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Conserved domains on  [gi|15236778|ref|NP_194387|]
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calcineurin B-like 3 [Arabidopsis thaliana]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000101)

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

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];
64-192 8.84e-10

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 8.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  64 DGLINKEEFQLALfktnkkeSLFADRVFDLFDTKHNGILGFEEFARALsVFHPNAPIEDKIDFSFQLYDLKQQGFIERQE 143
Cdd:COG5126  19 DGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15236778 144 VKQMVvatlaeSGMNLSDEIIESIidktFEEADTKHDGRIDKEEWRTLV 192
Cdd:COG5126  91 FRRLL------TALGVSEEEADEL----FARLDTDGDGKISFEEFVAAV 129
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7-118 3.09e-05

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 3.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778   7 GFKHVCSSFFRCFDIDiykQSGGLGDPELLA-RETVFSVSEIEALYELFkkissAVID---DGLINKEEFQLALFKTNKK 82
Cdd:COG5126  30 LFRRLWATLFSEADTD---GDGRISREEFVAgMESLFEATVEPFARAAF-----DLLDtdgDGKISADEFRRLLTALGVS 101

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15236778  83 ESLfADRVFDLFDTKHNGILGFEEFARALSVFH-PNA 118
Cdd:COG5126 102 EEE-ADELFARLDTDGDGKISFEEFVAAVRDYYtPDA 137
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
64-192 8.84e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 8.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  64 DGLINKEEFQLALfktnkkeSLFADRVFDLFDTKHNGILGFEEFARALsVFHPNAPIEDKIDFSFQLYDLKQQGFIERQE 143
Cdd:COG5126  19 DGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15236778 144 VKQMVvatlaeSGMNLSDEIIESIidktFEEADTKHDGRIDKEEWRTLV 192
Cdd:COG5126  91 FRRLL------TALGVSEEEADEL----FARLDTDGDGKISFEEFVAAV 129
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 95-192 4.95e-09

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 52.15  E-value: 4.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  95 DTKHNGILGFEEFARALSVFHPNAPIEDKIDFSFQLYDLKQQGFIERQEVKqMVVATLAESG--MNLSDEIIESIIdktf 172
Cdd:cd16252  10 EMRHHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIK-YILSTVPSSMpvAPLSDEEAEAMI---- 84

                        90       100
                ....*....|....*....|
gi 15236778 173 EEADTKHDGRIDKEEWRTLV 192
Cdd:cd16252  85 QAADTDGDGRIDFQEFSDMV 104
PTZ00183 PTZ00183
centrin; Provisional
 46-196 2.57e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 45.84  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778   46 EIEALYELFKKISSaviddGLINKEEFQLAL----FKTnKKESLFadRVFDLFDTKHNGILGFEEFARALSVFHPNAPIE 121
Cdd:PTZ00183  18 EIREAFDLFDTDGS-----GTIDPKELKVAMrslgFEP-KKEEIK--QMIADVDKDGSGKIDFEEFLDIMTKKLGERDPR 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15236778  122 DKIDFSFQLYDLKQQGFIERQEVKQmvVATlaESGMNLSDEIIESIIDktfeEADTKHDGRIDKEEWRTLVLRHP 196
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKR--VAK--ELGETITDEELQEMID----EADRNGDGEISEEEFYRIMKKTN 156
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7-118 3.09e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 3.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778   7 GFKHVCSSFFRCFDIDiykQSGGLGDPELLA-RETVFSVSEIEALYELFkkissAVID---DGLINKEEFQLALFKTNKK 82
Cdd:COG5126  30 LFRRLWATLFSEADTD---GDGRISREEFVAgMESLFEATVEPFARAAF-----DLLDtdgDGKISADEFRRLLTALGVS 101

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15236778  83 ESLfADRVFDLFDTKHNGILGFEEFARALSVFH-PNA 118
Cdd:COG5126 102 EEE-ADELFARLDTDGDGKISFEEFVAAVRDYYtPDA 137
EF-hand_7 pfam13499
EF-hand domain pair;
121-187 5.30e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15236778   121 EDKIDFSFQLYDLKQQGFIERQEVKQMVvaTLAESGMNLSDEIIESIidktFEEADTKHDGRIDKEE 187
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLL--RKLEEGEPLSDEEVEEL----FKEFDLDKDGRISFEE 61
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
64-192 8.84e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 8.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  64 DGLINKEEFQLALfktnkkeSLFADRVFDLFDTKHNGILGFEEFARALsVFHPNAPIEDKIDFSFQLYDLKQQGFIERQE 143
Cdd:COG5126  19 DGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15236778 144 VKQMVvatlaeSGMNLSDEIIESIidktFEEADTKHDGRIDKEEWRTLV 192
Cdd:COG5126  91 FRRLL------TALGVSEEEADEL----FARLDTDGDGKISFEEFVAAV 129
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 95-192 4.95e-09

