NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|9790115|ref|NP_062655|]
View 

neuronal calcium sensor 1 [Mus musculus]

Protein Classification

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

EF-hand (EFh) domain-containing protein similar to Homo sapiens guanylyl cyclase-activating proteins (GCAP1 and GCAP2), myosin regulatory light chain proteins, (MYL2, MYL5, MYL9, MYL10, and MYL12), and Kv channel-interacting proteins (KChIP1, KChIP2 and KChIP4)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
22-174 7.74e-17

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 7.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   22 FTEKEVQQWYKGFIKDCpSGQLDAAGFQKIYKQFFpfgdptkfaTFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKL 101
Cdd:COG5126   2 LQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9790115  102 RWAFKLYDLDNDGYITRNEMLDIVDAIyqmvgntvelpeeeNTPEKRVDRIFAMMDKNADGKLTLQEFQEGSK 174
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
22-174 7.74e-17

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 7.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   22 FTEKEVQQWYKGFIKDCpSGQLDAAGFQKIYKQFFpfgdptkfaTFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKL 101
Cdd:COG5126   2 LQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9790115  102 RWAFKLYDLDNDGYITRNEMLDIVDAIyqmvgntvelpeeeNTPEKRVDRIFAMMDKNADGKLTLQEFQEGSK 174
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-172 1.22e-15

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: 67.96  E-value: 1.22e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9790115  100 KLRWAFKLYDLDNDGYITRNEMLDIVDAIYqmvgntvelpeeENTPEKRVDRIFAMMDKNADGKLTLQEFQEG 172
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLG------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
98-171 5.72e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 58.42  E-value: 5.72e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9790115     98 DEKLRWAFKLYDLDNDGYITRNEMLDivdaIYQMVGNTVELPEEEntpekrVDRIFAMMDKNADGKLTLQEFQE 171
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK----LLRKLEEGEPLSDEE------VEELFKEFDLDKDGRISFEEFLE 64
PTZ00184 PTZ00184
calmodulin; Provisional
 70-169 3.45e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.75  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115    70 NVFDENKDGRIEFSEFIQALSVTSRGT-LDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQmvgntvELPEEEntpekr 148
Cdd:PTZ00184  54 NEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGE------KLTDEE------ 121

                         90       100
                 ....*....|....*....|.
gi 9790115   149 VDRIFAMMDKNADGKLTLQEF 169
Cdd:PTZ00184 122 VDEMIREADVDGDGQINYEEF 142
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 100-128 1.36e-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: 37.74  E-value: 1.36e-04
                           10        20
                   ....*....|....*....|....*....
gi 9790115     100 KLRWAFKLYDLDNDGYITRNEMLDIVDAI 128
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
22-174 7.74e-17

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 7.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   22 FTEKEVQQWYKGFIKDCpSGQLDAAGFQKIYKQFFpfgdptkfaTFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKL 101
Cdd:COG5126   2 LQRRKLDRRFDLLDADG-DGVLERDDFEALFRRLW---------ATLFSEADTDGDGRISREEFVAGMESLFEATVEPFA 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9790115  102 RWAFKLYDLDNDGYITRNEMLDIVDAIyqmvgntvelpeeeNTPEKRVDRIFAMMDKNADGKLTLQEFQEGSK 174
Cdd:COG5126  72 RAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 100-172 1.22e-15

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: 67.96  E-value: 1.22e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9790115  100 KLRWAFKLYDLDNDGYITRNEMLDIVDAIYqmvgntvelpeeENTPEKRVDRIFAMMDKNADGKLTLQEFQEG 172
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLG------------EGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 67-125 2.90e-14

