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Conserved domains on  [gi|58652122|ref|NP_001011661|]
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guanylate cyclase activator 1d [Danio rerio]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000101)

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
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
53-159 5.84e-17

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 5.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  53 YVDQVFCTFDMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFKLFDQDGNGKIDKDELETIFTAIQditrnrdiVPEEIV 132
Cdd:COG5126  34 LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG--------VSEEEA 105

                        90       100
                ....*....|....*....|....*..
gi 58652122 133 ALIFEKIDVNGEGELTLEEFIEGAKEH 159
Cdd:COG5126 106 DELFARLDTDGDGKISFEEFVAAVRDY 132
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 28-76 6.58e-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.


The actual alignment was detected with superfamily member pfam13833:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 6.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 58652122    28 PSGLITLFELKSILGLQGMNEDANSYVDQVFCTFDMDRDGYIDFVEYIA 76
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCV 49
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
53-159 5.84e-17

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 5.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  53 YVDQVFCTFDMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFKLFDQDGNGKIDKDELETIFTAIQditrnrdiVPEEIV 132
Cdd:COG5126  34 LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG--------VSEEEA 105

                        90       100
                ....*....|....*....|....*..
gi 58652122 133 ALIFEKIDVNGEGELTLEEFIEGAKEH 159
Cdd:COG5126 106 DELFARLDTDGDGKISFEEFVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 89-157 4.06e-12

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: 58.71  E-value: 4.06e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58652122  89 KLKWYFKLFDQDGNGKIDKDELETIFTAIqditrnRDIVPEEIVALIFEKIDVNGEGELTLEEFIEGAK 157
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL------GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
88-157 3.80e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.41  E-value: 3.80e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122    88 QKLKWYFKLFDQDGNGKIDKDELETIFTAIQditRNRDIVPEEIvALIFEKIDVNGEGELTLEEFIEGAK 157
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLE---EGEPLSDEEV-EELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 30-153 1.66e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 51.30  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122   30 GLITLFELKSILGLQGMNEDANSYVDQVfCTFDMDRDGYIDFVEYIAAISLMLK-GEINQKLKWYFKLFDQDGNGKIDKD 108
Cdd:PTZ00184  26 GTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGTIDFPEFLTLMARKMKdTDSEEEIKEAFKVFDRDGNGFISAA 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 58652122  109 ELETIFTAIQDITRNrdivpEEIVALIFEkIDVNGEGELTLEEFI 153
Cdd:PTZ00184 105 ELRHVMTNLGEKLTD-----EEVDEMIRE-ADVDGDGQINYEEFV 143
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
94-160 3.83e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 39.66  E-value: 3.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58652122   94 FKLFDQDGNGKIDKDELETIFTAIQDitrnrDIVPEEIVALiFEKIDVNGEGELTLEEFIEGAKEHP 160
Cdd:NF041410  33 FAKLDSDGDGSVSQDELSSALSSKSD-----DGSLIDLSEL-FSDLDSDGDGSLSSDELAAAAPPPP 93
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
29-152 5.80e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 39.28  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122   29 SGLITLFELKSILGlQGMNEDANSYVDQVFCTFDMDRDGYIDFVEYIAAISL----MLKGEINQKLKWYFKLFDQDGNGK 104
Cdd:NF041410  41 DGSVSQDELSSALS-SKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPppppPDQAPSTELADDLLSALDTDGDGS 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 58652122  105 IDKDELETIFTAIQDITRNRDivpeeivalIFEKIDVNGEGELTLEEF 152
Cdd:NF041410 120 ISSDELSAGLTSAGSSADSSQ---------LFSALDSDGDGSVSSDEL 158
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 89-117 6.48e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.82  E-value: 6.48e-04
                           10        20
                   ....*....|....*....|....*....
gi 58652122     89 KLKWYFKLFDQDGNGKIDKDELETIFTAI 117
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_8 pfam13833
EF-hand domain pair;
28-76 6.58e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 6.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 58652122    28 PSGLITLFELKSILGLQGMNEDANSYVDQVFCTFDMDRDGYIDFVEYIA 76
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCV 49
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
53-159 5.84e-17

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 5.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  53 YVDQVFCTFDMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFKLFDQDGNGKIDKDELETIFTAIQditrnrdiVPEEIV 132
Cdd:COG5126  34 LWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG--------VSEEEA 105

                        90       100
                ....*....|....*....|....*..
gi 58652122 133 ALIFEKIDVNGEGELTLEEFIEGAKEH 159
Cdd:COG5126 106 DELFARLDTDGDGKISFEEFVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 89-157 4.06e-12

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: 58.71  E-value: 4.06e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58652122  89 KLKWYFKLFDQDGNGKIDKDELETIFTAIqditrnRDIVPEEIVALIFEKIDVNGEGELTLEEFIEGAK 157
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSL------GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
88-157 3.80e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.41  E-value: 3.80e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122    88 QKLKWYFKLFDQDGNGKIDKDELETIFTAIQditRNRDIVPEEIvALIFEKIDVNGEGELTLEEFIEGAK 157
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLE---EGEPLSDEEV-EELFKEFDLDKDGRISFEEFLELYS 67
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 29-154 4.83e-09

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 52.99  E-value: 4.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  29 SGLITLFELKSILGLQGMNEDAnSYVDQVFCTFDMDRDGYIDFVEYIAA---ISLMLKGeinqklkwyFKLFDQDGNGKI 105
Cdd:cd16185  14 SGSIDVNELQKALAGGGLLFSL-ATAEKLIRMFDRDGNGTIDFEEFAALhqfLSNMQNG---------FEQRDTSRSGRL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 58652122 106 DKDEletIFTAIQDITRNrdiVPEEIVALIFEKIDVNGEGELTLEEFIE 154
Cdd:cd16185  84 DANE---VHEALAASGFQ---LDPPAFQALFRKFDPDRGGSLGFDDYIE 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 53-110 1.62e-08

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: 49.08  E-value: 1.62e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 58652122  53 YVDQVFCTFDMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFKLFDQDGNGKIDKDEL 110
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEF 58
PTZ00184 PTZ00184
calmodulin; Provisional
 30-153 1.66e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 51.30  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122   30 GLITLFELKSILGLQGMNEDANSYVDQVfCTFDMDRDGYIDFVEYIAAISLMLK-GEINQKLKWYFKLFDQDGNGKIDKD 108
Cdd:PTZ00184  26 GTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGTIDFPEFLTLMARKMKdTDSEEEIKEAFKVFDRDGNGFISAA 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 58652122  109 ELETIFTAIQDITRNrdivpEEIVALIFEkIDVNGEGELTLEEFI 153
Cdd:PTZ00184 105 ELRHVMTNLGEKLTD-----EEVDEMIRE-ADVDGDGQINYEEFV 143
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
88-152 4.20e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 4.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  88 QKLKWYFKLFDQDGNGKIDKDELETIFTAIQD----------------------ITRNRDIVPEEIVALIFEKIDVNGEG 145
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEALFRRLWAtlfseadtdgdgrisreefvagMESLFEATVEPFARAAFDLLDTDGDG 84


                ....*..
gi 58652122 146 ELTLEEF 152
Cdd:COG5126  85 KISADEF 91
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 30-161 5.75e-06

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: 45.27  E-value: 5.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  30 GLITLFELKS-ILGLQ--GMNEDansyVDQVFCTFDMDRDGYIDFVEYI--------AAISLMLKGEINQKLKWY----F 94
Cdd:cd16226  50 GFVTEEELKDwIKYVQkkYIRED----VDRQWKEYDPNKDGKLSWEEYKkatygfldDEEEDDDLHESYKKMIRRderrW 125

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58652122  95 KLFDQDGNGKIDKDELeTIFTAIQDITRNRDIVPEEIValifEKIDVNGEGELTLEEFI------EGAKEHPE 161
Cdd:cd16226 126 KAADQDGDGKLTKEEF-TAFLHPEEFPHMRDIVVQETL----EDIDKNKDGFISLEEYIgdmyrdDDEEEDPD 193
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 30-161 9.79e-06

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: 44.74  E-value: 9.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  30 GLITLFELKSILgLQGMNEDANSYVDQVFCTFDMDRDGYIDFVEYIAA------------ISLMLKGEINQKL----KWY 93
Cdd:cd15899  50 GFISAKELHSWI-LESFKRHAMEESKEQFRAVDPDEDGHVSWDEYKNDtygsvgddeenvADNIKEDEEYKKLllkdKKR 128

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58652122  94 FKLFDQDGNGKIDKDELeTIFTAIQDITRNRDIVPEEIValifEKIDVNGEGELTLEEFIEGAKEHPE 161
Cdd:cd15899 129 FEAADQDGDLILTLEEF-LAFLHPEESPYMLDFVIKETL----EDLDKNGDGFISLEEFISDPYSADE 191
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 29-153 1.03e-05

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 43.79  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  29 SGLITLFELKSILglqgMNEDANSYVDQVfCT-----FDMDRDGYIDFVEYIAaislmLKGEINQklkW--YFKLFDQDG 101
Cdd:cd16184  14 SGKISAKELQQAL----VNGNWSHFNDET-CRlmigmFDKDKSGTIDIYEFQA-----LWNYIQQ---WkqVFQQFDRDR 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 58652122 102 NGKIDKDELETIFTaiqdiTRNRDIVPEEIVALIFeKIDVNGEGELTLEEFI 153
Cdd:cd16184  81 SGSIDENELHQALS-----QMGYRLSPQFVQFLVS-KYDPRARRSLTLDQFI 126
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 62-154 2.54e-05

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


Pssm-ID: 320009  Cd Length: 107  Bit Score: 41.59  E-value: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  62 DMDRDGYIDfveYIAAISLMLKGEINQKLKWYFKLFDQDGNGKIDKDELETIFTAIqditrnrdIVPEEIVALIFEKIDV 141
Cdd:cd00252  22 EQDENRSYD---NNKRGHDLSGTMRKEIAQWEFDNLDNNKDGKLDKRELAPFRAPL--------MPLEHCARGFFESCDL 90

                        90
                ....*....|...
gi 58652122 142 NGEGELTLEEFIE 154
Cdd:cd00252  91 NKDKKISLQEWLG 103
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 94-154 4.76e-05

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 41.45  E-value: 4.76e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58652122  94 FKLFDQDGNGKIDKDELETIFTAIQDITRNRDIVPEEIVALIFEKIDV----------NGEGELTLEEFIE 154
Cdd:cd15900   6 FKMFDLDGDGELDKEEFNKVQSIIRSQTSVGQRHRDHTNGESTKLGMNstlaryffgkDGKQKLSIEKFLE 76
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 61-154 4.97e-05

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 41.86  E-value: 4.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  61 FDMDRDGYIDFVEYIAaislmLKGEINQklkWY--FKLFDQDGNGKIDKDELETIFTA----IQDitrnrdivpeEIVAL 134
Cdd:cd16183  46 FDRDNSGTINFQEFAA-----LWKYITD---WQncFRSFDRDNSGNIDKNELKQALTSfgyrLSD----------QFYDI 107

                        90       100
                ....*....|....*....|
gi 58652122 135 IFEKIDVNGEGELTLEEFIE 154
Cdd:cd16183 108 LVRKFDRQGRGTIAFDDFIQ 127
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 89-167 1.11e-04

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 40.34  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  89 KLKWYFKLFDQDGNGKIDKDELETIFTAIqDITrnrdiVPEEIVALIFEKIDVNGEGELTLEEFIEGAK---EHPEIMDM 165
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRL-NIR-----VSEKELKKLFKEVDTNGDGTLTFDEFEELYKsltERPELEPI 74


                ..
gi 58652122 166 LK 167
Cdd:cd15898  75 FK 76
PTZ00183 PTZ00183
centrin; Provisional
 45-164 3.01e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.29  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122   45 GMNEDANSYVDQVFCTFDMDRDGYIDFVE-YIAAISLMLKGEiNQKLKWYFKLFDQDGNGKIDKDELETIFTAiqdITRN 123
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKElKVAMRSLGFEPK-KEEIKQMIADVDKDGSGKIDFEEFLDIMTK---KLGE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 58652122  124 RDivPEEIVALIFEKIDVNGEGELTLEEFIEGAKEHPEIMD 164
Cdd:PTZ00183  86 RD--PREEILKAFRLFDDDKTGKISLKNLKRVAKELGETIT 124
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
94-160 3.83e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 39.66  E-value: 3.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58652122   94 FKLFDQDGNGKIDKDELETIFTAIQDitrnrDIVPEEIVALiFEKIDVNGEGELTLEEFIEGAKEHP 160
Cdd:NF041410  33 FAKLDSDGDGSVSQDELSSALSSKSD-----DGSLIDLSEL-FSDLDSDGDGSLSSDELAAAAPPPP 93
PTZ00183 PTZ00183
centrin; Provisional
 29-153 4.03e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.90  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122   29 SGLITLFELKSI---LGLQGMNEDansyVDQVFCTFDMDRDGYIDFVEYIAAI-SLMLKGEINQKLKWYFKLFDQDGNGK 104
Cdd:PTZ00183  31 SGTIDPKELKVAmrsLGFEPKKEE----IKQMIADVDKDGSGKIDFEEFLDIMtKKLGERDPREEILKAFRLFDDDKTGK 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 58652122  105 IDKDELETIFTAIQDitrnrDIVPEEIVALIfEKIDVNGEGELTLEEFI 153
Cdd:PTZ00183 107 ISLKNLKRVAKELGE-----TITDEELQEMI-DEADRNGDGEISEEEFY 149
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 68-152 4.66e-04

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 37.90  E-value: 4.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  68 YIDFVEYIAaiSLMLKGEINQKLKWYFKLFDQDGNGKIDKDELETIFTAIQDITRNRDIVPEEIVALIfEKIDVNGEGEL 147
Cdd:cd16252  19 YSKFFEYMQ--KFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMPVAPLSDEEAEAMI-QAADTDGDGRI 95


                ....*
gi 58652122 148 TLEEF 152
Cdd:cd16252  96 DFQEF 100
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 60-154 4.71e-04

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: 39.61  E-value: 4.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  60 TFDMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFK-LFDQDGNGKIDKDELetIFTAIQDitrNRDIVPEEIVALiFEK 138
Cdd:cd16227 167 DKDKDNDGFISFQEFLGDRAGHEDKEWLLVEKDRFDeDYDKDGDGKLDGEEI--LSWLVPD---NEEIAEEEVDHL-FAS 240

                        90
                ....*....|....*.
gi 58652122 139 IDVNGEGELTLEEFIE 154
Cdd:cd16227 241 ADDDHDDRLSFDEILD 256
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 93-153 4.99e-04

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


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 36.81  E-value: 4.99e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58652122  93 YFKLFDQDGNGKIDKDELETIFTAIQditrnrdiVPEEIVALIFEKIDVNGEGELTLEEFI 153
Cdd:cd00052   4 IFRSLDPDGDGLISGDEARPFLGKSG--------LPRSVLAQIWDLADTDKDGKLDKEEFA 56
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
29-152 5.80e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 39.28  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122   29 SGLITLFELKSILGlQGMNEDANSYVDQVFCTFDMDRDGYIDFVEYIAAISL----MLKGEINQKLKWYFKLFDQDGNGK 104
Cdd:NF041410  41 DGSVSQDELSSALS-SKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPppppPDQAPSTELADDLLSALDTDGDGS 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 58652122  105 IDKDELETIFTAIQDITRNRDivpeeivalIFEKIDVNGEGELTLEEF 152
Cdd:NF041410 120 ISSDELSAGLTSAGSSADSSQ---------LFSALDSDGDGSVSSDEL 158
EF-hand_7 pfam13499
EF-hand domain pair;
56-115 6.27e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.85  E-value: 6.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58652122    56 QVFCTFDMDRDGYI---DFVEYIAAISLMLKGEINQKLKWyFKLFDQDGNGKIDKDELETIFT 115
Cdd:pfam13499   6 EAFKLLDSDGDGYLdveELKKLLRKLEEGEPLSDEEVEEL-FKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 89-117 6.48e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 35.82  E-value: 6.48e-04
                           10        20
                   ....*....|....*....|....*....
gi 58652122     89 KLKWYFKLFDQDGNGKIDKDELETIFTAI 117
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_8 pfam13833
EF-hand domain pair;
28-76 6.58e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 6.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 58652122    28 PSGLITLFELKSILGLQGMNEDANSYVDQVFCTFDMDRDGYIDFVEYIA 76
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCV 49
EF-hand_6 pfam13405
EF-hand domain;
89-117 7.83e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.62  E-value: 7.83e-04
                          10        20
                  ....*....|....*....|....*....
gi 58652122    89 KLKWYFKLFDQDGNGKIDKDELETIFTAI 117
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
PPP2R3C cd21505
serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric ...
 53-153 8.97e-04

serine/threonine protein phosphatase 2A regulatory subunit B" subunit gamma; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This subfamily includes protein phosphatase subunit G5PR (also known as serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma, G4-1, G5pr, GDRM, SPGF36, or C14orf10) that is encoded by the PPP2R3C gene. It is involved in the control of the dynamic organization of the cortical cytoskeleton and plays an important role in the organization of interphase microtubule arrays in part through the regulation of nucleation geometry. G5PR is involved in the ontogeny of multiple organs, especially critical for testis development and spermatogenesis. PPP2R3C gene variants cause syndromic 46,XY gonadal dysgenesis and impaired spermatogenesis in humans, and thus is emerging as a potential therapeutic target for male infertility.


Pssm-ID: 410338 [Multi-domain]  Cd Length: 382  Bit Score: 39.09  E-value: 8.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  53 YVDQVF--C-TFD--MDRDGYIDFVeyiaaISLMLKGEInQKLKWYFKLFDQDGNGKIDKDELETIFTAIQDITRNRDIV 127
Cdd:cd21505 255 FIDRVFqeClTYNgeMDYKTFLDFV-----LAMENRKEP-QALQYFFRILDLKGQGYLTPFTLNYFFRAIQEKMKEHGQE 328

                        90       100
                ....*....|....*....|....*....
gi 58652122 128 P---EEIVALIFEKIDVNGEGELTLEEFI 153
Cdd:cd21505 329 PvsfEDVKDEIFDMVKPKDPLKITLQDLI 357
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 53-154 9.40e-04

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 37.65  E-value: 9.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  53 YVDQVFCTFDMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFKLFDQDGNGKIDKDELETIFTaiqDITRNRDIVPeeiv 132
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYK---SLTERPELEP---- 73

                        90       100
                ....*....|....*....|..
gi 58652122 133 alIFEKIDVNGEGELTLEEFIE 154
Cdd:cd15898  74 --IFKKYAGTNRDYMTLEEFIR 93
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 62-170 1.36e-03

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: 38.19  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  62 DMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFKLFDQDGNGKIDKDELETIFTAI----QDITRNRDIVPEEIVAL--- 134
Cdd:cd15899  45 DVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYKNDTYGSvgddEENVADNIKEDEEYKKLllk 124

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 58652122 135 ---IFEKIDVNGEGELTLEEFIegAKEHPEIMD-MLKILM 170
Cdd:cd15899 125 dkkRFEAADQDGDLILTLEEFL--AFLHPEESPyMLDFVI 162
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 62-154 1.85e-03

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: 37.80  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  62 DMDRDGYIDFVEYIAaiSLMLKGEINQKLKW-------YFKLFDQDGNGKIDKDELETIFtaiqdITRNRDIVPEEIVAL 134
Cdd:cd16224 171 DKDGDGFISLEEFLG--DYRKDPTANEDPEWiivekdrFVNDYDKDNDGKLDPQELLPWV-----VPNNYGIAQEEALHL 243

                        90       100
                ....*....|....*....|
gi 58652122 135 IFEkIDVNGEGELTLEEFIE 154
Cdd:cd16224 244 IDE-MDLNGDGRLSEEEILE 262
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 89-117 2.55e-03

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.91  E-value: 2.55e-03
                          10        20
                  ....*....|....*....|....*....
gi 58652122    89 KLKWYFKLFDQDGNGKIDKDELETIFTAI 117
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 62-154 2.96e-03

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: 37.42  E-value: 2.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  62 DMDRDGYIDFVEYIaaiSLMLKGEINQKLKWYFK--------LFDQDGNGKIDKDELETIFtaiqdITRNRDIVPEEIVA 133
Cdd:cd15899 170 DKNGDGFISLEEFI---SDPYSADENEEEPEWVKvekerfveLRDKDKDGKLDGEELLSWV-----DPSNQEIALEEAKH 241

                        90       100
                ....*....|....*....|.
gi 58652122 134 LIFEKiDVNGEGELTLEEFIE 154
Cdd:cd15899 242 LIAES-DENKDGKLSPEEILD 261
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 35-113 3.44e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 35.59  E-value: 3.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  35 FELKSILGLQGMNEDANSYVDQVFCTFDMDRDGYIDFVEyiaaISLMLKG-------EINQKLKWYFKLFDQDGNGKIDK 107
Cdd:cd16251  17 FNYKKFFEHVGLKQKSEDQIKKVFQILDKDKSGFIEEEE----LKYILKGfsiagrdLTDEETKALLAAGDTDGDGKIGV 92


                ....*.
gi 58652122 108 DELETI 113
Cdd:cd16251  93 EEFATL 98
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 62-154 5.60e-03

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: 36.41  E-value: 5.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  62 DMDRDGYIDFVEYIAAislMLKGEINQK-LKW------YFKLF-DQDGNGKIDKDELetiftaiqditrnRD-IVPE--- 129
Cdd:cd16226 166 DKNKDGFISLEEYIGD---MYRDDDEEEdPDWvksereQFKEFrDKNKDGKMDREEV-------------KDwILPEdyd 229

                        90       100
                ....*....|....*....|....*....
gi 58652122 130 ----EIVALIFEKiDVNGEGELTLEEFIE 154
Cdd:cd16226 230 haeaEAKHLIYEA-DDDKDGKLTKEEILD 257
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 60-122 5.83e-03

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 35.71  E-value: 5.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58652122  60 TFDMDRDGYIDFVEYIAAISLMLKGEINQKLKWYFKLFDqDGNGKIDKDELETIFTAIQDITR 122
Cdd:cd15901  62 LYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQLA-DSSGFISRERLTQFLQDLLQIPD 123
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 29-79 5.88e-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: 5.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 58652122  29 SGLITLFELKSILGLQGMNEDaNSYVDQVFCTFDMDRDGYIDFVEYIAAIS 79
Cdd:cd00051  14 DGTISADELKAALKSLGEGLS-EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 82-153 7.62e-03

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 34.41  E-value: 7.62e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58652122  82 LKGEINQKLKWYFKLFDQDGNGKIDKDELETIftaIQDITRN-RDIVPEEIVALIFEKiDVNGEGELTLEEFI 153
Cdd:cd16254  28 LKKKSADDVKKVFHILDKDKSGFIEEDELKFV---LKGFSPDgRDLSDKETKALLAAG-DKDGDGKIGIDEFA 96
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 35-113 8.33e-03

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 34.41  E-value: 8.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58652122  35 FELKSILGLQGMNEDANSYVDQVFCTFDMDRDGYIDFVEyiaaISLMLKG------EINQK-LKWYFKLFDQDGNGKIDK 107
Cdd:cd16254  17 FDYKKFFEMVGLKKKSADDVKKVFHILDKDKSGFIEEDE----LKFVLKGfspdgrDLSDKeTKALLAAGDKDGDGKIGI 92


                ....*.
gi 58652122 108 DELETI 113
Cdd:cd16254  93 DEFATL 98
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 90-154 9.79e-03

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


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 34.89  E-value: 9.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58652122  90 LKWYFKLFDQDGNGKIDKDEletiftaIQDITRNRDI-VPEEIVALIFEKIDVNGEGELTLEEFIE 154
Cdd:cd16202   2 LKDQFRKADKNGDGKLSFKE-------CKKLLKKLNVkVDKDYAKKLFQEADTSGEDVLDEEEFVQ 60
 
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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