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Conserved domains on  [gi|15866276|gb|AAL10300|]
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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

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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];
39-183 1.82e-11

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 59.42  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  39 LHDLFKKLSTSiiNDGLIHKEEFllALFRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAfMFK 118
Cdd:COG5126   7 LDRRFDLLDAD--GDGVLERDDF--EALFRRLWATLFSE-----ADTDGDGRISREEFVAGMESLFEATVEPFARA-AFD 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15866276 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 1.82e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 59.42  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  39 LHDLFKKLSTSiiNDGLIHKEEFllALFRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAfMFK 118
Cdd:COG5126   7 LDRRFDLLDAD--GDGVLERDDF--EALFRRLWATLFSE-----ADTDGDGRISREEFVAGMESLFEATVEPFARA-AFD 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15866276 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 2.20e-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: 57.17  E-value: 2.20e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15866276 115 FMFKLFDLHGTGFIEPHELKKMVGALLGETDlelseesiEAIVEQTMLEVDTNKDGKIDEEEWKELVA 182
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEGLS--------EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
 26-185 1.93e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 54.31  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276   26 ASETPFTVNEIEALHDLFKKLSTSiiNDGLIHKEEFLLAL------FRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRS 99
Cdd:PTZ00183   6 SERPGLTEDQKKEIREAFDLFDTD--GSGTIDPKELKVAMrslgfePKKEEIKQMIAD-----VDKDGSGKIDFEEFLDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  100 LSIFHPYTPEHEKSAFMFKLFDLHGTGFIEPHELKKmVGALLGETdleLSEESIEAIVEqtmlEVDTNKDGKIDEEEWKE 179
Cdd:PTZ00183  79 MTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKR-VAKELGET---ITDEELQEMID----EADRNGDGEISEEEFYR 150


                 ....*.
gi 15866276  180 LVAKNP 185
Cdd:PTZ00183 151 IMKKTN 156
EF-hand_7 pfam13499
EF-hand domain pair;
111-181 1.56e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 1.56e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15866276   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 8.39e-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: 32.74  E-value: 8.39e-03
                           10        20
                   ....*....|....*....|....*..
gi 15866276    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 1.82e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 59.42  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  39 LHDLFKKLSTSiiNDGLIHKEEFllALFRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAfMFK 118
Cdd:COG5126   7 LDRRFDLLDAD--GDGVLERDDF--EALFRRLWATLFSE-----ADTDGDGRISREEFVAGMESLFEATVEPFARA-AFD 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15866276 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 2.20e-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: 57.17  E-value: 2.20e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15866276 115 FMFKLFDLHGTGFIEPHELKKMVGALLGETDlelseesiEAIVEQTMLEVDTNKDGKIDEEEWKELVA 182
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEGLS--------EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
 26-185 1.93e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 54.31  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276   26 ASETPFTVNEIEALHDLFKKLSTSiiNDGLIHKEEFLLAL------FRNGSMQNLFADrvfymFDRKRNGVIEFGEFVRS 99
Cdd:PTZ00183   6 SERPGLTEDQKKEIREAFDLFDTD--GSGTIDPKELKVAMrslgfePKKEEIKQMIAD-----VDKDGSGKIDFEEFLDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  100 LSIFHPYTPEHEKSAFMFKLFDLHGTGFIEPHELKKmVGALLGETdleLSEESIEAIVEqtmlEVDTNKDGKIDEEEWKE 179
Cdd:PTZ00183  79 MTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKR-VAKELGET---ITDEELQEMID----EADRNGDGEISEEEFYR 150


                 ....*.
gi 15866276  180 LVAKNP 185
Cdd:PTZ00183 151 IMKKTN 156
EF-hand_7 pfam13499
EF-hand domain pair;
111-181 1.56e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 1.56e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15866276   111 EKSAFMFKLFDLHGTGFIEPHELKKMVGALlgETDLELSEESIEAIVEqtmlEVDTNKDGKIDEEEWKELV 181
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKL--EEGEPLSDEEVEELFK----EFDLDKDGRISFEEFLELY 66
PTZ00184 PTZ00184
calmodulin; Provisional
 84-181 7.60e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.37  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276   84 DRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAFMFKLFDLHGTGFIEPHELKKmVGALLGEtdlELSEESieaiVEQTMLE 163
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRH-VMTNLGE---KLTDEE----VDEMIRE 128

                         90
                 ....*....|....*...
gi 15866276  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 9.90e-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: 42.01  E-value: 9.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  52 NDGLIHKEE---FLLALFRNGSMQNL--------FADRVFYMFDRKRNGVIEFGEFVRSL---------SIF-HPYTPEH 110
Cdd:cd16179 108 NSGYIEADElknFLKHLLKEAKRDNDvsedklieYTDTILQLFDRNKDGKLQLSEMARLLpvkenflcrPIFkGAGKLTR 187

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15866276 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 1.63e-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: 41.24  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  70 SMQNLFADRVFYMFDRKRNGVIEFGEFVRSLS-------IFHPYTPEHEKSAFM--FKLFDLHGTGFIEPHELKKMVGAL 140
Cdd:cd16179  45 TALEELKEEFMEAYDENQDGRIDIRELAQLLPteenfllLFRRDNPLDSSVEFMkvWREYDKDNSGYIEADELKNFLKHL 124

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15866276 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 2.21e-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: 39.44  E-value: 2.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  84 DRKRNGVIEFGEFVRSLSIFHPYTPEHEKSAFMFKLFDLHGTGFIEPHELKKMVGALLGETDLE-LSEESIEAIVEQTml 162
Cdd:cd16252  10 EMRHHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPVApLSDEEAEAMIQAA-- 87

                        90       100
                ....*....|....*....|.
gi 15866276 163 evDTNKDGKIDEEEWKELVAK 183
Cdd:cd16252  88 --DTDGDGRIDFQEFSDMVKK 106
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
111-182 3.55e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 3.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276 111 EKSAFMFKLFDLHGTGFIEPHELKKM----VGALLGETD----------------LELSEESIEAIVEQTMLEVDTNKDG 170
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEALfrrlWATLFSEADtdgdgrisreefvagmESLFEATVEPFARAAFDLLDTDGDG 84

                        90
                ....*....|..
gi 15866276 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 1.72e-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: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  82 MFDRKRNGVIEFGEFVRSLSIFHPYtpeheKSAFMfkLFDLHGTGFIEPHELKKMVGALlgetDLELSEESIEAIVEQtm 161
Cdd:cd16186  48 MLDRDHTGKMGFNEFKELWAALNAW-----KQNFM--TVDQDRSGTVEPHELRQAIGAM----GYRLSPQTLTTIVKR-- 114

                        90
                ....*....|.
gi 15866276 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 2.68e-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: 2.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  75 FADRVFYMFDRKRNGVIEFGEFVRSLSI---------FHPYTPEHEKSAF--MFKLFDLHGTGFIEPHELKKMVGAL--- 140
Cdd:cd16178 137 YTDTMMKIFDKNKDGRLDLNDMARILALqenfllqfkMDAMSEEERKRDFekIFAHYDVSKTGALEGPEVDGFVKDMmel 216

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15866276 141 ----LGETDLELSEESIeaiveqtMLEVDTNKDGKIDEEE 176
Cdd:cd16178 217 vkpsISGVQLDKFKEII-------LNHCDVNKDGKIQKSE 249
EF-hand_5 pfam13202
EF hand;
157-181 4.38e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.45  E-value: 4.38e-03
                          10        20
                  ....*....|....*....|....*
gi 15866276   157 VEQTMLEVDTNKDGKIDEEEWKELV 181
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 156-183 5.40e-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: 5.40e-03
                          10        20
                  ....*....|....*....|....*...
gi 15866276   156 IVEQTMLEVDTNKDGKIDEEEWKELVAK 183
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
PPP2R3C cd21505
serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric ...
 31-133 6.39e-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: 36.78  E-value: 6.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15866276  31 FTVNEIEALHDLFKKLSTSiiNDGLIHKEEflLALFRNGSMQNLFADRVF---YMFDRKRNgVIEFGEFVrsLSIFHPYT 107
Cdd:cd21505 215 FSAPSALRVYGQYLNLDKD--HNGMLSKQE--LSRYGKGTLTSVFIDRVFqecLTYNGEMD-YKTFLDFV--LAMENRKE 287

                        90       100
                ....*....|....*....|....*.
gi 15866276 108 PEheKSAFMFKLFDLHGTGFIEPHEL 133
Cdd:cd21505 288 PQ--ALQYFFRILDLKGQGYLTPFTL 311
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 157-183 8.39e-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: 32.74  E-value: 8.39e-03
                           10        20
                   ....*....|....*....|....*..
gi 15866276    157 VEQTMLEVDTNKDGKIDEEEWKELVAK 183
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EFh_SPARC_SMOC cd16234
EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding ...
 108-180 9.59e-03

EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein SMOC-1, SMOC-2, and similar proteins; SMOC proteins corresponds to a group matricellular proteins that are involved in direct or indirect modulation of growth factor signaling pathways and play diverse roles in physiological processes involving extensive tissue remodeling, migration, proliferation, and angiogenesis. They may mediate intercellular signaling and cell type-specific differentiation during gonad and reproductive tract development. SMOC-1 is localized in basement membranes. Its mutations have been found to be associated with individuals with Warrdenburg Anopthalmia Syndrome. SMOC-2 is ubiquitously expressed and is involved in angiogenesis and the regulation of cell cycle progression. It enhances the angiogenic effect of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF). It has also been implicated in generalized vitiligo. SMOC proteins consist of a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain conserved only in SMOC proteins, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs.


Pssm-ID: 320013  Cd Length: 104  Bit Score: 34.56  E-value: 9.59e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15866276 108 PEHEKSAFMFKLFDLhgtgFIephelKKMVGALlGETDLELSEESIEAIVEQTMLEVDTNKDGKIDEEEWKEL 180
Cdd:cd16234   2 PEAKKTEFLNNLIDA----LK-----TEMVRSG-NSNSSAPDKSSEEQVLDWKFSQLDKNKNGVLERKEWKPF 64
 
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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