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Conserved domains on  [gi|24581831|ref|NP_723049|]
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uncharacterized protein Dmel_CG31650, isoform B [Drosophila melanogaster]

Protein Classification

CREC-EF hand family protein; EF-hand domain-containing protein( domain architecture ID 11610935)

CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family protein; the family consists of a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55, reticulocalbin-3 (RCN-3), cab45 Ca2+-binding protein, and calumenin (also known as crocalbin or CBP-50)| 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
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
58-322 1.37e-134

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


:

Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 383.59  E-value: 1.37e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  58 HGEDGEHNVEFDHEAIIGNTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEE 137
Cdd:cd16227   1 HAKDGEHNPEFDHEAVLGSRKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 138 IDQDADERITWKEYLQDTYAMEDEDFKKETIDydSYEDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLP 217
Cdd:cd16227  81 ADEDGDGKVTWEEYLADSFGYDDEDNEEMIKD--STEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 218 ILLEHTMQDKDADHDGKINFQEFVGDAASHHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEVDHLF 297
Cdd:cd16227 159 VLIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKEWLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLF 238
                       250       260
                ....*....|....*....|....*
gi 24581831 298 VSTDEDHDDRLSYLEILNNYDTFVG 322
Cdd:cd16227 239 ASADDDHDDRLSFDEILDHHEIFVG 263
 
Name Accession Description Interval E-value
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
58-322 1.37e-134

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 383.59  E-value: 1.37e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  58 HGEDGEHNVEFDHEAIIGNTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEE 137
Cdd:cd16227   1 HAKDGEHNPEFDHEAVLGSRKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 138 IDQDADERITWKEYLQDTYAMEDEDFKKETIDydSYEDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLP 217
Cdd:cd16227  81 ADEDGDGKVTWEEYLADSFGYDDEDNEEMIKD--STEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 218 ILLEHTMQDKDADHDGKINFQEFVGDAASHHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEVDHLF 297
Cdd:cd16227 159 VLIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKEWLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLF 238
                       250       260
                ....*....|....*....|....*
gi 24581831 298 VSTDEDHDDRLSYLEILNNYDTFVG 322
Cdd:cd16227 239 ASADDDHDDRLSFDEILDHHEIFVG 263
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
89-241 1.37e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 1.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  89 DESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLseeeaadrFEEIDQDADERITWKEYLQDTYAMEDEDFKKETi 168
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATL--------FSEADTDGDGRISREEFVAGMESLFEATVEPFA- 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581831 169 dydsyedeqkmikqdKEMFNAADTNKDGVLTLEEFVLFQ-----NPEEHPQMLPILlehtmqdkDADHDGKINFQEFV 241
Cdd:COG5126  72 ---------------RAAFDLLDTDGDGKISADEFRRLLtalgvSEEEADELFARL--------DTDGDGKISFEEFV 126
EF-hand_7 pfam13499
EF-hand domain pair;
184-241 1.62e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.94  E-value: 1.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24581831   184 KEMFNAADTNKDGVLTLEEFV-LFQNPEEHPQMLPILLEHTMQDKDADHDGKINFQEFV 241
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKkLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
PTZ00184 PTZ00184
calmodulin; Provisional
171-312 6.51e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.44  E-value: 6.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  171 DSYEDEQkmIKQDKEMFNAADTNKDGVLTLEEF-----VLFQNPEEHPqmlpilLEHTMQDKDADHDGKINFQEFVGDAA 245
Cdd:PTZ00184   3 DQLTEEQ--IAEFKEAFSLFDKDGDGTITTKELgtvmrSLGQNPTEAE------LQDMINEVDADGNGTIDFPEFLTLMA 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581831  246 SH----HDKEWLITEKERFDKDhdsnGDGVLTGDEVLSWIVPSNTAIANDEVDHLFVSTDEDHDDRLSYLE 312
Cdd:PTZ00184  75 RKmkdtDSEEEIKEAFKVFDRD----GNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEE 141
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
228-325 3.85e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 41.20  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  228 DADHDGKINFQEFVGDAASHHDKEWLITEKERFdKDHDSNGDGVLTGDEVLSWIVP----SNTAIANDEVDHLFVSTDED 303
Cdd:NF041410  37 DSDGDGSVSQDELSSALSSKSDDGSLIDLSELF-SDLDSDGDGSLSSDELAAAAPPppppPDQAPSTELADDLLSALDTD 115
                         90       100
                 ....*....|....*....|..
gi 24581831  304 HDDRLSYLEiLNNYDTFVGSEA 325
Cdd:NF041410 116 GDGSISSDE-LSAGLTSAGSSA 136
 
