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Conserved domains on  [gi|3023439|sp|Q99653|]
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RecName: Full=Calcineurin B homologous protein 1; AltName: Full=Calcineurin B-like protein; AltName: Full=Calcium-binding protein CHP; AltName: Full=Calcium-binding protein p22; AltName: Full=EF-hand calcium-binding domain-containing protein p22

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];
27-182 3.03e-11

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 58.65  E-value: 3.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439   27 QITRLYSRFTSLDKGENGTLSREDFQRIPELAInplgDRIINAFFPEGEDQVNFRGFmRTLAHFRPIEDNEkskdvngpe 106
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLW----ATLFSEADTDGDGRISREEF-VAGMESLFEATVE--------- 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3023439  107 plnsrsNKLHFAFRLYDLDKDEKISRDELLQVLRMMvgvNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEK 182
Cdd:COG5126  69 ------PFARAAFDLLDTDGDGKISADEFRRLLTAL---GVSEEE----ADELFARLDTDGDGKISFEEFVAAVRD 131
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-182 3.03e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 58.65  E-value: 3.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439   27 QITRLYSRFTSLDKGENGTLSREDFQRIPELAInplgDRIINAFFPEGEDQVNFRGFmRTLAHFRPIEDNEkskdvngpe 106
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLW----ATLFSEADTDGDGRISREEF-VAGMESLFEATVE--------- 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3023439  107 plnsrsNKLHFAFRLYDLDKDEKISRDELLQVLRMMvgvNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEK 182
Cdd:COG5126  69 ------PFARAAFDLLDTDGDGKISADEFRRLLTAL---GVSEEE----ADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 114-180 4.38e-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: 56.02  E-value: 4.38e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3023439  114 KLHFAFRLYDLDKDEKISRDELLQVLRMMvGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 180
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEI----DEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
113-180 1.32e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.26  E-value: 1.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3023439    113 NKLHFAFRLYDLDKDEKISRDELLQVLRM-MVGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 180
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEV----EELFKEFDLDKDGRISFEEFLELY 66
PTZ00184 PTZ00184
calmodulin; Provisional
 24-180 1.07e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 46.29  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439    24 SHSQITRLYSRFTSLDKGENGTLSREDFQRI-PELAINP----LGDrIINAFFPEGEDQVNFRGFMRTLAhfrpiednEK 98
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVmRSLGQNPteaeLQD-MINEVDADGNGTIDFPEFLTLMA--------RK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439    99 SKDVNGPEPLNSrsnklhfAFRLYDLDKDEKISRDELLQVLRMMvGVNISDEQlgsiADRTIQEADQDGDSAISFTEFVK 178
Cdd:PTZ00184  77 MKDTDSEEEIKE-------AFKVFDRDGNGFISAAELRHVMTNL-GEKLTDEE----VDEMIREADVDGDGQINYEEFVK 144


                 ..
gi 3023439   179 VL 180
Cdd:PTZ00184 145 MM 146
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 114-142 7.17e-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: 7.17e-03
                           10        20
                   ....*....|....*....|....*....
gi 3023439     114 KLHFAFRLYDLDKDEKISRDELLQVLRMM 142
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-182 3.03e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 58.65  E-value: 3.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439   27 QITRLYSRFTSLDKGENGTLSREDFQRIPELAInplgDRIINAFFPEGEDQVNFRGFmRTLAHFRPIEDNEkskdvngpe 106
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLW----ATLFSEADTDGDGRISREEF-VAGMESLFEATVE--------- 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3023439  107 plnsrsNKLHFAFRLYDLDKDEKISRDELLQVLRMMvgvNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEK 182
Cdd:COG5126  69 ------PFARAAFDLLDTDGDGKISADEFRRLLTAL---GVSEEE----ADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 114-180 4.38e-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: 56.02  E-value: 4.38e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3023439  114 KLHFAFRLYDLDKDEKISRDELLQVLRMMvGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 180
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEI----DEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
113-180 1.32e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.26  E-value: 1.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3023439    113 NKLHFAFRLYDLDKDEKISRDELLQVLRM-MVGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVL 180
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPLSDEEV----EELFKEFDLDKDGRISFEEFLELY 66
PTZ00184 PTZ00184
calmodulin; Provisional
 24-180 1.07e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 46.29  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439    24 SHSQITRLYSRFTSLDKGENGTLSREDFQRI-PELAINP----LGDrIINAFFPEGEDQVNFRGFMRTLAhfrpiednEK 98
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVmRSLGQNPteaeLQD-MINEVDADGNGTIDFPEFLTLMA--------RK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439    99 SKDVNGPEPLNSrsnklhfAFRLYDLDKDEKISRDELLQVLRMMvGVNISDEQlgsiADRTIQEADQDGDSAISFTEFVK 178
Cdd:PTZ00184  77 MKDTDSEEEIKE-------AFKVFDRDGNGFISAAELRHVMTNL-GEKLTDEE----VDEMIREADVDGDGQINYEEFVK 144


                 ..
gi 3023439   179 VL 180
Cdd:PTZ00184 145 MM 146
PTZ00183 PTZ00183
centrin; Provisional
 18-182 1.13e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 46.61  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439    18 KKETGFSHSQITRLYSRFTSLDKGENGTLS-REDFQRIPELAINPLGDRIINAFFP---EGEDQVNFRGFMRTLAHFRPI 93
Cdd:PTZ00183   6 SERPGLTEDQKKEIREAFDLFDTDGSGTIDpKELKVAMRSLGFEPKKEEIKQMIADvdkDGSGKIDFEEFLDIMTKKLGE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439    94 EDNEKSKDVngpeplnsrsnklhfAFRLYDLDKDEKISRDELLQVLRMMvGVNISDEQLGSIadrtIQEADQDGDSAISF 173
Cdd:PTZ00183  86 RDPREEILK---------------AFRLFDDDKTGKISLKNLKRVAKEL-GETITDEELQEM----IDEADRNGDGEISE 145


                 ....*....
gi 3023439   174 TEFVKVLEK 182
Cdd:PTZ00183 146 EEFYRIMKK 154
PPP2R3C cd21505
serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric ...
 9-143 3.79e-05

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: 43.33  E-value: 3.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439    9 LRDEELEEIKKETG-FSHSQITRLYSRFTSLDKGENGTLSREDFQRIPElaiNPLGDRIINAFFPE-----GE-DQVNFR 81
Cdd:cd21505 200 LRDEELSEELQESNwFSAPSALRVYGQYLNLDKDHNGMLSKQELSRYGK---GTLTSVFIDRVFQEcltynGEmDYKTFL 276

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3023439   82 GFMrtLAHfrpieDNEKSkdvngPEplnsrsnKLHFAFRLYDLDKDEKISRDELLQVLRMMV 143
Cdd:cd21505 277 DFV--LAM-----ENRKE-----PQ-------ALQYFFRILDLKGQGYLTPFTLNYFFRAIQ 319
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 115-183 5.03e-05

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 41.44  E-value: 5.03e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3023439  115 LHFAFRLYDLDKDEKISRDELLQVLRMMvGVNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEKV 183
Cdd:cd16202   2 LKDQFRKADKNGDGKLSFKECKKLLKKL-NVKVDKDY----AKKLFQEADTSGEDVLDEEEFVQFYNRL 65
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
119-185 8.22e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 8.22e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3023439  119 FRLYDLDKDEKISRDELLQVLrmmvgVNISDEQLGSIADRTIQEADQDGDSAISFTEFVKVLEKVDV 185
Cdd:COG5126  39 FSEADTDGDGRISREEFVAGM-----ESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGV 100
EF-hand_8 pfam13833
EF-hand domain pair;
126-182 1.41e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.37  E-value: 1.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 3023439    126 KDEKISRDELLQVLRMMVGVNISDEQLGSIadrtIQEADQDGDSAISFTEFVKVLEK 182
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDIL----FREFDTDGDGYISFDEFCVLLER 53
EF-hand_6 pfam13405
EF-hand domain;
114-142 1.47e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 1.47e-03
                          10        20
                  ....*....|....*....|....*....
gi 3023439    114 KLHFAFRLYDLDKDEKISRDELLQVLRMM 142
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
PTZ00184 PTZ00184
calmodulin; Provisional
 118-182 1.60e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.43  E-value: 1.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3023439   118 AFRLYDLDKDEKISRDELLQVLRMMvGVNISDEQLgsiaDRTIQEADQDGDSAISFTEFVKVLEK 182
Cdd:PTZ00184  16 AFSLFDKDGDGTITTKELGTVMRSL-GQNPTEAEL----QDMINEVDADGNGTIDFPEFLTLMAR 75
PPP2R3 cd21339
serine/threonine protein phosphatase 2A regulatory subunit B"; Heterotrimeric serine/threonine ...
 8-135 2.02e-03

serine/threonine protein phosphatase 2A regulatory subunit B"; 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 family includes PP2A regulatory B'' subunits alpha, beta and gamma, encoded by PPP2R3A, PPP2R3B and PPP2R3C, respectively. It also includes subunit delta encoded by PPP2R3D in mouse. These B-family regulatory subunits play various roles including regulation of cytoskeletal assembly, neuronal differentiation, mitogen-activated protein kinase signaling, and apoptosis. Subunits alpha and beta contain two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity.


Pssm-ID: 410336  Cd Length: 259  Bit Score: 37.95  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439    8 LLRDEELeeIKKETG-FSHSQITRLYSRFTSLDKGENGTLSREDFQRIPELAI-NPLGDRIINAFFPEGEdQVNFRGFM- 84
Cdd:cd21339  85 LLEEEED--INQETNwFSYEHFYVIYCKFWELDTDHDLMISKEDLSRYNDAAMsNVFIDRIFSGAVTRGK-TIQKEGEMs 161

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 3023439   85 -RTLAHFRPIEDNEKskdvngpEPlnsrsNKLHFAFRLYDLDKDEKISRDEL 135
Cdd:cd21339 162 yADFVWFLISEEDKK-------EP-----TSIEYWFRCLDIDGDGYLSVFEL 201
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 119-177 2.53e-03

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 35.27  E-value: 2.53e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3023439  119 FRLYDLDKDEKISRDELLQVLRMmvgVNISDEQLGSIadrtIQEADQDGDSAISFTEFV 177
Cdd:cd00052   5 FRSLDPDGDGLISGDEARPFLGK---SGLPRSVLAQI----WDLADTDKDGKLDKEEFA 56
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 114-142 2.69e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.30  E-value: 2.69e-03
                          10        20
                  ....*....|....*....|....*....
gi 3023439    114 KLHFAFRLYDLDKDEKISRDELLQVLRMM 142
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 91-180 2.87e-03

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


Pssm-ID: 320009  Cd Length: 107  Bit Score: 35.81  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3023439   91 RPIEDNEKSKDVNGPEPL-NSRSNKLHFAFRLYDLDKDEKISRDELLQVLRMMvgvnisdEQLGSIADRTIQEADQDGDS 169
Cdd:cd00252  22 EQDENRSYDNNKRGHDLSgTMRKEIAQWEFDNLDNNKDGKLDKRELAPFRAPL-------MPLEHCARGFFESCDLNKDK 94

                        90
                ....*....|.
gi 3023439  170 AISFTEFVKVL 180
Cdd:cd00252  95 KISLQEWLGCF 105
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 114-180 3.19e-03

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 36.49  E-value: 3.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3023439  114 KLHFAFRLYDLDKDEKISRDELLQVLRMMvGVNISDEQLGSIadrtIQEADQDGDSAISFTEFVKVL 180
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRL-NIRVSEKELKKL----FKEVDTNGDGTLTFDEFEELY 62
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 114-142 7.17e-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: 7.17e-03
                           10        20
                   ....*....|....*....|....*....
gi 3023439     114 KLHFAFRLYDLDKDEKISRDELLQVLRMM 142
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
114-184 8.37e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 35.15  E-value: 8.37e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3023439  114 KLHFAFRLYDLDKDEKISRDELLQVLRMMVgvnisdeqlgsiaDRTIQEADQDGDSAISFTEFVKVLEKVD 184
Cdd:COG5126   6 KLDRRFDLLDADGDGVLERDDFEALFRRLW-------------ATLFSEADTDGDGRISREEFVAGMESLF 63
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 118-182 9.17e-03

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: 34.43  E-value: 9.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3023439  118 AFRLYDLDKDEKISRDELLQVLRM----MVGVNISDEQlgsiADRTIQEADQDGDSAISFTEFVKVLEK 182
Cdd:cd16252  42 AFQMLDKDKSGFIEWNEIKYILSTvpssMPVAPLSDEE----AEAMIQAADTDGDGRIDFQEFSDMVKK 106
 
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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