NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1063696934|ref|NP_001322654|]
View 

calcineurin B-like protein 8 [Arabidopsis thaliana]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
39-183 4.93e-12

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.58  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  39 LHDLFKKLSTSiiNDGLIHKEEFllALFRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAfMFK 118
Cdd:COG5126     7 LDRRFDLLDAD--GDGVLERDDF--EALFRRLWATLFSE-----ADTDGDGRISREEFVAGMESLFEATVEPFARA-AFD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063696934 119 LFDLHGTGFIEPHELKKMVGALlgetdlELSEESIEAIVEQtmleVDTNKDGKIDEEEWKELVAK 183
Cdd:COG5126    77 LLDTDGDGKISADEFRRLLTAL------GVSEEEADELFAR----LDTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
39-183 4.93e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.58  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  39 LHDLFKKLSTSiiNDGLIHKEEFllALFRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAfMFK 118
Cdd:COG5126     7 LDRRFDLLDAD--GDGVLERDDF--EALFRRLWATLFSE-----ADTDGDGRISREEFVAGMESLFEATVEPFARA-AFD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063696934 119 LFDLHGTGFIEPHELKKMVGALlgetdlELSEESIEAIVEQtmleVDTNKDGKIDEEEWKELVAK 183
Cdd:COG5126    77 LLDTDGDGKISADEFRRLLTAL------GVSEEEADELFAR----LDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 115-182 1.33e-11

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 57.56  E-value: 1.33e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063696934 115 FMFKLFDLHGTGFIEPHELKKMVGALLGETDlelseesiEAIVEQTMLEVDTNKDGKIDEEEWKELVA 182
Cdd:cd00051     4 EAFRLFDKDGDGTISADELKAALKSLGEGLS--------EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
 26-185 1.22e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 54.70  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  26 ASETPFTVNEIEALHDLFKKLSTSiiNDGLIHKEEFLLAL------FRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRS 99
Cdd:PTZ00183    6 SERPGLTEDQKKEIREAFDLFDTD--GSGTIDPKELKVAMrslgfePKKEEIKQMIAD-----VDKDGSGKIDFEEFLDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934 100 LSIFHPYTPEHEKSAFMFKLFDLHGTGFIEPHELKKmVGALLGETdleLSEESIEAIVEqtmlEVDTNKDGKIDEEEWKE 179
Cdd:PTZ00183   79 MTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKR-VAKELGET---ITDEELQEMID----EADRNGDGEISEEEFYR 150


                  ....*.
gi 1063696934 180 LVAKNP 185
Cdd:PTZ00183  151 IMKKTN 156
EF-hand_7 pfam13499
EF-hand domain pair;
111-181 8.53e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 8.53e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063696934 111 EKSAFMFKLFDLHGTGFIEPHELKKMVGALlgETDLELSEESIEAIVEqtmlEVDTNKDGKIDEEEWKELV 181
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKL--EEGEPLSDEEVEELFK----EFDLDKDGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 157-183 6.91e-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: 33.12  E-value: 6.91e-03
                           10        20
                   ....*....|....*....|....*..
gi 1063696934  157 VEQTMLEVDTNKDGKIDEEEWKELVAK 183
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
39-183 4.93e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.58  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  39 LHDLFKKLSTSiiNDGLIHKEEFllALFRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAfMFK 118
Cdd:COG5126     7 LDRRFDLLDAD--GDGVLERDDF--EALFRRLWATLFSE-----ADTDGDGRISREEFVAGMESLFEATVEPFARA-AFD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063696934 119 LFDLHGTGFIEPHELKKMVGALlgetdlELSEESIEAIVEQtmleVDTNKDGKIDEEEWKELVAK 183
Cdd:COG5126    77 LLDTDGDGKISADEFRRLLTAL------GVSEEEADELFAR----LDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 115-182 1.33e-11

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 57.56  E-value: 1.33e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063696934 115 FMFKLFDLHGTGFIEPHELKKMVGALLGETDlelseesiEAIVEQTMLEVDTNKDGKIDEEEWKELVA 182
Cdd:cd00051     4 EAFRLFDKDGDGTISADELKAALKSLGEGLS--------EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
 26-185 1.22e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 54.70  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  26 ASETPFTVNEIEALHDLFKKLSTSiiNDGLIHKEEFLLAL------FRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRS 99
Cdd:PTZ00183    6 SERPGLTEDQKKEIREAFDLFDTD--GSGTIDPKELKVAMrslgfePKKEEIKQMIAD-----VDKDGSGKIDFEEFLDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934 100 LSIFHPYTPEHEKSAFMFKLFDLHGTGFIEPHELKKmVGALLGETdleLSEESIEAIVEqtmlEVDTNKDGKIDEEEWKE 179
Cdd:PTZ00183   79 MTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKR-VAKELGET---ITDEELQEMID----EADRNGDGEISEEEFYR 150