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: 64.11  E-value: 2.90e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 9790115   67 FVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIV 125
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
98-171 5.72e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 58.42  E-value: 5.72e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9790115     98 DEKLRWAFKLYDLDNDGYITRNEMLDivdaIYQMVGNTVELPEEEntpekrVDRIFAMMDKNADGKLTLQEFQE 171
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK----LLRKLEEGEPLSDEE------VEELFKEFDLDKDGRISFEEFLE 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
64-130 1.04e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 51.72  E-value: 1.04e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9790115   64 FATFVFNVFDENKDGRIEFSEFIQALSVtsRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQ 130
Cdd:COG5126  70 FARAAFDLLDTDGDGKISADEFRRLLTA--LGVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYT 134
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 67-129 2.58e-07

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: 48.04  E-value: 2.58e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   67 FVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDlDNDGYITR-------NEMLDIVDAIY 129
Cdd:cd15901  58 WLLNLYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQLA-DSSGFISRerltqflQDLLQIPDLIG 126
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 72-168 4.01e-07

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: 48.85  E-value: 4.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   72 FDENKDGRIEFSEFI--QALSVTSRGTLDEKLRWAfKLYDLDNDGYITRNEMLDIVdaiyqmvgntveLPEEENTPEKRV 149
Cdd:cd16227 168 KDKDNDGFISFQEFLgdRAGHEDKEWLLVEKDRFD-EDYDKDGDGKLDGEEILSWL------------VPDNEEIAEEEV 234

                        90
                ....*....|....*....
gi 9790115  150 DRIFAMMDKNADGKLTLQE 168
Cdd:cd16227 235 DHLFASADDDHDDRLSFDE 253
EF-hand_7 pfam13499
EF-hand domain pair;
67-125 4.71e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 45.32  E-value: 4.71e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9790115     67 FVFNVFDENKDGRIEFSEFIQALSVTSRG--TLDEKLRWAFKLYDLDNDGYITRNEMLDIV 125
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 73-168 1.75e-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: 46.67  E-value: 1.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   73 DENKDGRIEFSEFIQALSVTSRGT------LDEKLRWAfKLYDLDNDGYITRNEMLDIVDaiyqmvgntvelPEEENTPE 146
Cdd:cd15899 170 DKNGDGFISLEEFISDPYSADENEeepewvKVEKERFV-ELRDKDKDGKLDGEELLSWVD------------PSNQEIAL 236

                        90       100
                ....*....|....*....|..
gi 9790115  147 KRVDRIFAMMDKNADGKLTLQE 168
Cdd:cd15899 237 EEAKHLIAESDENKDGKLSPEE 258
PTZ00184 PTZ00184
calmodulin; Provisional
 70-169 3.45e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 44.75  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115    70 NVFDENKDGRIEFSEFIQALSVTSRGT-LDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQmvgntvELPEEEntpekr 148
Cdd:PTZ00184  54 NEVDADGNGTIDFPEFLTLMARKMKDTdSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGE------KLTDEE------ 121

                         90       100
                 ....*....|....*....|.
gi 9790115   149 VDRIFAMMDKNADGKLTLQEF 169
Cdd:PTZ00184 122 VDEMIREADVDGDGQINYEEF 142
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
 72-168 1.06e-05

EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t specific neurons of the central and peripheral nervous system. It possibly functions as a calcium buffer, calcium sensor, and apoptosis regulator, which may be implicated in many biological processes, including cell proliferation, differentiation, and cell death. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. CR I-II consists of EF-hand motifs 1 and 2, and CR III-VI consists of EF-hand motifs 3-6. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. Thus, CR has two pairs of cooperative binding sites (I-II and III-IV), which display high affinity calcium-binding sites, and one independent calcium ion-binding site (V), which displays lower affinity binding.


