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Conserved domains on  [gi|453225954|ref|NP_491936|]
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EF-hand domain-containing protein [Caenorhabditis elegans]

Protein Classification

CREC-EF hand family protein( domain architecture ID 707362)

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)

Gene Ontology:  GO:0005509
PubMed:  28707401

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_CREC super family cl25354
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 54-265 1.35e-66

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.


The actual alignment was detected with superfamily member cd16227:

Pssm-ID: 330175 [Multi-domain]  Cd Length: 263  Bit Score: 208.33  E-value: 1.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  54 AKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLADSFPDEELHN--------KEEESLI 125
Cdd:cd16227   42 AKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEEADEDGDGKVTWEEYLADSFGYDDEDNeemikdstEDDLKLL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 126 AQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGELDEQRGSEWYKVEVERF 205
Cdd:cd16227  122 EDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPVLIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKEWLLVEKDRF 201

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 206 RTVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHALF 265
Cdd:cd16227  202 DEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFDEILDHHEIF 261
 
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 ...
 54-265 1.35e-66

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: 208.33  E-value: 1.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  54 AKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLADSFPDEELHN--------KEEESLI 125
Cdd:cd16227   42 AKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEEADEDGDGKVTWEEYLADSFGYDDEDNeemikdstEDDLKLL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 126 AQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGELDEQRGSEWYKVEVERF 205
Cdd:cd16227  122 EDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPVLIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKEWLLVEKDRF 201

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 206 RTVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHALF 265
Cdd:cd16227  202 DEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFDEILDHHEIF 261
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
47-186 1.27e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 58.26  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  47 QESVEKFAKALDTNNDGFVDKSEILAwvsesyqkTVDREAVERISELDENADGFVSWEEYLAdsfpdeELHNKEEESLIA 126
Cdd:COG5126    4 RRKLDRRFDLLDADGDGVLERDDFEA--------LFRRLWATLFSEADTDGDGRISREEFVA------GMESLFEATVEP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 127 QDKMYFKQADEDNDGKLNLEELASFLNPehhPHMHPVLIAVTLLEKDQNGDGAIEEKEFL 186
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADELFARLDTDGDGKISFEEFV 126
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
46-257 1.61e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 48.14  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  46 GQESVEKFAKALDTNNDGFVDKSEILAWVSEsyqktvdreaveriseldenadgfvsweeyladsfpdeelhNKEEESLI 125
Cdd:NF041410  25 SQQFQKQLFAKLDSDGDGSVSQDELSSALSS-----------------------------------------KSDDGSLI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 126 AQDKMyFKQADEDNDGKLNLEELASFLNPEHHPHMHPvliavtllekdQNGDGAieeKEFLGELDEqrgsewykveverf 205
Cdd:NF041410  64 DLSEL-FSDLDSDGDGSLSSDELAAAAPPPPPPPDQA-----------PSTELA---DDLLSALDT-------------- 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 453225954 206 rtvydkNKDGKLAGDELTDWLLVDGTTAGSyeaESLLTNSDDDKDGQLSYEE 257
Cdd:NF041410 115 ------DGDGSISSDELSAGLTSAGSSADS---SQLFSALDSDGDGSVSSDE 157
PTZ00184 PTZ00184
calmodulin; Provisional
 122-260 6.99e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 45.14  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 122 ESLIAQDKMYFKQADEDNDGKLNLEELASFL-----NPEHHPhmhpvlIAVTLLEKDQNGDGAIEEKEFLG----ELDEQ 192
Cdd:PTZ00184   7 EEQIAEFKEAFSLFDKDGDGTITTKELGTVMrslgqNPTEAE------LQDMINEVDADGNGTIDFPEFLTlmarKMKDT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 453225954 193 RGSEWYKvevERFRtVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVK 260
Cdd:PTZ00184  81 DSEEEIK---EAFK-VFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVK 144
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
88-223 7.41e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 46.21  E-value: 7.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  88 ERISELDENADGFVSWEEY---LADsfpdeelhNKEEESLIAQDKMyFKQADEDNDGKLNLEELASFLNPEHHPHMHP-- 162
Cdd:NF041410  31 QLFAKLDSDGDGSVSQDELssaLSS--------KSDDGSLIDLSEL-FSDLDSDGDGSLSSDELAAAAPPPPPPPDQAps 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 453225954 163 VLIAVTLLEK-DQNGDGAIEEKEFLGELDEQRGSEwykvEVERFRTVYDKNKDGKLAGDELT 223
Cdd:NF041410 102 TELADDLLSAlDTDGDGSISSDELSAGLTSAGSSA----DSSQLFSALDSDGDGSVSSDELA 159
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
24-158 5.14e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.52  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  24 DGSVSpSDHKKPASEQKLNlKSGQESVEKFAKALDTNNDGFVDKSEILAW------VSESYQKTVDREAVerISELDENA 97
Cdd:NF041410  41 DGSVS-QDELSSALSSKSD-DGSLIDLSELFSDLDSDGDGSLSSDELAAAapppppPPDQAPSTELADDL--LSALDTDG 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453225954  98 DGFVSWEEYLAdsfpdeELHNKEEESLIAQDkmyFKQADEDNDGKLNLEELASFLNPEHHP 158
Cdd:NF041410 117 DGSISSDELSA------GLTSAGSSADSSQL---FSALDSDGDGSVSSDELAAALQPPPPP 168
EF-hand_7 pfam13499
EF-hand domain pair;
55-108 1.21e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 1.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 453225954   55 KALDTNNDGFVDKSEILAWV-SESYQKTVDREAVERI-SELDENADGFVSWEEYLA 108
Cdd:pfam13499   9 KLLDSDGDGYLDVEELKKLLrKLEEGEPLSDEEVEELfKEFDLDKDGRISFEEFLE 64
 
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 ...
 54-265 1.35e-66

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: 208.33  E-value: 1.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  54 AKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLADSFPDEELHN--------KEEESLI 125
Cdd:cd16227   42 AKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANERFEEADEDGDGKVTWEEYLADSFGYDDEDNeemikdstEDDLKLL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 126 AQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGELDEQRGSEWYKVEVERF 205
Cdd:cd16227  122 EDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPVLIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKEWLLVEKDRF 201

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 206 RTVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHALF 265
Cdd:cd16227  202 DEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFDEILDHHEIF 261
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 58-265 1.65e-53

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: 174.69  E-value: 1.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  58 DTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLADSFPDEELHNKEEES------LIAQDKMY 131
Cdd:cd16226   45 DKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEYDPNKDGKLSWEEYKKATYGFLDDEEEDDDLhesykkMIRRDERR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 132 FKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGEL----DEQRGSEWYKVEVERFRT 207
Cdd:cd16226  125 WKAADQDGDGKLTKEEFTAFLHPEEFPHMRDIVVQETLEDIDKNKDGFISLEEYIGDMyrddDEEEDPDWVKSEREQFKE 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 453225954 208 VYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHALF 265
Cdd:cd16226  205 FRDKNKDGKMDREEVKDWILPEDYDHAEAEAKHLIYEADDDKDGKLTKEEILDKYDLF 262
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 40-265 1.10e-49

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: 165.31  E-value: 1.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  40 KLNLKSGQESVEKFAKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLADSF----PDEE 115
Cdd:cd15899   27 QLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYKNDTYgsvgDDEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 116 LH------NKEEESLIAQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGEL 189
Cdd:cd15899  107 NVadnikeDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDFVIKETLEDLDKNGDGFISLEEFISDP 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 190 ----DEQRGSEWYKVEVERFRTVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHALF 265
Cdd:cd15899  187 ysadENEEEPEWVKVEKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEEAKHLIAESDENKDGKLSPEEILDNHELF 266
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 60-265 1.51e-38