                  ....*.
gi 1063696934 180 LVAKNP 185
Cdd:PTZ00183  151 IMKKTN 156
EF-hand_7 pfam13499
EF-hand domain pair;
111-181 8.53e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 8.53e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063696934 111 EKSAFMFKLFDLHGTGFIEPHELKKMVGALlgETDLELSEESIEAIVEqtmlEVDTNKDGKIDEEEWKELV 181
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKL--EEGEPLSDEEVEELFK----EFDLDKDGRISFEEFLELY 66
PTZ00184 PTZ00184
calmodulin; Provisional
 84-181 4.89e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.37  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  84 DRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAFMFKLFDLHGTGFIEPHELKKmVGALLGEtdlELSEESieaiVEQTMLE 163
Cdd:PTZ00184   57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRH-VMTNLGE---KLTDEE----VDEMIRE 128

                          90
                  ....*....|....*...
gi 1063696934 164 VDTNKDGKIDEEEWKELV 181
Cdd:PTZ00184  129 ADVDGDGQINYEEFVKMM 146
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 52-181 6.40e-05

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: 42.40  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  52 NDGLIHKEE---FLLALFRNGSMQNL--------FADRVFYMFDRKRNGVIEFGEFVRSL---------SIF-HPYTPEH 110
Cdd:cd16179   108 NSGYIEADElknFLKHLLKEAKRDNDvsedklieYTDTILQLFDRNKDGKLQLSEMARLLpvkenflcrPIFkGAGKLTR 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063696934 111 EKSAFMFKLFDLHGTGFIEPHELKKMVGALLGETDLELSEESIEAIVEQTMLEVDTNKDGKIDEEEWKELV 181
Cdd:cd16179   188 EDIDRVFALYDRDNNGTIENEELTGFLKDLLELVQEDYDEQDLEEFKEIILRGWDFNNDGKISRKELTMLL 258
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 70-181 1.06e-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: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  70 SMQNLFADRVFYMFDRKRNGVIEFGEFVRSLS-------IFHPYTPEHEKSAFM--FKLFDLHGTGFIEPHELKKMVGAL 140
Cdd:cd16179    45 TALEELKEEFMEAYDENQDGRIDIRELAQLLPteenfllLFRRDNPLDSSVEFMkvWREYDKDNSGYIEADELKNFLKHL 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063696934 141 L--GETDLELSEESIEAIVEqTMLEV-DTNKDGKIDEEEWKELV 181
Cdd:cd16179   125 LkeAKRDNDVSEDKLIEYTD-TILQLfDRNKDGKLQLSEMARLL 167
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 84-183 1.37e-04

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: 39.82  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  84 DRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAFMFKLFDLHGTGFIEPHELKKMVGALLGETDLE-LSEESIEAIVEQTml 162
Cdd:cd16252    10 EMRHHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPVApLSDEEAEAMIQAA-- 87

                          90       100
                  ....*....|....*....|.
gi 1063696934 163 evDTNKDGKIDEEEWKELVAK 183
Cdd:cd16252    88 --DTDGDGRIDFQEFSDMVKK 106
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
111-182 1.72e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934 111 EKSAFMFKLFDLHGTGFIEPHELKKM----VGALLGETD----------------LELSEESIEAIVEQTMLEVDTNKDG 170
Cdd:COG5126     5 RKLDRRFDLLDADGDGVLERDDFEALfrrlWATLFSEADtdgdgrisreefvagmESLFEATVEPFARAAFDLLDTDGDG 84

                          90
                  ....*....|..
gi 1063696934 171 KIDEEEWKELVA 182
Cdd:COG5126    85 KISADEFRRLLT 96
EFh_PEF_grancalcin cd16186
Penta-EF hand, calcium binding motifs, found in grancalcin; Grancalcin (GCA) is a cytosolic ...
 82-172 1.47e-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: 37.92  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  82 MFDRKRNGVIEFGEFVRSLSIFHPYtpeheKSAFMfkLFDLHGTGFIEPHELKKMVGALlgetDLELSEESIEAIVEQtm 161
Cdd:cd16186    48 MLDRDHTGKMGFNEFKELWAALNAW-----KQNFM--TVDQDRSGTVEPHELRQAIGAM----GYRLSPQTLTTIVKR-- 114

