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Conserved domains on  [gi|15241101|ref|NP_200410|]
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calcineurin B-like protein 2 [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 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
64-192 5.89e-09

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: 52.87  E-value: 5.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  64 DGLINKEEFQLALfktnkkeSLFADRVFDLFDTKHNGILGFEEFARALsVFHPNAPIDDKIHFSFQLYDLKQQGFIERQE 143
Cdd:COG5126  19 DGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15241101 144 VKQMVvatlaeSGMNLKDTVIEDIidktFEEADTKHDGKIDKEEWRSLV 192
Cdd:COG5126  91 FRRLL------TALGVSEEEADEL----FARLDTDGDGKISFEEFVAAV 129
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
64-192 5.89e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.87  E-value: 5.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  64 DGLINKEEFQLALfktnkkeSLFADRVFDLFDTKHNGILGFEEFARALsVFHPNAPIDDKIHFSFQLYDLKQQGFIERQE 143
Cdd:COG5126  19 DGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15241101 144 VKQMVvatlaeSGMNLKDTVIEDIidktFEEADTKHDGKIDKEEWRSLV 192
Cdd:COG5126  91 FRRLL------TALGVSEEEADEL----FARLDTDGDGKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 123-192 1.84e-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: 44.08  E-value: 1.84e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101 123 KIHFSFQLYDLKQQGFIERQEVKQMvvatLAESGMNLKdtviEDIIDKTFEEADTKHDGKIDKEEWRSLV 192
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAA----LKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELM 62
PTZ00183 PTZ00183
centrin; Provisional
 46-196 1.27e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.91  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101   46 EIEALYELFKKISSaviddGLINKEEFQLAL----FKTNKKE--SLFADrvfdlFDTKHNGILGFEEFARALSVFHPNAP 119
Cdd:PTZ00183  18 EIREAFDLFDTDGS-----GTIDPKELKVAMrslgFEPKKEEikQMIAD-----VDKDGSGKIDFEEFLDIMTKKLGERD 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241101  120 IDDKIHFSFQLYDLKQQGFIERQEVKQmvVATlaESGMNLKDTVIEDIIDktfeEADTKHDGKIDKEEWRSLVLRHP 196
Cdd:PTZ00183  88 PREEILKAFRLFDDDKTGKISLKNLKR--VAK--ELGETITDEELQEMID----EADRNGDGEISEEEFYRIMKKTN 156
EF-hand_7 pfam13499
EF-hand domain pair;
121-187 1.60e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.47  E-value: 1.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241101   121 DDKIHFSFQLYDLKQQGFIERQEVKQMVvaTLAESGMNLKDTVIEDIidktFEEADTKHDGKIDKEE 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 5.89e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.87  E-value: 5.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  64 DGLINKEEFQLALfktnkkeSLFADRVFDLFDTKHNGILGFEEFARALsVFHPNAPIDDKIHFSFQLYDLKQQGFIERQE 143
Cdd:COG5126  19 DGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTDGDGKISADE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15241101 144 VKQMVvatlaeSGMNLKDTVIEDIidktFEEADTKHDGKIDKEEWRSLV 192
Cdd:COG5126  91 FRRLL------TALGVSEEEADEL----FARLDTDGDGKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 123-192 1.84e-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: 44.08  E-value: 1.84e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101 123 KIHFSFQLYDLKQQGFIERQEVKQMvvatLAESGMNLKdtviEDIIDKTFEEADTKHDGKIDKEEWRSLV 192
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAA----LKSLGEGLS----EEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 65-193 2.26e-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: 46.05  E-value: 2.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  65 GLINKEEFQLALFKTNKKESL-FADRVFDLFDTKHNGILGFEEFArALSVFHPNapiddkIHFSFQLYDLKQQGFIERQE 143
Cdd:cd16185  15 GSIDVNELQKALAGGGLLFSLaTAEKLIRMFDRDGNGTIDFEEFA-ALHQFLSN------MQNGFEQRDTSRSGRLDANE 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15241101 144 VKQmvvaTLAESGMNLKDTVIEDIidktFEEADTKHDGKIDKEEWRSLVL 193
Cdd:cd16185  88 VHE----ALAASGFQLDPPAFQAL----FRKFDPDRGGSLGFDDYIELCI 129
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 95-192 3.27e-06

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: 44.44  E-value: 3.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  95 DTKHNGILGFEEFARALSVFHPNAPIDDKIHFSFQLYDLKQQGFIERQEVKqMVVATLAESG--MNLKDTVIEDIIdktf 172
Cdd:cd16252  10 EMRHHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIK-YILSTVPSSMpvAPLSDEEAEAMI---- 84