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: 136.26  E-value: 1.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  60 NNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLADSF----PDEELHNKEE----ESLIAQDKMY 131
Cdd:cd16230   49 DGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQTYDTDRDGRVGWEELRNATYghyePGEEFHDVEDaetyKKMLARDERR 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 132 FKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGEL-DEQRGSE---WYKVEVERFRT 207
Cdd:cd16230  129 FRVADQDGDSMATREELTAFLHPEEFPHMRDIVVAETLEDLDKNKDGYVQVEEYIADLySGEPGEEepaWVQTERQQFRQ 208

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 453225954 208 VYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHALF 265
Cdd:cd16230  209 FRDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMF 266
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 39-265 1.64e-38

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: 136.41  E-value: 1.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  39 QKLNLKSGQESVEKFAKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEY-------LADSF 111
Cdd:cd16224   27 AKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWIQQSFRHYALEDAKQQFPEYDKDGDGAVTWDEYnmqmydrVIDYD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 112 PDEELHNKEEES---LIAQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGE 188
Cdd:cd16224  107 EDTVLDDEEEESfrqLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMTEFVIQEALEEHDKDGDGFISLEEFLGD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 189 LDEQRGS----EWYKVEVERFRTVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHAL 264
Cdd:cd16224  187 YRKDPTAnedpEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEALHLIDEMDLNGDGRLSEEEILENQDL 266


                 .
gi 453225954 265 F 265
Cdd:cd16224  267 F 267
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 40-265 2.86e-37

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: 132.76  E-value: 2.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  40 KLNLKSGQESVEKFAKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEY--------LADSF 111
Cdd:cd16228   27 QLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKGHDLNEDGLVSWEEYknatygyiLDDPD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 112 PDEELHNKEeesLIAQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGELDE 191
Cdd:cd16228  107 PDDGFNYKQ---MMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIVVLETMEDIDKNGDGFIDLEEYIGDMYS 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 453225954 192 QRGS----EWYKVEVERFRTVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHALF 265
Cdd:cd16228  184 QDGDadepEWVKTEREQFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLF 261
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 40-265 8.48e-30

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: 113.44  E-value: 8.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  40 KLNLKSGQESVEKFAKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLADSF------PD 113
Cdd:cd16229   27 QLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKVWKDYDLNKDNKISWEEYKQATYgyylgnPE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 114 EELHNKEEES---LIAQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFLGEL- 189
Cdd:cd16229  107 EFQDATDQFSfkkMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMKDIVVLETLEDIDKNGDGFVDEDEYIADMf 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 453225954 190 -DEQRGSE--WYKVEVERFRTVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHALF 265
Cdd:cd16229  187 sHEEGGPEpdWVKTEREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQAEARHLVYESDKDKDQKLTKEEILDNWNMF 265
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 50-266 1.95e-29

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: 112.78  E-value: 1.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  50 VEKFAKAlDTNNDGFVDKSEILAWVSESYQKTVDrEAVER----ISELDENADGFVSWEEY-----LADSFPDEELHNK- 119
Cdd:cd16225   37 KEIFKKV-DVNTDGFLSAEELEDWIMEKTQEHFQ-EAVEEneqiFKAVDTDKDGNVSWEEYrvhflLSKGYSEEEAEEKi 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 120 ----------EEESLIAQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFL--- 186
Cdd:cd16225  115 knneelkldeDDKEVLDRYKDRWSQADEPEDGLLDVEEFLSFRHPEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVslp 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 187 ----GELDEQRGSEWYKVEVERFRTVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHH 262
Cdd:cd16225  195 pgtvEEQQAEDDDEWKKERKKEFEEVIDLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDGKLSLEEILKNS 274


