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Conserved domains on  [gi|21361559|ref|NP_003376|]
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visinin-like protein 1 isoform 1 [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];
21-177 3.43e-18

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 76.75  E-value: 3.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  21 EFNEHELKQWYKGFLKDCpSGRLNLEEFQQLYVKFFpygdaskfaQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQK 100
Cdd:COG5126   1 DLQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPF 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361559 101 LNWAFNMYDLDGDGKITRVEMLEIIEAIykmvgtvimmkmnedGLTPEQrVDKIFSKMDKNKDDQITLDEFKEAAKS 177
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLLTAL---------------GVSEEE-ADELFARLDTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
21-177 3.43e-18

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 76.75  E-value: 3.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  21 EFNEHELKQWYKGFLKDCpSGRLNLEEFQQLYVKFFpygdaskfaQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQK 100
Cdd:COG5126   1 DLQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPF 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361559 101 LNWAFNMYDLDGDGKITRVEMLEIIEAIykmvgtvimmkmnedGLTPEQrVDKIFSKMDKNKDDQITLDEFKEAAKS 177
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLLTAL---------------GVSEEE-ADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 65-125 1.83e-15

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: 67.57  E-value: 1.83e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361559  65 AQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDLDGDGKITRVEMLEII 125
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
98-176 2.33e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.18  E-value: 2.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361559    98 EQKLNWAFNMYDLDGDGKITRVEMLEIIEAIykmvgtvimmkmNEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAK 176
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKL------------EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
63-180 1.91e-08

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 52.38  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559   63 KFAQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDLDGDGKITRVEMLEiieaiykmvgtviMMKM-- 140
Cdd:NF041410  27 QFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAA-------------AAPPpp 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 21361559  141 -NEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAKSDPS 180
Cdd:NF041410  94 pPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTSAGS 134
PTZ00183 PTZ00183
centrin; Provisional
 68-176 1.02e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 46.61  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559   68 AFRTFDKNGDGTIDFREFICALSitSRGsFEQKLNWAFNMY---DLDGDGKITRVEMLEIIEAiykmvgtvimmKMNEDg 144
Cdd:PTZ00183  22 AFDLFDTDGSGTIDPKELKVAMR--SLG-FEPKKEEIKQMIadvDKDGSGKIDFEEFLDIMTK-----------KLGER- 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 21361559  145 lTPEQRVDKIFSKMDKNKDDQITLDEFKEAAK 176
Cdd:PTZ00183  87 -DPREEILKAFRLFDDDKTGKISLKNLKRVAK 117
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 66-90 3.37e-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: 3.37e-04
                           10        20
                   ....*....|....*....|....*
gi 21361559     66 QHAFRTFDKNGDGTIDFREFICALS 90
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
21-177 3.43e-18

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 76.75  E-value: 3.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  21 EFNEHELKQWYKGFLKDCpSGRLNLEEFQQLYVKFFpygdaskfaQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQK 100
Cdd:COG5126   1 DLQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPF 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361559 101 LNWAFNMYDLDGDGKITRVEMLEIIEAIykmvgtvimmkmnedGLTPEQrVDKIFSKMDKNKDDQITLDEFKEAAKS 177
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLLTAL---------------GVSEEE-ADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 65-125 1.83e-15

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: 67.57  E-value: 1.83e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361559  65 AQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDLDGDGKITRVEMLEII 125
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-176 7.18e-12

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 57.94  E-value: 7.18e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361559 100 KLNWAFNMYDLDGDGKITRVEMLEIIEAIYkmvgtvimmkmnedGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAK 176
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLG--------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
40-129 2.48e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 58.65  E-value: 2.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  40 SGRLNLEEFQQLYVKFFPYGDAsKFAQHAFRTFDKNGDGTIDFREFicALSITSRGSFEQKLNWAFNMYDLDGDGKITRV 119
Cdd:COG5126  47 DGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEF--RRLLTALGVSEEEADELFARLDTDGDGKISFE 123

                        90
                ....*....|
gi 21361559 120 EMLEIIEAIY 129
Cdd:COG5126 124 EFVAAVRDYY 133
EF-hand_7 pfam13499
EF-hand domain pair;
98-176 2.33e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.18  E-value: 2.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361559    98 EQKLNWAFNMYDLDGDGKITRVEMLEIIEAIykmvgtvimmkmNEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAK 176
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKL------------EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
63-180 1.91e-08

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 52.38  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559   63 KFAQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDLDGDGKITRVEMLEiieaiykmvgtviMMKM-- 140
Cdd:NF041410  27 QFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAA-------------AAPPpp 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 21361559  141 -NEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAKSDPS 180
Cdd:NF041410  94 pPPDQAPSTELADDLLSALDTDGDGSISSDELSAGLTSAGS 134
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 26-171 3.70e-08

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: 50.68  E-value: 3.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  26 ELKQWYKGFLKDCpSGRLNLEEFQQLYVK---FFPYGDASKFaqhaFRTFDKNGDGTIDFREFIcALSitsrgSFEQKLN 102
Cdd:cd16185   1 ELRQWFRAVDRDR-SGSIDVNELQKALAGgglLFSLATAEKL----IRMFDRDGNGTIDFEEFA-ALH-----QFLSNMQ 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559 103 WAFNMYDLDGDGKITRVEMLE-IIEAIYKMvgtvimmkmnedgltPEQRVDKIFSKMDKNKDDQITLDEF 171
Cdd:cd16185  70 NGFEQRDTSRSGRLDANEVHEaLAASGFQL---------------DPPAFQALFRKFDPDRGGSLGFDDY 124
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 41-170 4.08e-08

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: 51.55  E-value: 4.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  41 GRLNLEEFqqlyVKFF-PYGDASKFA---QHAFRTFDKNGDGTIDFREFIC-ALSITSRGSFEQKLNWAFNMYDLDGDGK 115
Cdd:cd16227 137 GKLDKTEF----SAFQhPEEYPHMHPvliEQTLRDKDKDNDGFISFQEFLGdRAGHEDKEWLLVEKDRFDEDYDKDGDGK 212

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21361559 116 ITRVEMLeiieaiykmvgTVIMMKMNEdglTPEQRVDKIFSKMDKNKDDQITLDE 170
Cdd:cd16227 213 LDGEEIL-----------SWLVPDNEE---IAEEEVDHLFASADDDHDDRLSFDE 253
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 26-174 3.24e-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: 47.91  E-value: 3.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  26 ELKQWYKGFLKDCpSGRLNLEEFQQLYVkffpYGDASKFAQHA----FRTFDKNGDGTIDFREFiCALsitsrgsFEQKL 101
Cdd:cd16180   1 ELRRIFQAVDRDR-SGRISAKELQRALS----NGDWTPFSIETvrlmINMFDRDRSGTINFDEF-VGL-------WKYIQ 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361559 102 NW--AFNMYDLDGDGKITRVEMLEIIEAI-YKMvgtvimmkmnedgltPEQRVDKIFSKMDKNKDDQITLDEFKEA 174
Cdd:cd16180  68 DWrrLFRRFDRDRSGSIDFNELQNALSSFgYRL---------------SPQFVQLLVRKFDRRRRGSISFDDFVEA 128
PTZ00183 PTZ00183
centrin; Provisional
 68-176 1.02e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 46.61  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559   68 AFRTFDKNGDGTIDFREFICALSitSRGsFEQKLNWAFNMY---DLDGDGKITRVEMLEIIEAiykmvgtvimmKMNEDg 144
Cdd:PTZ00183  22 AFDLFDTDGSGTIDPKELKVAMR--SLG-FEPKKEEIKQMIadvDKDGSGKIDFEEFLDIMTK-----------KLGER- 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 21361559  145 lTPEQRVDKIFSKMDKNKDDQITLDEFKEAAK 176
Cdd:PTZ00183  87 -DPREEILKAFRLFDDDKTGKISLKNLKRVAK 117
EF-hand_7 pfam13499
EF-hand domain pair;
65-125 2.22e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.40  E-value: 2.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361559    65 AQHAFRTFDKNGDGTIDFREFICALSITSRG-SF-EQKLNWAFNMYDLDGDGKITRVEMLEII 125
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKLEEGePLsDEEVEELFKEFDLDKDGRISFEEFLELY 66
PTZ00184 PTZ00184
calmodulin; Provisional
 73-171 3.90e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.75  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559   73 DKNGDGTIDFREFICALSITSRGS-FEQKLNWAFNMYDLDGDGKITRVEMLEIieaiykmvgtviMMKMNEDgLTpEQRV 151
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHV------------MTNLGEK-LT-DEEV 122

                         90       100
                 ....*....|....*....|
gi 21361559  152 DKIFSKMDKNKDDQITLDEF 171
Cdd:PTZ00184 123 DEMIREADVDGDGQINYEEF 142
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 66-170 1.02e-05

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: 44.74  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  66 QHAFRTFDKNGDGTIDFREFICALSITSRGsfEQKLNWAF-------NMYDLDGDGKITRVEMLEiieaiykmvgtvIMM 138
Cdd:cd15899 163 KETLEDLDKNGDGFISLEEFISDPYSADEN--EEEPEWVKvekerfvELRDKDKDGKLDGEELLS------------WVD 228

                        90       100       110
                ....*....|....*....|....*....|..
gi 21361559 139 KMNEDglTPEQRVDKIFSKMDKNKDDQITLDE 170
Cdd:cd15899 229 PSNQE--IALEEAKHLIAESDENKDGKLSPEE 258
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 40-171 3.93e-05

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 41.50  E-value: 3.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  40 SGRLNLEEFQQLYVKFFPYGDASKFAQhAFRTFDKNGDGTIDFREFICAL-SITSRGSFEQklnwAFNMYDLDGDGKITR 118
Cdd:cd15898  14 DGKLSLKEIKKLLKRLNIRVSEKELKK-LFKEVDTNGDGTLTFDEFEELYkSLTERPELEP----IFKKYAGTNRDYMTL 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 21361559 119 VEMLEIIEAIYKMVgtvimmkmnedglTPEQRVDKIFSKMDKN-KDDQITLDEF 171
Cdd:cd15898  89 EEFIRFLREEQGEN-------------VSEEECEELIEKYEPErENRQLSFEGF 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 40-90 2.64e-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: 2.64e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 21361559  40 SGRLNLEEFQQLYVKFFPYGDASKFAQhAFRTFDKNGDGTIDFREFICALS 90
Cdd:cd00051  14 DGTISADELKAALKSLGEGLSEEEIDE-MIREVDKDGDGKIDFEEFLELMA 63
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 66-90 3.37e-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: 3.37e-04
                           10        20
                   ....*....|....*....|....*
gi 21361559     66 QHAFRTFDKNGDGTIDFREFICALS 90
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLLK 27
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 109-174 9.21e-04

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


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 38.72  E-value: 9.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361559 109 DLDGDGKITRVEMLEIIEAIYKMVgtvimmkMNEDgltpeqrVDKIFSKMDKNKDDQITLDEFKEA 174
Cdd:cd16226  45 DKNGDGFVTEEELKDWIKYVQKKY-------IRED-------VDRQWKEYDPNKDGKLSWEEYKKA 96
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 143-173 1.44e-03

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


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 38.33  E-value: 1.44e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 21361559 143 DGLTPEQ---RVDKIFSKMDKNKDDQITLDEFKE 173
Cdd:cd16226  26 DQLTPEEskeRLGIIVDKIDKNGDGFVTEEELKD 59
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 68-90 2.06e-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: 2.06e-03
                          10        20
                  ....*....|....*....|...
gi 21361559    68 AFRTFDKNGDGTIDFREFICALS 90
Cdd:pfam00036   5 IFRLFDKDGDGKIDFEEFKELLK 27
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 100-128 2.11e-03

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.28  E-value: 2.11e-03
                           10        20
                   ....*....|....*....|....*....
gi 21361559    100 KLNWAFNMYDLDGDGKITRVEMLEIIEAI 128
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_7 pfam13499
EF-hand domain pair;
40-90 2.12e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.31  E-value: 2.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21361559    40 SGRLNLEEFQQLYVKFFPYGDASK-FAQHAFRTFDKNGDGTIDFREFICALS 90
Cdd:pfam13499  16 DGYLDVEELKKLLRKLEEGEPLSDeEVEELFKEFDLDKDGRISFEEFLELYS 67
PRK12309 PRK12309
transaldolase;
105-170 3.05e-03

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 37.41  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361559  105 FNMYDLDGDGKITRVEMLeiieaiykmvGTvimmkmnedgltpeqrvDKIFSKMDKNKDDQITLDE 170
Cdd:PRK12309 340 FRLYDLDGDGFITREEWL----------GS-----------------DAVFDALDLNHDGKITPEE 378
EF-hand_6 pfam13405
EF-hand domain;
66-89 3.17e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.07  E-value: 3.17e-03
                          10        20
                  ....*....|....*....|....
gi 21361559    66 QHAFRTFDKNGDGTIDFREFICAL 89
Cdd:pfam13405   3 REAFKLFDKDGDGKISLEELRKAL 26
PTZ00183 PTZ00183
centrin; Provisional
 73-179 4.01e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 36.21  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559   73 DKNGDGTIDFREF--ICALSITSRGSFEQKLNwAFNMYDLDGDGKITRVEMleiieaiyKMVGTVIMMKMNEDGLtpeqr 150
Cdd:PTZ00183  63 DKDGSGKIDFEEFldIMTKKLGERDPREEILK-AFRLFDDDKTGKISLKNL--------KRVAKELGETITDEEL----- 128

                         90       100
                 ....*....|....*....|....*....
gi 21361559  151 vDKIFSKMDKNKDDQITLDEFKEAAKSDP 179
Cdd:PTZ00183 129 -QEMIDEADRNGDGEISEEEFYRIMKKTN 156
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 100-177 4.28e-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: 36.11  E-value: 4.28e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361559 100 KLNWAFNMYDLDGDGKITRVEMLEIIEaiykmvgtvimmKMNedGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAKS 177
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLK------------RLN--IRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKS 64
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 151-177 4.55e-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: 33.51  E-value: 4.55e-03
                           10        20
                   ....*....|....*....|....*..
gi 21361559    151 VDKIFSKMDKNKDDQITLDEFKEAAKS 177
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 26-121 5.23e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, 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+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 36.09  E-value: 5.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  26 ELKQWYKGFLKDcPSGRLNLEEFQQLYVKffpyGDASKFAQHAFR----TFDKNGDGTIDFREFicalsitsrgsfeQKL 101
Cdd:cd16184   1 EVQQWFQAVDRD-RSGKISAKELQQALVN----GNWSHFNDETCRlmigMFDKDKSGTIDIYEF-------------QAL 62

                        90       100
                ....*....|....*....|....*..
gi 21361559 102 -----NW--AFNMYDLDGDGKITRVEM 121
Cdd:cd16184  63 wnyiqQWkqVFQQFDRDRSGSIDENEL 89
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 40-81 5.63e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 36.05  E-value: 5.63e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 21361559  40 SGRLNLEEFQQLYVKFfpygdasKFAQHAFRTFDKNGDGTID 81
Cdd:cd16182  56 SGRLDLEEFKTLWSDL-------KKWQAIFKKFDTDRSGTLS 90
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 150-177 5.64e-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: 33.14  E-value: 5.64e-03
                          10        20
                  ....*....|....*....|....*...
gi 21361559   150 RVDKIFSKMDKNKDDQITLDEFKEAAKS 177
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 28-117 5.69e-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: 36.08  E-value: 5.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361559  28 KQWYKGFLKDcPSGRLNLEEFQQLYVKFfPYGDASKFAQHAFRTFDKNGDGTIDFREFI-CALSItsrgsfeQKLNWAFN 106
Cdd:cd16183  70 QNCFRSFDRD-NSGNIDKNELKQALTSF-GYRLSDQFYDILVRKFDRQGRGTIAFDDFIqCCVVL-------QTLTDSFR 140

                        90
                ....*....|.
gi 21361559 107 MYDLDGDGKIT 117
Cdd:cd16183 141 RYDTDQDGWIQ 151
Dockerin_1 pfam00404
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
 73-128 8.96e-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: 33.31  E-value: 8.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21361559    73 DKNGDGTI---DFREFICALSITSRGSFEQKLNwafnmYDLDGDGKITRVEMLEIIEAI 128
Cdd:pfam00404   2 DVNGDGKVnalDALLLKNYLLGSGTGSSINKKA-----ADVNGDGKVNALDALLLKNYL 55
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 105-171 9.43e-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: 33.35  E-value: 9.43e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361559 105 FNMYDLDGDGKITRVEMLEIieaiykmvgtviMMKMNedglTPEQRVDKIFSKMDKNKDDQITLDEF 171
Cdd:cd00052   5 FRSLDPDGDGLISGDEARPF------------LGKSG----LPRSVLAQIWDLADTDKDGKLDKEEF 55
EF-hand_6 pfam13405
EF-hand domain;
100-128 9.49e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 32.53  E-value: 9.49e-03
                          10        20
                  ....*....|....*....|....*....
gi 21361559   100 KLNWAFNMYDLDGDGKITRVEMLEIIEAI 128
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
 
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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