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Conserved domains on  [gi|194377428|dbj|BAG57662|]
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unnamed protein product [Homo sapiens]

Protein Classification

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

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

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-169 2.67e-16

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 71.36  E-value: 2.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQLYIKFFpygdaskfaQHAFRTFDKNGDGTIDFREFICALSVTSRGSFEQKLNWAFEMYDLDGDGRITRL 111
Cdd:COG5126   19 DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISAD 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194377428 112 EMLEIIEAIykmvgtvimmrmnqdGLTPQQrVDKIFKKMDQDKDDQITLEEFKEAAKS 169
Cdd:COG5126   90 EFRRLLTAL---------------GVSEEE-ADELFARLDTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-169 2.67e-16

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 71.36  E-value: 2.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQLYIKFFpygdaskfaQHAFRTFDKNGDGTIDFREFICALSVTSRGSFEQKLNWAFEMYDLDGDGRITRL 111
Cdd:COG5126   19 DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISAD 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194377428 112 EMLEIIEAIykmvgtvimmrmnqdGLTPQQrVDKIFKKMDQDKDDQITLEEFKEAAKS 169
Cdd:COG5126   90 EFRRLLTAL---------------GVSEEE-ADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 57-117 7.36e-16

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: 68.34  E-value: 7.36e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194377428  57 AQHAFRTFDKNGDGTIDFREFICALSVTSRGSFEQKLNWAFEMYDLDGDGRITRLEMLEII 117
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
90-168 1.81e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.18  E-value: 1.81e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194377428   90 EQKLNWAFEMYDLDGDGRITRLEMLEIIEAIYKmvgtvimmrmnQDGLTPQQrVDKIFKKMDQDKDDQITLEEFKEAAK 168
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEE-----------GEPLSDEE-VEELFKEFDLDKDGRISFEEFLELYS 67
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
55-172 5.93e-08

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 50.83  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  55 KFAQHAFRTFDKNGDGTIDFREFICALSVTSRGSFEQKLNWAFEMYDLDGDGRITRLEMLEiieaiykmvgtviMMRM-- 132
Cdd:NF041410  27 QFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAA-------------AAPPpp 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 194377428 133 -NQDGLTPQQRVDKIFKKMDQDKDDQITLEEFKEAAKSDPS 172
Cdd:NF041410  94 pPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTSAGS 134
PTZ00184 PTZ00184
calmodulin; Provisional
 65-163 1.27e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 45.91  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  65 DKNGDGTIDFREFICALSVTSRGS-FEQKLNWAFEMYDLDGDGRITRLEMleiieaiyKMVGTVIMMRMNQDgltpqqRV 143
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAEL--------RHVMTNLGEKLTDE------EV 122

                         90       100
                 ....*....|....*....|
gi 194377428 144 DKIFKKMDQDKDDQITLEEF 163
Cdd:PTZ00184 123 DEMIREADVDGDGQINYEEF 142
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 58-82 3.24e-04

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: 36.59  E-value: 3.24e-04
                           10        20
                   ....*....|....*....|....*
gi 194377428    58 QHAFRTFDKNGDGTIDFREFICALS 82
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-169 2.67e-16

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 71.36  E-value: 2.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQLYIKFFpygdaskfaQHAFRTFDKNGDGTIDFREFICALSVTSRGSFEQKLNWAFEMYDLDGDGRITRL 111
Cdd:COG5126   19 DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISAD 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194377428 112 EMLEIIEAIykmvgtvimmrmnqdGLTPQQrVDKIFKKMDQDKDDQITLEEFKEAAKS 169
Cdd:COG5126   90 EFRRLLTAL---------------GVSEEE-ADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 57-117 7.36e-16

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: 68.34  E-value: 7.36e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194377428  57 AQHAFRTFDKNGDGTIDFREFICALSVTSRGSFEQKLNWAFEMYDLDGDGRITRLEMLEII 117
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 92-168 2.30e-11

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 56.40  E-value: 2.30e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194377428  92 KLNWAFEMYDLDGDGRITRLEMLEIIEAIYkmvgtvimmrmnqdGLTPQQRVDKIFKKMDQDKDDQITLEEFKEAAK 168
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLG--------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
90-168 1.81e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.18  E-value: 1.81e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194377428   90 EQKLNWAFEMYDLDGDGRITRLEMLEIIEAIYKmvgtvimmrmnQDGLTPQQrVDKIFKKMDQDKDDQITLEEFKEAAK 168
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEE-----------GEPLSDEE-VEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-121 7.88e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.41  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQLYIKFFPYGDAsKFAQHAFRTFDKNGDGTIDFREFICALSVtsRGSFEQKLNWAFEMYDLDGDGRITRL 111
Cdd:COG5126   47 DGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLLTA--LGVSEEEADELFARLDTDGDGKISFE 123