Pssm-ID: 320077 [Multi-domain]  Cd Length: 248  Bit Score: 44.48  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   72 FDENKDGRIEFSEFIQALSVTSRGTL--------DEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQmvgnTVELPEEEN 143
Cdd:cd16177  55 YDKNADGRIEMAELAQILPTEENFLLcfrqhvgsSSEFMEAWRKYDTDRSGYIEANELKGFLSDLLK----KANRPYDEK 130

                        90       100
                ....*....|....*....|....*
gi 9790115  144 TPEKRVDRIFAMMDKNADGKLTLQE 168
Cdd:cd16177 131 KLQEYTQTILRMFDLNGDGKLGLSE 155
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 68-168 1.41e-05

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: 44.32  E-value: 1.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   68 VFNVFDENKDGRIEFSEFIQALSVTSRGTL----DEKLRWA------FKLYDLDNDGYITRNEMLDIVDAIyqMVGNTVE 137
Cdd:cd16179  54 FMEAYDENQDGRIDIRELAQLLPTEENFLLlfrrDNPLDSSvefmkvWREYDKDNSGYIEADELKNFLKHL--LKEAKRD 131

                        90       100       110
                ....*....|....*....|....*....|.
gi 9790115  138 LPEEENTPEKRVDRIFAMMDKNADGKLTLQE 168
Cdd:cd16179 132 NDVSEDKLIEYTDTILQLFDRNKDGKLQLSE 162
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 40-164 2.05e-05

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 43.50  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   40 SGQLDAAGFQKIYKQFF----PFGDPTKFATFV---FNVFDENKDGRIEFSEFIQALSV------TSRGTLDEKLRW--- 103
Cdd:cd15902 104 SGFIEAKELKGFLKDLLlknkKHVSPPKLDEYTkliLKEFDANKDGKLELDEMAKLLPVqenfllKFQILGAMDLTKedf 183

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9790115  104 --AFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTpekrVDRIFAMMDKNADGKL 164
Cdd:cd15902 184 ekVFEHYDKDNNGVIEGNELDALLKDLLEKNKADIDKPDLENF----RDAILRACDKNKDGKI 242
PTZ00183 PTZ00183
centrin; Provisional
 69-167 2.77e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.37  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115    69 FNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVdaiyqmvgnTVELPEEENTPEkr 148
Cdd:PTZ00183  23 FDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIM---------TKKLGERDPREE-- 91

                         90
                 ....*....|....*....
gi 9790115   149 VDRIFAMMDKNADGKLTLQ 167
Cdd:PTZ00183  92 ILKAFRLFDDDKTGKISLK 110
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 81-171 6.59e-05

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: 40.59  E-value: 6.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   81 EFSEFIQalSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIyQMVGNTVELPEEEntpekrVDRIFAMMDKNA 160
Cdd:cd16252  21 KFFEYMQ--KFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTV-PSSMPVAPLSDEE------AEAMIQAADTDG 91

                        90
                ....*....|.
gi 9790115  161 DGKLTLQEFQE 171
Cdd:cd16252  92 DGRIDFQEFSD 102
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 21-169 1.10e-04

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 41.57  E-value: 1.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   21 YFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFpfgdptkfatfvfNVFDENKDGRIEFSEFIQALsVTSRGTLDEK 100
Cdd:cd15902  15 YIEGKELDSFLRELLKALNGKDKTDDEVAEKKKEFM-------------EKYDENEDGKIEIRELANIL-PTEENFLLLF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115  101 LRW-----------AFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEentpEKRVDRIFAMMDKNADGKLTLQEF 169
Cdd:cd15902  81 RREqplissvefmkIWRKYDTDGSGFIEAKELKGFLKDLLLKNKKHVSPPKL----DEYTKLILKEFDANKDGKLELDEM 156
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 100-128 1.36e-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: 37.74  E-value: 1.36e-04
                           10        20
                   ....*....|....*....|....*....
gi 9790115     100 KLRWAFKLYDLDNDGYITRNEMLDIVDAI 128
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 25-117 1.86e-04

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: 40.20  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   25 KEVQQWYKGFIK---DcPSGQLDAAGFQKIYKQFfPFGDPTKFATFVFNVFDENKDGRIEFSEFIQALSVTSRgtldekL 101
Cdd:cd16180  64 KYIQDWRRLFRRfdrD-RSGSIDFNELQNALSSF-GYRLSPQFVQLLVRKFDRRRRGSISFDDFVEACVTLKR------L 135

                        90
                ....*....|....*.
gi 9790115  102 RWAFKLYDLDNDGYIT 117
Cdd:cd16180 136 TDAFRKYDTNRTGYAT 151
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 26-131 2.28e-04

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: 39.82  E-value: 2.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   26 EVQQWYKGFIKDCpSGQLDAAGFQKIYKQffpfGDPTKFAT----FVFNVFDENKDGRIEFSEFIQalsvtsrgtLDEKL 101
Cdd:cd16180   1 ELRRIFQAVDRDR-SGRISAKELQRALSN----GDWTPFSIetvrLMINMFDRDRSGTINFDEFVG---------LWKYI 66

                        90       100       110
                ....*....|....*....|....*....|...
gi 9790115  102 R-W--AFKLYDLDNDGYITRNEMldiVDAIYQM 131
Cdd:cd16180  67 QdWrrLFRRFDRDRSGSIDFNEL---QNALSSF 96
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 31-168 2.54e-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: 40.47  E-value: 2.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   31 YKGFIKDCpSGQLDAAGFQKIYKQFFPFGDPTK---------FATFVFNVFDENKDGRIEFSEFIQALSV---------- 91
Cdd:cd16179 101 WREYDKDN-SGYIEADELKNFLKHLLKEAKRDNdvsedklieYTDTILQLFDRNKDGKLQLSEMARLLPVkenflcrpif 179

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9790115   92 TSRGTLD-EKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKrvdrIFAMMDKNADGKLTLQE 168
Cdd:cd16179 180 KGAGKLTrEDIDRVFALYDRDNNGTIENEELTGFLKDLLELVQEDYDEQDLEEFKEI----ILRGWDFNNDGKISRKE 253
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 26-121 2.62e-04

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: 39.94  E-value: 2.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   26 EVQQWYKGFIKDcPSGQLDAAGFQkiykQFFPFGDPTKFA----TFVFNVFDENKDGRIEFSEFiQALSvtsrgTLDEKL 101
Cdd:cd16184   1 EVQQWFQAVDRD-RSGKISAKELQ----QALVNGNWSHFNdetcRLMIGMFDKDKSGTIDIYEF-QALW-----NYIQQW 69

                        90       100
                ....*....|....*....|
gi 9790115  102 RWAFKLYDLDNDGYITRNEM 121
Cdd:cd16184  70 KQVFQQFDRDRSGSIDENEL 89
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 73-169 3.59e-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: 40.12  E-value: 3.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   73 DENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYIT----RNEMLDIVDAIYQMVGNTVELPEEENTPEKR 148
Cdd:cd15899  45 DVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSwdeyKNDTYGSVGDDEENVADNIKEDEEYKKLLLK 124

                        90       100
                ....*....|....*....|.
gi 9790115  149 VDRIFAMMDKNADGKLTLQEF 169
Cdd:cd15899 125 DKKRFEAADQDGDLILTLEEF 145
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 105-169 3.86e-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: 37.20  E-value: 3.86e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9790115  105 FKLYDLDNDGYITRNEMLDIVdaiyqmvgntvelpEEENTPEKRVDRIFAMMDKNADGKLTLQEF 169
Cdd:cd00052   5 FRSLDPDGDGLISGDEARPFL--------------GKSGLPRSVLAQIWDLADTDKDGKLDKEEF 55
PRK12309 PRK12309
transaldolase;
105-172 4.34e-04

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 40.10  E-value: 4.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9790115   105 FKLYDLDNDGYITRNEMLDivdaiyqmvgntvelpeeentpekrVDRIFAMMDKNADGKLTLQEFQEG 172
Cdd:PRK12309 340 FRLYDLDGDGFITREEWLG-------------------------SDAVFDALDLNHDGKITPEEMRAG 382
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
 67-118 4.78e-04

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: 39.14  E-value: 4.78e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9790115   67 FVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDlDNDGYITR 118
Cdd:cd16242  58 WLLNVYDSGRSGKIRVLSFKVGLVLLCNAHLEEKYRYLFSLIA-DPNGCVDQ 108
EF-hand_6 pfam13405
EF-hand domain;
100-128 5.34e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 5.34e-04
                          10        20
                  ....*....|....*....|....*....
gi 9790115    100 KLRWAFKLYDLDNDGYITRNEMLDIVDAI 128
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 76-169 5.74e-04

