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Conserved domains on  [gi|351049917|emb|CCD63971|]
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Neuronal calcium sensor 1 [Caenorhabditis elegans]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 10040236)

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

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-174 2.20e-14

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: 64.49  E-value: 2.20e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351049917 100 KLHWAFKLYDLDQDGFITRNEMLSIVDSIYkmvgssvqlpeeENTPEKRVDRIFRMMDKNNDAQLTLEEFKEGAK 174
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 67-125 1.77e-12

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: 59.48  E-value: 1.77e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 351049917  67 FVFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRNEMLSIV 125
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-174 2.20e-14

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: 64.49  E-value: 2.20e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351049917 100 KLHWAFKLYDLDQDGFITRNEMLSIVDSIYkmvgssvqlpeeENTPEKRVDRIFRMMDKNNDAQLTLEEFKEGAK 174
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
40-174 6.62e-14

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 65.58  E-value: 6.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  40 NGMLTEAGFQKIYKQFFpqgdpsdfaSFVFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRN 119
Cdd:COG5126   19 DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISAD 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 351049917 120 EmlsivdsiYKMVGSSVQLPEEEntpekrVDRIFRMMDKNNDAQLTLEEFKEGAK 174
Cdd:COG5126   90 E--------FRRLLTALGVSEEE------ADELFARLDTDGDGKISFEEFVAAVR 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 67-125 1.77e-12

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: 59.48  E-value: 1.77e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 351049917  67 FVFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRNEMLSIV 125
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
98-174 8.88e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 55.34  E-value: 8.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351049917   98 DEKLHWAFKLYDLDQDGFITRNEMLsivdSIYKMVGSSVQLPEEEntpekrVDRIFRMMDKNNDAQLTLEEFKEGAK 174
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELK----KLLRKLEEGEPLSDEE------VEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
40-129 3.66e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  40 NGMLTEAGFQKIYKQFFPQGDPsDFASFVFKVFDENKDGAIEFHEFIRALSI--TSRGNLDEklhwAFKLYDLDQDGFIT 117
Cdd:COG5126   47 DGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLLTAlgVSEEEADE----LFARLDTDGDGKIS 121

                         90
                 ....*....|..
gi 351049917 118 RNEMLSIVDSIY 129
Cdd:COG5126  122 FEEFVAAVRDYY 133
PTZ00184 PTZ00184
calmodulin; Provisional
 73-169 1.02e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 46.29  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  73 DENKDGAIEFHEFIRALSITSR-GNLDEKLHWAFKLYDLDQDGFITRNEMLSIVDSIYKmvgssvQLPEEEntpekrVDR 151
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKdTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGE------KLTDEE------VDE 124

                         90
                 ....*....|....*...
gi 351049917 152 IFRMMDKNNDAQLTLEEF 169
Cdd:PTZ00184 125 MIREADVDGDGQINYEEF 142
EF-hand_7 pfam13499
EF-hand domain pair;
67-125 2.75e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.70  E-value: 2.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351049917   67 FVFKVFDENKDGAIEFHEFIRALSITSRGN--LDEKLHWAFKLYDLDQDGFITRNEMLSIV 125
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 149-175 2.05e-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: 34.28  E-value: 2.05e-03
                           10        20
                   ....*....|....*....|....*..
gi 351049917   149 VDRIFRMMDKNNDAQLTLEEFKEGAKA 175
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
 
Name Accession Description Interval E-value
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-174 2.20e-14

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: 64.49  E-value: 2.20e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351049917 100 KLHWAFKLYDLDQDGFITRNEMLSIVDSIYkmvgssvqlpeeENTPEKRVDRIFRMMDKNNDAQLTLEEFKEGAK 174
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
40-174 6.62e-14

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 65.58  E-value: 6.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  40 NGMLTEAGFQKIYKQFFpqgdpsdfaSFVFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRN 119
Cdd:COG5126   19 DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISAD 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 351049917 120 EmlsivdsiYKMVGSSVQLPEEEntpekrVDRIFRMMDKNNDAQLTLEEFKEGAK 174
Cdd:COG5126   90 E--------FRRLLTALGVSEEE------ADELFARLDTDGDGKISFEEFVAAVR 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 67-125 1.77e-12

