFAGESEKIDYHAFLSGINWREN 700
Cdd:cd16192   69 WDKLKKWIGLFLKYDADRSGTMSSYELRSALKAAGFQLNNQLLQLIVLRYADDYLQIDFDDFLNCLVRLEN 139
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 635-695 8.66e-03

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: 35.22  E-value: 8.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 831360224 635 EMIQAFTHEDRDRCGQLSSKEARIICKAFRLPLSDDLLRALLEKF-AGESEKIDYHAFLSGI 695
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELM 62
 
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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