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: 37.74  E-value: 5.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   76 KDGRIEFSEFIQALSVTSRgtlDEKLRWAFKLYDLDNDGYITRNEMLDIVdaiYQMVgntvelpeeenTPEKRVDRIFAM 155
Cdd:cd00252  25 ENRSYDNNKRGHDLSGTMR---KEIAQWEFDNLDNNKDGKLDKRELAPFR---APLM-----------PLEHCARGFFES 87

                        90
                ....*....|....
gi 9790115  156 MDKNADGKLTLQEF 169
Cdd:cd00252  88 CDLNKDKKISLQEW 101
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 68-171 6.41e-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: 39.34  E-value: 6.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   68 VFNVFDENKDGRIEFSEFIQALSVTSRGTLD------EKLRWAfKLYDLDNDGYITRNEMLDIVdaiyqmVGNTVELPEE 141
Cdd:cd16224 166 ALEEHDKDGDGFISLEEFLGDYRKDPTANEDpewiivEKDRFV-NDYDKDNDGKLDPQELLPWV------VPNNYGIAQE 238

                        90       100       110
                ....*....|....*....|....*....|
gi 9790115  142 EntpekrVDRIFAMMDKNADGKLTLQEFQE 171
Cdd:cd16224 239 E------ALHLIDEMDLNGDGRLSEEEILE 262
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 100-125 7.57e-04

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: 35.45  E-value: 7.57e-04
                          10        20
                  ....*....|....*....|....*.
gi 9790115    100 KLRWAFKLYDLDNDGYITRNEMLDIV 125
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELL 26
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 73-169 8.28e-04

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: 39.10  E-value: 8.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   73 DENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEmldIVDAIYqmvGNTVELPEEENTPE------ 146
Cdd:cd16226  45 DKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEYDPNKDGKLSWEE---YKKATY---GFLDDEEEDDDLHEsykkmi 118

                        90       100
                ....*....|....*....|...
gi 9790115  147 KRVDRIFAMMDKNADGKLTLQEF 169
Cdd:cd16226 119 RRDERRWKAADQDGDGKLTKEEF 141
EF-hand_7 pfam13499
EF-hand domain pair;
40-90 9.52e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.46  E-value: 9.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 9790115     40 SGQLDAAGFQKIYKQFFPFGDPTK-FATFVFNVFDENKDGRIEFSEFIQALS 90
Cdd:pfam13499  16 DGYLDVEELKKLLRKLEEGEPLSDeEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 104-171 1.22e-03

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: 37.59  E-value: 1.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9790115  104 AFKLYDLDNDGYITRNEMLDIVDAIYQ--MVGNTVELPEEENTPEKRVDRIFAM--MDKNADGKLTLQEFQE 171
Cdd:cd15900   5 AFKMFDLDGDGELDKEEFNKVQSIIRSqtSVGQRHRDHTNGESTKLGMNSTLARyfFGKDGKQKLSIEKFLE 76
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 72-168 2.17e-03

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 37.51  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   72 FDENKDGRIEFSEFIQALSVTSRGTL--------DEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVElpeeEN 143
Cdd:cd16176  50 YGQSTDGKIGIVELAQILPTEENFLLffrqqlksSEEFMQTWRKYDADHSGFIEADELKSFLKDLLKKANKPFD----ES 125

                        90       100
                ....*....|....*....|....*
gi 9790115  144 TPEKRVDRIFAMMDKNADGKLTLQE 168
Cdd:cd16176 126 KLEEYTHTMLKMFDSNNDGKLGLTE 150
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 25-117 2.25e-03