                          90
                  ....*....|.
gi 1063696934 162 levdTNKDGKI 172
Cdd:cd16186   115 ----YSKNGRI 121
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 75-176 2.01e-03

EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a calcium sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. It also serves as a calcium buffer in neurons. Thus, SCGN may be linked to the pathogenesis of neurological diseases such as Alzheimer's, and also acts as a serum marker of neuronal damage, or as a tumor biomarker. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. All six EF hand motifs of SCGN in some eukaryotes, including D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, could potentially bind six calcium ions. In contrast, SCGNs from higher eukaryotes have at least one non-functional EF-hand motif due to the mutation(s) or deletions. For instance, the EF1 loop does not coordinate calcium ion due to the key residue asparagine replaced by lysine in SCGNs of many mammalian species. Moreover, the EF2 loop seems to be competent for calcium-binding in most mammalian SCGNs except for human and chimpanzee orthologs.


Pssm-ID: 320078 [Multi-domain]  Cd Length: 257  Bit Score: 37.77  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  75 FADRVFYMFDRKRNGVIEFGEFVRSLSI---------FHPYTPEHEKSAF--MFKLFDLHGTGFIEPHELKKMVGAL--- 140
Cdd:cd16178   137 YTDTMMKIFDKNKDGRLDLNDMARILALqenfllqfkMDAMSEEERKRDFekIFAHYDVSKTGALEGPEVDGFVKDMmel 216

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063696934 141 ----LGETDLELSEESIeaiveqtMLEVDTNKDGKIDEEE 176
Cdd:cd16178   217 vkpsISGVQLDKFKEII-------LNHCDVNKDGKIQKSE 249
EF-hand_5 pfam13202
EF hand;
157-181 3.32e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.83  E-value: 3.32e-03
                          10        20
                  ....*....|....*....|....*
gi 1063696934 157 VEQTMLEVDTNKDGKIDEEEWKELV 181
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
PPP2R3C cd21505
serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric ...
 31-133 4.28e-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: 37.16  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  31 FTVNEIEALHDLFKKLSTSiiNDGLIHKEEflLALFRNGSMQNLFADRVF---YMFDRKRNgVIEFGEFVrsLSIFHPYT 107
Cdd:cd21505   215 FSAPSALRVYGQYLNLDKD--HNGMLSKQE--LSRYGKGTLTSVFIDRVFqecLTYNGEMD-YKTFLDFV--LAMENRKE 287

                          90       100
                  ....*....|....*....|....*.
gi 1063696934 108 PEheKSAFMFKLFDLHGTGFIEPHEL 133
Cdd:cd21505   288 PQ--ALQYFFRILDLKGQGYLTPFTL 311
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 156-183 4.53e-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: 33.53  E-value: 4.53e-03
                          10        20
                  ....*....|....*....|....*...
gi 1063696934 156 IVEQTMLEVDTNKDGKIDEEEWKELVAK 183
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 157-183 6.91e-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: 33.12  E-value: 6.91e-03
                           10        20
                   ....*....|....*....|....*..
gi 1063696934  157 VEQTMLEVDTNKDGKIDEEEWKELVAK 183
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 53-176 7.50e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 36.18  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696934  53 DGLIHkeEFLLALFRNGSMQNLFADRVFYM---FDRKRNGVIEFGEFVR-------SLSIFHPYTPEHEKSAFM--FKLF 120
Cdd:cd15902    22 DSFLR--ELLKALNGKDKTDDEVAEKKKEFmekYDENEDGKIEIRELANilpteenFLLLFRREQPLISSVEFMkiWRKY 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063696934 121 DLHGTGFIEPHELKKMVGALLGETDLELSEESIEAIVEQTMLEVDTNKDGKIDEEE 176
Cdd:cd15902   100 DTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLELDE 155
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 154-176 9.29e-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: 36.02  E-value: 9.29e-03
                          10        20
                  ....*....|....*....|...
gi 1063696934 154 EAIVEQTMLEVDTNKDGKIDEEE 176
Cdd:cd16226   155 DIVVQETLEDIDKNKDGFISLEE 177
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH