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Conserved domains on  [gi|568996053|ref|XP_006522537|]
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calaxin isoform X1 [Mus musculus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11473824)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
67-177 1.38e-12

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.89  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  67 DMIMDRVFRGFDKDNDGCISVSEWIHGLSLFLRGTLDEKMKYCFEVFDLNGDGFISKEEMFHMLKNsllKQPSEEDPDEG 146
Cdd:COG5126   32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADEL 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568996053 147 IkdlveitlKKMDHDHDGKLSFVDYEKAVRE 177
Cdd:COG5126  109 F--------ARLDTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
67-177 1.38e-12

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.89  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  67 DMIMDRVFRGFDKDNDGCISVSEWIHGLSLFLRGTLDEKMKYCFEVFDLNGDGFISKEEMFHMLKNsllKQPSEEDPDEG 146
Cdd:COG5126   32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADEL 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568996053 147 IkdlveitlKKMDHDHDGKLSFVDYEKAVRE 177
Cdd:COG5126  109 F--------ARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
103-176 1.67e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 58.03  E-value: 1.67e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996053  103 DEKMKYCFEVFDLNGDGFISKEEMFHMLKNSLLKQPSEEDPdegikdlVEITLKKMDHDHDGKLSFVDYEKAVR 176
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEE-------VEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 72-131 3.05e-11

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: 57.17  E-value: 3.05e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  72 RVFRGFDKDNDGCISVSEWIHGLSLFLRGTLDEKMKYCFEVFDLNGDGFISKEEMFHMLK 131
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00184 PTZ00184
calmodulin; Provisional
 66-173 4.35e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 48.22  E-value: 4.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  66 DDMIMDrvfrgFDKDNDGCISVSEWIHGLSLFLRGT-LDEKMKYCFEVFDLNGDGFISKEEMFHMLKNsLLKQPSEEDPD 144
Cdd:PTZ00184  50 QDMINE-----VDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMTN-LGEKLTDEEVD 123

                         90       100
                 ....*....|....*....|....*....
gi 568996053 145 EGIKDlveitlkkMDHDHDGKLSFVDYEK 173
Cdd:PTZ00184 124 EMIRE--------ADVDGDGQINYEEFVK 144
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 110-132 1.37e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.43  E-value: 1.37e-03
                           10        20
                   ....*....|....*....|...
gi 568996053   110 FEVFDLNGDGFISKEEMFHMLKN 132
Cdd:smart00054   6 FRLFDKDGDGKIDFEEFKDLLKA 28
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
67-177 1.38e-12

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.89  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  67 DMIMDRVFRGFDKDNDGCISVSEWIHGLSLFLRGTLDEKMKYCFEVFDLNGDGFISKEEMFHMLKNsllKQPSEEDPDEG 146
Cdd:COG5126   32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADEL 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568996053 147 IkdlveitlKKMDHDHDGKLSFVDYEKAVRE 177
Cdd:COG5126  109 F--------ARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
103-176 1.67e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 58.03  E-value: 1.67e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996053  103 DEKMKYCFEVFDLNGDGFISKEEMFHMLKNSLLKQPSEEDPdegikdlVEITLKKMDHDHDGKLSFVDYEKAVR 176
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEE-------VEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 72-131 3.05e-11

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: 57.17  E-value: 3.05e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  72 RVFRGFDKDNDGCISVSEWIHGLSLFLRGTLDEKMKYCFEVFDLNGDGFISKEEMFHMLK 131
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 105-168 4.53e-08

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: 48.70  E-value: 4.53e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568996053 105 KMKYCFEVFDLNGDGFISKEEMFHMLKnSLLKQPSEEDPDEgikdlveiTLKKMDHDHDGKLSF 168
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALK-SLGEGLSEEEIDE--------MIREVDKDGDGKIDF 55
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-131 9.84e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 9.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  49 LDRNVFRNILHVTFGMTDDMIMDRVFRGFDKDNDGCISVSEWIHGLSLFlrGTLDEKMKYCFEVFDLNGDGFISKEEMFH 128
Cdd:COG5126   50 ISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISFEEFVA 127


                 ...
gi 568996053 129 MLK 131
Cdd:COG5126  128 AVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
72-131 3.96e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 3.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568996053   72 RVFRGFDKDNDGCISVSEWIHGLSLFLRG--TLDEKMKYCFEVFDLNGDGFISKEEMFHMLK 131
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 66-173 4.35e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 48.22  E-value: 4.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  66 DDMIMDrvfrgFDKDNDGCISVSEWIHGLSLFLRGT-LDEKMKYCFEVFDLNGDGFISKEEMFHMLKNsLLKQPSEEDPD 144
Cdd:PTZ00184  50 QDMINE-----VDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMTN-LGEKLTDEEVD 123

                         90       100
                 ....*....|....*....|....*....
gi 568996053 145 EGIKDlveitlkkMDHDHDGKLSFVDYEK 173
Cdd:PTZ00184 124 EMIRE--------ADVDGDGQINYEEFVK 144
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 69-168 2.45e-05

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 44.23  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  69 IMDRVFRGFDKDNDGCISVSEWIHGlslflRGTLDEKMKYCFEV------FDLNGDGFISKEEMFHMLKNSLLKQPSEEd 142
Cdd:cd16227  160 LIEQTLRDKDKDNDGFISFQEFLGD-----RAGHEDKEWLLVEKdrfdedYDKDGDGKLDGEEILSWLVPDNEEIAEEE- 233

                         90       100
                 ....*....|....*....|....*.
gi 568996053 143 pdegikdlVEITLKKMDHDHDGKLSF 168
Cdd:cd16227  234 --------VDHLFASADDDHDDRLSF 251
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 77-183 7.68e-05

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 42.90  E-value: 7.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  77 FDKDNDGCISVSEWIHGLS------LFLRGTLD--EKMKYCFEVFDLNGDGFISKEEMFHMLKNsLLKQPSEEDPDEGIK 148
Cdd:cd16176   50 YGQSTDGKIGIVELAQILPteenflLFFRQQLKssEEFMQTWRKYDADHSGFIEADELKSFLKD-LLKKANKPFDESKLE 128

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568996053 149 DLVEITLKKMDHDHDGKLSFVDYEKAV-REENLLLE 183
Cdd:cd16176  129 EYTHTMLKMFDSNNDGKLGLTEMARLLpVQENFLLK 164
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 49-171 2.00e-04

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 41.53  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  49 LDRNVFRNILHVTFGMTDDMIMDRVFRGFDKDNDGCISVSEWIHG---------LSLFLRGTLDEKM-----KYCFEVFD 114
Cdd:cd16227   53 IDRKELKAWILRSFKMLDEEEANERFEEADEDGDGKVTWEEYLADsfgyddednEEMIKDSTEDDLKlleddKEMFEAAD 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568996053 115 LNGDGFISKEEmFHMLKNSllkqpsEEDPDEgIKDLVEITLKKMDHDHDGKLSFVDY 171
Cdd:cd16227  133 LNKDGKLDKTE-FSAFQHP------EEYPHM-HPVLIEQTLRDKDKDNDGFISFQEF 181
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 39-168 3.95e-04

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 40.50  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  39 VAERPGVvTGLDRNVFRNILHVTF--GMTDDMIMDRVfRGFDKDNDGCISVSEWIHGLSLFLRGT------LDEKMKYcF 110
Cdd:cd15899  131 AADQDGD-LILTLEEFLAFLHPEEspYMLDFVIKETL-EDLDKNGDGFISLEEFISDPYSADENEeepewvKVEKERF-V 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568996053 111 EVFDLNGDGFISKEEMFHMlknslLKQPSEEDPDEGIKDLVEitlkKMDHDHDGKLSF 168
Cdd:cd15899  208 ELRDKDKDGKLDGEELLSW-----VDPSNQEIALEEAKHLIA----ESDENKDGKLSP 256
EF-hand_6 pfam13405
EF-hand domain;
105-132 8.50e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 8.50e-04
                          10        20
                  ....*....|....*....|....*...
gi 568996053  105 KMKYCFEVFDLNGDGFISKEEMFHMLKN 132
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRS 28
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 110-167 1.31e-03

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 38.93  E-value: 1.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568996053 110 FEVFDLNGDGFISKEEMFHMLKNsLLKQPSEEDPDEGIKDLVEITLKKMDHDHDGKLS 167
Cdd:cd16179  194 FALYDRDNNGTIENEELTGFLKD-LLELVQEDYDEQDLEEFKEIILRGWDFNNDGKIS 250
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 110-132 1.37e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.43  E-value: 1.37e-03
                           10        20
                   ....*....|....*....|...
gi 568996053   110 FEVFDLNGDGFISKEEMFHMLKN 132
Cdd:smart00054   6 FRLFDKDGDGKIDFEEFKDLLKA 28
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 49-95 1.58e-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: 35.99  E-value: 1.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568996053  49 LDRNVFRNILHVTFGMTDDMIMDRVFRGFDKDNDGCISVSEWIHGLS 95
Cdd:cd00051   17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PRK12309 PRK12309
transaldolase;
73-126 1.59e-03

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 39.33  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568996053  73 VFRGFDKDNDGCISVSEWIhglslflrGTldekmKYCFEVFDLNGDGFISKEEM 126
Cdd:PRK12309 339 IFRLYDLDGDGFITREEWL--------GS-----DAVFDALDLNHDGKITPEEM 379
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 73-167 1.83e-03

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 38.72  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  73 VFRGFDKDNDGCISVSE---WIHGLSL-FLRGTLDEKMKycfeVFDLNGDGFISKEEMFHMLKNSLLKQPSEEDPDEGIK 148
Cdd:cd16226   40 IVDKIDKNGDGFVTEEElkdWIKYVQKkYIREDVDRQWK----EYDPNKDGKLSWEEYKKATYGFLDDEEEDDDLHESYK 115

                         90       100
                 ....*....|....*....|..
gi 568996053 149 DLVEITLKKM---DHDHDGKLS 167
Cdd:cd16226  116 KMIRRDERRWkaaDQDGDGKLT 137
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
101-180 1.87e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053 101 TLDEKMKYCFEVFDLNGDGFISKEEMFHMLKNSLLKQPSEEDPD-------------------EGIKDLVEITLKKMDHD 161
Cdd:COG5126    2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEADTDgdgrisreefvagmeslfeATVEPFARAAFDLLDTD 81

                         90
                 ....*....|....*....
gi 568996053 162 HDGKLSFVDYEKAVREENL 180
Cdd:COG5126   82 GDGKISADEFRRLLTALGV 100
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 105-131 2.27e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.68  E-value: 2.27e-03
                          10        20
                  ....*....|....*....|....*..
gi 568996053  105 KMKYCFEVFDLNGDGFISKEEMFHMLK 131
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLK 27
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 72-171 2.36e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 37.58  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  72 RVFRGFDKDNDGCISVSEWiHGLSLFLrgtldEKMKYCFEVFDLNGDGFISKEEMFHMLKNSLLKqpseeDPDEGIKDLv 151
Cdd:cd16185   40 KLIRMFDRDGNGTIDFEEF-AALHQFL-----SNMQNGFEQRDTSRSGRLDANEVHEALAASGFQ-----LDPPAFQAL- 107

                         90       100
                 ....*....|....*....|
gi 568996053 152 eitLKKMDHDHDGKLSFVDY 171
Cdd:cd16185  108 ---FRKFDPDRGGSLGFDDY 124
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 113-194 3.50e-03

EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a calcium sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. It also serves as a calcium buffer in neurons. Thus, SCGN may be linked to the pathogenesis of neurological diseases such as Alzheimer's, and also acts as a serum marker of neuronal damage, or as a tumor biomarker. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. All six EF hand motifs of SCGN in some eukaryotes, including D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, could potentially bind six calcium ions. In contrast, SCGNs from higher eukaryotes have at least one non-functional EF-hand motif due to the mutation(s) or deletions. For instance, the EF1 loop does not coordinate calcium ion due to the key residue asparagine replaced by lysine in SCGNs of many mammalian species. Moreover, the EF2 loop seems to be competent for calcium-binding in most mammalian SCGNs except for human and chimpanzee orthologs.


Pssm-ID: 320078 [Multi-domain]  Cd Length: 257  Bit Score: 37.77  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053 113 FDLNGDGFISKEEMFHMLKNsLLKQPSEEDPDEGIKDLVEITLKKMDHDHDGKLSFVDYEK--AVREENLLLEAFGPCLP 190
Cdd:cd16178  101 YDADSSGYISAAELKNFLRD-LFLQHKKVITEDKLDEYTDTMMKIFDKNKDGRLDLNDMARilALQENFLLQFKMDAMSE 179


                 ....
gi 568996053 191 DPKR 194
Cdd:cd16178  180 EERK 183
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 72-166 3.84e-03

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 37.81  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  72 RVFRGFDKDNDGCISVSEWIhglsLFL-----RGTLDEKMKYCFEVFDLNGDGFISKEEMFHMLKNSllkQPSEEDPdEG 146
Cdd:cd15899  127 KRFEAADQDGDLILTLEEFL----AFLhpeesPYMLDFVIKETLEDLDKNGDGFISLEEFISDPYSA---DENEEEP-EW 198

                         90       100
                 ....*....|....*....|
gi 568996053 147 IKDLVEITLKKMDHDHDGKL 166
Cdd:cd15899  199 VKVEKERFVELRDKDKDGKL 218
EF-hand_5 pfam13202
EF hand;
109-126 4.97e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.45  E-value: 4.97e-03
                          10
                  ....*....|....*...
gi 568996053  109 CFEVFDLNGDGFISKEEM 126
Cdd:pfam13202   4 TFRQIDLNGDGKISKEEL 21
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 73-166 7.59e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 36.56  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568996053  73 VFRGFDKDNDGCISVSEwihgLSLFLR------------GTLDEKMKYCFEVFDLNGDGFISKEEMFHML---KNSLLKQ 137
Cdd:cd15902   95 IWRKYDTDGSGFIEAKE----LKGFLKdlllknkkhvspPKLDEYTKLILKEFDANKDGKLELDEMAKLLpvqENFLLKF 170

                         90       100
                 ....*....|....*....|....*....
gi 568996053 138 PSEEDPDEGIKDLVEItLKKMDHDHDGKL 166
Cdd:cd15902  171 QILGAMDLTKEDFEKV-FEHYDKDNNGVI 198
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 105-177 9.59e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 35.34  E-value: 9.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568996053 105 KMKYCFEVFDLNGDGFISKEEMfHMLKNSLLKQPSEEDpdegIKDLveitLKKMDHDHDGKLSFVDYEKAVRE 177
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEI-KKLLKRLNIRVSEKE----LKKL----FKEVDTNGDGTLTFDEFEELYKS 64
 
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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