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: 37.23  E-value: 2.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   25 KEVQQW---YKGFIKDcPSGQLDAAGFQKIYKQF-FPFGDPtkFATFVFNVFDENKDGRIEFSEFIQALSVTSRgtldek 100
Cdd:cd16183  64 KYITDWqncFRSFDRD-NSGNIDKNELKQALTSFgYRLSDQ--FYDILVRKFDRQGRGTIAFDDFIQCCVVLQT------ 134

                        90
                ....*....|....*..
gi 9790115  101 LRWAFKLYDLDNDGYIT 117
Cdd:cd16183 135 LTDSFRRYDTDQDGWIQ 151
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 69-169 2.56e-03

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


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 37.68  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   69 FNVFDENKDGRIEFSEFIQA---------LSVTSRGTLDEKL-----RWAFKLYDLDNDGYITRNEMLdivdAIYQmvgn 134
Cdd:cd16227  78 FEEADEDGDGKVTWEEYLADsfgyddednEEMIKDSTEDDLKlleddKEMFEAADLNKDGKLDKTEFS----AFQH---- 149

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 9790115  135 tvelPEE-ENTPEKRVDRIFAMMDKNADGKLTLQEF 169
Cdd:cd16227 150 ----PEEyPHMHPVLIEQTLRDKDKDNDGFISFQEF 181
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 70-168 2.80e-03

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 37.28  E-value: 2.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   70 NVFDENKDGRIEFSEFIqALSVtsrGTLDEKLRWAFKLY------------DLDNDGYITRNEMLDIVDaiyqmvgntve 137
Cdd:cd16225 175 HDLDQDGDEKLTLDEFV-SLPP---GTVEEQQAEDDDEWkkerkkefeeviDLNHDGKVTKEELEEYMD----------- 239

                        90       100       110
                ....*....|....*....|....*....|.
gi 9790115  138 lPEEENTPEKRVDRIFAMMDKNADGKLTLQE 168
Cdd:cd16225 240 -PRNERHALNEAKQLIAVADENKDGKLSLEE 269
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 73-168 3.89e-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: 36.79  E-value: 3.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115   73 DENKDGRIEFSEFIQALsVTSRGTLDE-----KLRWAFKLY-DLDNDGYITRNEMLDIVdaiyqmvgntveLPEEENTPE 146
Cdd:cd16226 166 DKNKDGFISLEEYIGDM-YRDDDEEEDpdwvkSEREQFKEFrDKNKDGKMDREEVKDWI------------LPEDYDHAE 232

                        90       100
                ....*....|....*....|..
gi 9790115  147 KRVDRIFAMMDKNADGKLTLQE 168
Cdd:cd16226 233 AEAKHLIYEADDDKDGKLTKEE 254
EF-hand_8 pfam13833
EF-hand domain pair;
76-123 4.18e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 34.21  E-value: 4.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 9790115     76 KDGRIEFSEFIQALSVTSRGTL-DEKLRWAFKLYDLDNDGYITRNEMLD 123
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLsEDEVDILFREFDTDGDGYISFDEFCV 49
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 149-175 6.54e-03

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: 33.12  E-value: 6.54e-03
                           10        20
                   ....*....|....*....|....*..
gi 9790115     149 VDRIFAMMDKNADGKLTLQEFQEGSKA 175
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
PLN02964 PLN02964
phosphatidylserine decarboxylase
 62-121 6.68e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 36.76  E-value: 6.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9790115    62 TKFATFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEM 121
Cdd:PLN02964 178 RSFARRILAIVDYDEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDEL 237
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 68-90 7.78e-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: 32.76  E-value: 7.78e-03
                          10        20
                  ....*....|....*....|...
gi 9790115     68 VFNVFDENKDGRIEFSEFIQALS 90
Cdd:pfam00036   5 IFRLFDKDGDGKIDFEEFKELLK 27
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 68-90 7.98e-03

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: 32.74  E-value: 7.98e-03
                           10        20
                   ....*....|....*....|...
gi 9790115      68 VFNVFDENKDGRIEFSEFIQALS 90
Cdd:smart00054   5 AFRLFDKDGDGKIDFEEFKDLLK 27
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH