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Conserved domains on  [gi|2003413237|emb|CAE6250374|]
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unnamed protein product [Karlodinium veneficum]

Protein Classification

EFh domain-containing protein( domain architecture ID 11656620)

EFh domain-containing protein

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];
193-325 4.32e-13

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.12  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 193 VHAGMNDNWAQFFADADKDGTDRLSLQEFDEVVRKRLRATVsRFELRALWRRIDANGSGLATRQEFVLLMYKISLSEWpd 272
Cdd:COG5126    27 FEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEE-- 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2003413237 273 lsqqdlhRITEtlneavnrwhnaggnwykIFKHIDAENSGRIGFDEFVQYVRG 325
Cdd:COG5126   104 -------EADE------------------LFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
784-851 2.87e-08

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 51.10  E-value: 2.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2003413237 784 YKVFRLVDVDGSAKLDFDELQQICRGPLpclgiTSEKVTDDELRGLWRALDADMSGAVTVQEFMIFMR 851
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLE-----EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 543-609 3.81e-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: 50.62  E-value: 3.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2003413237 543 KVFAKFDVDRSGTMEFDELVSFLRRplpgLRIPLTllpDEAVRGFWRALDVDRSGTVSTREFTAFMR 609
Cdd:cd00051     4 EAFRLFDKDGDGTISADELKAALKS----LGEGLS---EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
193-325 4.32e-13

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.12  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 193 VHAGMNDNWAQFFADADKDGTDRLSLQEFDEVVRKRLRATVsRFELRALWRRIDANGSGLATRQEFVLLMYKISLSEWpd 272
Cdd:COG5126    27 FEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEE-- 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2003413237 273 lsqqdlhRITEtlneavnrwhnaggnwykIFKHIDAENSGRIGFDEFVQYVRG 325
Cdd:COG5126   104 -------EADE------------------LFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
784-851 2.87e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 51.10  E-value: 2.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2003413237 784 YKVFRLVDVDGSAKLDFDELQQICRGPLpclgiTSEKVTDDELRGLWRALDADMSGAVTVQEFMIFMR 851
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLE-----EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 543-609 3.81e-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: 50.62  E-value: 3.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2003413237 543 KVFAKFDVDRSGTMEFDELVSFLRRplpgLRIPLTllpDEAVRGFWRALDVDRSGTVSTREFTAFMR 609
Cdd:cd00051     4 EAFRLFDKDGDGTISADELKAALKS----LGEGLS---EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
481-611 6.23e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.49  E-value: 6.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 481 RAFWCAVDADCSGESTRDEFINFVyklqlkswPDLDPEALERVVRilngaadhyyrcsgnwyKVFAKFDVDRSGTMEFDE 560
Cdd:COG5126    36 ATLFSEADTDGDGRISREEFVAGM--------ESLFEATVEPFAR-----------------AAFDLLDTDGDGKISADE 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2003413237 561 LVSFLRrplpGLRipltlLPDEAVRGFWRALDVDRSGTVSTREFTAFMRQF 611
Cdd:COG5126    91 FRRLLT----ALG-----VSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
EF-hand_7 pfam13499
EF-hand domain pair;
542-609 1.47e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.17  E-value: 1.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2003413237 542 YKVFAKFDVDRSGTMEFDELVSFLRRPLPGlrIPLTllpDEAVRGFWRALDVDRSGTVSTREFTAFMR 609
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEG--EPLS---DEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 237-324 2.35e-07

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 48.70  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 237 ELRALWRRIDANGSGLATRQEFVLLMYKISlsewPDLSQQDLHritetlneavnrwhnaggnwyKIFKHIDAENSGRIGF 316
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLG----EGLSEEEID---------------------EMIREVDKDGDGKIDF 55


                  ....*...
gi 2003413237 317 DEFVQYVR 324
Cdd:cd00051    56 EEFLELMA 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 785-851 6.92e-07

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 47.16  E-value: 6.92e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2003413237 785 KVFRLVDVDGSAKLDFDELQQICRGplpclgiTSEKVTDDELRGLWRALDADMSGAVTVQEFMIFMR 851
Cdd:cd00051     4 EAFRLFDKDGDGTISADELKAALKS-------LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
785-853 2.86e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 2.86e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2003413237 785 KVFRLVDVDGSAKLDFDELQQIcrgplpclgITSEKVTDDELRGLWRALDADMSGAVTVQEFMIFMRRH 853
Cdd:COG5126    73 AAFDLLDTDGDGKISADEFRRL---------LTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
EF-hand_7 pfam13499
EF-hand domain pair;
235-324 1.94e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 235 RFELRALWRRIDANGSGLATRQEFVLLMYKISLSEwpDLSQQDLhritetlneavnrwhnaggnwYKIFKHIDAENSGRI 314
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGE--PLSDEEV---------------------EELFKEFDLDKDGRI 57