Name Accession Description Interval E-value
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
58-322 1.37e-134

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 383.59  E-value: 1.37e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  58 HGEDGEHNVEFDHEAIIGNTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEE 137
Cdd:cd16227   1 HAKDGEHNPEFDHEAVLGSRKEAEEFDELPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 138 IDQDADERITWKEYLQDTYAMEDEDFKKETIDydSYEDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLP 217
Cdd:cd16227  81 ADEDGDGKVTWEEYLADSFGYDDEDNEEMIKD--STEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 218 ILLEHTMQDKDADHDGKINFQEFVGDAASHHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEVDHLF 297
Cdd:cd16227 159 VLIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKEWLLVEKDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLF 238
                       250       260
                ....*....|....*....|....*
gi 24581831 298 VSTDEDHDDRLSYLEILNNYDTFVG 322
Cdd:cd16227 239 ASADDDHDDRLSFDEILDHHEIFVG 263
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
58-322 6.52e-81

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: 247.11  E-value: 6.52e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  58 HGEDGEHNVEFDHEAIIGnTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEE 137
Cdd:cd16226   1 HDDDGEHNPEYDHEAFLG-KEEAKEFDQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 138 IDQDADERITWKEYLQDTYAMEDEdfkkETIDYDSYEDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLP 217
Cdd:cd16226  80 YDPNKDGKLSWEEYKKATYGFLDD----EEEDDDLHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 218 ILLEHTMQDKDADHDGKINFQEFVGDAASHH----DKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEV 293
Cdd:cd16226 156 IVVQETLEDIDKNKDGFISLEEYIGDMYRDDdeeeDPDWVKSEREQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEA 235
                       250       260
                ....*....|....*....|....*....
gi 24581831 294 DHLFVSTDEDHDDRLSYLEILNNYDTFVG 322
Cdd:cd16226 236 KHLIYEADDDKDGKLTKEEILDKYDLFVG 264
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
58-321 1.98e-80

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 245.81  E-value: 1.98e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  58 HGEDGEHNVEFDHEAIIGnTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEE 137
Cdd:cd15899   1 HEMDGHLNSDYDHEAFLG-KEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 138 IDQDADERITWKEYLQDTYAMEDEDFKKETIDYDSYEDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLP 217
Cdd:cd15899  80 VDPDEDGHVSWDEYKNDTYGSVGDDEENVADNIKEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 218 ILLEHTMQDKDADHDGKINFQEFVGDAASH----HDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEV 293
Cdd:cd15899 160 FVIKETLEDLDKNGDGFISLEEFISDPYSAdeneEEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEEA 239
                       250       260
                ....*....|....*....|....*...
gi 24581831 294 DHLFVSTDEDHDDRLSYLEILNNYDTFV 321
Cdd:cd15899 240 KHLIAESDENKDGKLSPEEILDNHELFV 267
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
58-320 2.33e-61

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 197.27  E-value: 2.33e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  58 HGEDGEHNVEFDHEAIIGNTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEE 137
Cdd:cd16224   1 HYPNGEHNAEYDKEAFLGGEEDADEFAKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 138 IDQDADERITWKEYlqdTYAMEDE--DFKKETIDYDSYEDEQKMIK-QDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQ 214
Cdd:cd16224  81 YDKDGDGAVTWDEY---NMQMYDRviDYDEDTVLDDEEEESFRQLHlKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 215 MLPILLEHTMQDKDADHDGKINFQEFVGD----AASHHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIAN 290
Cdd:cd16224 158 MTEFVIQEALEEHDKDGDGFISLEEFLGDyrkdPTANEDPEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQ 237
                       250       260       270
                ....*....|....*....|....*....|
gi 24581831 291 DEVDHLFVSTDEDHDDRLSYLEILNNYDTF 320
Cdd:cd16224 238 EEALHLIDEMDLNGDGRLSEEEILENQDLF 267
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
55-322 1.48e-53