                        90       100
                ....*....|....*....|
gi 15241101 173 EEADTKHDGKIDKEEWRSLV 192
Cdd:cd16252  85 QAADTDGDGRIDFQEFSDMV 104
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
88-191 4.66e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 4.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  88 DRVFDLFDTKHNGILGFEEFARALsvfhpnapiDDKIHFSFQLYDLKQQGFIERQEVKQMVVATLAEsgmnlkdtVIEDI 167
Cdd:COG5126   8 DRRFDLLDADGDGVLERDDFEALF---------RRLWATLFSEADTDGDGRISREEFVAGMESLFEA--------TVEPF 70

                        90       100
                ....*....|....*....|....
gi 15241101 168 IDKTFEEADTKHDGKIDKEEWRSL 191
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRL 94
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 121-192 6.67e-06

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: 43.68  E-value: 6.67e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241101 121 DDKIHFSFQLYDLKQQGFIERQEVKqMVVATLAESGMNLKDTVIEDIIdktfEEADTKHDGKIDKEEWRSLV 192
Cdd:cd16251  33 EDQIKKVFQILDKDKSGFIEEEELK-YILKGFSIAGRDLTDEETKALL----AAGDTDGDGKIGVEEFATLV 99
PTZ00183 PTZ00183
centrin; Provisional
 46-196 1.27e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.91  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101   46 EIEALYELFKKISSaviddGLINKEEFQLAL----FKTNKKE--SLFADrvfdlFDTKHNGILGFEEFARALSVFHPNAP 119
Cdd:PTZ00183  18 EIREAFDLFDTDGS-----GTIDPKELKVAMrslgFEPKKEEikQMIAD-----VDKDGSGKIDFEEFLDIMTKKLGERD 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241101  120 IDDKIHFSFQLYDLKQQGFIERQEVKQmvVATlaESGMNLKDTVIEDIIDktfeEADTKHDGKIDKEEWRSLVLRHP 196
Cdd:PTZ00183  88 PREEILKAFRLFDDDKTGKISLKNLKR--VAK--ELGETITDEELQEMID----EADRNGDGEISEEEFYRIMKKTN 156
EF-hand_7 pfam13499
EF-hand domain pair;
121-187 1.60e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.47  E-value: 1.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241101   121 DDKIHFSFQLYDLKQQGFIERQEVKQMVvaTLAESGMNLKDTVIEDIidktFEEADTKHDGKIDKEE 187
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLL--RKLEEGEPLSDEEVEEL----FKEFDLDKDGRISFEE 61
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
64-118 3.31e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.47  E-value: 3.31e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241101  64 DGLINKEEFQLALFKTNKKESLfADRVFDLFDTKHNGILGFEEFARALSVFH-PNA 118
Cdd:COG5126  83 DGKISADEFRRLLTALGVSEEE-ADELFARLDTDGDGKISFEEFVAAVRDYYtPDA 137
EF-hand_5 pfam13202
EF hand;
168-192 2.22e-04

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 37.30  E-value: 2.22e-04
                          10        20
                  ....*....|....*....|....*
gi 15241101   168 IDKTFEEADTKHDGKIDKEEWRSLV 192
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
PTZ00184 PTZ00184
calmodulin; Provisional
 95-194 2.72e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 40.13  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101   95 DTKHNGILGFEEFARALSVFHPNAPIDDKIHFSFQLYDLKQQGFIERQEVKQMVVatlaesgmNLKDTVIEDIIDKTFEE 174
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMT--------NLGEKLTDEEVDEMIRE 128

                         90       100
                 ....*....|....*....|
gi 15241101  175 ADTKHDGKIDKEEWRSLVLR 194
Cdd:PTZ00184 129 ADVDGDGQINYEEFVKMMMS 148
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 50-209 2.94e-04

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: 40.75  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  50 LYELFKKISsaVIDDGLINKEEFQ-------LALFKTNKKESlfaDRVFDLFDTKHNGILGFEEFaralsvfhpnapidd 122
Cdd:cd16225  36 LKEIFKKVD--VNTDGFLSAEELEdwimektQEHFQEAVEEN---EQIFKAVDTDKDGNVSWEEY--------------- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101 123 KIHFsfqlydLKQQGFiERQEVKQMVVAtlaESGMNLKDTVIEDIID--KTFEEADTKHDGKIDKEEWrsLVLRHP---- 196
Cdd:cd16225  96 RVHF------LLSKGY-SEEEAEEKIKN---NEELKLDEDDKEVLDRykDRWSQADEPEDGLLDVEEF--LSFRHPehsr 163

                       170
                ....*....|...
gi 15241101 197 SLLKNMTLQYLKD 209
Cdd:cd16225 164 GMLKNMVKEILHD 176
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 86-193 7.08e-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: 39.70  E-value: 7.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  86 FADRVFDLFDTKHNGILGFEEFARALSV---------FHPNAPIDDK-IHFSFQLYDLKQQGFIERQEVKQMV--VATLA 153
Cdd:cd16179 142 YTDTILQLFDRNKDGKLQLSEMARLLPVkenflcrpiFKGAGKLTREdIDRVFALYDRDNNGTIENEELTGFLkdLLELV 221

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15241101 154 ESGMNLKDtvIEDIIDKTFEEADTKHDGKIDKEEWRSLVL 193
Cdd:cd16179 222 QEDYDEQD--LEEFKEIILRGWDFNNDGKISRKELTMLLL 259
EF-hand_7 pfam13499
EF-hand domain pair;
47-112 1.08e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.46  E-value: 1.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15241101    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 1.19e-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: 1.19e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15241101  63 DDGLINKEEFQLALFKTNKKESL-FADRVFDLFDTKHNGILGFEEFARALS 112
Cdd:cd00051  13 GDGTISADELKAALKSLGEGLSEeEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
 50-168 1.40e-03

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: 38.12  E-value: 1.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  50 LYELFkkisSAVI-DDGLINKEEFQLALFK-----TNKKESLFADRVF-DLFDTKHNGILGFEEFA---RALSVFHPNap 119
Cdd:cd16181   2 LYGYF----SAVAgQDGQIDADELQRCLTQsgisgNYQPFSLETCRLMiAMLDRDHSGKMGFNEFKelwAALNQWKTT-- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15241101 120 iddkihfsFQLYDLKQQGFIERQEVKQMVVATlaesGMNLKDTVIEDII 168
Cdd:cd16181  76 --------FMQYDRDRSGTVEPQELQQAIRSF----GYNLSPQALNVIV 112
EF-hand_7 pfam13499
EF-hand domain pair;
89-148 1.58e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241101    89 RVFDLFDTKHNGILGFEEFARALSVFHPNAPIDDK-IHFSFQLYDLKQQGFIERQEVKQMV 148
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEeVEELFKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
121-194 3.62e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 3.62e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241101 121 DDKIHFSFQLYDLKQQGFIERQEVKQMVVAtlaesgmnlkdtviedIIDKTFEEADTKHDGKIDKEEWRSLVLR 194
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALFRR----------------LWATLFSEADTDGDGRISREEFVAGMES 61
PPP2R3C cd21505
serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric ...
 64-183 4.58e-03

serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This subfamily includes protein phosphatase subunit G5PR (also known as serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma, G4-1, G5pr, GDRM, SPGF36, or C14orf10) that is encoded by the PPP2R3C gene. It is involved in the control of the dynamic organization of the cortical cytoskeleton and plays an important role in the organization of interphase microtubule arrays in part through the regulation of nucleation geometry. G5PR is involved in the ontogeny of multiple organs, especially critical for testis development and spermatogenesis. PPP2R3C gene variants cause syndromic 46,XY gonadal dysgenesis and impaired spermatogenesis in humans, and thus is emerging as a potential therapeutic target for male infertility.


Pssm-ID: 410338 [Multi-domain]  Cd Length: 382  Bit Score: 37.55  E-value: 4.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241101  64 DGLINKEEfqLALFKTNKKESLFADRVFDLFDTKhNGIL---GFEEFARALSvfHPNAPidDKIHFSFQLYDLKQQGFIE 140
Cdd:cd21505 235 NGMLSKQE--LSRYGKGTLTSVFIDRVFQECLTY-NGEMdykTFLDFVLAME--NRKEP--QALQYFFRILDLKGQGYLT 307

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15241101 141 RQEVK---QMVVATLAESGmnLKDTVIEDIIDKTFEEADTKHDGKI 183
Cdd:cd21505 308 PFTLNyffRAIQEKMKEHG--QEPVSFEDVKDEIFDMVKPKDPLKI 351
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 167-192 7.56e-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: 7.56e-03
                          10        20
                  ....*....|....*....|....*.
gi 15241101   167 IIDKTFEEADTKHDGKIDKEEWRSLV 192
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELL 26
 
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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