                 ....
gi 453225954 263 ALFA 266
Cdd:cd16225  275 DLFT 278
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
47-186 1.27e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 58.26  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  47 QESVEKFAKALDTNNDGFVDKSEILAwvsesyqkTVDREAVERISELDENADGFVSWEEYLAdsfpdeELHNKEEESLIA 126
Cdd:COG5126    4 RRKLDRRFDLLDADGDGVLERDDFEA--------LFRRLWATLFSEADTDGDGRISREEFVA------GMESLFEATVEP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 127 QDKMYFKQADEDNDGKLNLEELASFLNPehhPHMHPVLIAVTLLEKDQNGDGAIEEKEFL 186
Cdd:COG5126   70 FARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADELFARLDTDGDGKISFEEFV 126
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
24-158 1.00e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.57  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  24 DGSVSPSDHKKPASEQklnlksgqesVEKFAKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSW 103
Cdd:COG5126   19 DGVLERDDFEALFRRL----------WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISA 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 453225954 104 EEYL----ADSFPDEELhnkeeesliaqdKMYFKQADEDNDGKLNLEELASFLNPEHHP 158
Cdd:COG5126   89 DEFRrlltALGVSEEEA------------DELFARLDTDGDGKISFEEFVAAVRDYYTP 135
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
130-261 6.13e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 6.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 130 MYFKQADEDNDGKLNLEELASflnpehhphMHPVLIAVTLLEKDQNGDGAIEEKEFLGELDEQRGSEWYKVEVERFRtVY 209
Cdd:COG5126    9 RRFDLLDADGDGVLERDDFEA---------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFD-LL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 453225954 210 DKNKDGKLAGDELTDWLLVDGTTAGsyEAESLLTNSDDDKDGQLSYEEIVKH 261
Cdd:COG5126   79 DTDGDGKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAA 128
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
83-226 2.82e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.63  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  83 DREAVERISELDENADGFVSWEEYLADsfpdeelhnkeeesLIAQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHP 162
Cdd:COG5126    4 RRKLDRRFDLLDADGDGVLERDDFEAL--------------FRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 453225954 163 VLIAvtLLEK-DQNGDGAIEEKEFLGELDEQRGSEWykvEVERFRTVYDKNKDGKLAGDELTDWL 226
Cdd:COG5126   70 FARA--AFDLlDTDGDGKISADEFRRLLTALGVSEE---EADELFARLDTDGDGKISFEEFVAAV 129
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
46-257 1.61e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 48.14  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  46 GQESVEKFAKALDTNNDGFVDKSEILAWVSEsyqktvdreaveriseldenadgfvsweeyladsfpdeelhNKEEESLI 125
Cdd:NF041410  25 SQQFQKQLFAKLDSDGDGSVSQDELSSALSS-----------------------------------------KSDDGSLI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 126 AQDKMyFKQADEDNDGKLNLEELASFLNPEHHPHMHPvliavtllekdQNGDGAieeKEFLGELDEqrgsewykveverf 205
Cdd:NF041410  64 DLSEL-FSDLDSDGDGSLSSDELAAAAPPPPPPPDQA-----------PSTELA---DDLLSALDT-------------- 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 453225954 206 rtvydkNKDGKLAGDELTDWLLVDGTTAGSyeaESLLTNSDDDKDGQLSYEE 257
Cdd:NF041410 115 ------DGDGSISSDELSAGLTSAGSSADS---SQLFSALDSDGDGSVSSDE 157
PTZ00184 PTZ00184
calmodulin; Provisional
 122-260 6.99e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 45.14  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 122 ESLIAQDKMYFKQADEDNDGKLNLEELASFL-----NPEHHPhmhpvlIAVTLLEKDQNGDGAIEEKEFLG----ELDEQ 192
Cdd:PTZ00184   7 EEQIAEFKEAFSLFDKDGDGTITTKELGTVMrslgqNPTEAE------LQDMINEVDADGNGTIDFPEFLTlmarKMKDT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 453225954 193 RGSEWYKvevERFRtVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVK 260
Cdd:PTZ00184  81 DSEEEIK---EAFK-VFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVK 144
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
88-223 7.41e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 46.21  E-value: 7.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  88 ERISELDENADGFVSWEEY---LADsfpdeelhNKEEESLIAQDKMyFKQADEDNDGKLNLEELASFLNPEHHPHMHP-- 162
Cdd:NF041410  31 QLFAKLDSDGDGSVSQDELssaLSS--------KSDDGSLIDLSEL-FSDLDSDGDGSLSSDELAAAAPPPPPPPDQAps 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 453225954 163 VLIAVTLLEK-DQNGDGAIEEKEFLGELDEQRGSEwykvEVERFRTVYDKNKDGKLAGDELT 223
Cdd:NF041410 102 TELADDLLSAlDTDGDGSISSDELSAGLTSAGSSA----DSSQLFSALDSDGDGSVSSDELA 159
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 47-227 7.81e-06

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: 46.25  E-value: 7.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  47 QESVEKFAKALDTNNDGFVDKSE------------ILAWVSESYQKTVDREAVERisELDENADGFVSWEE---YLADSF 111
Cdd:cd16179   48 EELKEEFMEAYDENQDGRIDIRElaqllpteenflLLFRRDNPLDSSVEFMKVWR--EYDKDNSGYIEADElknFLKHLL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 112 PDEELHN-KEEESLIAQDKMYFKQADEDNDGKLNLEELASFLNPEHHPHMHPVLIAVTLLEK----------DQNGDGAI 180
Cdd:cd16179  126 KEAKRDNdVSEDKLIEYTDTILQLFDRNKDGKLQLSEMARLLPVKENFLCRPIFKGAGKLTRedidrvfalyDRDNNGTI 205

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 453225954 181 EEKE---FLGELDEQRGSEWYKVEVERFRTV----YDKNKDGKLAGDELTDWLL 227
Cdd:cd16179  206 ENEEltgFLKDLLELVQEDYDEQDLEEFKEIilrgWDFNNDGKISRKELTMLLL 259
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 91-259 3.08e-05

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: 44.27  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  91 SELDENADGFVSWEEyLADSFPDEE---LHNKEEESLIAQDKMY--FKQADEDNDGKLNLEELASFLNP---EHHPHMHP 162
Cdd:cd15902   51 EKYDENEDGKIEIRE-LANILPTEEnflLLFRREQPLISSVEFMkiWRKYDTDGSGFIEAKELKGFLKDlllKNKKHVSP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 163 VLIAV---TLLEK-DQNGDGAIEEKE----------FLGELDEQRGSEWYKVEVERFRTVYDKNKDGKLAGDELTDWL-- 226
Cdd:cd15902  130 PKLDEytkLILKEfDANKDGKLELDEmakllpvqenFLLKFQILGAMDLTKEDFEKVFEHYDKDNNGVIEGNELDALLkd 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 453225954 227 -------LVDGTTAGSYEaESLLTNSDDDKDGQLSYEEIV 259
Cdd:cd15902  210 lleknkaDIDKPDLENFR-DAILRACDKNKDGKIQKTELA 248
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
24-158 5.14e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.52  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  24 DGSVSpSDHKKPASEQKLNlKSGQESVEKFAKALDTNNDGFVDKSEILAW------VSESYQKTVDREAVerISELDENA 97
Cdd:NF041410  41 DGSVS-QDELSSALSSKSD-DGSLIDLSELFSDLDSDGDGSLSSDELAAAapppppPPDQAPSTELADDL--LSALDTDG 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453225954  98 DGFVSWEEYLAdsfpdeELHNKEEESLIAQDkmyFKQADEDNDGKLNLEELASFLNPEHHP 158
Cdd:NF041410 117 DGSISSDELSA------GLTSAGSSADSSQL---FSALDSDGDGSVSSDELAAALQPPPPP 168
EF-hand_7 pfam13499
EF-hand domain pair;
55-108 1.21e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 1.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 453225954   55 KALDTNNDGFVDKSEILAWV-SESYQKTVDREAVERI-SELDENADGFVSWEEYLA 108
Cdd:pfam13499   9 KLLDSDGDGYLDVEELKKLLrKLEEGEPLSDEEVEELfKEFDLDKDGRISFEEFLE 64
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 47-228 1.66e-04

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: 42.34  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  47 QESVEKFAKALDTNNDGFVDKSE---ILAwVSESYQKTVDREAVERIS--------ELDENADGFVSWEEyLADSFPDEE 115
Cdd:cd15902   43 AEKKKEFMEKYDENEDGKIEIRElanILP-TEENFLLLFRREQPLISSvefmkiwrKYDTDGSGFIEAKE-LKGFLKDLL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 116 LHNK---EEESLIAQDKMYFKQADEDNDGKLNLEELASFL-NPEHHPHMHPVLIAVTLLEK---------DQNGDGAIEE 182
Cdd:cd15902  121 LKNKkhvSPPKLDEYTKLILKEFDANKDGKLELDEMAKLLpVQENFLLKFQILGAMDLTKEdfekvfehyDKDNNGVIEG 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 453225954 183 KE---FLGELDEQRGSEWYKVEVERFRTV----YDKNKDGKLAGDELTDWLLV 228
Cdd:cd15902  201 NEldaLLKDLLEKNKADIDKPDLENFRDAilraCDKNKDGKIQKTELALFLSA 253
EF-hand_7 pfam13499
EF-hand domain pair;
129-186 2.25e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 2.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 453225954  129 KMYFKQADEDNDGKLNLEELASFL-NPEHHPHMHPVLIAVTLLEKDQNGDGAIEEKEFL 186
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLrKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 55-108 2.63e-04

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: 38.30  E-value: 2.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 453225954  55 KALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLA 108
Cdd:cd00051    7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
PLN02964 PLN02964
phosphatidylserine decarboxylase
 48-152 3.11e-04

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  48 ESVEKFAKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEY--LADSFPDEELHNKEEEsli 125
Cdd:PLN02964 143 ESACESFDLLDPSSSNKVVGSIFVSCSIEDPVETERSFARRILAIVDYDEDGQLSFSEFsdLIKAFGNLVAANKKEE--- 219

                         90       100
                 ....*....|....*....|....*..
gi 453225954 126 aqdkmYFKQADEDNDGKLNLEELASFL 152
Cdd:PLN02964 220 -----LFKAADLNGDGVVTIDELAALL 241
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 203-263 6.19e-04

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: 37.14  E-value: 6.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 453225954 203 ERFRtVYDKNKDGKLAGDELTDWLLVDGTTAGSYEAESLLTNSDDDKDGQLSYEEIVKHHA 263
Cdd:cd00051    4 EAFR-LFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
203-260 2.06e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 2.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954  203 ERFRTvYDKNKDGKLAGDELTDWLLVDGTTAG--SYEAESLLTNSDDDKDGQLSYEEIVK 260
Cdd:pfam13499   6 EAFKL-LDSDGDGYLDVEELKKLLRKLEEGEPlsDEEVEELFKEFDLDKDGRISFEEFLE 64
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 50-108 2.09e-03

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: 38.84  E-value: 2.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 453225954  50 VEKFAKALDTNNDGFVDKSEILAWVSESYQKTVDREAVERISELDENADGFVSWEEYLA 108
Cdd:cd16227  198 KDRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFDEILD 256
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
 136-222 9.34e-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: 37.00  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 453225954 136 DEDNDGKLNLEELASFLNPEHHPHM------HPVLIAVTLLE----KDQNGDGAI---EEKEFLGELDEQRGSEWYKVEV 202
Cdd:cd16178   55 DVTGDGRIQIQELANIILPDDENFLlffrreEPLDSSVEFMRiwrkYDADSSGYIsaaELKNFLRDLFLQHKKVITEDKL 134

                         90       100
                 ....*....|....*....|....
gi 453225954 203 ERFR----TVYDKNKDGKLAGDEL 222
Cdd:cd16178  135 DEYTdtmmKIFDKNKDGRLDLNDM 158
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 85-152 9.58e-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: 9.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 453225954  85 EAVERISELDENADGFVSWEEY------LADSFPDEELhnkeeesliaqDKMyFKQADEDNDGKLNLEELASFL 152
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELkaalksLGEGLSEEEI-----------DEM-IREVDKDGDGKIDFEEFLELM 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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