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, 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 His-Asp-Glu-Leu (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: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 177.09  E-value: 1.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  55 AHHhgeDGEHNVEFDHEAIIGNtKEAQEFDSLSPDESKRRLLILIKMMDL--NKDEFIDRHELKAWILRSFKKLSEEEAA 132
Cdd:cd16230   1 PHD---DAHGNFQYDHEAFLGR-EVAKEFDQLSPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 133 DRFEEIDQDADERITWKEYLQDTYAMEDEDFkkETIDYDSYEDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEH 212
Cdd:cd16230  77 AAWQTYDTDRDGRVGWEELRNATYGHYEPGE--EFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 213 PQMLPILLEHTMQDKDADHDGKINFQEFVGDAAS----HHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAI 288
Cdd:cd16230 155 PHMRDIVVAETLEDLDKNKDGYVQVEEYIADLYSgepgEEEPAWVQTERQQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQ 234
                       250       260       270
                ....*....|....*....|....*....|....
gi 24581831 289 ANDEVDHLFVSTDEDHDDRLSYLEILNNYDTFVG 322
Cdd:cd16230 235 PLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 268
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
61-322 6.19e-48

EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF SSP 9302, 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 is highly expressed in various brain regions. Thus it plays an important role in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons. Calumenin is involved in Ca2+ homeostasis through interacting with ryanodine receptor RyR2 and SERCA2. It acts as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. Calumenin also forms a Ca2+-dependent complex with thrombospondin-1, which is broadly involved in haemostasis and thrombosis. Moreover, calumenin is a molecular chaperone that endogenously regulates the vitamin K-dependent gamma-carboxylation of several proteins, including blood coagulation factors (such as FII, FVII, FIX, FX, and proteins C, S and Z), cell survival factors (Gas6) and bone metabolism proteins (such as matrix Gla protein or MGP, osteocalcin and periostin), through targeting the gamma-glutamyl carboxylase. It also functions as a charged F508del-cystic fibrosis transmembrane regulator (CFTR) folding modulator, as well as a G551D-CFTR associated protein. Furthermore, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. It binds to and stabilizes fibulin-1, and further inactivates extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling.


Pssm-ID: 320026 [Multi-domain]  Cd Length: 263  Bit Score: 162.42  E-value: 6.19e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  61 DGEHNVEFDHEAIIGnTKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEEIDQ 140
Cdd:cd16228   4 DDAQNFDYDHDAFLG-AEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGHDL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 141 DADERITWKEYLQDTYAMEDEDFKKEtidyDSYEDEQKMIKqDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLPILL 220
Cdd:cd16228  83 NEDGLVSWEEYKNATYGYILDDPDPD----DGFNYKQMMVR-DERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 221 EHTMQDKDADHDGKINFQEFVGDAASH----HDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEVDHL 296
Cdd:cd16228 158 LETMEDIDKNGDGFIDLEEYIGDMYSQdgdaDEPEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHL 237
                       250       260
                ....*....|....*....|....*.
gi 24581831 297 FVSTDEDHDDRLSYLEILNNYDTFVG 322
Cdd:cd16228 238 VYESDQNKDGKLTKEEIVDKYDLFVG 263
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
58-322 2.03e-47

EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance.


Pssm-ID: 320027 [Multi-domain]  Cd Length: 267  Bit Score: 161.20  E-value: 2.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  58 HGEDGEHNVEFDHEAIIGNtKEAQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEE 137
Cdd:cd16229   1 QLHEDNQSFQYDHEAFLGK-EEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 138 IDQDADERITWKEYLQDTYA--MEDEDFKKETIDYDSYedeQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEEHPQM 215
Cdd:cd16229  80 YDLNKDNKISWEEYKQATYGyyLGNPEEFQDATDQFSF---KKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 216 LPILLEHTMQDKDADHDGKINFQEFVGDAASHHDK----EWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPSNTAIAND 291
Cdd:cd16229 157 KDIVVLETLEDIDKNGDGFVDEDEYIADMFSHEEGgpepDWVKTEREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQA 236
                       250       260       270
                ....*....|....*....|....*....|.
gi 24581831 292 EVDHLFVSTDEDHDDRLSYLEILNNYDTFVG 322
Cdd:cd16229 237 EARHLVYESDKDKDQKLTKEEILDNWNMFVG 267
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
61-320 7.63e-39

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: 138.97  E-value: 7.63e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  61 DGEHNVEFDHEAIIGNTKEaqEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFK---KLSEEEAADRFEE 137
Cdd:cd16225   4 DGHLNKEFHKEVFLGNEKE--EFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQehfQEAVEENEQIFKA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 138 IDQDADERITWKEYLQDTYAME---DEDFKKETIDYDSY---EDEQKMIKQDKEMFNAADTNKDGVLTLEEFVLFQNPEE 211
Cdd:cd16225  82 VDTDKDGNVSWEEYRVHFLLSKgysEEEAEEKIKNNEELkldEDDKEVLDRYKDRWSQADEPEDGLLDVEEFLSFRHPEH 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 212 HPQMLPILLEHTMQDKDADHDGKINFQEFV-------GDAASHHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWIVPS 284
Cdd:cd16225 162 SRGMLKNMVKEILHDLDQDGDEKLTLDEFVslppgtvEEQQAEDDDEWKKERKKEFEEVIDLNHDGKVTKEELEEYMDPR 241
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 24581831 285 NTAIANDEVDHLFVSTDEDHDDRLSYLEILNNYDTF 320
Cdd:cd16225 242 NERHALNEAKQLIAVADENKDGKLSLEEILKNSDLF 277
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
89-241 1.37e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 1.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  89 DESKRRLLILIKMMDLNKDEFIDRHELKAWILRSFKKLseeeaadrFEEIDQDADERITWKEYLQDTYAMEDEDFKKETi 168
Cdd:COG5126   1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWATL--------FSEADTDGDGRISREEFVAGMESLFEATVEPFA- 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581831 169 dydsyedeqkmikqdKEMFNAADTNKDGVLTLEEFVLFQ-----NPEEHPQMLPILlehtmqdkDADHDGKINFQEFV 241
Cdd:COG5126  72 ---------------RAAFDLLDTDGDGKISADEFRRLLtalgvSEEEADELFARL--------DTDGDGKISFEEFV 126
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
185-315 6.29e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 59.42  E-value: 6.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 185 EMFNAADTNKDGVLTLEEFVlfqnpeehpQMLPILLEHTMQDKDADHDGKINFQEFVGDAASHHDKEWLITEKERFDKdH 264
Cdd:COG5126   9 RRFDLLDADGDGVLERDDFE---------ALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDL-L 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24581831 265 DSNGDGVLTGDEVLSWIvpSNTAIANDEVDHLFVSTDEDHDDRLSYLEILN 315
Cdd:COG5126  79 DTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVA 127
EF-hand_7 pfam13499
EF-hand domain pair;
184-241 1.62e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.94  E-value: 1.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24581831   184 KEMFNAADTNKDGVLTLEEFV-LFQNPEEHPQMLPILLEHTMQDKDADHDGKINFQEFV 241
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKkLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
100-153 3.42e-05

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: 40.99  E-value: 3.42e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24581831 100 KMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEEIDQDADERITWKEYLQ 153
Cdd:cd00051   7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
184-241 5.38e-05

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: 40.61  E-value: 5.38e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24581831 184 KEMFNAADTNKDGVLTLEEFVLFQNPEEHPQMLPILLEhTMQDKDADHDGKINFQEFV 241
Cdd:cd00051   3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDE-MIREVDKDGDGKIDFEEFL 59
PTZ00184 PTZ00184
calmodulin; Provisional
171-312 6.51e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 42.44  E-value: 6.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  171 DSYEDEQkmIKQDKEMFNAADTNKDGVLTLEEF-----VLFQNPEEHPqmlpilLEHTMQDKDADHDGKINFQEFVGDAA 245
Cdd:PTZ00184   3 DQLTEEQ--IAEFKEAFSLFDKDGDGTITTKELgtvmrSLGQNPTEAE------LQDMINEVDADGNGTIDFPEFLTLMA 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581831  246 SH----HDKEWLITEKERFDKDhdsnGDGVLTGDEVLSWIVPSNTAIANDEVDHLFVSTDEDHDDRLSYLE 312
Cdd:PTZ00184  75 RKmkdtDSEEEIKEAFKVFDRD----GNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEE 141
EF-hand_7 pfam13499
EF-hand domain pair;
100-153 1.04e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.93  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581831   100 KMMDLNKDEFIDRHELKAWI--LRSFKKLSEEEAADRFEEIDQDADERITWKEYLQ 153
Cdd:pfam13499   9 KLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
80-153 1.67e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 1.67e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581831  80 AQEFDSLSPDESKRRLLILIKMMDLNKDEFIDRHELKAWIlrSFKKLSEEEAADRFEEIDQDADERITWKEYLQ 153
Cdd:COG5126  56 VAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVA 127
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
228-325 3.85e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 41.20  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831  228 DADHDGKINFQEFVGDAASHHDKEWLITEKERFdKDHDSNGDGVLTGDEVLSWIVP----SNTAIANDEVDHLFVSTDED 303
Cdd:NF041410  37 DSDGDGSVSQDELSSALSSKSDDGSLIDLSELF-SDLDSDGDGSLSSDELAAAAPPppppPDQAPSTELADDLLSALDTD 115
                         90       100
                 ....*....|....*....|..
gi 24581831  304 HDDRLSYLEiLNNYDTFVGSEA 325
Cdd:NF041410 116 GDGSISSDE-LSAGLTSAGSSA 136
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
220-309 6.07e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 6.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 220 LEHTMQDKDADHDGKINFQEFVgdAASHHDKEWLItekerfdKDHDSNGDGVLTGDEVLSWIVPSNTAIANDEVDHLFVS 299
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFE--ALFRRLWATLF-------SEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDL 77
                        90
                ....*....|
gi 24581831 300 TDEDHDDRLS 309
Cdd:COG5126  78 LDTDGDGKIS 87
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
130-204 1.73e-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: 1.73e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581831 130 EAADRFEEIDQDADERITWKEYLQDTYAMEDEDFKKETidydsyedeqkmikqdKEMFNAADTNKDGVLTLEEFV 204
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEI----------------DEMIREVDKDGDGKIDFEEFL 59
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
94-151 2.44e-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: 37.65  E-value: 2.44e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24581831  94 RLLILIKMMDLNKDEFIDRHELKAWILRSFKKLSEEEAADRFEEIDQDADERITWKEY 151
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
257-317 2.59e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 2.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581831   257 KERFDKdHDSNGDGVLTGDEVLSWIVPSNTA--IANDEVDHLFVSTDEDHDDRLSYLEILNNY 317
Cdd:pfam13499   5 KEAFKL-LDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
184-241 2.61e-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: 37.65  E-value: 2.61e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24581831 184 KEMFNAADTNKDGVLTLEEFV-LFQnpEEHPQMLPILLEHTMQDKDADHDGKINFQEFV 241
Cdd:cd15898   3 RRQWIKADKDGDGKLSLKEIKkLLK--RLNIRVSEKELKKLFKEVDTNGDGTLTFDEFE 59
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
103-297 4.14e-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: 38.10  E-value: 4.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 103 DLNKDEFIDRHELKAWILRSFKKL-----SEEEAADRFEEI----DQDADERITWKEYLQdtYAMEDEDFKKETIDYDSY 173
Cdd:cd15902   9 DADGNGYIEGKELDSFLRELLKALngkdkTDDEVAEKKKEFmekyDENEDGKIEIRELAN--ILPTEENFLLLFRREQPL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 174 EDEQKMIKqdkeMFNAADTNKDGVLTLEEFVLF-------QNPEEHPQMLPILLEHTMQDKDADHDGKINFQEFVGdaas 246
Cdd:cd15902  87 ISSVEFMK----IWRKYDTDGSGFIEAKELKGFlkdlllkNKKHVSPPKLDEYTKLILKEFDANKDGKLELDEMAK---- 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24581831 247 hhdkewLITEKERFDKDHDSNGDGVLTGDEVLS----WIVPSNTAIANDEVDHLF 297
Cdd:cd15902 159 ------LLPVQENFLLKFQILGAMDLTKEDFEKvfehYDKDNNGVIEGNELDALL 207
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
228-313 4.54e-03

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: 37.19  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581831 228 DADHDGKINFQEFvgdAASHhdkEWLITEKERFDKdHDSNGDGVLTGDEVLSWIVPSNTAIANDEVDHLFVSTDEDHDDR 307
Cdd:cd16185  46 DRDGNGTIDFEEF---AALH---QFLSNMQNGFEQ-RDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGS 118

                ....*....
gi 24581831 308 LS---YLEI 313
Cdd:cd16185 119 LGfddYIEL 127
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
217-241 7.89e-03

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 35.16  E-value: 7.89e-03
                        10        20
                ....*....|....*....|....*
gi 24581831 217 PILLEHTMQDKDADHDGKINFQEFV 241
Cdd:cd00213  50 PEAVDKIMKDLDVNKDGKVDFQEFL 74
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
228-281 9.51e-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: 34.06  E-value: 9.51e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24581831 228 DADHDGKINFQEFvGDAASHHDKEWLITEKERFDKDHDSNGDGVLTGDEVLSWI 281
Cdd:cd00051  10 DKDGDGTISADEL-KAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
 
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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