                         90
                 ....*....|
gi 194377428 112 EMLEIIEAIY 121
Cdd:COG5126  124 EFVAAVRDYY 133
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
55-172 5.93e-08

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 50.83  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  55 KFAQHAFRTFDKNGDGTIDFREFICALSVTSRGSFEQKLNWAFEMYDLDGDGRITRLEMLEiieaiykmvgtviMMRM-- 132
Cdd:NF041410  27 QFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAA-------------AAPPpp 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 194377428 133 -NQDGLTPQQRVDKIFKKMDQDKDDQITLEEFKEAAKSDPS 172
Cdd:NF041410  94 pPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTSAGS 134
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
90-166 2.03e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  90 EQKLNWAFEMYDLDGDGRITRLEMLEIIEAIYKMV---------GTV-----IMMRMNQDGLTPQQRVDKIFKKMDQDKD 155
Cdd:COG5126    4 RRKLDRRFDLLDADGDGVLERDDFEALFRRLWATLfseadtdgdGRIsreefVAGMESLFEATVEPFARAAFDLLDTDGD 83

                         90
                 ....*....|.
gi 194377428 156 DQITLEEFKEA 166
Cdd:COG5126   84 GKISADEFRRL 94
PTZ00184 PTZ00184
calmodulin; Provisional
 65-163 1.27e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 45.91  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  65 DKNGDGTIDFREFICALSVTSRGS-FEQKLNWAFEMYDLDGDGRITRLEMleiieaiyKMVGTVIMMRMNQDgltpqqRV 143
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAEL--------RHVMTNLGEKLTDE------EV 122

                         90       100
                 ....*....|....*....|
gi 194377428 144 DKIFKKMDQDKDDQITLEEF 163
Cdd:PTZ00184 123 DEMIREADVDGDGQINYEEF 142
EF-hand_7 pfam13499
EF-hand domain pair;
57-117 1.74e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.78  E-value: 1.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194377428   57 AQHAFRTFDKNGDGTIDFREFICALSVTSRG-SF-EQKLNWAFEMYDLDGDGRITRLEMLEII 117
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKLEEGePLsDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 33-162 1.74e-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: 46.54  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  33 GILNLEEFqqlyIKFF-PYGDASKFA---QHAFRTFDKNGDGTIDFREFIcalsvTSRGSFEQKLNWAFEM------YDL 102
Cdd:cd16227  137 GKLDKTEF----SAFQhPEEYPHMHPvliEQTLRDKDKDNDGFISFQEFL-----GDRAGHEDKEWLLVEKdrfdedYDK 207

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428 103 DGDGRITRLEMLEiieaiykmvgtviMMRMNQDGlTPQQRVDKIFKKMDQDKDDQITLEE 162
Cdd:cd16227  208 DGDGKLDGEEILS-------------WLVPDNEE-IAEEEVDHLFASADDDHDDRLSFDE 253
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 33-162 2.79e-06

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: 46.28  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  33 GILNLEEFQQ-LYIKFFPYgdASKFA-QHAFRTFDKNGDGTIDFREFICALSVTSRGsfEQKLNWAF-------EMYDLD 103
Cdd:cd15899  138 LILTLEEFLAfLHPEESPY--MLDFViKETLEDLDKNGDGFISLEEFISDPYSADEN--EEEPEWVKvekerfvELRDKD 213

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194377428 104 GDGRITRLEMLEIIEAiykmvgtvimmrMNQDglTPQQRVDKIFKKMDQDKDDQITLEE 162
Cdd:cd15899  214 KDGKLDGEELLSWVDP------------SNQE--IALEEAKHLIAESDENKDGKLSPEE 258
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 32-163 8.43e-06

