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Conserved domains on  [gi|25150298|ref|NP_508201|]
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EF-hand domain-containing protein [Caenorhabditis elegans]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11473824)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Gene Ontology:  GO:0005509
PubMed:  2479149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-184 6.69e-15

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 68.28  E-value: 6.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  32 FTKKELKKWYKDFVRDCpSGELKMEEFQGIYKQFFpngdpskfaAFVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKL 111
Cdd:COG5126   2 LQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150298 112 DWAFSLYDVDKDGFITKDEMADIVDAIysmignmlelpkdeDTPQKRVEKIFTNMDRNLDGQLTREEFKEGSK 184
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-184 6.69e-15

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 68.28  E-value: 6.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  32 FTKKELKKWYKDFVRDCpSGELKMEEFQGIYKQFFpngdpskfaAFVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKL 111
Cdd:COG5126   2 LQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150298 112 DWAFSLYDVDKDGFITKDEMADIVDAIysmignmlelpkdeDTPQKRVEKIFTNMDRNLDGQLTREEFKEGSK 184
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 77-135 1.36e-13

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: 62.57  E-value: 1.36e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25150298  77 FVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEMADIV 135
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
73-186 8.06e-10

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 56.23  E-value: 8.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298   73 KFAAFVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEMAdivdaiysmigNMLELP--- 149
Cdd:NF041410  27 QFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELA-----------AAAPPPppp 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 25150298  150 KDEDTPQKRVEKIFTNMDRNLDGQLTREEF-----KEGSKAD 186
Cdd:NF041410  96 PDQAPSTELADDLLSALDTDGDGSISSDELsagltSAGSSAD 137
EF-hand_7 pfam13499
EF-hand domain pair;
108-181 1.63e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.56  E-value: 1.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150298   108 DEKLDWAFSLYDVDKDGFITKDEMADivdaIYSMIGNMLELPKDEdtpqkrVEKIFTNMDRNLDGQLTREEFKE 181
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK----LLRKLEEGEPLSDEE------VEELFKEFDLDKDGRISFEEFLE 64
PTZ00184 PTZ00184
calmodulin; Provisional
 80-179 9.87e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 40.90  E-value: 9.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298   80 NVFDDNHDGHISFSEFIAALSITSRGT-LDEKLDWAFSLYDVDKDGFITKDEMADIvdaiysmIGNMLELPKDEDtpqkr 158
Cdd:PTZ00184  54 NEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHV-------MTNLGEKLTDEE----- 121

                         90       100
                 ....*....|....*....|.
gi 25150298  159 VEKIFTNMDRNLDGQLTREEF 179
Cdd:PTZ00184 122 VDEMIREADVDGDGQINYEEF 142
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 110-138 5.19e-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: 36.20  E-value: 5.19e-04
                           10        20
                   ....*....|....*....|....*....
gi 25150298    110 KLDWAFSLYDVDKDGFITKDEMADIVDAI 138
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
32-184 6.69e-15

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 68.28  E-value: 6.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  32 FTKKELKKWYKDFVRDCpSGELKMEEFQGIYKQFFpngdpskfaAFVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKL 111
Cdd:COG5126   2 LQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150298 112 DWAFSLYDVDKDGFITKDEMADIVDAIysmignmlelpkdeDTPQKRVEKIFTNMDRNLDGQLTREEFKEGSK 184
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 77-135 1.36e-13

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: 62.57  E-value: 1.36e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25150298  77 FVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEMADIV 135
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
50-140 1.34e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.72  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  50 SGELKMEEFQGIYKQFFPNGDPsKFAAFVFNVFDDNHDGHISFSEFIAALsiTSRGTLDEKLDWAFSLYDVDKDGFITKD 129
Cdd:COG5126  47 DGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFE 123

                        90
                ....*....|.
gi 25150298 130 EMADIVDAIYS 140
Cdd:COG5126 124 EFVAAVRDYYT 134
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 110-182 1.35e-10

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: 54.86  E-value: 1.35e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150298 110 KLDWAFSLYDVDKDGFITKDEMADIVDAIYsmignmlelpkdEDTPQKRVEKIFTNMDRNLDGQLTREEFKEG 182
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLG------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
73-186 8.06e-10

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 56.23  E-value: 8.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298   73 KFAAFVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEMAdivdaiysmigNMLELP--- 149
Cdd:NF041410  27 QFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELA-----------AAAPPPppp 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 25150298  150 KDEDTPQKRVEKIFTNMDRNLDGQLTREEF-----KEGSKAD 186
Cdd:NF041410  96 PDQAPSTELADDLLSALDTDGDGSISSDELsagltSAGSSAD 137
EF-hand_7 pfam13499
EF-hand domain pair;
108-181 1.63e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.56  E-value: 1.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150298   108 DEKLDWAFSLYDVDKDGFITKDEMADivdaIYSMIGNMLELPKDEdtpqkrVEKIFTNMDRNLDGQLTREEFKE 181
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK----LLRKLEEGEPLSDEE------VEELFKEFDLDKDGRISFEEFLE 64
EF-hand_7 pfam13499
EF-hand domain pair;
77-135 2.53e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.70  E-value: 2.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150298    77 FVFNVFDDNHDGHISFSEFIAALSITSRG--TLDEKLDWAFSLYDVDKDGFITKDEMADIV 135
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 77-139 3.12e-05

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: 42.64  E-value: 3.12e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  77 FVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYDvDKDGFITK-------DEMADIVDAIY 139
Cdd:cd15901  58 WLLNLYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQLA-DSSGFISRerltqflQDLLQIPDLIG 126
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 83-178 3.98e-05

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: 42.96  E-value: 3.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  83 DDNHDGHISFSEFIAalSITSRGTLDEKLDW------AFSLY-DVDKDGFITKDEMADIVdaiysmignmleLPKDEDTP 155
Cdd:cd16226 166 DKNKDGFISLEEYIG--DMYRDDDEEEDPDWvksereQFKEFrDKNKDGKMDREEVKDWI------------LPEDYDHA 231

                        90       100
                ....*....|....*....|...
gi 25150298 156 QKRVEKIFTNMDRNLDGQLTREE 178
Cdd:cd16226 232 EAEAKHLIYEADDDKDGKLTKEE 254
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 83-178 5.38e-05

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: 42.81  E-value: 5.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  83 DDNHDGHISFSEFIAALSITSRGTldEKLDWAFS-------LYDVDKDGFITKDEMADIVDaiysmignmlelPKDEDTP 155
Cdd:cd15899 170 DKNGDGFISLEEFISDPYSADENE--EEPEWVKVekerfveLRDKDKDGKLDGEELLSWVD------------PSNQEIA 235

                        90       100
                ....*....|....*....|...
gi 25150298 156 QKRVEKIFTNMDRNLDGQLTREE 178
Cdd:cd15899 236 LEEAKHLIAESDENKDGKLSPEE 258
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 83-180 6.55e-05

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: 42.19  E-value: 6.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  83 DDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEmadIVDAIYsmiGNMLELPKDEDTP------Q 156
Cdd:cd16226  45 DKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEYDPNKDGKLSWEE---YKKATY---GFLDDEEEDDDLHesykkmI 118

                        90       100
                ....*....|....*....|....
gi 25150298 157 KRVEKIFTNMDRNLDGQLTREEFK 180
Cdd:cd16226 119 RRDERRWKAADQDGDGKLTKEEFT 142
PTZ00184 PTZ00184
calmodulin; Provisional
 80-179 9.87e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 40.90  E-value: 9.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298   80 NVFDDNHDGHISFSEFIAALSITSRGT-LDEKLDWAFSLYDVDKDGFITKDEMADIvdaiysmIGNMLELPKDEDtpqkr 158
Cdd:PTZ00184  54 NEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHV-------MTNLGEKLTDEE----- 121

                         90       100
                 ....*....|....*....|.
gi 25150298  159 VEKIFTNMDRNLDGQLTREEF 179
Cdd:PTZ00184 122 VDEMIREADVDGDGQINYEEF 142
PLN02964 PLN02964
phosphatidylserine decarboxylase
 73-135 1.33e-04

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 1.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150298   73 KFAAFVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEMADIV 135
Cdd:PLN02964 179 SFARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALL 241
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 87-179 1.69e-04

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: 41.11  E-value: 1.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  87 DGHISFSEFIAALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEMADIVDAIYS--MIGNMLELPKDEDTPQKRVEKIFT 164
Cdd:cd16230  51 DGWVSLAELRAWIAHTQQRHIRDSVSAAWQTYDTDRDGRVGWEELRNATYGHYEpgEEFHDVEDAETYKKMLARDERRFR 130

                        90
                ....*....|....*
gi 25150298 165 NMDRNLDGQLTREEF 179
Cdd:cd16230 131 VADQDGDSMATREEL 145
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 82-178 1.75e-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: 41.15  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  82 FDDNHDGHISFSEFIA-ALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEMADIVdaiysmignmleLPKDEDTPQKRVE 160
Cdd:cd16227 168 KDKDNDGFISFQEFLGdRAGHEDKEWLLVEKDRFDEDYDKDGDGKLDGEEILSWL------------VPDNEEIAEEEVD 235

                        90
                ....*....|....*...
gi 25150298 161 KIFTNMDRNLDGQLTREE 178
Cdd:cd16227 236 HLFASADDDHDDRLSFDE 253
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 36-180 3.57e-04

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 40.09  E-value: 3.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  36 ELKKWYKDFVRDCpSGELKMEEFQGIYKQFFPNGDPSK---------FAAFVFNVFDDNHDGHISFSE----------FI 96
Cdd:cd16179  96 EFMKVWREYDKDN-SGYIEADELKNFLKHLLKEAKRDNdvsedklieYTDTILQLFDRNKDGKLQLSEmarllpvkenFL 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  97 AALSITSRGTLD-EKLDWAFSLYDVDKDGFITKDEMadivdaiYSMIGNMLELPKDEDTPQ---KRVEKIFTNMDRNLDG 172
Cdd:cd16179 175 CRPIFKGAGKLTrEDIDRVFALYDRDNNGTIENEEL-------TGFLKDLLELVQEDYDEQdleEFKEIILRGWDFNNDG 247


                ....*...
gi 25150298 173 QLTREEFK 180
Cdd:cd16179 248 KISRKELT 255
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 110-138 5.19e-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: 36.20  E-value: 5.19e-04
                           10        20
                   ....*....|....*....|....*....
gi 25150298    110 KLDWAFSLYDVDKDGFITKDEMADIVDAI 138
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 78-181 5.24e-04

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: 39.72  E-value: 5.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  78 VFNVFDDNHDGHISFSEFIAALsiTSRGTLDEKLDWAF-------SLYDVDKDGFITKDEMADIVdaiysmignmleLPK 150
Cdd:cd16224 166 ALEEHDKDGDGFISLEEFLGDY--RKDPTANEDPEWIIvekdrfvNDYDKDNDGKLDPQELLPWV------------VPN 231

                        90       100       110
                ....*....|....*....|....*....|.
gi 25150298 151 DEDTPQKRVEKIFTNMDRNLDGQLTREEFKE 181
Cdd:cd16224 232 NYGIAQEEALHLIDEMDLNGDGRLSEEEILE 262
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 83-179 6.93e-04

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: 39.35  E-value: 6.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  83 DDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYDVDKDGFITKDEM-ADIVDAIYSMIGNMLELPKDEDTPQK---R 158
Cdd:cd15899  45 DVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYkNDTYGSVGDDEENVADNIKEDEEYKKlllK 124

                        90       100
                ....*....|....*....|.
gi 25150298 159 VEKIFTNMDRNLDGQLTREEF 179
Cdd:cd15899 125 DKKRFEAADQDGDLILTLEEF 145
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 36-141 2.02e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. 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. Peflin 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+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 37.12  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  36 ELKKWYKDFVRDCpSGELKMEEFQGIYKqffpNGDPSKFA----AFVFNVFDDNHDGHISFSEFIaalsitsrGTLDEKL 111
Cdd:cd16180   1 ELRRIFQAVDRDR-SGRISAKELQRALS----NGDWTPFSietvRLMINMFDRDRSGTINFDEFV--------GLWKYIQ 67

                        90       100       110
                ....*....|....*....|....*....|..
gi 25150298 112 DW--AFSLYDVDKDGFITKDEMAdivDAIYSM 141
Cdd:cd16180  68 DWrrLFRRFDRDRSGSIDFNELQ---NALSSF 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 115-179 2.38e-03

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


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 35.27  E-value: 2.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150298 115 FSLYDVDKDGFITKDEMADIVdaiySMIGnmleLPKDEdtpqkrVEKIFTNMDRNLDGQLTREEF 179
Cdd:cd00052   5 FRSLDPDGDGLISGDEARPFL----GKSG----LPRSV------LAQIWDLADTDKDGKLDKEEF 55
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 110-135 2.87e-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: 2.87e-03
                          10        20
                  ....*....|....*....|....*.
gi 25150298   110 KLDWAFSLYDVDKDGFITKDEMADIV 135
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELL 26
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 74-179 3.31e-03

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 36.49  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  74 FAAFVFNVFDDNHDGHISFSEF---IAALSITSRGTLDEKLdwaFSLYDVDKDGFITKDEMADivdaIYSMIgnmlelpk 150
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIkklLKRLNIRVSEKELKKL---FKEVDTNGDGTLTFDEFEE----LYKSL-------- 65

                        90       100
                ....*....|....*....|....*....
gi 25150298 151 dedTPQKRVEKIFTNMDRNLDGQLTREEF 179
Cdd:cd15898  66 ---TERPELEPIFKKYAGTNRDYMTLEEF 91
PRK12309 PRK12309
transaldolase;
115-182 3.42e-03

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 37.41  E-value: 3.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150298  115 FSLYDVDKDGFITKDEMADiVDAiysmignmlelpkdedtpqkrvekIFTNMDRNLDGQLTREEFKEG 182
Cdd:PRK12309 340 FRLYDLDGDGFITREEWLG-SDA------------------------VFDALDLNHDGKITPEEMRAG 382
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 77-132 3.59e-03

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.


Pssm-ID: 320000  Cd Length: 163  Bit Score: 36.44  E-value: 3.59e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25150298  77 FVFNVFDDNHDGHISFSEFIAALSITSRGTLDEKLDWAFSLYdVDKDGFITKDEMA 132
Cdd:cd16242  58 WLLNVYDSGRSGKIRVLSFKVGLVLLCNAHLEEKYRYLFSLI-ADPNGCVDQRRLG 112
EF-hand_7 pfam13499
EF-hand domain pair;
50-100 3.82e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.54  E-value: 3.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 25150298    50 SGELKMEEFQGIYKQFFPNGDPSK-FAAFVFNVFDDNHDGHISFSEFIAALS 100
Cdd:pfam13499  16 DGYLDVEELKKLLRKLEEGEPLSDeEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 36-131 6.53e-03

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: 35.70  E-value: 6.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150298  36 ELKKWYKDFVRDcPSGELKMEEFQgiykQFFPNGDPSKFAA----FVFNVFDDNHDGHISFSEFIAALSITSRgtldekl 111
Cdd:cd16184   1 EVQQWFQAVDRD-RSGKISAKELQ----QALVNGNWSHFNDetcrLMIGMFDKDKSGTIDIYEFQALWNYIQQ------- 68

                        90       100
                ....*....|....*....|..
gi 25150298 112 dW--AFSLYDVDKDGFITKDEM 131
Cdd:cd16184  69 -WkqVFQQFDRDRSGSIDENEL 89
 
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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