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Conserved domains on  [gi|1958774494|ref|XP_038965122|]
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45 kDa calcium-binding protein isoform X2 [Rattus norvegicus]

Protein Classification

CREC-EF hand family protein; EF-hand domain-containing protein( domain architecture ID 11610931)

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_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
87-383 5.04e-148

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: 420.55  E-value: 5.04e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  87 LEMDGHLNKDFHQEVFLGKDMDGFDEDSEPRRsRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKENKLHF 166
Cdd:cd16225     1 LERDGHLNKEFHKEVFLGNEKEEFEEDSEPKK-RKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEENEQIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 167 RAVDPDGDGHVSWDEYKVKFLASKGHNEREIADAIKNHEELKVDEEswpqtqrliclsagsqAQEVLGNLRDRWYQADnP 246
Cdd:cd16225    80 KAVDTDKDGNVSWEEYRVHFLLSKGYSEEEAEEKIKNNEELKLDED----------------DKEVLDRYKDRWSQAD-E 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 247 PADLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISLPVGTVENQQGQDiDDNWVKDRKKEFEELI 326
Cdd:cd16225   143 PEDGLLDVEEFLSFRHPEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAED-DDEWKKERKKEFEEVI 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774494 327 DSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFT 383
Cdd:cd16225   222 DLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDGKLSLEEILKNSDLFT 278
 
Name Accession Description Interval E-value
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
87-383 5.04e-148

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: 420.55  E-value: 5.04e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  87 LEMDGHLNKDFHQEVFLGKDMDGFDEDSEPRRsRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKENKLHF 166
Cdd:cd16225     1 LERDGHLNKEFHKEVFLGNEKEEFEEDSEPKK-RKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEENEQIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 167 RAVDPDGDGHVSWDEYKVKFLASKGHNEREIADAIKNHEELKVDEEswpqtqrliclsagsqAQEVLGNLRDRWYQADnP 246
Cdd:cd16225    80 KAVDTDKDGNVSWEEYRVHFLLSKGYSEEEAEEKIKNNEELKLDED----------------DKEVLDRYKDRWSQAD-E 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 247 PADLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISLPVGTVENQQGQDiDDNWVKDRKKEFEELI 326
Cdd:cd16225   143 PEDGLLDVEEFLSFRHPEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAED-DDEWKKERKKEFEEVI 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774494 327 DSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFT 383
Cdd:cd16225   222 DLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDGKLSLEEILKNSDLFT 278
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
252-377 8.10e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 252 LTEDEFLSFLHpehsrgmlkFMVKEIVRDLDQDGDKQLSLPEFISLPVGTVENQQGQDIDdnwvkdrkKEFEeLIDSNHD 331
Cdd:COG5126    22 LERDDFEALFR---------RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFAR--------AAFD-LLDTDGD 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958774494 332 GIVTMEELENYMDPMNEYNAlnEAKQMIAIADENQNHHLEPEEILK 377
Cdd:COG5126    84 GKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVA 127
EF-hand_7 pfam13499
EF-hand domain pair;
120-183 6.13e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.40  E-value: 6.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774494 120 RRKLMVIFSKVDVNTDRRISAKEMQHwIMEKTAEHFQEAVKENKLHFRAVDPDGDGHVSWDEYK 183
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK-LLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
PTZ00184 PTZ00184
calmodulin; Provisional
266-377 4.76e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.43  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 266 SRGMLKFMVKEIvrdlDQDGDKQLSLPEFISLpvgtvenqQGQDIDDNWVKDRKKEFEELIDSNHDGIVTMEELENYMDP 345
Cdd:PTZ00184   45 TEAELQDMINEV----DADGNGTIDFPEFLTL--------MARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTN 112
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958774494 346 MNEYNALNEAKQMIAIADENQNHHLEPEEILK 377
Cdd:PTZ00184  113 LGEKLTDEEVDEMIREADVDGDGQINYEEFVK 144
 
Name Accession Description Interval E-value
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
87-383 5.04e-148

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: 420.55  E-value: 5.04e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  87 LEMDGHLNKDFHQEVFLGKDMDGFDEDSEPRRsRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKENKLHF 166
Cdd:cd16225     1 LERDGHLNKEFHKEVFLGNEKEEFEEDSEPKK-RKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEENEQIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 167 RAVDPDGDGHVSWDEYKVKFLASKGHNEREIADAIKNHEELKVDEEswpqtqrliclsagsqAQEVLGNLRDRWYQADnP 246
Cdd:cd16225    80 KAVDTDKDGNVSWEEYRVHFLLSKGYSEEEAEEKIKNNEELKLDED----------------DKEVLDRYKDRWSQAD-E 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 247 PADLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISLPVGTVENQQGQDiDDNWVKDRKKEFEELI 326
Cdd:cd16225   143 PEDGLLDVEEFLSFRHPEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAED-DDEWKKERKKEFEEVI 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774494 327 DSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFT 383
Cdd:cd16225   222 DLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDGKLSLEEILKNSDLFT 278
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
87-383 2.84e-111

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: 326.71  E-value: 2.84e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  87 LEMDGHLNKDFHQEVFLGKDMDGFDEDSEPRRSRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKEnklHF 166
Cdd:cd15899     1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKE---QF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 167 RAVDPDGDGHVSWDEYKVKFLASKGHNEREIADAIKNHEELKvdeeswpqtqrliclsagsqaqEVLGNLRDRWYQADnP 246
Cdd:cd15899    78 RAVDPDEDGHVSWDEYKNDTYGSVGDDEENVADNIKEDEEYK----------------------KLLLKDKKRFEAAD-Q 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 247 PADLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISLPVGTVENQQGQdiddNWVKDRKKEFEELI 326
Cdd:cd15899   135 DGDLILTLEEFLAFLHPEESPYMLDFVIKETLEDLDKNGDGFISLEEFISDPYSADENEEEP----EWVKVEKERFVELR 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774494 327 DSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFT 383
Cdd:cd15899   211 DKDKDGKLDGEELLSWVDPSNQEIALEEAKHLIAESDENKDGKLSPEEILDNHELFV 267
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
90-384 1.26e-42

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: 150.04  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  90 DGHLNKDFHQEVFLGKDMDG-FDEDSePRRSRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKEnklHFRA 168
Cdd:cd16226     4 DGEHNPEYDHEAFLGKEEAKeFDQLT-PEESKERLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDR---QWKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 169 VDPDGDGHVSWDEYKVKFLASKGHNEREIADAIKNHEELKVDEEswpqtqrliclsagsqaqevlgnlrdRWYQADNPpA 248
Cdd:cd16226    80 YDPNKDGKLSWEEYKKATYGFLDDEEEDDDLHESYKKMIRRDER--------------------------RWKAADQD-G 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 249 DLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFIslpvGTVENQQGQDIDDNWVKDRKKEFEELIDS 328
Cdd:cd16226   133 DGKLTKEEFTAFLHPEEFPHMRDIVVQETLEDIDKNKDGFISLEEYI----GDMYRDDDEEEDPDWVKSEREQFKEFRDK 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774494 329 NHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFTG 384
Cdd:cd16226   209 NKDGKMDREEVKDWILPEDYDHAEAEAKHLIYEADDDKDGKLTKEEILDKYDLFVG 264
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
89-382 1.47e-28

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: 112.53  E-value: 1.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  89 MDGHLNKDFHQEVFLG--KDMDGFDEDSePRRSRRKLMVIFSKVDVNTDRRISAKEMQHWImEKTAEHFqeAVKENKLHF 166
Cdd:cd16224     3 PNGEHNAEYDKEAFLGgeEDADEFAKLS-PEEQQKRLKSIIKKIDTDSDGFLTEEELSSWI-QQSFRHY--ALEDAKQQF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 167 RAVDPDGDGHVSWDEYKVkflaskghnerEIADAIKNHEELKVDEESWPQTQRLIclsagsqaqevlgNLRD-RWYQADN 245
Cdd:cd16224    79 PEYDKDGDGAVTWDEYNM-----------QMYDRVIDYDEDTVLDDEEEESFRQL-------------HLKDkKRFDKAN 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 246 PPADLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFIslpvGTVENQQGQDIDDNWVKDRKKEFEEL 325
Cdd:cd16224   135 TDGGPGLNLTEFIAFEHPEEVDYMTEFVIQEALEEHDKDGDGFISLEEFL----GDYRKDPTANEDPEWIIVEKDRFVND 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774494 326 IDSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFF 382
Cdd:cd16224   211 YDKDNDGKLDPQELLPWVVPNNYGIAQEEALHLIDEMDLNGDGRLSEEEILENQDLF 267
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
90-384 2.88e-28

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: 111.64  E-value: 2.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  90 DGHLNKDFHQEVFLG--KDMDGFDEDSePRRSRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKENklhFR 167
Cdd:cd16227     4 DGEHNPEFDHEAVLGsrKEAEEFDELP-PEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSFKMLDEEEANER---FE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 168 AVDPDGDGHVSWDEYKVKflaSKGHNEREIADAIKNH--EELKVDEESwpqtqrliclsagsqaqevlgnlRDRWYQADN 245
Cdd:cd16227    80 EADEDGDGKVTWEEYLAD---SFGYDDEDNEEMIKDSteDDLKLLEDD-----------------------KEMFEAADL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 246 pPADLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISlpvgtvenQQGQDIDDNWVKDRKKEFEEL 325
Cdd:cd16227   134 -NKDGKLDKTEFSAFQHPEEYPHMHPVLIEQTLRDKDKDNDGFISFQEFLG--------DRAGHEDKEWLLVEKDRFDED 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774494 326 IDSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFTG 384
Cdd:cd16227   205 YDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFDEILDHHEIFVG 263
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
90-384 9.68e-28

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: 110.42  E-value: 9.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  90 DGHLNKDFHQEVFLG-KDMDGFDEDSePRRSRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKEnklHFRA 168
Cdd:cd16228     4 DDAQNFDYDHDAFLGaEEAKTFDQLT-PEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVER---QWKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 169 VDPDGDGHVSWDEYKVkflASKGH--NEREIADAIkNHEELKVDEEswpqtqrliclsagsqaqevlgnlrdRWYQADNP 246
Cdd:cd16228    80 HDLNEDGLVSWEEYKN---ATYGYilDDPDPDDGF-NYKQMMVRDE--------------------------RRFKMADK 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 247 PADLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFIslpvGTVENQQGQDIDDNWVKDRKKEFEELI 326
Cdd:cd16228   130 DGDLRATKEEFTAFLHPEEYDYMKDIVVLETMEDIDKNGDGFIDLEEYI----GDMYSQDGDADEPEWVKTEREQFTEFR 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774494 327 DSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFTG 384
Cdd:cd16228   206 DKNKDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLFVG 263
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
94-384 2.97e-23

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: 98.03  E-value: 2.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  94 NKDFHQ--EVFLGKDMDGFDEDSEPRRSRRKLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKENklhFRAVDP 171
Cdd:cd16229     6 NQSFQYdhEAFLGKEEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKV---WKDYDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 172 DGDGHVSWDEYKVkflASKGH---NEREIADAIKNHEELKVdeesWPQTQRliclsagsqaqevlgnlrdRWYQADNPpA 248
Cdd:cd16229    83 NKDNKISWEEYKQ---ATYGYylgNPEEFQDATDQFSFKKM----LPRDER-------------------RFKAADLD-G 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 249 DLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISLPVGTVENQQGQDiddnWVKDRKKEFEELIDS 328
Cdd:cd16229   136 DLAATREEFTAFLHPEEFEHMKDIVVLETLEDIDKNGDGFVDEDEYIADMFSHEEGGPEPD----WVKTEREQFSDFRDL 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774494 329 NHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFTG 384
Cdd:cd16229   212 NKDGKMDKEEIRHWILPQDYDHAQAEARHLVYESDKDKDQKLTKEEILDNWNMFVG 267
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
90-384 2.76e-21

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: 92.34  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494  90 DGHLNKDFHQEVFLGKDM-DGFDEDSePRRSRRKLMVIFSKVDV--NTDRRISAKEMQHWIMEKTAEHFQEAVKENklhF 166
Cdd:cd16230     4 DAHGNFQYDHEAFLGREVaKEFDQLS-PEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAA---W 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 167 RAVDPDGDGHVSWDEYKVkflASKGHNEreiaDAIKNHeelkvdEESWPQTQRliclsagsqaqEVLGnlRD-RWYQADN 245
Cdd:cd16230    80 QTYDTDRDGRVGWEELRN---ATYGHYE----PGEEFH------DVEDAETYK-----------KMLA--RDeRRFRVAD 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 246 PPADLLLTEDEFLSFLHPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFIS-LPVGTVENQQGQdiddnWVKDRKKEFEE 324
Cdd:cd16230   134 QDGDSMATREELTAFLHPEEFPHMRDIVVAETLEDLDKNKDGYVQVEEYIAdLYSGEPGEEEPA-----WVQTERQQFRQ 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 325 LIDSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILKYSEFFTG 384
Cdd:cd16230   209 FRDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 268
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
252-377 8.10e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 252 LTEDEFLSFLHpehsrgmlkFMVKEIVRDLDQDGDKQLSLPEFISLPVGTVENQQGQDIDdnwvkdrkKEFEeLIDSNHD 331
Cdd:COG5126    22 LERDDFEALFR---------RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFAR--------AAFD-LLDTDGD 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958774494 332 GIVTMEELENYMDPMNEYNAlnEAKQMIAIADENQNHHLEPEEILK 377
Cdd:COG5126    84 GKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVA 127
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
110-181 1.93e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 1.93e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774494 110 FDEDSEPRRSRRKLMVIFSKVDVNTDRRISAKEMQHWI--MEKTAEHFQEAvkenklhFRAVDPDGDGHVSWDE 181
Cdd:COG5126    58 GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLtaLGVSEEEADEL-------FARLDTDGDGKISFEE 124
EF-hand_7 pfam13499
EF-hand domain pair;
120-183 6.13e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.40  E-value: 6.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774494 120 RRKLMVIFSKVDVNTDRRISAKEMQHwIMEKTAEHFQEAVKENKLHFRAVDPDGDGHVSWDEYK 183
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK-LLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
281-378 1.79e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.01  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 281 LDQDGDKQLSLPEFISLPVGTVENQQGQdiddnwvkdrkkefeelIDSNHDGIVTMEELENYMDPMNEYNALNEAKQMIA 360
Cdd:COG5126    14 LDADGDGVLERDDFEALFRRLWATLFSE-----------------ADTDGDGRISREEFVAGMESLFEATVEPFARAAFD 76
                          90
                  ....*....|....*...
gi 1958774494 361 IADENQNHHLEPEEILKY 378
Cdd:COG5126    77 LLDTDGDGKISADEFRRL 94
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
122-181 7.02e-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: 7.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 122 KLMVIFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKEnklHFRAVDPDGDGHVSWDE 181
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDE---MIREVDKDGDGKIDFEE 57
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
126-202 9.07e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 9.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774494 126 IFSKVDVNTDRRISAKEMQHWIMEKTAEHFQEAVKEnklHFRAVDPDGDGHVSWDEYKvKFLASKGHNEREIADAIK 202
Cdd:COG5126    38 LFSEADTDGDGRISREEFVAGMESLFEATVEPFARA---AFDLLDTDGDGKISADEFR-RLLTALGVSEEEADELFA 110
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
238-346 1.99e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 238 DRWYQADNPPADLLLTEDEFLSFLHPEHSRGMLKFmVKEIVRDLDQDGDKQLSLPEFISLpvgtvenQQGQDIDDnwvkD 317
Cdd:COG5126    36 ATLFSEADTDGDGRISREEFVAGMESLFEATVEPF-ARAAFDLLDTDGDGKISADEFRRL-------LTALGVSE----E 103
                          90       100
                  ....*....|....*....|....*....
gi 1958774494 318 RKKEFEELIDSNHDGIVTMEELENYMDPM 346
Cdd:COG5126   104 EADELFARLDTDGDGKISFEEFVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
324-377 3.10e-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: 38.68  E-value: 3.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958774494 324 ELIDSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNHHLEPEEILK 377
Cdd:cd00051     7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
166-297 1.73e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 166 FRAVDPDGDGHVSWDEYKVKFLASKGHNeREIADAIKNHeelKVDEESWpqtqrliCLSAGSQAQEVLGNLRDRWYQADN 245
Cdd:COG5126    11 FDLLDADGDGVLERDDFEALFRRLWATL-FSEADTDGDG---RISREEF-------VAGMESLFEATVEPFARAAFDLLD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958774494 246 PPADLLLTEDEFLSFLHpehSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISL 297
Cdd:COG5126    80 TDGDGKISADEFRRLLT---ALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
PTZ00184 PTZ00184
calmodulin; Provisional
266-377 4.76e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.43  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 266 SRGMLKFMVKEIvrdlDQDGDKQLSLPEFISLpvgtvenqQGQDIDDNWVKDRKKEFEELIDSNHDGIVTMEELENYMDP 345
Cdd:PTZ00184   45 TEAELQDMINEV----DADGNGTIDFPEFLTL--------MARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTN 112
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958774494 346 MNEYNALNEAKQMIAIADENQNHHLEPEEILK 377
Cdd:PTZ00184  113 LGEKLTDEEVDEMIREADVDGDGQINYEEFVK 144
EF-hand_7 pfam13499
EF-hand domain pair;
249-297 5.56e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.31  E-value: 5.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958774494 249 DLLLTEDEFLSFLHP-EHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISL 297
Cdd:pfam13499  16 DGYLDVEELKKLLRKlEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
276-345 6.96e-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: 37.72  E-value: 6.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 276 EIVRDLDQDGDKQLSLPEFISLPVGTVENQQGQDIDDNWVKDRKKEFEELIDSNHDGIVTMEELENYMDP 345
Cdd:cd15902     3 EVWMHFDADGNGYIEGKELDSFLRELLKALNGKDKTDDEVAEKKKEFMEKYDENEDGKIEIRELANILPT 72
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
252-297 8.72e-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: 34.45  E-value: 8.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958774494 252 LTEDEFLSFLhPEHSRGMLKFMVKEIVRDLDQDGDKQLSLPEFISL 297
Cdd:cd00051    17 ISADELKAAL-KSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
314-395 9.56e-03

EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 36.16  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774494 314 WVKdrkKEFEElIDSNHDGIVTMEELENYMDPMNEYNALNEAKQMIAIADENQNhhlepEEILKYSEFFTGSKLMDYARN 393
Cdd:cd16220     1 WVK---QTFEE-ADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTDEN-----QGTLTFEEFCVFYKMMSLRRD 71

                  ..
gi 1958774494 394 VH 395
Cdd:cd16220    72 LY 73
 
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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