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 43.74  E-value: 8.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQLYIK---FFPYGDASKFaqhaFRTFDKNGDGTIDFREFIcALSvtsrgSFEQKLNWAFEMYDLDGDGRI 108
Cdd:cd16185   14 SGSIDVNELQKALAGgglLFSLATAEKL----IRMFDRDGNGTIDFEEFA-ALH-----QFLSNMQNGFEQRDTSRSGRL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 194377428 109 TRLEMLE-IIEAIYKMVGTVimmrmnqdgltpqqrVDKIFKKMDQDKDDQITLEEF 163
Cdd:cd16185   84 DANEVHEaLAASGFQLDPPA---------------FQALFRKFDPDRGGSLGFDDY 124
PTZ00183 PTZ00183
centrin; Provisional
 60-168 2.34e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.37  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  60 AFRTFDKNGDGTIDFREFICALSvtSRGsFEQKLNWAFEMY---DLDGDGRITRLEMLEIIeaiykmvgTVIMMRMNqdg 136
Cdd:PTZ00183  22 AFDLFDTDGSGTIDPKELKVAMR--SLG-FEPKKEEIKQMIadvDKDGSGKIDFEEFLDIM--------TKKLGERD--- 87

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194377428 137 ltPQQRVDKIFKKMDQDKDDQITLEEFKEAAK 168
Cdd:PTZ00183  88 --PREEILKAFRLFDDDKTGKISLKNLKRVAK 117
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 32-109 1.75e-04

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 40.28  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQLYiKF-------FPYGDASK-----------------FA------QHAFRTFDKNGDGTIDFREFIcAL 81
Cdd:cd16185   50 NGTIDFEEFAALH-QFlsnmqngFEQRDTSRsgrldanevhealaasgFQldppafQALFRKFDPDRGGSLGFDDYI-EL 127

                         90       100
                 ....*....|....*....|....*...
gi 194377428  82 SVtsrgsFEQKLNWAFEMYDLDGDGRIT 109
Cdd:cd16185  128 CI-----FLASARNLFQAFDRQRTGRVT 150
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 58-82 3.24e-04

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: 36.59  E-value: 3.24e-04
                           10        20
                   ....*....|....*....|....*
gi 194377428    58 QHAFRTFDKNGDGTIDFREFICALS 82
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLLK 27
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 32-82 3.24e-04

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: 39.43  E-value: 3.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194377428  32 SGILNLEEFQQL--YIKFFpygdaskfaQHAFRTFDKNGDGTIDFREFICALS 82
Cdd:cd16180   51 SGTINFDEFVGLwkYIQDW---------RRLFRRFDRDRSGSIDFNELQNALS 94
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 32-82 3.31e-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: 37.53  E-value: 3.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 194377428  32 SGILNLEEFQQLYIKFFPYGDASKFAQhAFRTFDKNGDGTIDFREFICALS 82
Cdd:cd00051   14 DGTISADELKAALKSLGEGLSEEEIDE-MIREVDKDGDGKIDFEEFLELMA 63
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 56-163 6.65e-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: 38.03  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  56 FAQHAFRTFDKNGDGTIDFREF---ICALSVTSRGSFEQKLnwaFEMYDLDGDGRITRLEMleiiEAIYKMvgtvimmrm 132
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIkklLKRLNIRVSEKELKKL---FKEVDTNGDGTLTFDEF----EELYKS--------- 64

                         90       100       110
                 ....*....|....*....|....*....|.
gi 194377428 133 nqdgLTPQQRVDKIFKKMDQDKDDQITLEEF 163
Cdd:cd15898   65 ----LTERPELEPIFKKYAGTNRDYMTLEEF 91
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 97-163 1.17e-03

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: 36.04  E-value: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194377428  97 FEMYDLDGDGRITRLEMLEIieaiykmvgtviMMRMNqdglTPQQRVDKIFKKMDQDKDDQITLEEF 163
Cdd:cd00052    5 FRSLDPDGDGLISGDEARPF------------LGKSG----LPRSVLAQIWDLADTDKDGKLDKEEF 55
PRK12309 PRK12309
transaldolase;
97-162 1.44e-03

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 38.18  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194377428  97 FEMYDLDGDGRITRLEMLeiieaiykmvGTvimmrmnqdgltpqqrvDKIFKKMDQDKDDQITLEE 162
Cdd:PRK12309 340 FRLYDLDGDGFITREEWL----------GS-----------------DAVFDALDLNHDGKITPEE 378
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 101-166 1.68e-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: 1.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194377428 101 DLDGDGRITRLEMLEIIEAIYKmvgtvimmRMNQDGltpqqrVDKIFKKMDQDKDDQITLEEFKEA 166
Cdd:cd16226   45 DKNGDGFVTEEELKDWIKYVQK--------KYIRED------VDRQWKEYDPNKDGKLSWEEYKKA 96
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 60-82 1.93e-03

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.30  E-value: 1.93e-03
                          10        20
                  ....*....|....*....|...
gi 194377428   60 AFRTFDKNGDGTIDFREFICALS 82
Cdd:pfam00036   5 IFRLFDKDGDGKIDFEEFKELLK 27
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 32-163 2.36e-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: 36.74  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQLYIkffpYGDASKFAQHA----FRTFDKNGDGTIDFREFiCALsvtsrgsFEQKLNW--AFEMYDLDGD 105
Cdd:cd16180   14 SGRISAKELQRALS----NGDWTPFSIETvrlmINMFDRDRSGTINFDEF-VGL-------WKYIQDWrrLFRRFDRDRS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194377428 106 GRITRLEMLEIIEAI-YKMVGTVIMMRMNQDGLTPQ---------------QRVDKIFKKMDQDKDDQITL--EEF 163
Cdd:cd16180   82 GSIDFNELQNALSSFgYRLSPQFVQLLVRKFDRRRRgsisfddfveacvtlKRLTDAFRKYDTNRTGYATIsyEDF 157
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 143-169 2.63e-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: 33.89  E-value: 2.63e-03
                           10        20
                   ....*....|....*....|....*..
gi 194377428   143 VDKIFKKMDQDKDDQITLEEFKEAAKS 169
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 92-120 2.68e-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: 33.89  E-value: 2.68e-03
                           10        20
                   ....*....|....*....|....*....
gi 194377428    92 KLNWAFEMYDLDGDGRITRLEMLEIIEAI 120
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
Dockerin_1 pfam00404
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
 65-120 2.85e-03

Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. This family contains two copies of the repeat.


Pssm-ID: 459805 [Multi-domain]  Cd Length: 56  Bit Score: 34.47  E-value: 2.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 194377428   65 DKNGDGTI---DFREFICALSVTSRGSFEQKLNwafemYDLDGDGRITRLEMLEIIEAI 120
Cdd:pfam00404   2 DVNGDGKVnalDALLLKNYLLGSGTGSSINKKA-----ADVNGDGKVNALDALLLKNYL 55
EF-hand_6 pfam13405
EF-hand domain;
58-81 2.90e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.07  E-value: 2.90e-03
                          10        20
                  ....*....|....*....|....
gi 194377428   58 QHAFRTFDKNGDGTIDFREFICAL 81
Cdd:pfam13405   3 REAFKLFDKDGDGKISLEELRKAL 26
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 142-169 3.04e-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: 33.91  E-value: 3.04e-03
                          10        20
                  ....*....|....*....|....*...
gi 194377428  142 RVDKIFKKMDQDKDDQITLEEFKEAAKS 169
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 135-165 3.20e-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: 37.18  E-value: 3.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 194377428 135 DGLTP---QQRVDKIFKKMDQDKDDQITLEEFKE 165
Cdd:cd16226   26 DQLTPeesKERLGIIVDKIDKNGDGFVTEEELKD 59
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 32-163 7.28e-03

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 35.34  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQLYIKFFPYGDASKFAQhAFRTFDKNGDGTIDFREFICAL-SVTSRGSFEQklnwAFEMYDLDGDGRITR 110
Cdd:cd15898   14 DGKLSLKEIKKLLKRLNIRVSEKELKK-LFKEVDTNGDGTLTFDEFEELYkSLTERPELEP----IFKKYAGTNRDYMTL 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194377428 111 LEMLEIIEAiykmvgtvimmrmNQDGLTPQQRVDKIFKKMDQD-KDDQITLEEF 163
Cdd:cd15898   89 EEFIRFLRE-------------EQGENVSEEECEELIEKYEPErENRQLSFEGF 129
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 32-109 9.28e-03

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. 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.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 35.31  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194377428  32 SGILNLEEFQQL--YIKFFpygdaskfaQHAFRTFDKNGDGTIDFREFICALSV-------------------TSRGSFE 90
Cdd:cd16183   51 SGTINFQEFAALwkYITDW---------QNCFRSFDRDNSGNIDKNELKQALTSfgyrlsdqfydilvrkfdrQGRGTIA 121

                         90       100       110
                 ....*....|....*....|....*....|
gi 194377428  91 -----------QKLNWAFEMYDLDGDGRIT 109
Cdd:cd16183  122 fddfiqccvvlQTLTDSFRRYDTDQDGWIQ 151
 
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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