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 52.15  E-value: 4.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  95 DTKHNGILGFEEFARALSVFHPNAPIEDKIDFSFQLYDLKQQGFIERQEVKqMVVATLAESG--MNLSDEIIESIIdktf 172
Cdd:cd16252  10 EMRHHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIK-YILSTVPSSMpvAPLSDEEAEAMI---- 84

                        90       100
                ....*....|....*....|
gi 15236778 173 EEADTKHDGRIDKEEWRTLV 192
Cdd:cd16252  85 QAADTDGDGRIDFQEFSDMV 104
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 121-192 7.35e-07

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


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 46.37  E-value: 7.35e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236778 121 EDKIDFSFQLYDLKQQGFIERQEVKqMVVATLAESGMNLSDEIIESIIdktfEEADTKHDGRIDKEEWRTLV 192
Cdd:cd16251  33 EDQIKKVFQILDKDKSGFIEEEELK-YILKGFSIAGRDLTDEETKALL----AAGDTDGDGKIGVEEFATLV 99
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 123-192 1.15e-06

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: 44.46  E-value: 1.15e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778 123 KIDFSFQLYDLKQQGFIERQEVKQMvvatLAESGMNLSDEIIESIidktFEEADTKHDGRIDKEEWRTLV 192
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAA----LKSLGEGLSEEEIDEM----IREVDKDGDGKIDFEEFLELM 62
PTZ00183 PTZ00183
centrin; Provisional
 46-196 2.57e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 45.84  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778   46 EIEALYELFKKISSaviddGLINKEEFQLAL----FKTnKKESLFadRVFDLFDTKHNGILGFEEFARALSVFHPNAPIE 121
Cdd:PTZ00183  18 EIREAFDLFDTDGS-----GTIDPKELKVAMrslgFEP-KKEEIK--QMIADVDKDGSGKIDFEEFLDIMTKKLGERDPR 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15236778  122 DKIDFSFQLYDLKQQGFIERQEVKQmvVATlaESGMNLSDEIIESIIDktfeEADTKHDGRIDKEEWRTLVLRHP 196
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKR--VAK--ELGETITDEELQEMID----EADRNGDGEISEEEFYRIMKKTN 156
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
88-191 3.27e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 3.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  88 DRVFDLFDTKHNGILGFEEFARALSVFhpnapiedkIDFSFQLYDLKQQGFIERQEVKQMVVAtlaesgmnLSDEIIESI 167
Cdd:COG5126   8 DRRFDLLDADGDGVLERDDFEALFRRL---------WATLFSEADTDGDGRISREEFVAGMES--------LFEATVEPF 70

                        90       100
                ....*....|....*....|....
gi 15236778 168 IDKTFEEADTKHDGRIDKEEWRTL 191
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRL 94
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 65-193 7.41e-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: 44.51  E-value: 7.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  65 GLINKEEFQLALFKTNKKESL-FADRVFDLFDTKHNGILGFEEFArALSVFHPNapiedkIDFSFQLYDLKQQGFIERQE 143
Cdd:cd16185  15 GSIDVNELQKALAGGGLLFSLaTAEKLIRMFDRDGNGTIDFEEFA-ALHQFLSN------MQNGFEQRDTSRSGRLDANE 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15236778 144 VKQmvvaTLAESGMNLSDEIIESIidktFEEADTKHDGRIDKEEWRTLVL 193
Cdd:cd16185  88 VHE----ALAASGFQLDPPAFQAL----FRKFDPDRGGSLGFDDYIELCI 129
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
 50-168 2.18e-05

Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320056 [Multi-domain]  Cd Length: 165  Bit Score: 43.51  E-value: 2.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  50 LYELFkkisSAVI-DDGLINKEEFQLALFK-----TNKKESLFADRVF-DLFDTKHNGILGFEEFA---RALSVFHPNap 119
Cdd:cd16181   2 LYGYF----SAVAgQDGQIDADELQRCLTQsgisgNYQPFSLETCRLMiAMLDRDHSGKMGFNEFKelwAALNQWKTT-- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15236778 120 iedkidfsFQLYDLKQQGFIERQEVKQMVVATlaesGMNLSDEIIESII 168
Cdd:cd16181  76 --------FMQYDRDRSGTVEPQELQQAIRSF----GYNLSPQALNVIV 112
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7-118 3.09e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 3.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778   7 GFKHVCSSFFRCFDIDiykQSGGLGDPELLA-RETVFSVSEIEALYELFkkissAVID---DGLINKEEFQLALFKTNKK 82
Cdd:COG5126  30 LFRRLWATLFSEADTD---GDGRISREEFVAgMESLFEATVEPFARAAF-----DLLDtdgDGKISADEFRRLLTALGVS 101

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15236778  83 ESLfADRVFDLFDTKHNGILGFEEFARALSVFH-PNA 118
Cdd:COG5126 102 EEE-ADELFARLDTDGDGKISFEEFVAAVRDYYtPDA 137
EF-hand_7 pfam13499
EF-hand domain pair;
121-187 5.30e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 5.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15236778   121 EDKIDFSFQLYDLKQQGFIERQEVKQMVvaTLAESGMNLSDEIIESIidktFEEADTKHDGRIDKEE 187
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLL--RKLEEGEPLSDEEVEEL----FKEFDLDKDGRISFEE 61
PTZ00184 PTZ00184
calmodulin; Provisional
 95-194 1.09e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 40.90  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778   95 DTKHNGILGFEEFARALSVFHPNAPIEDKIDFSFQLYDLKQQGFIERQEVKQMvvatLAESGMNLSDEIIESIIdktfEE 174
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHV----MTNLGEKLTDEEVDEMI----RE 128

                         90       100
                 ....*....|....*....|
gi 15236778  175 ADTKHDGRIDKEEWRTLVLR 194
Cdd:PTZ00184 129 ADVDGDGQINYEEFVKMMMS 148
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 86-193 1.60e-04

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


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 41.63  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  86 FADRVFDLFDTKHNGILGFEEFARALSV---------FHPNAPIEDK-IDFSFQLYDLKQQGFIERQEVKQMV--VATLA 153
Cdd:cd16179 142 YTDTILQLFDRNKDGKLQLSEMARLLPVkenflcrpiFKGAGKLTREdIDRVFALYDRDNNGTIENEELTGFLkdLLELV 221

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15236778 154 ESGMNLSD-EIIESIIdktFEEADTKHDGRIDKEEWRTLVL 193
Cdd:cd16179 222 QEDYDEQDlEEFKEII---LRGWDFNNDGKISRKELTMLLL 259
EF-hand_5 pfam13202
EF hand;
168-192 2.73e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 36.91  E-value: 2.73e-04
                          10        20
                  ....*....|....*....|....*
gi 15236778   168 IDKTFEEADTKHDGRIDKEEWRTLV 192
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
EF-hand_7 pfam13499
EF-hand domain pair;
89-148 4.63e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 4.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15236778    89 RVFDLFDTKHNGILGFEEFARALSVFHPNAPI-EDKIDFSFQLYDLKQQGFIERQEVKQMV 148
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsDEEVEELFKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
121-194 7.54e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 7.54e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15236778 121 EDKIDFSFQLYDLKQQGFIERQEVKQMVVAtlaesgmnlsdeiiesIIDKTFEEADTKHDGRIDKEEWRTLVLR 194
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALFRR----------------LWATLFSEADTDGDGRISREEFVAGMES 61
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 87-148 1.05e-03

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.37  E-value: 1.05e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15236778  87 ADRVFDLFDTKHNGILGFEEFARALSVFHPNAPiEDKIDFSFQLYDLKQQGFIERQEVKQMV 148
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLS-EEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 65-170 1.37e-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: 37.89  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  65 GLINKEEFQLALfkTNKKESLFADRV----FDLFDTKHNGILGFEEFARalsVFHpnaPIED--KIdfsFQLYDLKQQGF 138
Cdd:cd16180  15 GRISAKELQRAL--SNGDWTPFSIETvrlmINMFDRDRSGTINFDEFVG---LWK---YIQDwrRL---FRRFDRDRSGS 83

                        90       100       110
                ....*....|....*....|....*....|..
gi 15236778 139 IERQEVKQmvvaTLAESGMNLSDEIIESIIDK 170
Cdd:cd16180  84 IDFNELQN----ALSSFGYRLSPQFVQLLVRK 111
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 65-170 1.54e-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: 38.01  E-value: 1.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  65 GLINKEEFQLALfkTNKKESLFAD----RVFDLFDTKHNGILGFEEFArALSVFhpnapiedkID---FSFQLYDLKQQG 137
Cdd:cd16184  15 GKISAKELQQAL--VNGNWSHFNDetcrLMIGMFDKDKSGTIDIYEFQ-ALWNY---------IQqwkQVFQQFDRDRSG 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 15236778 138 FIERQEVKQmvvaTLAESGMNLSDEIIESIIDK 170
Cdd:cd16184  83 SIDENELHQ----ALSQMGYRLSPQFVQFLVSK 111
EF-hand_7 pfam13499
EF-hand domain pair;
47-112 1.63e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 1.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15236778    47 IEALYELFKKISSAviDDGLINKEEFQLALFKTNKKESL---FADRVFDLFDTKHNGILGFEEFARALS 112
Cdd:pfam13499   1 EEKLKEAFKLLDSD--GDGYLDVEELKKLLRKLEEGEPLsdeEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 63-112 1.65e-03

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.99  E-value: 1.65e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15236778  63 DDGLINKEEFQLALFKTNKKESL-FADRVFDLFDTKHNGILGFEEFARALS 112
Cdd:cd00051  13 GDGTISADELKAALKSLGEGLSEeEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 50-209 4.10e-03

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 37.28  E-value: 4.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  50 LYELFKKISsaVIDDGLINKEEFQ-------LALFKTNKKESlfaDRVFDLFDTKHNGILGFEEFaralsvfhpnapied 122
Cdd:cd16225  36 LKEIFKKVD--VNTDGFLSAEELEdwimektQEHFQEAVEEN---EQIFKAVDTDKDGNVSWEEY--------------- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778 123 KIDFsfqlydLKQQGFiERQEVKQMVVAtlaESGMNLSDEIIESIID--KTFEEADTKHDGRIDKEEWrtLVLRHP---- 196
Cdd:cd16225  96 RVHF------LLSKGY-SEEEAEEKIKN---NEELKLDEDDKEVLDRykDRWSQADEPEDGLLDVEEF--LSFRHPehsr 163

                       170
                ....*....|...
gi 15236778 197 SLLKNMTLQYLKD 209
Cdd:cd16225 164 GMLKNMVKEILHD 176
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 50-170 5.59e-03

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 36.25  E-value: 5.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  50 LYELFKKISSaviDDGLINKEEFQLALFK--TNKKESLFA----DRVFDLFDTKHNGILGFEEFARalsvFHPNAPIEDK 123
Cdd:cd15897   2 LRNVFQAVAG---DDGEISATELQQALSNvgWTHFDLGFSletcRSMIAMMDRDHSGKLNFSEFKG----LWNYIKAWQE 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15236778 124 IdfsFQLYDLKQQGFIERQEVKQmvvaTLAESGMNLSDEIIESIIDK 170
Cdd:cd15897  75 I---FRTYDTDGSGTIDSNELRQ----ALSGAGYRLSEQTYDIIIRR 114
EFh_PEF_grancalcin cd16186
Penta-EF hand, calcium binding motifs, found in grancalcin; Grancalcin (GCA) is a cytosolic ...
 64-170 6.23e-03

Penta-EF hand, calcium binding motifs, found in grancalcin; Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It displays a Ca2+-dependent translocation to granules and plasma membrane upon neutrophil activation, suggesting roles in granule-membrane fusion and degranulation of neutrophils. It may also play a role in the regulation of vesicle/granule exocytosis through the reversible binding of secretory vesicles and plasma membranes upon the presence of calcium. Moreover, GCA is involved in inflammation, as well as in the process of adhesion of neutrophils to fibronectin. It plays a key role in leukocyte-specific functions that are responsible for host defense, and affects the function of integrin receptors on immune cells through binding to L-plastin in the absence of calcium. Furthermore, GCA can strongly interact with sorcin to form a heterodimer, and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320061 [Multi-domain]  Cd Length: 165  Bit Score: 36.38  E-value: 6.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236778  64 DGLINKEEFQLALFK-----TNKKESLFADRVF-DLFDTKHNGILGFEEFAR---ALSVFHPNapiedkidfsFQLYDLK 134
Cdd:cd16186  13 DGEVDAEELQRCLTQsgingTYTPFSLETCRIMiAMLDRDHTGKMGFNEFKElwaALNAWKQN----------FMTVDQD 82

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15236778 135 QQGFIERQEVKQMVVATlaesGMNLSDEIIESIIDK 170
Cdd:cd16186  83 RSGTVEPHELRQAIGAM----GYRLSPQTLTTIVKR 114
 
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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