                          90
                  ....*....|
gi 2003413237 315 GFDEFVQYVR 324
Cdd:pfam13499  58 SFEEFLELYS 67
PTZ00183 PTZ00183
centrin; Provisional
 785-852 2.07e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.67  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2003413237 785 KVFRLVDVDGSAKLDFDELQQICRGplpcLGitsEKVTDDELRGLWRALDADMSGAVTVQEFMIFMRR 852
Cdd:PTZ00183   94 KAFRLFDDDKTGKISLKNLKRVAKE----LG---ETITDEELQEMIDEADRNGDGEISEEEFYRIMKK 154
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 543-567 7.65e-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: 34.66  E-value: 7.65e-03
                           10        20
                   ....*....|....*....|....*
gi 2003413237  543 KVFAKFDVDRSGTMEFDELVSFLRR 567
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKA 28
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
193-325 4.32e-13

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.12  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 193 VHAGMNDNWAQFFADADKDGTDRLSLQEFDEVVRKRLRATVsRFELRALWRRIDANGSGLATRQEFVLLMYKISLSEWpd 272
Cdd:COG5126    27 FEALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEE-- 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2003413237 273 lsqqdlhRITEtlneavnrwhnaggnwykIFKHIDAENSGRIGFDEFVQYVRG 325
Cdd:COG5126   104 -------EADE------------------LFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
784-851 2.87e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 51.10  E-value: 2.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2003413237 784 YKVFRLVDVDGSAKLDFDELQQICRGPLpclgiTSEKVTDDELRGLWRALDADMSGAVTVQEFMIFMR 851
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLE-----EGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 543-609 3.81e-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: 50.62  E-value: 3.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2003413237 543 KVFAKFDVDRSGTMEFDELVSFLRRplpgLRIPLTllpDEAVRGFWRALDVDRSGTVSTREFTAFMR 609
Cdd:cd00051     4 EAFRLFDKDGDGTISADELKAALKS----LGEGLS---EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
481-611 6.23e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.49  E-value: 6.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 481 RAFWCAVDADCSGESTRDEFINFVyklqlkswPDLDPEALERVVRilngaadhyyrcsgnwyKVFAKFDVDRSGTMEFDE 560
Cdd:COG5126    36 ATLFSEADTDGDGRISREEFVAGM--------ESLFEATVEPFAR-----------------AAFDLLDTDGDGKISADE 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2003413237 561 LVSFLRrplpGLRipltlLPDEAVRGFWRALDVDRSGTVSTREFTAFMRQF 611
Cdd:COG5126    91 FRRLLT----ALG-----VSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
EF-hand_7 pfam13499
EF-hand domain pair;
542-609 1.47e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.17  E-value: 1.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2003413237 542 YKVFAKFDVDRSGTMEFDELVSFLRRPLPGlrIPLTllpDEAVRGFWRALDVDRSGTVSTREFTAFMR 609
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEG--EPLS---DEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 237-324 2.35e-07

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 48.70  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 237 ELRALWRRIDANGSGLATRQEFVLLMYKISlsewPDLSQQDLHritetlneavnrwhnaggnwyKIFKHIDAENSGRIGF 316
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLG----EGLSEEEID---------------------EMIREVDKDGDGKIDF 55


                  ....*...
gi 2003413237 317 DEFVQYVR 324
Cdd:cd00051    56 EEFLELMA 63
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 479-609 3.68e-07

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 50.99  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 479 QMRAFWCAVDADCSGESTRDEFINfvyKLQLKSWPDLDPEalerVVRIL--------NGAADHY-----YRCSGNWYKVF 545
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQR---ALSNGDWTPFSIE----TVRLMinmfdrdrSGTINFDefvglWKYIQDWRRLF 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2003413237 546 AKFDVDRSGTMEFDELVSFLRrplpGLRIPltlLPDEAVRGFWRALDVDRSGTVStreFTAFMR 609
Cdd:cd16180    74 RRFDRDRSGSIDFNELQNALS----SFGYR---LSPQFVQLLVRKFDRRRRGSIS---FDDFVE 127
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 785-851 6.92e-07

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 47.16  E-value: 6.92e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2003413237 785 KVFRLVDVDGSAKLDFDELQQICRGplpclgiTSEKVTDDELRGLWRALDADMSGAVTVQEFMIFMR 851
Cdd:cd00051     4 EAFRLFDKDGDGTISADELKAALKS-------LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
539-612 5.92e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.71  E-value: 5.92e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2003413237 539 GNWYKVFAKFDVDRSGTMEFDELVSFLRRPLPGLRIPltllpdeAVRGFWRALDVDRSGTVSTREFTAFMRQFG 612
Cdd:COG5126    33 RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEP-------FARAAFDLLDTDGDGKISADEFRRLLTALG 99
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
785-853 2.86e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 2.86e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2003413237 785 KVFRLVDVDGSAKLDFDELQQIcrgplpclgITSEKVTDDELRGLWRALDADMSGAVTVQEFMIFMRRH 853
Cdd:COG5126    73 AAFDLLDTDGDGKISADEFRRL---------LTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132
EF-hand_7 pfam13499
EF-hand domain pair;
235-324 1.94e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 235 RFELRALWRRIDANGSGLATRQEFVLLMYKISLSEwpDLSQQDLhritetlneavnrwhnaggnwYKIFKHIDAENSGRI 314
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGE--PLSDEEV---------------------EELFKEFDLDKDGRI 57

                          90
                  ....*....|
gi 2003413237 315 GFDEFVQYVR 324
Cdd:pfam13499  58 SFEEFLELYS 67
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 203-322 2.07e-04

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: 42.27  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 203 QFFADADKDGTDRLSLQEFDEVVrKRLRATVSRFELRALWRRIDANGSGLATRQEFVLLMykISLSEWPDLSQ-----QD 277
Cdd:cd15898     4 RQWIKADKDGDGKLSLKEIKKLL-KRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELY--KSLTERPELEPifkkyAG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2003413237 278 LHRITETLNEAVNRWHNAGG-NWY-----KIF-KHIDAENSGRIGFDEFVQY 322
Cdd:cd15898    81 TNRDYMTLEEFIRFLREEQGeNVSeeeceELIeKYEPERENRQLSFEGFTNF 132
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 545-610 2.23e-04

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain 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 C-terminal C2 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. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 42.21  E-value: 2.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2003413237 545 FAKFDVDRSGTMEFDELVSFLRRplpgLRIPltlLPDEAVRGFWRALDVDRSGTVSTREFTAFMRQ 610
Cdd:cd16202     6 FRKADKNGDGKLSFKECKKLLKK----LNVK---VDKDYAKKLFQEADTSGEDVLDEEEFVQFYNR 64
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 205-262 5.76e-04

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: 39.07  E-value: 5.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2003413237 205 FADADKDGTDRLSLQEFDEVVRKrLRATVSRFELRALWRRIDANGSGLATRQEFVLLM 262
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKS-LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 203-267 9.93e-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: 38.35  E-value: 9.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2003413237 203 QFFADADKDGTDRLSlqefDEVVRKRLRAT-VSRFELRALWRRIDANGSGLATRQEFVLLMYKISL 267
Cdd:cd00052     3 QIFRSLDPDGDGLIS----GDEARPFLGKSgLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIAL 64
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 543-606 1.12e-03

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 39.33  E-value: 1.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2003413237 543 KVFAKFDVDRSGTMEFDELVSFLRRPLPGLRIpltlLPDEAVRGFWRALDVDRSGTVSTREFTA 606
Cdd:cd16255    38 KVFEIIDQDKSGFIEEEELKLFLQNFSSGARE----LTDAETKAFLKAGDSDGDGKIGVEEFQA 97
EFh_ScPlc1p_like cd16207
EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar ...
 203-322 1.68e-03

EF-hand motif found in Saccharomyces cerevisiae phospholipase C-1 (ScPlc1p) and similar proteins; This family represents a group of putative phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) encoded by PLC1 genes from yeasts, which are homologs of the delta isoforms of mammalian PI-PLC in terms of overall sequence similarity and domain organization. Mammalian PI-PLC is a signaling enzyme that hydrolyzes 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 then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. The prototype of this family is protein Plc1p (also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1) encoded by PLC1 genes from Saccharomyces cerevisiae. ScPlc1p contains both highly conserved X- and Y- regions of PLC catalytic core domain, as well as a presumptive EF-hand like calcium binding motif. Experiments show that ScPlc1p displays calcium dependent catalytic properties with high similarity to those of the mammalian PLCs, and plays multiple roles in modulating the membrane/protein interactions in filamentation control. CaPlc1p encoded by CAPLC1 from the closely related yeast Candida albicans, an orthologue of S. cerevisiae Plc1p, is also included in this group. Like SCPlc1p, CaPlc1p has conserved presumptive catalytic domain, shows PLC activity when expressed in E. coli, and is involved in multiple cellular processes. There are two other gene copies of CAPLC1 in C. albicans, CAPLC2 (also named as PIPLC) and CAPLC3. Experiments show CaPlc1p is the only enzyme in C. albicans which functions as PLC. The biological functions of CAPLC2 and CAPLC3 gene products must be clearly different from CaPlc1p, but their exact roles remain unclear. Moreover, CAPLC2 and CAPLC3 gene products are more similar to extracellular bacterial PI-PLC than to the eukaryotic PI-PLC, and they are not included in this subfamily.


Pssm-ID: 320037 [Multi-domain]  Cd Length: 142  Bit Score: 39.92  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 203 QFFADADKDGTDRLSLQEFDEVVrKRLRAtvsRFELRALWRRIDANGSGLATRQEFVLLMYKISLSewpDLSQQDLHRIt 282
Cdd:cd16207    42 ELFDKADTDKKGYLNFEEFQEFV-KLLKR---RKDIKAIFKQLTKPGSDGLTLEEFLKFLRDVQKE---DVDRETWEKI- 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2003413237 283 etlneavnrwhnaggnWYKIFKHIDAENSGRIGFDEFVQY 322
Cdd:cd16207   114 ----------------FEKFARRIDDSDSLTMTLEGFTSF 137
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 776-847 1.83e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 40.20  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2003413237 776 WHRVGgNWYKVFRLVDVDGSAKLDFDELQQIcrgpLPCLGItseKVTDDELRGLWRALDADMSGAVTVQEFM 847
Cdd:cd16180    63 WKYIQ-DWRRLFRRFDRDRSGSIDFNELQNA----LSSFGY---RLSPQFVQLLVRKFDRRRRGSISFDDFV 126
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 203-275 2.05e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain 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 C-terminal C2 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. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 39.52  E-value: 2.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2003413237 203 QFFADADKDGTDRLSlqeFDEVVR--KRLRATVSRFELRALWRRIDANGSGLATRQEFVLLmYKiSLSEWPDLSQ 275
Cdd:cd16202     4 DQFRKADKNGDGKLS---FKECKKllKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQF-YN-RLTKRPEIEE 73
PTZ00183 PTZ00183
centrin; Provisional
 785-852 2.07e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.67  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2003413237 785 KVFRLVDVDGSAKLDFDELQQICRGplpcLGitsEKVTDDELRGLWRALDADMSGAVTVQEFMIFMRR 852
Cdd:PTZ00183   94 KAFRLFDDDKTGKISLKNLKRVAKE----LG---ETITDEELQEMIDEADRNGDGEISEEEFYRIMKK 154
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
 543-609 2.13e-03

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 38.70  E-value: 2.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2003413237 543 KVFAKFDVDRSGTMEFDELVSFLRRPLPGLRIpltlLPDEAVRGFWRALDVDRSGTVSTREFTAFMR 609
Cdd:cd16253    38 KVFNILDQDKSGFIEEEELKLFLKNFSDGARV----LSDKETKNFLAAGDSDGDGKIGVDEFKSMVK 100
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 541-567 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: 36.22  E-value: 2.27e-03
                          10        20
                  ....*....|....*....|....*..
gi 2003413237 541 WYKVFAKFDVDRSGTMEFDELVSFLRR 567
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
EF-hand_6 pfam13405
EF-hand domain;
540-566 4.86e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.62  E-value: 4.86e-03
                          10        20
                  ....*....|....*....|....*..
gi 2003413237 540 NWYKVFAKFDVDRSGTMEFDELVSFLR 566
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALR 27
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 299-324 5.95e-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: 35.07  E-value: 5.95e-03
                          10        20
                  ....*....|....*....|....*.
gi 2003413237 299 WYKIFKHIDAENSGRIGFDEFVQYVR 324
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLK 27
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
768-851 7.22e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 7.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003413237 768 EMDRAADHWhrvggnWYKVFRLVDVDGSAKLDFDELQQicrgplpCLGITSEKVTDDELRGLWRALDADMSGAVTVQEFM 847
Cdd:COG5126    26 DFEALFRRL------WATLFSEADTDGDGRISREEFVA-------GMESLFEATVEPFARAAFDLLDTDGDGKISADEFR 92


                  ....
gi 2003413237 848 IFMR 851
Cdd:COG5126    93 RLLT 96
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 543-567 7.65e-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: 34.66  E-value: 7.65e-03
                           10        20
                   ....*....|....*....|....*
gi 2003413237  543 KVFAKFDVDRSGTMEFDELVSFLRR 567
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKA 28
 
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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