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: 59.48  E-value: 1.77e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 351049917  67 FVFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRNEMLSIV 125
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
98-174 8.88e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 55.34  E-value: 8.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351049917   98 DEKLHWAFKLYDLDQDGFITRNEMLsivdSIYKMVGSSVQLPEEEntpekrVDRIFRMMDKNNDAQLTLEEFKEGAK 174
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELK----KLLRKLEEGEPLSDEE------VEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
40-129 3.66e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  40 NGMLTEAGFQKIYKQFFPQGDPsDFASFVFKVFDENKDGAIEFHEFIRALSI--TSRGNLDEklhwAFKLYDLDQDGFIT 117
Cdd:COG5126   47 DGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLLTAlgVSEEEADE----LFARLDTDGDGKIS 121

                         90
                 ....*....|..
gi 351049917 118 RNEMLSIVDSIY 129
Cdd:COG5126  122 FEEFVAAVRDYY 133
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
98-171 4.12e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  98 DEKLHWAFKLYDLDQDGFITRNEMLSIVDSIYKMVGS----------------SVQLPEEENTPEKRVDRIFRMMDKNND 161
Cdd:COG5126    4 RRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLFSeadtdgdgrisreefvAGMESLFEATVEPFARAAFDLLDTDGD 83

                         90
                 ....*....|
gi 351049917 162 AQLTLEEFKE 171
Cdd:COG5126   84 GKISADEFRR 93
PTZ00184 PTZ00184
calmodulin; Provisional
 73-169 1.02e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 46.29  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  73 DENKDGAIEFHEFIRALSITSR-GNLDEKLHWAFKLYDLDQDGFITRNEMLSIVDSIYKmvgssvQLPEEEntpekrVDR 151
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKdTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGE------KLTDEE------VDE 124

                         90
                 ....*....|....*...
gi 351049917 152 IFRMMDKNNDAQLTLEEF 169
Cdd:PTZ00184 125 MIREADVDGDGQINYEEF 142
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 70-168 9.58e-06

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: 44.62  E-value: 9.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  70 KVFDENKDGAIEFHEFI--RALSITSRGNLDEKLHWAfKLYDLDQDGFITRNEMLSIVdsiykmvgssvqLPEEENTPEK 147
Cdd:cd16227  166 RDKDKDNDGFISFQEFLgdRAGHEDKEWLLVEKDRFD-EDYDKDGDGKLDGEEILSWL------------VPDNEEIAEE 232

                         90       100
                 ....*....|....*....|.
gi 351049917 148 RVDRIFRMMDKNNDAQLTLEE 168
Cdd:cd16227  233 EVDHLFASADDDHDDRLSFDE 253
EF-hand_7 pfam13499
EF-hand domain pair;
67-125 2.75e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.70  E-value: 2.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351049917   67 FVFKVFDENKDGAIEFHEFIRALSITSRGN--LDEKLHWAFKLYDLDQDGFITRNEMLSIV 125
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 68-170 3.73e-05

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: 42.96  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  68 VFKVFDENKDGAI---EFHEFIRalsITSRGNLDEKLHWAFKLYDLDQDGFITRNEmlsivdsiYKMV--GSSVQLPEEE 142
Cdd:cd16226   40 IVDKIDKNGDGFVteeELKDWIK---YVQKKYIREDVDRQWKEYDPNKDGKLSWEE--------YKKAtyGFLDDEEEDD 108

                         90       100       110
                 ....*....|....*....|....*....|....
gi 351049917 143 NTPE------KRVDRIFRMMDKNNDAQLTLEEFK 170
Cdd:cd16226  109 DLHEsykkmiRRDERRWKAADQDGDGKLTKEEFT 142
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 40-169 6.64e-05

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: 41.11  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  40 NGMLTEAGFQKIYKQFFPQGDPSDFASfVFKVFDENKDGAIEFHEFIRAL-SITSRGNLDEklhwAFKLYDLDQDGFITR 118
Cdd:cd15898   14 DGKLSLKEIKKLLKRLNIRVSEKELKK-LFKEVDTNGDGTLTFDEFEELYkSLTERPELEP----IFKKYAGTNRDYMTL 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 351049917 119 NEMlsiVDSIYKmvgssVQlpeEENTPEKRVDRIFRMMDKN-NDAQLTLEEF 169
Cdd:cd15898   89 EEF---IRFLRE-----EQ---GENVSEEECEELIEKYEPErENRQLSFEGF 129
PRK12309 PRK12309
transaldolase;
105-172 9.23e-05

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 42.03  E-value: 9.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351049917 105 FKLYDLDQDGFITRNEMLsivdsiykmvGSsvqlpeeentpekrvDRIFRMMDKNNDAQLTLEEFKEG 172
Cdd:PRK12309 340 FRLYDLDGDGFITREEWL----------GS---------------DAVFDALDLNHDGKITPEEMRAG 382
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 77-169 1.37e-04

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, 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 His-Asp-Glu-Leu (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: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 41.50  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  77 DGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRNEMLSIVDSIYK--MVGSSVQLPEEENTPEKRVDRIFR 154
Cdd:cd16230   51 DGWVSLAELRAWIAHTQQRHIRDSVSAAWQTYDTDRDGRVGWEELRNATYGHYEpgEEFHDVEDAETYKKMLARDERRFR 130

                         90
                 ....*....|....*
gi 351049917 155 MMDKNNDAQLTLEEF 169
Cdd:cd16230  131 VADQDGDSMATREEL 145
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 68-169 1.98e-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: 40.89  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  68 VFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFIT----RNEMLSIVDSIYKMVGSSVQLPEEEN 143
Cdd:cd15899   40 IVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSwdeyKNDTYGSVGDDEENVADNIKEDEEYK 119

                         90       100
                 ....*....|....*....|....*.
gi 351049917 144 TPEKRVDRIFRMMDKNNDAQLTLEEF 169
Cdd:cd15899  120 KLLLKDKKRFEAADQDGDLILTLEEF 145
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 73-168 5.76e-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: 39.35  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  73 DENKDGAIEFHEFIRALSITSRGN------LDEKLHWAfKLYDLDQDGFITRNEMLSIVDsiykmvgssvqlPEEENTPE 146
Cdd:cd15899  170 DKNGDGFISLEEFISDPYSADENEeepewvKVEKERFV-ELRDKDKDGKLDGEELLSWVD------------PSNQEIAL 236

                         90       100
                 ....*....|....*....|..
gi 351049917 147 KRVDRIFRMMDKNNDAQLTLEE 168
Cdd:cd15899  237 EEAKHLIAESDENKDGKLSPEE 258
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 105-169 9.26e-04

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 36.43  E-value: 9.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351049917 105 FKLYDLDQDGFITRNEMLSIvdsiykMVGSSvqLPEEEntpekrVDRIFRMMDKNNDAQLTLEEF 169
Cdd:cd00052    5 FRSLDPDGDGLISGDEARPF------LGKSG--LPRSV------LAQIWDLADTDKDGKLDKEEF 55
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 73-171 1.27e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 38.57  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  73 DENKDGAIEFHEFIRALSITSRGNLD------EKLHWAfKLYDLDQDGFITRNEMLSIVdsiykmvgssvqLPEEENTPE 146
Cdd:cd16224  171 DKDGDGFISLEEFLGDYRKDPTANEDpewiivEKDRFV-NDYDKDNDGKLDPQELLPWV------------VPNNYGIAQ 237

                         90       100
                 ....*....|....*....|....*
gi 351049917 147 KRVDRIFRMMDKNNDAQLTLEEFKE 171
Cdd:cd16224  238 EEALHLIDEMDLNGDGRLSEEEILE 262
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
 72-168 1.38e-03

EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, 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 possibly functions as a calcium buffer, calcium sensor, and apoptosis regulator, which may be implicated in many biological processes, including cell proliferation, differentiation, and cell death. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. CR I-II consists of EF-hand motifs 1 and 2, and CR III-VI consists of EF-hand motifs 3-6. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. Thus, CR has two pairs of cooperative binding sites (I-II and III-IV), which display high affinity calcium-binding sites, and one independent calcium ion-binding site (V), which displays lower affinity binding.


Pssm-ID: 320077 [Multi-domain]  Cd Length: 248  Bit Score: 38.32  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  72 FDENKDGAIEFHEFIRALSITSRGNLDEKLHW--------AFKLYDLDQDGFITRNEMLSIVDSIYKmvgsSVQLPEEEN 143
Cdd:cd16177   55 YDKNADGRIEMAELAQILPTEENFLLCFRQHVgsssefmeAWRKYDTDRSGYIEANELKGFLSDLLK----KANRPYDEK 130

                         90       100
                 ....*....|....*....|....*
gi 351049917 144 TPEKRVDRIFRMMDKNNDAQLTLEE 168
Cdd:cd16177  131 KLQEYTQTILRMFDLNGDGKLGLSE 155
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 73-168 1.98e-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: 37.95  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  73 DENKDGAIEFHEFIRALsITSRGNLDEkLHW------AFKLY-DLDQDGFITRNEMLSIVdsiykmvgssvqLPEEENTP 145
Cdd:cd16226  166 DKNKDGFISLEEYIGDM-YRDDDEEED-PDWvksereQFKEFrDKNKDGKMDREEVKDWI------------LPEDYDHA 231

                         90       100
                 ....*....|....*....|...
gi 351049917 146 EKRVDRIFRMMDKNNDAQLTLEE 168
Cdd:cd16226  232 EAEAKHLIYEADDDKDGKLTKEE 254
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 149-175 2.05e-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: 34.28  E-value: 2.05e-03
                           10        20
                   ....*....|....*....|....*..
gi 351049917   149 VDRIFRMMDKNNDAQLTLEEFKEGAKA 175
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 66-129 2.83e-03

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 36.87  E-value: 2.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351049917  66 SFVFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDlDQDGFITR-------NEMLSIVDSIY 129
Cdd:cd15901   57 NWLLNLYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQLA-DSSGFISRerltqflQDLLQIPDLIG 126
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 63-170 3.65e-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: 36.95  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  63 DFASFVFKVFDENKDGAIEFHEFIRALSI------TSRGNLDEKL-----HWAFKLYDLDQDGFITRNEMLSIVDSIYKM 131
Cdd:cd15902  134 EYTKLILKEFDANKDGKLELDEMAKLLPVqenfllKFQILGAMDLtkedfEKVFEHYDKDNNGVIEGNELDALLKDLLEK 213

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 351049917 132 VGSSVQLPEEENTpekrVDRIFRMMDKNNDAQLTLEEFK 170
Cdd:cd15902  214 NKADIDKPDLENF----RDAILRACDKNKDGKIQKTELA 248
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 50-169 4.98e-03

EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF SSP 9302, 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 is highly expressed in various brain regions. Thus it plays an important role in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons. Calumenin is involved in Ca2+ homeostasis through interacting with ryanodine receptor RyR2 and SERCA2. It acts as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. Calumenin also forms a Ca2+-dependent complex with thrombospondin-1, which is broadly involved in haemostasis and thrombosis. Moreover, calumenin is a molecular chaperone that endogenously regulates the vitamin K-dependent gamma-carboxylation of several proteins, including blood coagulation factors (such as FII, FVII, FIX, FX, and proteins C, S and Z), cell survival factors (Gas6) and bone metabolism proteins (such as matrix Gla protein or MGP, osteocalcin and periostin), through targeting the gamma-glutamyl carboxylase. It also functions as a charged F508del-cystic fibrosis transmembrane regulator (CFTR) folding modulator, as well as a G551D-CFTR associated protein. Furthermore, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. It binds to and stabilizes fibulin-1, and further inactivates extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling.


Pssm-ID: 320026 [Multi-domain]  Cd Length: 263  Bit Score: 36.84  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  50 KIYKQFFPQGDPSDFASFVFKVfDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRNEmlsivdsiY 129
Cdd:cd16228   23 KTFDQLTPEESKERLGKIVGKI-DEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGHDLNEDGLVSWEE--------Y 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 351049917 130 KMVGSSVQLpeEENTPEK---------RVDRIFRMMDKNNDAQLTLEEF 169
Cdd:cd16228   94 KNATYGYIL--DDPDPDDgfnykqmmvRDERRFKMADKDGDLRATKEEF 140
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 100-128 5.84e-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: 33.12  E-value: 5.84e-03
                           10        20
                   ....*....|....*....|....*....
gi 351049917   100 KLHWAFKLYDLDQDGFITRNEMLSIVDSI 128
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 63-170 5.95e-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: 36.23  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  63 DFASFVFKVFDENKDGAIEFHEFIRALSI----------TSRGNLD-EKLHWAFKLYDLDQDGFITRNEMLSIVDSIYKM 131
Cdd:cd16179  141 EYTDTILQLFDRNKDGKLQLSEMARLLPVkenflcrpifKGAGKLTrEDIDRVFALYDRDNNGTIENEELTGFLKDLLEL 220

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 351049917 132 VGSSVQLPEEENTPEKrvdrIFRMMDKNNDAQLTLEEFK 170
Cdd:cd16179  221 VQEDYDEQDLEEFKEI----ILRGWDFNNDGKISRKELT 255
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 72-168 6.92e-03

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: 36.35  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  72 FDENKDGAIEFHEFIRALSITS------RGNLD--EKLHWAFKLYDLDQDGFITRNEMLSIVDSIYKmvgsSVQLPEEEN 143
Cdd:cd16176   50 YGQSTDGKIGIVELAQILPTEEnfllffRQQLKssEEFMQTWRKYDADHSGFIEADELKSFLKDLLK----KANKPFDES 125

                         90       100
                 ....*....|....*....|....*
gi 351049917 144 TPEKRVDRIFRMMDKNNDAQLTLEE 168
Cdd:cd16176  126 KLEEYTHTMLKMFDSNNDGKLGLTE 150
EF-hand_6 pfam13405
EF-hand domain;
100-128 7.11e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 32.92  E-value: 7.11e-03
                          10        20
                  ....*....|....*....|....*....
gi 351049917  100 KLHWAFKLYDLDQDGFITRNEMLSIVDSI 128
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 69-170 7.12e-03

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: 36.14  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  69 FKVFDENKDGAIEFHEFIRALsITSRGNLD-EKLHWAFKLYDLDQDGFITRNEMLSivDSIykmvgsSVQLPEEENTPEK 147
Cdd:cd16227   42 AKKMDLNDDGFIDRKELKAWI-LRSFKMLDeEEANERFEEADEDGDGKVTWEEYLA--DSF------GYDDEDNEEMIKD 112

                         90       100       110
                 ....*....|....*....|....*....|...
gi 351049917 148 RVDRIFRMM----------DKNNDAQLTLEEFK 170
Cdd:cd16227  113 STEDDLKLLeddkemfeaaDLNKDGKLDKTEFS 145
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 100-128 7.45e-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: 32.76  E-value: 7.45e-03
                          10        20
                  ....*....|....*....|....*....
gi 351049917  100 KLHWAFKLYDLDQDGFITRNEMLSIVDSI 128
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 57-168 8.24e-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: 35.85  E-value: 8.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351049917  57 PQGDPSDFASFVFKVFDENKDGAIEFHEFIRALSITS-------RGN-LDEKLHW--AFKLYDLDQDGFITRNEMLSIVD 126
Cdd:cd16179   43 SETALEELKEEFMEAYDENQDGRIDIRELAQLLPTEEnflllfrRDNpLDSSVEFmkVWREYDKDNSGYIEADELKNFLK 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 351049917 127 SIYKMvgSSVQLPEEENTPEKRVDRIFRMMDKNNDAQLTLEE 168
Cdd:cd16179  123 HLLKE--AKRDNDVSEDKLIEYTDTILQLFDRNKDGKLQLSE 162
 
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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